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Database: UniProt
Entry: A0A2S1GL63_9CAUD
LinkDB: A0A2S1GL63_9CAUD
Original site: A0A2S1GL63_9CAUD 
ID   A0A2S1GL63_9CAUD        Unreviewed;       387 AA.
AC   A0A2S1GL63;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274};
DE            EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274};
OS   Synechococcus phage S-B64.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Kyanoviridae; Shandvirus; Shandvirus sb64.
OX   NCBI_TaxID=2163901 {ECO:0000313|EMBL:AWD90125.1, ECO:0000313|Proteomes:UP000246725};
RN   [1] {ECO:0000313|Proteomes:UP000246725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   You S.;
RL   Submitted (MAR-2018) 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; MH107246; AWD90125.1; -; Genomic_DNA.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000246725; 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   Reference proteome {ECO:0000313|Proteomes:UP000246725}.
SQ   SEQUENCE   387 AA;  44865 MW;  D673F808A9D4879A CRC64;
     MSPVKSKEVK GMTVFNKKKV DTKKQPMFFG APLSVQRYDS YKYPVFDRLT QQQLGYFWRP
     EEVSLQKDRS DYQQLTPQQK HIFTSNLKYQ IMLDSVQGRG PGMAFIPYCS LPELEACMTV
     WEFMEMIHSR SYTHIIKNVY PNPSEVFDTI LDDENILERA ASVTESYDSF IEAAHQYDGG
     TMWELAKEGH YAGTFERIEL KRKLYRAVAN VNILEGIRFY VSFACSFAFG ENKLMEGSAK
     ILSLIARDEN QHLVITQNIL NKWREGDDSE MQQIANEEQD YVIEMFKRTV NEEKCWAEYL
     FRDGSMIGLN DRLLNNYVEW IANRRMKAIG LKPIYDIPAK NNPLPWTEHW LNSKGQQNAP
     QETEIESYVV GGIKQDITAG TFAGFSL
//
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