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Database: UniProt
Entry: A0A142EZL6_9CAUD
LinkDB: A0A142EZL6_9CAUD
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ID   A0A142EZL6_9CAUD        Unreviewed;       766 AA.
AC   A0A142EZL6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   13-SEP-2023, entry version 27.
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=AAY80_086 {ECO:0000313|EMBL:AMQ65903.1};
OS   Stenotrophomonas phage vB_SmaS-DLP_6.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes.
OX   NCBI_TaxID=1651816 {ECO:0000313|EMBL:AMQ65903.1, ECO:0000313|Proteomes:UP000222594};
RN   [1] {ECO:0000313|EMBL:AMQ65903.1, ECO:0000313|Proteomes:UP000222594}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Peters D.L., Dennis J.;
RT   "The isolation and characterization of chimeric Stenotrophomonas
RT   maltophilia phage DLP6.";
RL   Submitted (FEB-2016) 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; KU682439; AMQ65903.1; -; Genomic_DNA.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000222594; 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; 1.10.1650.20; -; 1.
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.
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:UP000222594}.
FT   DOMAIN          2..92
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
FT   REGION          745..766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   766 AA;  86704 MW;  8DC5FC6F87CE7D5A CRC64;
     MSTVTKRDGT REPRDLNKIH KVVFEACEGL TGVSASEVEL KAQLQFYEGM PTEHIQDSLV
     RAAAGLISEE NPNYQYVAGR LINYDLRKRV YGEFEPPHIY DHVEKYVRLG YYHESLLTKY
     TRADWDAIQA FIKHERDSDF VFAAMEQFRG KYLMKNRHTG EFYETPQMLC AILPAFAFQN
     YPIDKRISYI KRTYDMLSTS EISLPTPIMA GVRTSQLQFS SCVLIECADS IDSIFTTTHA
     VGKYVSQKAG IGIGAGAIRP LGSPIRNGDA FSTGAIPYFR TFQAATKSCS QGGVRGGAAT
     IYYQMWHQEI EDLLVLKNNK GTEFNRVRQV DYGVQVNRLM YERLMQGGNI SCFNPKDVPG
     LYESFFADQD KFRELYEAAE KNKKIPRKVY PAIELWSLFA GERKGTGRIY GMNVDNVNDH
     GAFIPELAPI RMSNLCTEVT LPTKPLKHIA DPDGEIALCI LAAQNWGTAK TPHDFRDTAD
     IIVRLLDELI DLQTYPVLAA EIGTRNRRSL GVGIINFAYW LAKHDLTYDG ITPEGLALID
     EWAEWWSYYL LKASADLAVE KGACGWFEQT KYSKGILPND TYKKTVDELV PYKSRAPWAE
     LRLQLLSTGI RNSTLMTLMP AETSAQIANA TNGIEAPREL VSIKQSKDGV LAQVVPEIRR
     LKNKYNLKWD QKSPVGYLKI VAVLQKHIDQ AISVNTAYNP KFYENEEIPV SEILQHMIMH
     YRYGGKTLYY FETYDGAGEL NIESKGEYTT PSDELPPEED CDSCKI
//
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