ID V9D569_9EURO Unreviewed; 912 AA.
AC V9D569;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=G647_06085 {ECO:0000313|EMBL:ETI22015.1};
OS Cladophialophora carrionii CBS 160.54.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1279043 {ECO:0000313|EMBL:ETI22015.1, ECO:0000313|Proteomes:UP000030678};
RN [1] {ECO:0000313|EMBL:ETI22015.1, ECO:0000313|Proteomes:UP000030678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 160.54 {ECO:0000313|EMBL:ETI22015.1,
RC ECO:0000313|Proteomes:UP000030678};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora carrionii CBS 160.54.";
RL Submitted (MAR-2013) 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; KB822706; ETI22015.1; -; Genomic_DNA.
DR RefSeq; XP_008728632.1; XM_008730410.1.
DR AlphaFoldDB; V9D569; -.
DR GeneID; 19984578; -.
DR VEuPathDB; FungiDB:G647_06085; -.
DR HOGENOM; CLU_000404_1_2_1; -.
DR OrthoDB; 5472715at2759; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000030678; 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}.
FT DOMAIN 1..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 789..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 912 AA; 102287 MW; 193414D05E6EF919 CRC64;
MFVYKRDGRK ERVQFDKITA RVSRLCYGLD PEHVDAAAIT QKVISGVYQG VTTIELDNLA
AETAAYMTVT HPDYAILAAR IAVSNLHKQT KKQFSAVISD LYHYTNPKNN KFSPMISKET
YECVMRHADE LNSAIVYDRD FNYQYFGFKT LEKSYLLKIG KQVAERPQHM IMRVAVGIHG
DDIEKAIETY NLMSQKCFTH ASPTLFNAGT PQPQLSSCFL IDMKEDSIEG IYDTLKTCAM
ISKTAGGIGL NAHCIRATGS YIAGTNGTSN GLIPMLRVFN NTARYVDQGG NKRPGAFAIY
LEPWHADVFE FLNLRKNHGK EEVRARDLFY AMWTPDLFME RVEKNQEWTL FCPHEAPGLA
DVYGDDFKEL YERYEKEGRG RQTVKAQKLW YAILEAQTET GTPYMLYKDA CNRKSNQKNL
GTIRSSNLCT EIVEYTAPDE VAVCNLASLA LPTFVDQARG EYDFGRLHEV TQVVTRNLNK
IIDINYYPVP EAKKSNMRHR PIGLGVQGLA DAFLALRLPF DSPEARQLNI QIFETIYHAA
LTASCELARE QGAYETYEGS PVSQGILQYD MWNVTPSDLW DWDSLKADIA KYGVRNSLLV
APMPTASTSQ ILGNNECFEP YTSNIYSRRV LAGEFQVVNP WLLKDLVDLG LWSDNMKNRI
IADGGSVQNI PNIPADIKAL YKTVWEISQR TILQMAADRG AFIDQSQSLN IHLKEPTMGK
ITSMHFAGWK MGLKTGMYYL RTMAATQPIQ FTVDQEQLKV ADTNIARERS GPKKRTSVGF
SSSVSNYNSI PRPMYQSKSS NLGGNNTASI NGIPTPTSTP PAVSDDNKQI GSVAHKLAKT
RLSEGESSTE VSPRILATDA TSSPPDAIAE ESLESRSKGE QEEDKESENG EREEDIYAQK
VLACEYTLSL FR
//
