ID M1ZVC7_CLOBO Unreviewed; 372 AA.
AC M1ZVC7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Putative electron transport protein {ECO:0000313|EMBL:EKN40590.1};
GN ORFNames=CFSAN001627_18623 {ECO:0000313|EMBL:EKN40590.1};
OS Clostridium botulinum CFSAN001627.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1232189 {ECO:0000313|EMBL:EKN40590.1, ECO:0000313|Proteomes:UP000011944};
RN [1] {ECO:0000313|EMBL:EKN40590.1, ECO:0000313|Proteomes:UP000011944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFSAN001627 {ECO:0000313|EMBL:EKN40590.1,
RC ECO:0000313|Proteomes:UP000011944};
RA Strain E.A., Brown E., Allard M.W., Gonzalez-Escalona N., Timme R.;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EKN40590.1, ECO:0000313|Proteomes:UP000011944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFSAN001627 {ECO:0000313|EMBL:EKN40590.1,
RC ECO:0000313|Proteomes:UP000011944};
RA Timme R.E., Allard M., Luo Y., Strain E., Gonzalez-Escalona N., Brown E.;
RT "Diversity in Clostridium botulinum.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:EKN40590.1}.
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; AMXI01001143; EKN40590.1; -; Genomic_DNA.
DR AlphaFoldDB; M1ZVC7; -.
DR PATRIC; fig|1232189.3.peg.2915; -.
DR Proteomes; UP000011944; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.11540; NADH-ubiquinone oxidoreductase 51kDa subunit; 1.
DR InterPro; IPR011538; Nuo51_FMN-bd.
DR InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR InterPro; IPR031001; PR_assoc_PrdC.
DR InterPro; IPR026902; RnfC_N.
DR NCBIfam; TIGR04481; PR_assoc_PrdC; 1.
DR PANTHER; PTHR43578; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR PANTHER; PTHR43578:SF3; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR Pfam; PF01512; Complex1_51K; 1.
DR Pfam; PF13375; RnfC_N; 1.
DR SUPFAM; SSF142019; Nqo1 FMN-binding domain-like; 1.
DR SUPFAM; SSF142984; Nqo1 middle domain-like; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 3..62
FT /note="RnfC Barrel sandwich hybrid"
FT /evidence="ECO:0000259|Pfam:PF13375"
FT DOMAIN 84..227
FT /note="NADH-ubiquinone oxidoreductase 51kDa subunit FMN-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF01512"
SQ SEQUENCE 372 AA; 39653 MW; 8F2F65ECC187A458 CRC64;
MEKMFSFPLR MHVGAPDAPC VKEGQKVKRG ECIAEPNGLG AKIHTSVSGI VEKVTDKEII
IKADEAQTTE FVKIKKCDNL VDTVFEAGIV GAGGAGFPTH IKLKADNKDG YIIANCVECE
PALHHNIKVI EETPELIING VRYAMKATNS TKGYIAIKAK HPEAIASLEK ALKGATDVEV
KPLADLYPMG EERAIINAIF DKWLDVTELP IEAKCIVMNA ETLANITRAV EEGKPVIDKD
ITVIGKLKSG NKPNIFLQVP VGTPVKDLIE KSGGIDGEYG ELVIGGPYTG KAGDIEKDTV
TKISGGAIVT IPLPEYNGPL GLLVCACGAN EERLKDVATK MNAKVAGIVD CKNIEYPKGK
GNGPGKCKTP GE
//