UniProt: A0A167FQX0

Database: UniProt
Entry: A0A167FQX0_9ASCO

LinkDB:  A0A167FQX0_9ASCO 
Original site:  A0A167FQX0_9ASCO

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (5)   
   Pfam (2)   
   PROSITE (1)   
All databases (17)   

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ID   A0A167FQX0_9ASCO        Unreviewed;       801 AA.
AC   A0A167FQX0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
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   Name=RNR1 {ECO:0000313|EMBL:ANB15584.1};
GN   ORFNames=AWJ20_3212 {ECO:0000313|EMBL:ANB15584.1};
OS   Sugiyamaella lignohabitans.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Trichomonascaceae; Sugiyamaella.
OX   NCBI_TaxID=796027 {ECO:0000313|EMBL:ANB15584.1, ECO:0000313|Proteomes:UP000189580};
RN   [1] {ECO:0000313|EMBL:ANB15584.1, ECO:0000313|Proteomes:UP000189580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10342 {ECO:0000313|EMBL:ANB15584.1,
RC   ECO:0000313|Proteomes:UP000189580};
RA   Bellasio M., Peymann A., Valli M., Sipitzky M., Graf A., Sauer M., Marx H.,
RA   Mattanovich D.;
RT   "Complete genome sequence and transcriptome regulation of the pentose
RT   utilising yeast Sugiyamaella lignohabitans.";
RL   Submitted (FEB-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|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; CP014503; ANB15584.1; -; Genomic_DNA.
DR   RefSeq; XP_018738061.1; XM_018880221.1.
DR   AlphaFoldDB; A0A167FQX0; -.
DR   GeneID; 30035210; -.
DR   KEGG; slb:AWJ20_3212; -.
DR   OrthoDB; 5472715at2759; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000189580; Chromosome b.
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; cd01679; RNR_I; 1.
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.
DR   PROSITE; PS00089; RIBORED_LARGE; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW   ECO:0000256|RuleBase:RU003410};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003410};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189580}.
FT   DOMAIN          518..540
FT                   /note="Ribonucleotide reductase large subunit"
FT                   /evidence="ECO:0000259|PROSITE:PS00089"
SQ   SEQUENCE   801 AA;  89725 MW;  9603AB2C2E5EF05A CRC64;
     MTTQHPDYAI LAARIAVSNL HKQTKKQFSQ VIYDLYHYTN PRNGKLSPMI ADDVYEVVQK
     HADELNSAIV YDRDFSYNYF GFKTLERSYL LKINGKIAER PQHMIMRVAV GIHGSDITKA
     IETYNYMSQK YFTHASPTLY NAGTPKPQMS SCFLVNMKDD SIDGIYDTLK TCALISKSAG
     GIGLSVHNIR ATGSYIAGTN GTSNGIVPML RVFNNTARYV DQGGNKRPGA FAMYLEPWHD
     DVFEFIELRK NHGKEEVRAR DLFLALWIPD LFMKRVKANE DWTLMCPNEC PGLDDVYGDE
     FVALYEKYEK EGRGRRTIKA QKLWYAILEA QTETGNPFML YKDACNSKSN QQNLGTIKSS
     NLCCEIVEYS SPEEVAVCNL ASLSLPAFVE SDEEGLWYNF NKLHEVAKVV TRNLNVIIDR
     NFYPVKEAER SNFRHRPIAL GIQGLADAFM ALRLPFDSPE AKQLNVQIAE TIYHAAVESS
     VELAELYGPY ETYQGSPASK GLLQFDLWDI TPTDLWDWAA LKKKMAKHGL RNSLLVAPMP
     TASTSQILGN NECFEPYTSN IYSRRVLAGE FQIVNQWLLK DLVDLGLWGE NMKNRIIANN
     GSIQNIPNIP EDIKALYKTV WELSQKTIID MAADRAAFID QSQSLNIYIQ APTMGKLTSM
     HFYGWQKGLK TGMYYLRTQA ASAPIQFTVD QEALKVSDGN VAKNLVRKQY RQGFPGQGSE
     VDKLAEKVSN LTTQPVPVAA TVVAAENNKE NLDVSTTTTT KLSDTDGVAA ADGDKSEIDI
     YNEKVLACSI ANPGACEMCS G
//

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