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Database: UniProt
Entry: A0A410T6P8_9CAUD
LinkDB: A0A410T6P8_9CAUD
Original site: A0A410T6P8_9CAUD 
ID   A0A410T6P8_9CAUD        Unreviewed;       781 AA.
AC   A0A410T6P8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   13-SEP-2023, entry version 14.
DE   RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE            EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
GN   ORFNames=ValB1MD_236 {ECO:0000313|EMBL:QAU04533.1};
OS   Vibrio phage Va1.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes.
OX   NCBI_TaxID=2508852 {ECO:0000313|EMBL:QAU04533.1, ECO:0000313|Proteomes:UP000289494};
RN   [1] {ECO:0000313|EMBL:QAU04533.1, ECO:0000313|Proteomes:UP000289494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Li C., Zhang Y., Liang Y.;
RL   Submitted (JAN-2019) 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; MK387337; QAU04533.1; -; Genomic_DNA.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000289494; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.70.20; -; 1.
DR   InterPro; IPR005144; ATP-cone_dom.
DR   InterPro; IPR013346; NrdE_NrdA_C.
DR   InterPro; IPR000788; RNR_lg_C.
DR   InterPro; IPR013509; RNR_lsu_N.
DR   InterPro; IPR008926; RNR_R1-su_N.
DR   InterPro; IPR039718; Rrm1.
DR   NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR   PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR   PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR   Pfam; PF03477; ATP-cone; 1.
DR   Pfam; PF02867; Ribonuc_red_lgC; 1.
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.
DR   PROSITE; PS51161; ATP_CONE; 1.
DR   PROSITE; PS00089; RIBORED_LARGE; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00492};
KW   Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW   ECO:0000256|RuleBase:RU003410};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00492};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003410};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289494}.
FT   DOMAIN          36..125
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   781 AA;  89943 MW;  788B4CC110EF8788 CRC64;
     MSKRYNKLSL DKVSEAVQQN EKIDISNQDT MKASQITIIK RKGHKEPFKP EKLRKVCLWA
     ADNKEYLADE LIRDTEIKLH KEIHIKDMYQ QLIVTAVNKI SMLQPVWEEI AAKLQLLSYY
     KETYNIASDN QYPHLRDVLA LGVERKIYDK ETVQSYTPQE IDALNDAIKP ERDLLFNFKG
     LVSFFDKYCL NYTKTKKLEL PQHAYMRVAM ALMANEKERV KRVIEEYNNV SSHNYTRATP
     IMLNALTPGQ QLSSCVLSTL ADDSHSILDT GKNLGIYSKF KGGTALDISA MRAKGGYIEG
     TQGYSSGPVP FNKFFEAIMK AWNQGGKRPG ALAVYFSWWH LDVMDLLSLK SNGGTDENRA
     RGLQFGCKLN DLFIEAVIED EDIHLFDPKD TPELIGKFGE EFNELYRSYV QKTNVRSKKV
     RAREIWNKIF KERSETGNIY LFHEENVNES TLLKRYIGSS NLCTEILLPS RPSESISEQL
     VTMEDGSTEI VKRYKAGEIA LCNLSSFNLL KWYYMSTEER METIRTLVRG LDNTVDLANY
     PVKEGKHSNM MYRYLGVGVL NYTNYLALKE IVIDSKAAAE ETDALFDEFS YMVISASCEL
     AIEKGKFEKF YETEWSEGIL PIHKANQNAM KLTDYEPDWN RWNELAEKVR TFGIRNAQLM
     AIAPTATSGK AINAIESIEP IHDFFYKEEG TMTVPTVVPN FRKNNRFYKK SFDCNQYALI
     NNAAVRQKWL DQTQSVNVYY KRPDSLWDMS KLHIYGFKLG MCTFYYLKQT KDSDDACESC
     T
//
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