ID   A0A2R8FF52_9VIRU        Unreviewed;      1066 AA.
AC   A0A2R8FF52;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=BRZCDTV_354 {ECO:0000313|EMBL:SPN79451.1};
OS   Brazilian cedratvirus IHUMI.
OC   Viruses; Pithoviruses.
OX   NCBI_TaxID=2126980 {ECO:0000313|EMBL:SPN79451.1};
RN   [1] {ECO:0000313|EMBL:SPN79451.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IHUMI-27.7 {ECO:0000313|EMBL:SPN79451.1};
RG   Urmite Genomes;
RL   Submitted (MAR-2018) 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; LT994651; SPN79451.1; -; Genomic_DNA.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000273054; Chromosome scaffold_1.
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   CDD; cd00081; Hint; 1.
DR   Gene3D; 3.20.70.20; -; 2.
DR   InterPro; IPR003587; Hint_dom_N.
DR   InterPro; IPR036844; Hint_dom_sf.
DR   InterPro; IPR030934; Intein_C.
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; TIGR01443; intein_Cterm; 1.
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; 2.
DR   Pfam; PF00317; Ribonuc_red_lgN; 1.
DR   PRINTS; PR01183; RIBORDTASEM1.
DR   SMART; SM00306; HintN; 1.
DR   SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR   SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR   SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
DR   PROSITE; PS50818; INTEIN_C_TER; 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:UP000273054}.
FT   DOMAIN          485..507
FT                   /note="Intein C-terminal splicing"
FT                   /evidence="ECO:0000259|PROSITE:PS50818"
SQ   SEQUENCE   1066 AA;  120811 MW;  2AF86B7E2794D661 CRC64;
     MHLCQGLKVN KEKVEKLLSS FSDYETVARN LGHDVENYDH LMLAGRLLIE SKKKVTPANI
     ETYCEAFSDF FDEKILFFFL QNKDALNKLL DDTSFTDYMY DWVGANVLYK TYIAKSEIPV
     NGVLYEESPR FWHLRVAAYM YHPNLTKVSM AYHDLCSQYI LHATPTNINA GRKKPQPSSC
     FLLKIKDRLE DITLTGVHKV AQISKHNGGL GIDVSRVRHS NIKHAGMSQG LVAMIVMFNY
     VIRYVNQCFA PGSKVMTNSG LINIEDILPG QEVLTRDGTY CKVVKVLPHA LQEEEKIYHI
     TTPLGSAKAL GEHPMLSLRP CASLPSHKLD LIYTPARDLC DGDVLFYPMG ESKDVDYSEE
     ELYIYGAAFA SGRLEENKII LPAQGNVVSV LSKLGLSIEL LSDDFVSFKL GGMIRITPNM
     MKNFPAAFYS LPQKKALSLY EGLCCNSNLF QSKYLEMYVG KSKYAKKENG YLVPITSIEK
     ETCSFVYDLE VDKNHNFTTE VGLAHNGGRR KGAATIYTRP HHIDIVEFVE LNQLTGDIYS
     RAHDIDLAVW TPWLFWKRVE EDGQWSLFCP ALTKSLNKIW GIKFAQEYER LEKDESVPRK
     TIPARKLLEI ICTNQQAGGR LYTLNGDGAN QKSNQKNLGY ISHGNLCLEV LQYSSSKEIA
     ACNLAQISLP HMVENGEINY DLLARIAKRA CENLNAVIDR AWFPFEEISR SNKKHRPMGI
     GVSGFAEMLH KLDLPFEDVT VRDLNKKIFA CIYFNAVAQS IMLSIEEGMK EGLESKPYDS
     FAGSPASEGK FQFDLWAEEF DILKQNGIPC NRKKEDDLPV DPASWGQKSI LLPNGDTLLP
     TYDDLRRCTL KYGWRNSLLI ALMPTATSSI VLRNCESVEA HQTNIYSRKL QSGNYPMVNR
     FLIDDLEKIG LWNLNTVQLI QADEGSVSKL DRFVKAHPQL YPEFTGDYKR LAHIQKKYKT
     MWEIPQNLFI KLAAERARYV CQSQSTNLYF KYPQVSTLIK AQKFGFACGL KTLVYYIRQQ
     PAVEALKITI NHSILSFVNA VNKETKSPVF DRSKVVCTAE VCIACQ
//