ID   Q6Y7N6_BPPGK            Unreviewed;       349 AA.
AC   Q6Y7N6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274};
DE            EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274};
GN   ORFNames=PhageK_136 {ECO:0000313|EMBL:AHB80051.1};
OS   Staphylococcus phage K.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Herelleviridae; Twortvirinae; Kayvirus.
OX   NCBI_TaxID=221915 {ECO:0000313|EMBL:AAO47530.1, ECO:0000313|Proteomes:UP000001246};
OH   NCBI_TaxID=1280; Staphylococcus aureus.
RN   [1] {ECO:0000313|EMBL:AAO47530.1, ECO:0000313|Proteomes:UP000001246}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15090528; DOI=10.1128/JB.186.9.2862-2871.2004;
RA   O'Flaherty S., Coffey A., Edwards R., Meaney W., Fitzgerald G.F.,
RA   Ross R.P.;
RT   "Genome of staphylococcal phage K: a new lineage of Myoviridae infecting
RT   gram-positive bacteria with a low G+C content.";
RL   J. Bacteriol. 186:2862-2871(2004).
RN   [2] {ECO:0000313|EMBL:AHB80051.1, ECO:0000313|Proteomes:UP000211020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24459260;
RA   Gill J.J.;
RT   "Revised Genome Sequence of Staphylococcus aureus Bacteriophage K.";
RL   Genome Announc. 2:E01173-E01173(2014).
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962};
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC       chain family. {ECO:0000256|ARBA:ARBA00009303}.
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DR   EMBL; AY176327; AAO47530.1; -; Genomic_DNA.
DR   EMBL; KF766114; AHB80051.1; -; Genomic_DNA.
DR   RefSeq; YP_009041358.1; NC_005880.2.
DR   GeneID; 19621981; -.
DR   KEGG; vg:19621981; -.
DR   OrthoDB; 4477at10239; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000001246; Genome.
DR   Proteomes; UP000211020; Segment.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR   GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:InterPro.
DR   CDD; cd01049; RNRR2; 1.
DR   Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR012348; RNR-like.
DR   InterPro; IPR033909; RNR_small.
DR   InterPro; IPR000358; RNR_small_fam.
DR   PANTHER; PTHR23409; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN; 1.
DR   PANTHER; PTHR23409:SF18; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2; 1.
DR   Pfam; PF00268; Ribonuc_red_sm; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ   SEQUENCE   349 AA;  40446 MW;  23BD79557ECCE263 CRC64;
     MDITQKVKQH NKNAVLKATN WNIEDDGMSD IYWEQGISQF WTPEEFDVSR DLSSWNSLTE
     SEKNTYKKVL AGLTGLDTKQ GGEGMNLVSY HEPRPKYQAV FAFMGGMEEI HAKSYSHIFT
     TLLSNKETSY LLDTWVEEND FLKVKAQFIG YYYDQLLKPN PTIFDRYMAK VASAFLESAL
     FYSGFYYPLL LAGRGQMTQS GAIIYKITQD EAYHGSAVGL TAQYDYNLLT EEEKKQADKE
     TYELLDILYT NEVAYTHSLY DPLELSEDVI NYVQYNFNRA LQNLGREDYF NPEPYNPIVE
     NQTNVDRLRN VDFFSGKADY EKSTNIKDIK DEDFSFLDSK EYSTAKEFL
//