ID A0A222YT67_9CAUD Unreviewed; 358 AA.
AC A0A222YT67;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274};
OS Vibrio phage vB_ValP_IME271.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes.
OX NCBI_TaxID=2024229 {ECO:0000313|EMBL:ASR73851.1, ECO:0000313|Proteomes:UP000224772};
RN [1] {ECO:0000313|EMBL:ASR73851.1, ECO:0000313|Proteomes:UP000224772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Li F., Li L., Sun Q., Xing S., Zhou L., Tong Y.-G.;
RT "Genomic and biological characterization of Podoviridae bacteriophage
RT vB_ValP_IME271 infecting Vibrio alginolyticus.";
RL Submitted (JUL-2017) 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; MF431726; ASR73851.1; -; Genomic_DNA.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000224772; Genome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 175..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 358 AA; 40905 MW; 6F941138086305BA CRC64;
MTVFNANNKG YSEGYPLFLG EELGLFDTIN RTYPELEELY QQQMAQLWNE FEVDLTQDKM
DMQKVDPKVT ELMVKTISWQ HLADSVASKS ITGLLMKHVT NSELEGLINC WGLFETIHAR
TYSHIVKQTF QNPVEMLQET YNNLKVLDRS QAIVEAFDRL EDLPKDATRE ETMQAILGAL
FALFALEAIA FMASFSVTFG IAETGVFQGI AQDVKLICRD EVMHTRFDYS ILRILLKDPE
WSKVYNNNIG QYKRILDSVV EGEMVWTDYL FSEGRQCIGL NAKLVKQYVL YMAQPVYEAA
GITFGFEAPK ENPLPYMENY IDGSRVQVAP QELQVTSYNI GAISDDTSDL DDLDFEDL
//
