ID F9RUH6_9VIBR Unreviewed; 706 AA.
AC F9RUH6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Anaerobic ribonucleoside triphosphate reductase {ECO:0000313|EMBL:EGU30245.1};
DE EC=1.17.4.2 {ECO:0000313|EMBL:EGU30245.1};
GN ORFNames=VIS19158_06950 {ECO:0000313|EMBL:EGU30245.1};
OS Vibrio scophthalmi LMG 19158.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=870967 {ECO:0000313|EMBL:EGU30245.1, ECO:0000313|Proteomes:UP000004349};
RN [1] {ECO:0000313|EMBL:EGU30245.1, ECO:0000313|Proteomes:UP000004349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 19158 {ECO:0000313|EMBL:EGU30245.1,
RC ECO:0000313|Proteomes:UP000004349};
RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT Scleritoderma cyanea.";
RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
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:EGU30245.1}.
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DR EMBL; AFWE01000218; EGU30245.1; -; Genomic_DNA.
DR RefSeq; WP_005599414.1; NZ_AFWE01000218.1.
DR AlphaFoldDB; F9RUH6; -.
DR eggNOG; COG1328; Bacteria.
DR Proteomes; UP000004349; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd01675; RNR_III; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR019777; Form_AcTrfase_GR_CS.
DR InterPro; IPR001150; Gly_radical.
DR InterPro; IPR012833; NrdD.
DR NCBIfam; TIGR02487; NrdD; 1.
DR PANTHER; PTHR21075; ANAEROBIC RIBONUCLEOSIDE-TRIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR21075:SF0; ANAEROBIC RIBONUCLEOSIDE-TRIPHOSPHATE REDUCTASE; 1.
DR Pfam; PF03477; ATP-cone; 1.
DR Pfam; PF13597; NRDD; 1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
DR PROSITE; PS00850; GLY_RADICAL_1; 1.
DR PROSITE; PS51149; GLY_RADICAL_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Organic radical {ECO:0000256|ARBA:ARBA00022818, ECO:0000256|PROSITE-
KW ProRule:PRU00493}; Oxidoreductase {ECO:0000313|EMBL:EGU30245.1}.
FT DOMAIN 3..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 583..706
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT MOD_RES 681
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 706 AA; 79618 MW; 5441819D62DEFFC5 CRC64;
MKPIVIKRDG SRAPFSRDRI QAAVEAAADQ VDNEIAIHAL NVALAVELQL KDHDEVHITE
IQTLVENELM QGPFKSLARS YIEYRHDRDI AREKQSTLTR EIEGLIEESN VDLINENANK
DGKVIPTQRD LLAGIVAKHY AKTHILPRDI VQAHEEGDIH YHDLDYAPFF PMFNCMLIDL
KGMLTHGFKM GNAEIDTPKS ISTATAVTAQ IIAQVASHIY GGTTINRIDE VLAPYVSASY
EKHLLTAKEW DIHTPEAFAI SRTEKECYDA FQSLEYEVNT LHTANGQTPF VTFGFGLGTS
WESRLIQQSI LKNRIAGLGK NSKTAVFPKL VFAIKDGLNH KAEDPSYDIK QLALECASKR
MYPDILNYDK IVEVTGSFKT PMGCRSFLNP YEENGELIHE GRNNLGVVSL NLPRIALRSN
GDEKTFYQLL DEKLDIARRA LETRISRLEN VKARVAPILY MEGACGVRLK ADDSIADIFK
NGRASISLGY IGIHETVNAL FGTETHVYDS EELRQKALDL VSYLKKNVEQ WAEETGYAFS
LYGTPSENLC SRFCRIDTKE FGVVEGVTNK GYYTNSFHLD VEKKVNPYDK IDFEMPYPHI
STGGFICYGE FPNMQRNIEA LENVWDYSYS RVPYYGTNTP IDECYECGYT GEFECTSKGF
TCPSCGNHDS SKVSVTRRVC GYLGSPDARP FNFGKQEEVK RRVKHL
//
