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Database: UniProt
Entry: A0A385ISF9_9CAUD
LinkDB: A0A385ISF9_9CAUD
Original site: A0A385ISF9_9CAUD 
ID   A0A385ISF9_9CAUD        Unreviewed;       357 AA.
AC   A0A385ISF9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274};
DE            EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274};
GN   ORFNames=Meda_020 {ECO:0000313|EMBL:AXY86280.1};
OS   Salmonella phage Meda.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Ounavirinae; Felixounavirus.
OX   NCBI_TaxID=2283282 {ECO:0000313|EMBL:AXY86280.1, ECO:0000313|Proteomes:UP000263364};
RN   [1] {ECO:0000313|Proteomes:UP000263364}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Neff J.K., Xie Y., O'Leary C.C., Liu M., Gill J.J.;
RL   Submitted (JUL-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; MH586731; AXY86280.1; -; Genomic_DNA.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000263364; 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; 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   357 AA;  41305 MW;  0B6A6BF1E34D6061 CRC64;
     MINQHPIFLG GERKTFDSLN KHYPKIFELY KQQKAQDWSE DEFPFEQSRL DFESVPASMS
     GVMLEILKWQ WEADTQVAKS LAFAFAPFIS DDIYATAIMK QSEIENLHAL TYSEIVRQCI
     KNPETILDEI NQNVAVQDRL KTVNRVLEEL LDEGINYRLS YVRDSLLDKD PLHFHKVILK
     GLFAVTALEG ISFMASFACT FALDAQDKFQ GIAQAVQKIM LDEILHTKID IEVLKETLRD
     DEWQKAFQQI LPEIKVILDE VVESEEKWSY YIFSEGRAVV GLNTKLLHEW VYYNAAPLYD
     MFGIPRDFVA PKEPPLKYMI KKMEIDKEQN ANQEQQNGAY LLNTVVDDLN SGFLEVP
//
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