Reviewed, UniProtKB/Swiss-Prot O49078 (UCRIA_FRIAG)

Names and origin

Protein names

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

Gene names

Name:

petC

Organism

Fritillaria agrestis (Stinkbells)

Taxonomic identifier

64177 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Liliales › Liliaceae › Fritillaria

Protein attributes

Sequence length	230 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 › chloroplast thylakoid membrane; Single-pass membrane proteinBy 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	Chloroplast Membrane Plastid Thylakoid
Domain	Transit peptide Transmembrane
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
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	chloroplast Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW thylakoid Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: InterPro 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 ubiquinol-cytochrome-c reductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 56	56	Chloroplast Potential
	Chain	57 – 230	174	Cytochrome b6-f complex iron-sulfur subunit, chloroplastic		PRO_0000030689
Regions
	Transmembrane	73 – 93	21	Potential
	Domain	116 – 212	97	Rieske
Sites
	Metal binding	158	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	160	1	Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
	Metal binding	176	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	179	1	Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
Amino acid modifications
	Disulfide bond	163 ↔ 178		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O49078-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: D1B914F0049AF51E	FASTA	230	24,298
	10 20 30 40 50 60 MASTTLSATP TPSQLSAAKN GAYSPSRALL GKTARGLYPE KEMVSRKVTC QATSIPADRV 70 80 90 100 110 120 PDMGKRQTMN LLLLGALSLP TAGMLIPYGA FFVPPSSGGG GGGIVAKDAV GNDIVAAAWL 130 140 150 160 170 180 KTHGPGDRTL AQGLRGDPTY LVVENDRSLA TYGINAVCTH LGCVVPWNKA ENKFLCPCHG 190 200 210 220 230 SQYNNQGKVV RGPAPLSLAL SHCDISEEGK VVFVPWVETD FRTGENPWWS

References

[1]	"Fritillaria genome analysis." Panico E., Baysdorfer C. Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF037456 mRNA. Translation: AAC04807.1.
3D structure databases
HSSP	HSSP built from PDB template 1RFS based on UniProtKB P08980.
SMR	O49078. Positions 105-230.
ModBase	Search...
Family and domain databases
InterPro	IPR014909. Cyt_b6-F_Fe-S_su. IPR014349. Rieske. IPR005805. Rieske_C. IPR005806. Rieske_reg. [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]
PRINTS	PR00162. RIESKE.
PROSITE	PS51296. RIESKE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UCRIA_FRIAG

Accession

Primary (citable) accession number: O49078

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	June 1, 1998
Last modified:	November 25, 2008
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)