ID   A0A172Q043_9CAUD        Unreviewed;       687 AA.
AC   A0A172Q043;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=ME3_67 {ECO:0000313|EMBL:AND75228.1};
OS   Acinetobacter phage vB_AbaM_ME3.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Metrivirus; Metrivirus ME3.
OX   NCBI_TaxID=1837876 {ECO:0000313|EMBL:AND75228.1, ECO:0000313|Proteomes:UP000225947};
RN   [1] {ECO:0000313|Proteomes:UP000225947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Buttimer C.T.H., Elbreki M., Coffey A.;
RT   "Characterization of Acinetobacter baumannii phage vB_AbaM_ME3.";
RL   Submitted (MAR-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   -!- 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; KU935715; AND75228.1; -; Genomic_DNA.
DR   OrthoDB; 2980at10239; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000225947; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:InterPro.
DR   Gene3D; 3.20.70.20; -; 1.
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; 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.
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:UP000225947}.
FT   DOMAIN          31..106
FT                   /note="Ribonucleotide reductase large subunit N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00317"
FT   DOMAIN          110..664
FT                   /note="Ribonucleotide reductase large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02867"
FT   REGION          665..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   687 AA;  78946 MW;  C1D3B25F0416C252 CRC64;
     MYEKGYYLKF DYTEEELDII DGWLTHHKDF DLSYTQINQM ESKYFVRDRV SKQTYETPRF
     MFARIALAVF EKDENRMYHI NNFLKYLDNL DMNLPSPNWS YIGTVRRTGA SCCLYSIEDT
     SRSIAAANHI TEMMTIAAAG LGNNYIIRSI GDSVKGGTII HQGKQGYHKA AQGITKSNKQ
     GSRGGALTTY VPINDPEIEV IVKARNPSTV AELKVDEIDY AFMYNRYFGI KVINDEQWML
     ISLKDAPDLY EAFYSNRYED YVELYEKYEL DDSVKKTFIR ARDLADVCLS EQYETGRLYS
     GDSYQINYHT PHKDPIYSSN LCLEITLPTK PFHSVRELYE EFSSEWAYIT YEDKSEEVIV
     DIESARWSLA NVKAGDTVNG KVVKKIESKN EIALCNIAGV NLHRDFTDEE YLDICYYLLR
     VIDYVILNSS YEFPNVKYTA AQRMNAGVGL TNFAYELARK GLYYSSKAGK QHAHFIAERH
     WYMLAKASLK ISKERGVAPW MFKSKLPEGW TPLDTYCHAV DGIADFEYRY DYKALSQEII
     ENGGLAHSSL VAHMPCESSS QVLNSVNGLY PIRRGKIVKT DGANVNVSIA PHFEELQWNY
     EIAWEVETKH LVDHYAIFQK FNDQSISADF YHDFTRSNSE LTKKKLYSDF LYKIKMGLKT
     QYYTNSKTNS EDEGSKAASC GSGGCSL
//