ID A0A166ZHN9_9PEZI Unreviewed; 895 AA.
AC A0A166ZHN9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=CI238_02271 {ECO:0000313|EMBL:KZL78930.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL78930.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL78930.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL78930.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) 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|ARBA:ARBA00024942,
CC 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZL78930.1}.
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DR EMBL; LFIW01002185; KZL78930.1; -; Genomic_DNA.
DR STRING; 1573173.A0A166ZHN9; -.
DR OrthoDB; 5472715at2759; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000076584; Unassembled WGS sequence.
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:InterPro.
DR CDD; cd01679; RNR_I; 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.
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};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000076584}.
SQ SEQUENCE 895 AA; 100281 MW; 34EE2CD4586D4876 CRC64;
MFVRKRDGRQ ERVQFDKITA RVSRLCYGLD MDHVDPVAIT QKVISGVYGG VTTVQLDDLA
AETAAYMTVT HPDYAILAAR IAVSNLHKQT KKQWSSVVSD LYHYVNPKNG KASPMIAKDT
YDAVMRHKEE LDSAIVYDRD FNYQYFGFKT LERSYLLKLD GKIAERPQHM IMRVAVGIWG
DDVERVIETY NLMSSKFFTH ASPTLFNAGT PQAQLSSCFL VDMKEDSIEG IYDTLKTCAM
ISKMAGGIGL NVHRIRATGS YIAGTNGTSN GVVPMLRVFN NTARYVDQGG NKRPGAFAIY
LEPWHADVFD FLDLRKNHGK EEVRARDLFL ALWIPDLFMK RVEKNGDWTL MCPNECPGLA
DCYGEEFEAL YEKYEQMGKG RKTMKAQKLW YAILEAQTET GNPFMLYKDA ANRKSNQKNL
GTIRSSNLCT EIIEYCAPDE VAVCNLASLA LPTFVDYNEG VYDFQKLHEV TQVVVRNLNR
IIDVNHYPVQ EARNSNMRHR PIGLGVQGLA DAFLALRMPF ESPEARDLNK KIFETIYHAA
LTMSVQLAKE EGPYQTYEGS PVSQGILQYD MWNVKPSDLW DWDALKEQIK QHGVRNSLLV
APMPTASTSQ ILGNNECFEP YTSNIYQRRV LAGEFQVVNP WLLKDLVDMG LWSDAMKNRI
IAENGSIQNI PNIPTEVKAL YKTVWEISQR TVVQMAADRG AFIDQSQSLN IHMKDPTMGK
ITSMHFAGWK LGLKTGMYYL RTQAAAAPIQ FTVDQEALKV TDSAIGKVLK KRAPPPGHVA
APVVNVPRPM YAKKDSSAQD NGIPTPSVTP PPPRTAPAQK PDTMKADVAE GDSPRALPTE
PAEKLKIEEL PVAGSKTPDV EDKTEDSKER EMDIYSEAVL ACSIENPESC VMCSG
//
