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Database: UniProt
Entry: W8QF08_9VIRU
LinkDB: W8QF08_9VIRU
Original site: W8QF08_9VIRU 
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
//
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