Biology as information

Bioinformatics: interdisciplinary field that develops methods and software tools for understanding biological data.

Biology + informatics.

Similar or related terms: computational biology, systems biology, etc.

A bit of pre-history

  • Schrodinger, What is life? (1944) - Mention to code-script of organism
  • Alexander Dounce (1952) - Comment about transcription and translation
  • Watson & Crick (1953) - Comment about permutation and genetic information
  • Crick (1958) - Central dogma of molecular biology

Central Dogma of Molecular Biology - https://commons.wikimedia.org/wiki/File:Central_Dogma_of_Molecular_Biochemistry_with_Enzymes.jpg

  • E. Zuckerland, L. Pauling (1964) - Molecules as documents of evolutionary history
  • M. Dayhoff et al. (1965) - Atlas of protein sequence and structure
  • Needleman-Wunsch (1970) - Sequence alignment algorithm
  • P. Hogeweg & B. Hesper (1970). First time Bioinformatics term is used

A bit of history

  • Sanger sequencing technique (1977)
  • GenBank and EMBL (1979-1980)
  • BLAST first implementation (1990)
  • First genome database (1993)
  • Influenza genome sequence (1995)
  • Human Genome Project - First Draft (1990-2003)

References

Sequences and file formats

Alphabets

Reference: Wikipedia article

Nucleic acids

Nucleic Acid Code Meaning Mnemonic
A A Adenine
C C Cytosine
G G Guanine
T T Thymine
U U Uracil
R A or G puRine
Y C, T or U pYrimidines
K G, T or U bases which are Ketones
M A or C bases with aMino groups
S C or G Strong interaction
W A, T or U Weak interaction
B not A (i.e. C, G, T or U) B comes after A
D not C (i.e. A, G, T or U) D comes after C
H not G (i.e., A, C, T or U) H comes after G
V neither T nor U (i.e. A, C or G) V comes after U
N A C G T U Nucleic acid
- gap of indeterminate length  

Amino acids

Amino Acid Code Meaning
A Alanine
B Aspartic acid (D) or Asparagine (N)
C Cysteine
D Aspartic acid
E Glutamic acid
F Phenylalanine
G Glycine
H Histidine
I Isoleucine
J Leucine (L) or Isoleucine (I)
K Lysine
L Leucine
M Methionine/Start codon
N Asparagine
O Pyrrolysine
P Proline
Q Glutamine
R Arginine
S Serine
T Threonine
U Selenocysteine
V Valine
W Tryptophan
Y Tyrosine
Z Glutamic acid (E) or Glutamine (Q)
X any
* translation stop
- gap of indeterminate length

FASTA file format

Reference: Wikipedia article

Two (three) parts

  1. Header - 1st line. Starting with >
  2. Comment - 2nd line. Starting with ; (deprecated)
  3. Sequence - 2nd, 3rd and following lines

Example with Name in Header

>MySequence
LCLYTHIGRNIYYGSYLYSETWNTGIMLLLITMATAFMGYVLPWGQMSFWGATVITNLFSAIPYIGTNLV
EWIWGGFSVDKATLNRFFAFHFILPFTMVALAGVHLTFLHETGSNNPLGLTSDSDKIPFHPYYTIKDFLG
LLILILLLLLLALLSPDMLGDPDNHMPADPLNTPLHIKPEWYFLFAYAILRSVPNKLGGVLALFLSIVIL
GLMPFLHTSKHRSMMLRPLSQALFWTLTMDLLTLTWIGSQPVEYPYTIIGQMASILYFSIILAFLPIAGX
IENY

Example with Name and Description in Header

>MySequence My description of a protein
LCLYTHIGRNIYYGSYLYSETWNTGIMLLLITMATAFMGYVLPWGQMSFWGATVITNLFSAIPYIGTNLV
EWIWGGFSVDKATLNRFFAFHFILPFTMVALAGVHLTFLHETGSNNPLGLTSDSDKIPFHPYYTIKDFLG
LLILILLLLLLALLSPDMLGDPDNHMPADPLNTPLHIKPEWYFLFAYAILRSVPNKLGGVLALFLSIVIL
GLMPFLHTSKHRSMMLRPLSQALFWTLTMDLLTLTWIGSQPVEYPYTIIGQMASILYFSIILAFLPIAGX
IENY

Example with Accessions or Identifiers, description and organism in Header

>gi|5524211|gb|AAD44166.1| cytochrome b [Elephas maximus maximus]
LCLYTHIGRNIYYGSYLYSETWNTGIMLLLITMATAFMGYVLPWGQMSFWGATVITNLFSAIPYIGTNLV
EWIWGGFSVDKATLNRFFAFHFILPFTMVALAGVHLTFLHETGSNNPLGLTSDSDKIPFHPYYTIKDFLG
LLILILLLLLLALLSPDMLGDPDNHMPADPLNTPLHIKPEWYFLFAYAILRSVPNKLGGVLALFLSIVIL
GLMPFLHTSKHRSMMLRPLSQALFWTLTMDLLTLTWIGSQPVEYPYTIIGQMASILYFSIILAFLPIAGX
IENY

Example with Accessions or Identifiers, description and organism in Header (NCBI FASTA format)

>AAD44166.1 cytochrome b, partial (mitochondrion) [Elephas maximus maximus]
LCLYTHIGRNIYYGSYLYSETWNTGIMLLLITMATAFMGYVLPWGQMSFWGATVITNLFSAIPYIGTNLV
EWIWGGFSVDKATLNRFFAFHFILPFTMVALAGVHLTFLHETGSNNPLGLTSDSDKIPFHPYYTIKDFLG
LLILILLLLLLALLSPDMLGDPDNHMPADPLNTPLHIKPEWYFLFAYAILRSVPNKLGGVLALFLSIVIL
GLMPFLHTSKHRSMMLRPLSQALFWTLTMDLLTLTWIGSQPVEYPYTIIGQMASILYFSIILAFLPIAGX
IENY

Example with Accessions or Identifiers, description and organism in Header (UniProt Fasta Headers)

>sp|O47885|CYB_ELEMA Cytochrome b OS=Elephas maximus OX=9783 GN=MT-CYB PE=3 SV=1
MTHTRKFHPLFKIINKSFIDLPTPSNISTWWNFGSLLGACLITQILTGLFLAMHYTPDTM
TAFSSMSHICRDVNYGWIIRQLHSNGASIFFLCLYTHIGRNIYYGSYLYSETWNTGIMLL
LITMATAFMGYVLPWGQMSFWGATVITNLFSAIPYIGTNLVEWIWGGFSVDKATLNRFFA
FHFILPFTMVALAGVHLTFLHETGSNNPLGLTSDSDKIPFHPYYTIKDFLGLLILILLLL
LLALLSPDMLGDPDNYMPADPLNTPLHIKPEWYFLFAYAILRSVPNKLGGVLALFLSILI
LGLMPLLHTSKHRSMMLRPLSQVLFWTLTMDLLTLTWIGSQPVEHPYIIIGQMASILYFS
IILAFLPIAGMIENYLIK

File extensions

Despite FASTA is a text file format in the end, some file extension prefixes are used as a convention for helping to identify file content among many different files.

  • Generic: .fa or .fasta
  • Protein: .faa
  • Nucleotide: .fna
  • etc.

TRIVIA: File format or type is not the same as file extension, despite the later should help to identify the former.

Files can also be compressed for helping distribution and saving space.

FASTA, as text files, they can be highly compressed. You can notice it with the following extensions: .gz, .bzip2 or .zip (among others).

.gz (Gzip) is, by far, the most common compression approach and, in many cases, it is recognized by many software applications. In most cases files can even be uncompressed and opened straight from the browser.

Sequences in lowercase or uppercase

In principle it does not matter whether letters are uppercase or lowercase. However, it is quite widespread that some programs (such as RepeatMasker) convert to lowercase some low complexity sequence regions (e.g. repeats). So, it is advisable to use uppercase by default.

NOTE:

  • Hard mask: Letters are converted to “X”
  • Soft mask: Letters are converted to lowercase

Derived extended format used in sequencing projects: FASTQ. We will discuss this in upcoming sessions.

Tools

  • FaBox. FASTA manipulation, generation and
  • EMBOSS seqret. Sequence file format conversion tool

NCBI resources

GenBank / GenPept format

Nucleotide example: AF132523

LOCUS       AF132523                 853 bp    DNA     linear   MAM 26-JUL-2016
DEFINITION  Elephas maximus maximus cytochrome b gene, partial cds;
            mitochondrial gene for mitochondrial product.
ACCESSION   AF132523
VERSION     AF132523.1
KEYWORDS    .
SOURCE      mitochondrion Elephas maximus maximus
  ORGANISM  Elephas maximus maximus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Elephas.
REFERENCE   1  (bases 1 to 853)
  AUTHORS   Barriel,V., Thuet,E. and Tassy,P.
  TITLE     Molecular phylogeny of Elephantidae. Extreme divergence of the
            extant forest African elephant
  JOURNAL   C. R. Acad. Sci. III, Sci. Vie 322 (6), 447-454 (1999)
   PUBMED   10457597
REFERENCE   2  (bases 1 to 853)
  AUTHORS   Barriel,V. and Thuet,E.
  TITLE     Direct Submission
  JOURNAL   Submitted (02-MAR-1999) Service de Systematique Moleculaire, Museum
            National d'Histoire Naturelle, 43 rue Cuvier, Paris 75005, France
FEATURES             Location/Qualifiers
     source          1..853
                     /organism="Elephas maximus maximus"
                     /organelle="mitochondrion"
                     /mol_type="genomic DNA"
                     /sub_species="maximus"
                     /db_xref="taxon:99488"
                     /country="Sri Lanka"
     CDS             <1..>853
                     /codon_start=1
                     /transl_table=2
                     /product="cytochrome b"
                     /protein_id="AAD44166.1"
                     /translation="LCLYTHIGRNIYYGSYLYSETWNTGIMLLLITMATAFMGYVLPW
                     GQMSFWGATVITNLFSAIPYIGTNLVEWIWGGFSVDKATLNRFFAFHFILPFTMVALA
                     GVHLTFLHETGSNNPLGLTSDSDKIPFHPYYTIKDFLGLLILILLLLLLALLSPDMLG
                     DPDNHMPADPLNTPLHIKPEWYFLFAYAILRSVPNKLGGVLALFLSIVILGLMPFLHT
                     SKHRSMMLRPLSQALFWTLTMDLLTLTWIGSQPVEYPYTIIGQMASILYFSIILAFLP
                     IAGXIENY"
ORIGIN      
        1 ctctgcctat acacacacat tggacgaaac atctactatg gatcctacct atactcagaa
       61 acctgaaaca caggtattat actactacta atcaccatag ccaccgcctt cataggatat
      121 gtccttccat gaggacaaat atcattctga ggggcaaccg taattactaa cctcttctca
      181 gcaattccct acatcggcac aaacctagta gaatgaattt gaggaggctt ttcggtagat
      241 aaagcaacct taaaccgatt cttcgccttc catttcatcc ttccatttac tatagttgca
      301 ctagcaggag tgcacctaac ctttcttcac gaaacaggct caaacaaccc actaggtctc
      361 acttcagact cagataaaat tcccttccac ccgtactata ctatcaaaga cttcctagga
      421 ctacttatcc taattttact ccttctactc ttagccctac tatctccaga catactagga
      481 gaccctgaca accacatacc agctgatcca ctaaataccc ccctacatat caaaccagag
      541 tgatacttcc tttttgctta cgccatccta cgatctgtac caaataaact aggaggcgtc
      601 ctagccctat tcctatcaat tgtgatttta ggattaatac catttctcca tacatccaag
      661 caccgaagta taatactccg acctctcagc caggccctat tctgaactct aacaatagat
      721 ttactaacac ttacatgaat tggcagtcaa ccagtagaat acccctacac cattattggc
      781 caaatagcct caattctata cttctccatt attctagctt tcctaccaat tgcagganta
      841 atcgaaaact acc
//

Protein example: AAD44166

LOCUS       AAD44166                 284 aa            linear   MAM 26-JUL-2016
DEFINITION  cytochrome b, partial (mitochondrion) [Elephas maximus maximus].
ACCESSION   AAD44166
VERSION     AAD44166.1
DBSOURCE    accession AF132523.1
KEYWORDS    .
SOURCE      mitochondrion Elephas maximus maximus
  ORGANISM  Elephas maximus maximus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Elephas.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Barriel,V., Thuet,E. and Tassy,P.
  TITLE     Molecular phylogeny of Elephantidae. Extreme divergence of the
            extant forest African elephant
  JOURNAL   C. R. Acad. Sci. III, Sci. Vie 322 (6), 447-454 (1999)
   PUBMED   10457597
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Barriel,V. and Thuet,E.
  TITLE     Direct Submission
  JOURNAL   Submitted (02-MAR-1999) Service de Systematique Moleculaire, Museum
            National d'Histoire Naturelle, 43 rue Cuvier, Paris 75005, France
COMMENT     Method: conceptual translation.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Elephas maximus maximus"
                     /organelle="mitochondrion"
                     /sub_species="maximus"
                     /db_xref="taxon:99488"
                     /country="Sri Lanka"
     Protein         <1..>284
                     /product="cytochrome b"
     Region          <1..115
                     /region_name="Cytochrome_b_N"
                     /note="Cytochrome b (N-terminus)/b6/petB: Cytochrome b is
                     a subunit of cytochrome bc1, an 11-subunit mitochondrial
                     respiratory enzyme. Cytochrome b spans the mitochondrial
                     membrane with 8 transmembrane helices (A-H) in eukaryotes.
                     In plants and cyanobacteria; cd00284"
                     /db_xref="CDD:238176"
     Site            order(30,33..34,37..38,51,54..55,59,87,90)
                     /site_type="other"
                     /note="Qo binding site"
                     /db_xref="CDD:238176"
     Region          116..263
                     /region_name="cytochrome_b_C"
                     /note="Cytochrome b(C-terminus)/b6/petD: Cytochrome b is a
                     subunit of cytochrome bc1, an 11-subunit mitochondrial
                     respiratory enzyme. Cytochrome b spans the mitochondrial
                     membrane with 8 transmembrane helices (A-H) in eukaryotes.
                     In plants and cyanobacteria; cd00290"
                     /db_xref="CDD:238179"
     Site            order(116..118,120..128,131..133,135..136,139,142..143,
                     146,149..150,153..154,156,162,165..166,220..221,225,227)
                     /site_type="other"
                     /note="interchain domain interface [polypeptide binding]"
                     /db_xref="CDD:238179"
     Site            order(116..117,122,125..127,129,133,136..137,140..141,144,
                     148..149,151..153,156,161,163..164,166..170,172..174,177,
                     179..182,197,207,210..211,213..215,217)
                     /site_type="other"
                     /note="intrachain domain interface"
                     /db_xref="CDD:238179"
     Site            order(129,137)
                     /site_type="other"
                     /note="Qi binding site"
                     /db_xref="CDD:238179"
     Site            order(177,179..180,183,186..187,203)
                     /site_type="other"
                     /note="Qo binding site"
                     /db_xref="CDD:238179"
     CDS             1..284
                     /coded_by="AF132523.1:<1..>853"
                     /transl_table=2
ORIGIN      
        1 lclythigrn iyygsylyse twntgimlll itmatafmgy vlpwgqmsfw gatvitnlfs
       61 aipyigtnlv ewiwggfsvd katlnrffaf hfilpftmva lagvhltflh etgsnnplgl
      121 tsdsdkipfh pyytikdflg llililllll lallspdmlg dpdnhmpadp lntplhikpe
      181 wyflfayail rsvpnklggv lalflsivil glmpflhtsk hrsmmlrpls qalfwtltmd
      241 lltltwigsq pveypytiig qmasilyfsi ilaflpiagx ieny
//

RefSeq

The Reference Sequence (RefSeq) collection provides a comprehensive, integrated, non-redundant, well-annotated set of sequences, including genomic DNA, transcripts, and proteins. RefSeq sequences form a foundation for medical, functional, and diversity studies. They provide a stable reference for genome annotation, gene identification and characterization, mutation and polymorphism analysis (especially RefSeqGene records), expression studies, and comparative analyses.

https://www.ncbi.nlm.nih.gov/refseq/

Category Description
NC Complete genomic molecules
NG Incomplete genomic region
NM mRNA
NR ncRNA
NP Protein
XM predicted mRNA model
XR predicted ncRNA model
XP predicted Protein model (eukaryotic sequences)
WP predicted Protein model (prokaryotic sequences)

Source: Wikipedia article

Other databases

Exercise

Search your favourite molecule from the global search and inspect the different matches.

Entrez

Original search system of NCBI. It is nowadays being replaced by a more Search engine approach. However it is still possible to use it from some interfaces.

Example query: ```carboxypeptidase AND rat[Organism] AND srcdb_refseq[PROP]``

Exercise

Get all cytochrome mRNA entries from both mouse and rat.

Batch Entrez

Batch Entrez website

Exercise: Get a list of IDs, submit them and check results.

My NCBI

Keeps track of all your searches, page visits. Allow creating collections to group entries of our interest, etc.

UniProt

Consortium: European Bioinformatics Institute (EBI), the Swiss Institute of Bioinformatics (SIB) and the Protein Information Resource (PIR).

Resources

  • UniProtKB
    • UniProtKB/Swiss-Prot. Curated anotation
    • UniProtKB/TrEMBL. Automatic annotation from EMBL
  • UniParc. Comprehensive and non-redundant database from different sources (sources: ENSEMBL, RefSeq, PDB, etc.)
  • UniRef. Redundancy datasets: UniRef100, UniRef90, UniRef50.

Other formats

  • SwissProt Format

  • Protein example: O47885

ID   CYB_ELEMA               Reviewed;         378 AA.
AC   O47885; O47886; Q34481;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   11-DEC-2019, entry version 90.
DE   RecName: Full=Cytochrome b;
DE   AltName: Full=Complex III subunit 3;
DE   AltName: Full=Complex III subunit III;
DE   AltName: Full=Cytochrome b-c1 complex subunit 3;
DE   AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome b subunit;
GN   Name=MT-CYB; Synonyms=COB, CYTB, MTCYB;
OS   Elephas maximus (Indian elephant).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Elephas.
OX   NCBI_TaxID=9783;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Hair, and Muscle;
RX   PubMed=9493356; DOI=10.1007/pl00006308;
RA   Noro M., Masuda R., Dubrovo I.A., Yoshida M.C., Kato M.;
RT   "Molecular phylogenetic inference of the woolly mammoth Mammuthus
RT   primigenius, based on complete sequences of mitochondrial cytochrome b and
RT   12S ribosomal RNA genes.";
RL   J. Mol. Evol. 46:314-326(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-335.
RC   TISSUE=Blood;
RX   PubMed=9089080; DOI=10.1007/pl00006160;
RA   Ozawa T., Hayashi S., Mikhelson V.M.;
RT   "Phylogenetic position of mammoth and Steller's sea cow within Tethytheria
RT   demonstrated by mitochondrial DNA sequences.";
RL   J. Mol. Evol. 44:406-413(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-106.
RX   PubMed=8577738; DOI=10.1073/pnas.93.3.1190;
RA   Yang H., Golenberg E.M., Shoshani J.;
RT   "Phylogenetic resolution within the Elephantidae using fossil DNA sequence
RT   from the American mastodon (Mammut americanum) as an outgroup.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:1190-1194(1996).
CC   -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase complex
CC       (complex III or cytochrome b-c1 complex) that is part of the
CC       mitochondrial respiratory chain. The b-c1 complex mediates electron
CC       transfer from ubiquinol to cytochrome c. Contributes to the generation
CC       of a proton gradient across the mitochondrial membrane that is then
CC       used for ATP synthesis. {ECO:0000250|UniProtKB:P00157}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P00157};
CC       Note=Binds 2 heme groups non-covalently.
CC       {ECO:0000250|UniProtKB:P00157};
CC   -!- SUBUNIT: The cytochrome bc1 complex contains 11 subunits: 3 respiratory
CC       subunits (MT-CYB, CYC1 and UQCRFS1), 2 core proteins (UQCRC1 and
CC       UQCRC2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7,
CC       UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of
CC       UQCRFS1). This cytochrome bc1 complex then forms a dimer.
CC       {ECO:0000250|UniProtKB:P00157}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00157}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P00157}.
CC   -!- MISCELLANEOUS: Heme 1 (or BL or b562) is low-potential and absorbs at
CC       about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs
CC       at about 566 nm. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome b family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00967, ECO:0000255|PROSITE-ProRule:PRU00968}.
CC   -!- CAUTION: The full-length protein contains only eight transmembrane
CC       helices, not nine as predicted by bioinformatics tools.
CC       {ECO:0000250|UniProtKB:P00157}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D50844; BAA25009.1; -; Genomic_DNA.
DR   EMBL; D50846; BAA25010.1; -; Genomic_DNA.
DR   EMBL; AB002412; BAA25017.1; -; Genomic_DNA.
DR   EMBL; D83048; BAA20278.1; -; Genomic_DNA.
DR   EMBL; U23740; AAA73783.1; -; Genomic_DNA.
DR   SMR; O47885; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045275; C:respiratory chain complex III; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:InterPro.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:InterPro.
DR   CDD; cd00290; cytochrome_b_C; 1.
DR   CDD; cd00284; Cytochrome_b_N; 1.
DR   Gene3D; 1.20.810.10; -; 1.
DR   InterPro; IPR005798; Cyt_b/b6_C.
DR   InterPro; IPR036150; Cyt_b/b6_C_sf.
DR   InterPro; IPR005797; Cyt_b/b6_N.
DR   InterPro; IPR027387; Cytb/b6-like_sf.
DR   InterPro; IPR030689; Cytochrome_b.
DR   InterPro; IPR016174; Di-haem_cyt_TM.
DR   Pfam; PF00032; Cytochrom_B_C; 1.
DR   Pfam; PF00033; Cytochrome_B; 1.
DR   PIRSF; PIRSF038885; COB; 1.
DR   SUPFAM; SSF81342; SSF81342; 1.
DR   SUPFAM; SSF81648; SSF81648; 1.
DR   PROSITE; PS51003; CYTB_CTER; 1.
DR   PROSITE; PS51002; CYTB_NTER; 1.
PE   3: Inferred from homology;
KW   Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Respiratory chain; Transmembrane;
KW   Transmembrane helix; Transport; Ubiquinone.
FT   CHAIN           1..378
FT                   /note="Cytochrome b"
FT                   /id="PRO_0000060911"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        77..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        320..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        347..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   METAL           83
FT                   /note="Iron 1 (heme b562 axial ligand)"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   METAL           97
FT                   /note="Iron 2 (heme b566 axial ligand)"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   METAL           182
FT                   /note="Iron 1 (heme b562 axial ligand)"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   METAL           196
FT                   /note="Iron 2 (heme b566 axial ligand)"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   BINDING         201
FT                   /note="Ubiquinone"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   VARIANT         7
FT                   /note="F -> S"
FT   VARIANT         306
FT                   /note="L -> F"
FT   VARIANT         345
FT                   /note="H -> Y"
FT   VARIANT         348
FT                   /note="I -> T"
SQ   SEQUENCE   378 AA;  42882 MW;  5A5FDF7BE9D15333 CRC64;
     MTHTRKFHPL FKIINKSFID LPTPSNISTW WNFGSLLGAC LITQILTGLF LAMHYTPDTM
     TAFSSMSHIC RDVNYGWIIR QLHSNGASIF FLCLYTHIGR NIYYGSYLYS ETWNTGIMLL
     LITMATAFMG YVLPWGQMSF WGATVITNLF SAIPYIGTNL VEWIWGGFSV DKATLNRFFA
     FHFILPFTMV ALAGVHLTFL HETGSNNPLG LTSDSDKIPF HPYYTIKDFL GLLILILLLL
     LLALLSPDML GDPDNYMPAD PLNTPLHIKP EWYFLFAYAI LRSVPNKLGG VLALFLSILI
     LGLMPLLHTS KHRSMMLRPL SQVLFWTLTM DLLTLTWIGS QPVEHPYIII GQMASILYFS
     IILAFLPIAG MIENYLIK
//

Notice ID and AC lines AC is recommended as more stable. Manual

  • GFF (General Feature Format)
##gff-version 3
##sequence-region O47885 1 378
O47885	UniProtKB	Chain	1	378	.	.	.	ID=PRO_0000060911;Note=Cytochrome b	
O47885	UniProtKB	Transmembrane	33	53	.	.	.	Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00157	
O47885	UniProtKB	Transmembrane	77	98	.	.	.	Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00157	
O47885	UniProtKB	Transmembrane	113	133	.	.	.	Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00157	
O47885	UniProtKB	Transmembrane	178	198	.	.	.	Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00157	
O47885	UniProtKB	Transmembrane	226	246	.	.	.	Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00157	
O47885	UniProtKB	Transmembrane	288	308	.	.	.	Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00157	
O47885	UniProtKB	Transmembrane	320	340	.	.	.	Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00157	
O47885	UniProtKB	Transmembrane	347	367	.	.	.	Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00157	
O47885	UniProtKB	Metal binding	83	83	.	.	.	Note=Iron 1 (heme b562 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00157	
O47885	UniProtKB	Metal binding	97	97	.	.	.	Note=Iron 2 (heme b566 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00157	
O47885	UniProtKB	Metal binding	182	182	.	.	.	Note=Iron 1 (heme b562 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00157	
O47885	UniProtKB	Metal binding	196	196	.	.	.	Note=Iron 2 (heme b566 axial ligand);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00157	
O47885	UniProtKB	Binding site	201	201	.	.	.	Note=Ubiquinone;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00157	
O47885	UniProtKB	Natural variant	7	7	.	.	.	Note=F->S	
O47885	UniProtKB	Natural variant	306	306	.	.	.	Note=L->F	
O47885	UniProtKB	Natural variant	345	345	.	.	.	Note=H->Y	
O47885	UniProtKB	Natural variant	348	348	.	.	.	Note=I->T	

Isoforms

Some entries may have isoforms. Example: P04150, P04150-2, P04150-3, etc. Reference

Search capabilities

Example query: carboxypeptidase AND reviewed:yes AND organism:"Rattus norvegicus (Rat) [10116]"

  • Exercise: Get all cytochrome unreviewed (TrEMBL) protein entries from both mouse and rat.

ID mapping

https://www.uniprot.org/uploadlists/

  • Exercise: Input different UniProt protein cytochrome entries and retrieve correspondent RefSeq IDs.

Other resources