ID A0A194UUD6_9PEZI Unreviewed; 913 AA.
AC A0A194UUD6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-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=VP1G_02608 {ECO:0000313|EMBL:KUI55273.1};
OS Valsa mali var. pyri (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI55273.1, ECO:0000313|Proteomes:UP000078576};
RN [1] {ECO:0000313|Proteomes:UP000078576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) 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}.
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DR EMBL; KN714679; KUI55273.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194UUD6; -.
DR STRING; 694573.A0A194UUD6; -.
DR OrthoDB; 5472715at2759; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000078576; 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, 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:UP000078576}.
FT DOMAIN 1..84
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 756..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 913 AA; 102370 MW; 0EF75E3035A835F2 CRC64;
MFERVQFDKI TARVSRLCYG LDMNHVDPVK ITQKVINGVY GGVTTIQLDD LAAETAAYMT
VTHPDYAILA ARIAVSNLHK QTKKQWSSVI SDLYHYVNPR NRTASPMISQ ETYDCVMRHK
DELDSAIVYD RDFGYQYFGF KTLERSYLLK LDGKVVERPQ HMIMRVAVGI WGDDIERVIE
TYNLMSHKFF THASPTLFNA GTPQPQLSSC FLVDMKDDSI EGIYDTLKTC AMISKMAGGI
GLNVHRIRAT GSYIAGTNGT SNGIIPMLRV FNNTARYVDQ GGNKRPGAFA IYLEPWHADV
FEFLDLRKNH GKEEVRARDL FLALWIPDLF MKRVEKNGDW TLMCPNECPG LADCYGDEFE
ALYEKYEREG RGRKTMKAQK LWYAILEAQT ETGNPFMLYK DACNRKSNQK NLGTIRSSNL
CTEIIEYCAP DEVAVCNLAS IALPAYVDYE NNCYNFQHLH EVTQVVVRNL NKIIDVNHYP
VKEAYNSNMR HRPIGVGVQG LADAFLALRM PFESPEARQL NKQIFETIYH AALTASCDIA
KVDGPYQTYE GSPVSQGQLQ YDMWGVQPSD LWDWDALKAK IKEHGIRNSL LMAPMPTAST
SQILGNNECF EPYTSNIYQR RVLAGEFQVV NPWLLRDLTE IGLWSEAMKN RIIAEDGSIQ
NIPSIPADIK ALYKTVWEVS QRTIVQMSAD RGAFIDQSQS LNIHMREPTM GKITSMHFTG
WKLGLKTGMY YLRTQAAAAP IQFTVDQEAL KIQEQTTTKH SGLGKRAPPA GMYTLPSTSV
RPMYIKKESI SNGGAGISNG IPTPSTTPPP AGKYTPVPSE AVSHVITSPS KPKDVPFKAD
LEEGESPKTL PVEPAGEQPT EEQLSEPSKD GKKPNGQSED KDEDSADREM DIYSEAALQC
SIDNPESCVM CSG
//
