ID A0A1B0VVG2_9CAUD Unreviewed; 392 AA.
AC A0A1B0VVG2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274};
GN ORFNames=CGG41_212 {ECO:0000313|EMBL:ANA49567.1};
OS Salmonella phage vB_SnwM_CGG4-1.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Straboviridae; Tevenvirinae; Gelderlandvirus; Gelderlandvirus cgg41.
OX NCBI_TaxID=1815631 {ECO:0000313|EMBL:ANA49567.1, ECO:0000313|Proteomes:UP000204511};
RN [1] {ECO:0000313|Proteomes:UP000204511}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Cucic S., Anany H., Brovko L., Kropinski A.M., Griffiths M.W.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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; KU867307; ANA49567.1; -; Genomic_DNA.
DR RefSeq; YP_009286579.1; NC_031065.1.
DR GeneID; 29060397; -.
DR KEGG; vg:29060397; -.
DR OrthoDB; 4477at10239; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000204511; Genome.
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,
KW ECO:0000313|EMBL:ANA49567.1}.
SQ SEQUENCE 392 AA; 45653 MW; 6CAFFF1955A961BD CRC64;
MSTVFNTQPV NVLNEPMFFG SGLGLARYDI QRHRTFEELI EKQLSFFWRP EEVNLMTDRA
QFDKLPEHQK NIFINNLKYQ SLLDSIQGRA PAAVLSALIS DPSLDTWNQT WTFSETIHSR
SYTHIMRNLF ADPAKIFDEI VLDDAIMARA ESIGRYYDDV ILKTRLWENA KENFKYFSEN
EFDLDANSNS FIHMEETKRD LMKALYLCLH VINGLEAIRF YVSFACTFNF HKNMEIMEGN
SKIMKFIARD EQLHLKGTQY IIRQLQQGTD GDEWVQIARE CEQEAVDIFM EINRQEKEWA
IHLFKDGGLP GLNVKILHDF VDYLTVSRMR SCGLPCPIVD APARHPIPWI REYLNSDAVQ
SAPQEVEISS YLVAQIDNDV DDNVVIGFKK YF
//
