ID A0A482JAX5_9CAUD Unreviewed; 676 AA. AC A0A482JAX5; DT 05-JUN-2019, integrated into UniProtKB/TrEMBL. DT 05-JUN-2019, sequence version 1. DT 12-AUG-2020, entry version 5. DE RecName: Full=Ribonucleoside-triphosphate reductase (thioredoxin) {ECO:0000256|ARBA:ARBA00012275}; DE EC=1.17.4.2 {ECO:0000256|ARBA:ARBA00012275}; GN Name=49 {ECO:0000313|EMBL:QBP29339.1}; GN ORFNames=SEA_DIRTYDUNNING_49 {ECO:0000313|EMBL:QBP29339.1}; OS Mycobacterium phage DirtyDunning. OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Caudovirales; Siphoviridae; Fromanvirus; unclassified Fromanvirus. OX NCBI_TaxID=2517947 {ECO:0000313|EMBL:QBP29339.1, ECO:0000313|Proteomes:UP000295268}; RN [1] {ECO:0000313|EMBL:QBP29339.1, ECO:0000313|Proteomes:UP000295268} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Stoner T.H., Garlena R.A., Russell D.A., Pope W.H., Jacobs-Sera D., RA Hatfull G.F.; RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'- CC triphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'- CC triphosphate; Xref=Rhea:RHEA:12701, Rhea:RHEA-COMP:10698, Rhea:RHEA- CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, CC ChEBI:CHEBI:61557, ChEBI:CHEBI:61560; EC=1.17.4.2; CC Evidence={ECO:0000256|ARBA:ARBA00001283}; CC -!- COFACTOR: CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408; CC Evidence={ECO:0000256|ARBA:ARBA00001922}; CC -!- SIMILARITY: Belongs to the class II ribonucleoside-triphosphate CC reductase family. {ECO:0000256|ARBA:ARBA00005654}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MK494094; QBP29339.1; -; Genomic_DNA. DR Proteomes; UP000295268; Genome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:InterPro. DR GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR InterPro; IPR040763; RNR_alpha_hel. DR InterPro; IPR000788; RNR_lg_C. DR InterPro; IPR013345; RTP_Rdtase_AdoCbl-dep. DR Pfam; PF02867; Ribonuc_red_lgC; 3. DR Pfam; PF17975; RNR_Alpha; 1. DR TIGRFAMs; TIGR02505; RTPR; 1. PE 3: Inferred from homology; KW Cobalamin {ECO:0000256|ARBA:ARBA00022628}; KW Cobalt {ECO:0000256|ARBA:ARBA00023285}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW DNA replication {ECO:0000256|ARBA:ARBA00022705}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Redox-active center {ECO:0000256|ARBA:ARBA00023284}. FT DOMAIN 6..79 FT /note="RNR_Alpha" FT /evidence="ECO:0000259|Pfam:PF17975" FT DOMAIN 248..316 FT /note="RIBORED_LARGE" FT /evidence="ECO:0000259|Pfam:PF02867" FT DOMAIN 325..480 FT /note="RIBORED_LARGE" FT /evidence="ECO:0000259|Pfam:PF02867" FT DOMAIN 490..611 FT /note="RIBORED_LARGE" FT /evidence="ECO:0000259|Pfam:PF02867" SQ SEQUENCE 676 AA; 75650 MW; D9A702BEE742DBB5 CRC64; MTTEVKWGPT GEIVYKRTYS RVKPDGSNET WPETVERVVD GNLALVDARY QEPDEREQLI RLITEFKMLP AGRHLWASGV KNAQHLFNCW VSGWTEKPSD HFEFTFMRLM EGGGVGANYS NRFLDYGPVQ QELYVHIVCD PEHPDYEAMK EAGVLSTEYD PEWAGAFVIE DSREGWAAAL VDLIDTHYRD EVSHFQRVYD VSRVRPFGAK LKTFGGRASG PLPLARMLID VCEVLSELAT EGGSLTGMDA MEIDHAIAQC VVAGGVRRSA RMSMMHWADP QIGSFMRCKS ETGKHWTTNI SVEVDEEFWR VVKETDAKPG WNSNPAAVLK AITEGMVANG EPGFWDSSLS NVGEPNEVVC TNPCGEITLQ EWEPCNLGHI NLAAFVKENG KVDTIDLVRS HRLMARFLIR ATFSPVGDPK SREVLDRNRR IGVGHLGVAS FLAMTGKRYS QAPLDKHFRK TLRELAAEVQ HAAQKFSHEL RIPVPVKTRT VAPTGTIAKM PGVSEGIHPI FAKYFNRRIR FSKGDEQLDE LIDQGYDFEP CQYAENTVVV TIPTKDTLVQ EVVDRYGRDA EEIVESVEDL TLNQMLAFQA MYQMLWADNA VSFTANVDPD RYKPHVVGEQ LRTFGGLLKG ATIFPESSMP QAPYERITKK QYKAATAVAV ADSVDEECAS GACPIR //