ID A0A0Q1FRJ2_9BACT Unreviewed; 57 AA.
AC A0A0Q1FRJ2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Ferredoxin {ECO:0000256|RuleBase:RU365098};
GN ORFNames=APR54_12080 {ECO:0000313|EMBL:KQC10325.1};
OS Candidatus Cloacimonas sp. SDB.
OC Bacteria; Candidatus Cloacimonadota; Candidatus Cloacimonadia;
OC Candidatus Cloacimonadales; Candidatus Cloacimonadaceae; Cloacimonas.
OX NCBI_TaxID=1732214 {ECO:0000313|EMBL:KQC10325.1, ECO:0000313|Proteomes:UP000052007};
RN [1] {ECO:0000313|EMBL:KQC10325.1, ECO:0000313|Proteomes:UP000052007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDB {ECO:0000313|EMBL:KQC10325.1};
RA Wawrik B., Marks C.R., Davidova I.A., Mcinerney M.J., Pruitt S., Duncan K.,
RA Suflita J.M., Callaghan A.V.;
RT "Methanogenic Paraffin-Utilizing Consortium.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions.
CC {ECO:0000256|RuleBase:RU365098}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966,
CC ECO:0000256|RuleBase:RU365098};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQC10325.1}.
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; LKUH01000141; KQC10325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q1FRJ2; -.
DR Proteomes; UP000052007; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.20; -; 2.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR000813; 7Fe_ferredoxin.
DR PANTHER; PTHR43687; ADENYLYLSULFATE REDUCTASE, BETA SUBUNIT; 1.
DR PANTHER; PTHR43687:SF1; L-ASPARTATE SEMIALDEHYDE SULFURTRANSFERASE IRON-SULFUR SUBUNIT; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR PRINTS; PR00354; 7FE8SFRDOXIN.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|RuleBase:RU365098};
KW Electron transport {ECO:0000256|RuleBase:RU365098};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU365098};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU365098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU365098}; Transport {ECO:0000256|RuleBase:RU365098}.
FT DOMAIN 2..31
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 32..57
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 57 AA; 5911 MW; 0A461C0C15F33E33 CRC64;
MMAVNINEET CIGCGACIDT CPVEALEMVD DKAKVDPDKC VDCGACIDAC PVSAISE
//
