ID   H6WXC5_9CAUD            Unreviewed;       717 AA.
AC   H6WXC5;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AFB83891.1};
GN   ORFNames=pVp-1_0034 {ECO:0000313|EMBL:AFB83891.1};
OS   Vibrio phage pVp-1.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Demerecviridae; Ermolyevavirinae; Vipunavirus; Vipunavirus pVp1.
OX   NCBI_TaxID=1150989 {ECO:0000313|EMBL:AFB83891.1, ECO:0000313|Proteomes:UP000007520};
RN   [1] {ECO:0000313|EMBL:AFB83891.1, ECO:0000313|Proteomes:UP000007520}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22628398; DOI=10.1128/JVI.00742-12;
RA   Kim J.H., Jun J.W., Choresca C.H., Shin S.P., Han J.E., Park S.C.;
RT   "Complete Genome Sequence of a Novel Marine Siphovirus, pVp-1, Infecting
RT   Vibrio parahaemolyticus.";
RL   J. Virol. 86:7013-7014(2012).
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DR   EMBL; JQ340389; AFB83891.1; -; Genomic_DNA.
DR   RefSeq; YP_007007857.1; NC_019529.1.
DR   GeneID; 14013300; -.
DR   KEGG; vg:14013300; -.
DR   OrthoDB; 420at10239; -.
DR   Proteomes; UP000007520; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IEA:InterPro.
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}.
FT   DOMAIN          1..95
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
FT   DOMAIN          594..717
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000259|PROSITE:PS51149"
FT   MOD_RES         692
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00493"
SQ   SEQUENCE   717 AA;  80902 MW;  B543A65102CEACEA CRC64;
     MIVIKRDNTR QAFNLHKIYE AVFMSASDAD CEYEEASQIA NDATQLVIHN LQEQGKEEAT
     VYEIETLVEN VLMSSCWKDV ARKYIEYRHD RQQARDLESD LHKNIVGLVD QTNPDILHEN
     ANKESTVFHV QRDLLAGEIS RHYALNYLLP REVAQEHIAG NIHFHDLDYF PMMGMTNCCL
     VDLEGMLSNG FKMGNARIEQ PKSIQTAATV VSQIAAAVAS SQYGGTSFDR LDEVLAPYVT
     KTYEKNIRLM SELAGYFGGE DSSKVIELAK EKTEKDVFDA CQTLEYQVNT IYSTNGQTPF
     LTFGFGLGTS WEAKLVQKGI LQNRIAGLGK EGTTPVFPKL VFGLKDGVNL KPEDPNYDIK
     QLALECATVR MYPDILNYDK TVEITGGYKA PMGCRSFLST WYDEDGKETY AGRNNLGVVS
     LNIPKIALEA QLDYDKFWTL LDNYCEIAHR ALQYRLERLS TVKAKSAPIM YMEGALGLHL
     DPEEYVLPHL LKRGASISLG YIGLEEAANA MLGSVIHTYD EPEKQQFVLD IVKFLDKKAK
     EWKEAEGVGY SIYATPSESL CNRFCKAIVR EYGEFEGVTD KGYLTNSFHL DVLKKVNPYD
     KIDFEAQFIP YSSGGHICYG EFPNMRHNIE ALENVWDYAY TKVPYYGTNT PIDECYSCGF
     KGEFNCTSKG FECPNCGNHD PEKCSVTRRV CGYLGNPGTR PFNAGKQSEM TKRVKHL
//