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P16366 (CYB_HYPNI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cytochrome b
Alternative name(s):
Complex III subunit 3
Complex III subunit III
Cytochrome b-c1 complex subunit 3
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Gene names
Name:mt-cyb
Synonyms:cob, cytb, mtcyb
Encoded onMitochondrion
OrganismHypsophrys nicaraguensis (Moga) (Cichlasoma nicaraguense)
Taxonomic identifier131240 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiEuteleosteiNeoteleosteiAcanthomorphaAcanthopterygiiPercomorphaPerciformesLabroideiCichlidaeNew World cichlidsCichlasomatinaeCichlasomatiniHypsophrys

Protein attributes

Sequence length79 AA.
Sequence statusFragment.
Protein existenceInferred from homology

General annotation (Comments)

Function

Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis By similarity.

Cofactor

Binds 2 heme groups non-covalently By similarity.

Subunit structure

The main subunits of complex b-c1 are: cytochrome b, cytochrome c1 and the Rieske protein By similarity.

Subcellular location

Mitochondrion inner membrane; Multi-pass membrane protein By similarity.

Miscellaneous

Heme 1 (or BL or b562) is low-potential and absorbs at about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs at about 566 nm By similarity.

Sequence similarities

Belongs to the cytochrome b family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›79›79Cytochrome b
PRO_0000060791

Regions

Transmembrane31 – 5323Helical; Potential

Sites

Metal binding371Iron 1 (heme b562 axial ligand)
Metal binding511Iron 2 (heme b566 axial ligand)

Experimental info

Non-terminal residue11
Non-terminal residue791

Sequences

Sequence LengthMass (Da)Tools
P16366 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: B7B82DD32FF975E7

FASTA799,080
        10         20         30         40         50         60 
TAMFLAMHYT SDIATAFSSV AHICRDVNYG WLIRNMHANG ASFFFICIYL HIGRGLYYGS 

        70 
YLYKETWNVG VILLLLTMM 

« Hide

References

[1]"Dynamics of mitochondrial DNA evolution in animals: amplification and sequencing with conserved primers."
Kocher T.D., Thomas W.K., Meyer A., Edwards S.V., Paeaebo S., Villablanca F.X., Wilson A.C.
Proc. Natl. Acad. Sci. U.S.A. 86:6196-6200(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M25694 Genomic DNA. Translation: AAA31688.1.
PIRE33286.

3D structure databases

ProteinModelPortalP16366.
SMRP16366. Positions 1-78.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR016175. Cyt_b/b6.
IPR005797. Cyt_b/b6_N.
IPR016174. Di-haem_cyt_TM.
[Graphical view]
PANTHERPTHR19271. PTHR19271. 1 hit.
PfamPF13631. Cytochrom_B_N_2. 1 hit.
[Graphical view]
SUPFAMSSF81342. Transmembr_di-haem_cytochrome. 1 hit.
PROSITEPS51002. CYTB_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYB_HYPNI
AccessionPrimary (citable) accession number: P16366
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families