ID A0A926TUV4_9CYAN Unreviewed; 111 AA.
AC A0A926TUV4;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 02-APR-2025, entry version 11.
DE RecName: Full=Rubredoxin {ECO:0000256|RuleBase:RU003820};
GN ORFNames=H6F76_29310 {ECO:0000313|EMBL:MBD2039054.1};
OS Leptolyngbya sp. FACHB-321.
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Leptolyngbyales;
OC Leptolyngbyaceae; Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=2692807 {ECO:0000313|EMBL:MBD2039054.1, ECO:0000313|Proteomes:UP000619131};
RN [1] {ECO:0000313|EMBL:MBD2039054.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FACHB-321 {ECO:0000313|EMBL:MBD2039054.1};
RX PubMed=32943748;
RA Chen M.Y., Teng W.K., Zhao L., Hu C.X., Zhou Y.K., Han B.P., Song L.R.,
RA Shu W.S.;
RT "Comparative genomics reveals insights into cyanobacterial evolution and
RT habitat adaptation.";
RL ISME J. 0:0-0(2020).
RN [2] {ECO:0000313|EMBL:MBD2039054.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FACHB-321 {ECO:0000313|EMBL:MBD2039054.1};
RA Chen M., Teng W., Zhao L., Hu C., Zhou Y., Han B., Song L., Shu W.;
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000256|RuleBase:RU003820};
CC -!- SIMILARITY: Belongs to the rubredoxin family.
CC {ECO:0000256|RuleBase:RU003820}.
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:MBD2039054.1}.
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DR EMBL; JACJPI010000090; MBD2039054.1; -; Genomic_DNA.
DR RefSeq; WP_190513661.1; NZ_JACJPI010000090.1.
DR Proteomes; UP000619131; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:TreeGrafter.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043448; P:alkane catabolic process; IEA:TreeGrafter.
DR CDD; cd00730; rubredoxin; 1.
DR FunFam; 2.20.28.10:FF:000001; Rubredoxin; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR InterPro; IPR024934; Rubredoxin-like_dom.
DR InterPro; IPR024935; Rubredoxin_dom.
DR InterPro; IPR050526; Rubredoxin_ET.
DR InterPro; IPR018527; Rubredoxin_Fe_BS.
DR PANTHER; PTHR47627; RUBREDOXIN; 1.
DR PANTHER; PTHR47627:SF1; RUBREDOXIN-1-RELATED; 1.
DR Pfam; PF00301; Rubredoxin; 1.
DR PRINTS; PR00163; RUBREDOXIN.
DR SUPFAM; SSF57802; Rubredoxin-like; 1.
DR PROSITE; PS00202; RUBREDOXIN; 1.
DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|RuleBase:RU003820};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003820};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003820};
KW Reference proteome {ECO:0000313|Proteomes:UP000619131};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 91..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..62
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50903"
SQ SEQUENCE 111 AA; 12066 MW; 3C27E45A65F27AE9 CRC64;
MSTETAEPTA LDRYECQACG YIYEPLKGDE RRQVSATTPF EAVPSNWRCP VCGAPKSRFS
NIGEVGSPSG FKENLGYGFG VNTLTPGQKN ILIFGALALG FLFFLSLYGL Q
//