ID A0A1D7SU39_9CAUD Unreviewed; 386 AA.
AC A0A1D7SU39;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274};
GN ORFNames=RW071112_183 {ECO:0000313|EMBL:AOO16740.1}, RW220110_183
GN {ECO:0000313|EMBL:AOO17171.1}, RW250210_182
GN {ECO:0000313|EMBL:AOO17386.1}, RW270310_182
GN {ECO:0000313|EMBL:AOO17601.1}, RW291109_183
GN {ECO:0000313|EMBL:AOO18032.1};
OS Cyanophage S-RIM12.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Kyanoviridae; Brizovirus; Brizovirus syn33.
OX NCBI_TaxID=1278402 {ECO:0000313|EMBL:AOO17171.1, ECO:0000313|Proteomes:UP000221266};
RN [1] {ECO:0000313|Proteomes:UP000221266, ECO:0000313|Proteomes:UP000222026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RW_07_1112 {ECO:0000313|EMBL:AOO16740.1}, RW_22_0110
RC {ECO:0000313|EMBL:AOO17171.1}, RW_25_0210
RC {ECO:0000313|EMBL:AOO17386.1}, RW_27_0310
RC {ECO:0000313|EMBL:AOO17601.1}, and RW_29_1109
RC {ECO:0000313|EMBL:AOO18032.1};
RX PubMed=27696643; DOI=10.1111/1462-2920.13556;
RA Marston M.F., Martiny J.B.;
RT "Genomic diversification of marine cyanophages into stable ecotypes.";
RL Environ. Microbiol. 18:4240-4253(2016).
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; KX349314; AOO16740.1; -; Genomic_DNA.
DR EMBL; KX349316; AOO17171.1; -; Genomic_DNA.
DR EMBL; KX349317; AOO17386.1; -; Genomic_DNA.
DR EMBL; KX349318; AOO17601.1; -; Genomic_DNA.
DR EMBL; KX349320; AOO18032.1; -; Genomic_DNA.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000221266; Segment.
DR Proteomes; UP000222026; Segment.
DR Proteomes; UP000223325; Genome.
DR Proteomes; UP000223608; Segment.
DR Proteomes; UP000225724; 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; IPR030475; RNR_small_AS.
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.
DR PROSITE; PS00368; RIBORED_SMALL; 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 386 AA; 44922 MW; 169ECA96EC76E10E CRC64;
MSPAKSELQG MTVFNKNKVD TKKQPMFFGQ PLGVQRYDSY KYPVFDKLTQ QQLGYFWRPE
EVSLQKDRAD YQTLSPEQKH IFTSNLKYQI MLDSVQGRGP GMAFIPYCSL PELEASMLVW
EFMEMIHSRS YTYIIKNVYP DPSEVFDTIL EDEKILDRAS SVTESYDDFI NHAHQYDTST
MWELAKDGHY AGQFDRRELK RKLYRAVANV NILEGIRFYT SFACSFAFGE NKLMEGSAKI
LSLIARDESQ HLVLTQNILN KWRDGDDPEM DIIAKEEQSW VMSMFQRAVD EEKMWAEYLF
KNGSMIGLNE RLLHNYVEWI ANRRMKAIGI KPMFDIPAKN NPLPWTEHWL NSKGQQNAPQ
ETEIESYVIG GIKQDVEANT FAGFSL
//
