ID W8QF08_9VIRU Unreviewed; 626 AA.
AC W8QF08;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN ORFNames=AMIV_044 {ECO:0000313|EMBL:AHL67539.1};
OS Anopheles minimus iridovirus.
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Pimascovirales; Iridoviridae; Betairidovirinae; Chloriridovirus.
OX NCBI_TaxID=1465751 {ECO:0000313|EMBL:AHL67539.1, ECO:0000313|Proteomes:UP000110868};
RN [1] {ECO:0000313|EMBL:AHL67539.1, ECO:0000313|Proteomes:UP000110868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMIV {ECO:0000313|EMBL:AHL67539.1};
RA Tong Y., Zhang J., Huang Y., Li S., Pei G., Zhang Z., Mi Z., An X.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC Evidence={ECO:0000256|RuleBase:RU003410};
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC {ECO:0000256|ARBA:ARBA00005160, ECO:0000256|RuleBase:RU003410}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406,
CC ECO:0000256|RuleBase:RU003410}.
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DR EMBL; KF938901; AHL67539.1; -; Genomic_DNA.
DR RefSeq; YP_009021123.1; NC_023848.1.
DR GeneID; 18938205; -.
DR KEGG; vg:18938205; -.
DR OrthoDB; 2980at10239; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000110868; Genome.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 2.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis {ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000110868}.
FT DOMAIN 15..82
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 86..440
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 446..598
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 626 AA; 71001 MW; 4ADC172899E30534 CRC64;
MTTSNLSIDL SRNELFDELG LLRLKSSYMK PEEKTPQDRF VFIATSFCNN DLALAQRLYD
YISKHWLSPS SPQLSFGRTK QGLPIACFLP YLPDTTRGLI DTWAEVSELS VIGGGIGIGV
GIRQPDEKSV GIIPHLRTYD ASCTAYKQGQ TRRGSYAAYL DITHPEIKTF LNTRRVSGDY
NFKLMNIHNG INIPDNFMKK IWFISLMTPI LKTKDCVRLT DVINELKNSD YFKNDEFLDL
LTIENLQHYI NETNKFDLVD PHTKKVTETV SATELWETII ITRAEVGEPF LHFVDTSNKA
LPDFQKKLGL SIKQSNLCSE ISLPTDENRT AVCCLASLNL NYFDEWSKDD QFYLDVVTYL
DNVLQYFIDN APKTVKRAIY SASQERAIGV GALGFHSYLQ SKQIAIESME AYNLNNKIFK
QISTYLLAAN LKLGSLRGEA PDCIGTGRRF SHTMAIAPNA TSSIIMGNTS PSCEPFRANV
YKQDTLSGSH ININKHLNKI LNERIKDPET LRDVISSIKG NDGSVQHLDV LTDHEKKVFK
TWPEINQMSL IRLAAARQKY IDQAQSTSLF FSPTSTKLHV HNVHLEAWKS GLKTLYYYRS
TKIINVDKIN HKIIKEDDNE CTFCEG
//