Reviewed, UniProtKB/Swiss-Prot Q5CC93 (UCRIA_CYAPA)

Names and origin

Protein names

Recommended name:
    Cytochrome b6-f complex iron-sulfur subunit 1, cyanelle
    EC=1.10.99.1
Alternative name(s):
    Rieske iron-sulfur protein 1
      Short name=RISP 1
      Short name=ISP 1
    Plastohydroquinone:plastocyanin oxidoreductase iron-sulfur protein 1

Gene names

Name:

petC-1

Organism

Cyanophora paradoxa

Taxonomic identifier

2762 [NCBI]

Taxonomic lineage

Eukaryota › Glaucocystophyceae › Cyanophoraceae › Cyanophora

Protein attributes

Sequence length	239 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions By similarity.
Catalytic activity	Plastoquinol-1 + 2 oxidized plastocyanin = plastoquinone + 2 reduced plastocyanin.
Cofactor	Binds 1 2Fe-2S cluster per subunit By similarity.
Subunit structure	The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and the Rieske protein, while the 4 small subunits are petG, petL, petM and petN. The complex functions as a dimer By similarity.
Subcellular location	Plastid › cyanelle thylakoid membrane; Single-pass membrane protein By similarity. Note: The transmembrane helix obliquely spans the membrane in one monomer, and its extrinsic C-terminal domain is part of the other monomer By similarity.
Miscellaneous	This protein is 1 of 2 subunits of the cytochrome b6-f complex that are encoded in the nucleus. The Rieske iron-sulfur protein is a high potential 2Fe-2S protein.
Sequence similarities	Contains 1 Rieske domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Cyanelle Membrane Plastid Thylakoid
Domain	Transit peptide Transmembrane
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cyanelle thylakoid membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW plastoquinol-plastocyanin reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 60	60	Cyanelle Potential
	Chain	61 – 239	179	Cytochrome b6-f complex iron-sulfur subunit 1, cyanelle		PRO_0000030687
Regions
	Transmembrane	81 – 101	21	Potential
	Domain	125 – 221	97	Rieske
Sites
	Metal binding	167	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	169	1	Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
	Metal binding	185	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	188	1	Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
Amino acid modifications
	Disulfide bond	172 ↔ 187		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5CC93-1 [UniParc]. Last modified April 12, 2005. Version 1. Checksum: 0D95E0A5458109CB	FASTA	239	24,735
	10 20 30 40 50 60 MAFTTTAVVA PRGAKITGQS STCAIQNGKT VAVGTSKQVG SFKPVFAAAK PAKETTFSVS 70 80 90 100 110 120 CSAASDDVPD MGKRKLMNLL LLGAIAGPVA GAGGPFVSFL VPPKAGGGAG AGQAAKDALG 130 140 150 160 170 180 NDVKVSSWLE THKPGDRSLA QGLKGDATYL IVKEDGTLEN YGLNAVCTHL GCVVPWNASE 190 200 210 220 230 NKFMCPCHGS QYDRTGKVVR GPAPLSLALA HVSVLEDGVV AFEPWTETDF RTNTAPWWK

References

[1]

"Conservative sorting in a primitive plastid. The cyanelle of Cyanophora paradoxa." Steiner J.M., Berghoefer J., Yusa F., Pompe J.A., Kloesgen R.B., Loeffelhardt W. FEBS J. 272:987-998(2005) [PubMed: 15691332] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN IMPORT INTO ISOLATED CYANELLES. Strain: UTEX LB 555 / Pringsheim.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ784852 mRNA. Translation: CAH04960.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.10.99.1. 11.
Family and domain databases
InterPro	IPR014909. Cyt_b6-f_cplx_Fe-S_su. IPR017941. Rieske_2Fe-2S. IPR014349. Rieske_Fe-S_prot. [Graphical view]
Gene3D	G3DSA:2.102.10.10. Rieske_reg. 1 hit.
PANTHER	PTHR10134. Rieske. 1 hit.
Pfam	PF08802. CytB6-F_Fe-S. 1 hit. PF00355. Rieske. 1 hit. [Graphical view]
PROSITE	PS51296. RIESKE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UCRIA_CYAPA

Accession

Primary (citable) accession number: Q5CC93

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	April 12, 2005
Last modified:	June 16, 2009
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)