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Database: UniProt
Entry: A0A0V0UZA8_9BILA
LinkDB: A0A0V0UZA8_9BILA
Original site: A0A0V0UZA8_9BILA 
ID   A0A0V0UZA8_9BILA        Unreviewed;       814 AA.
AC   A0A0V0UZA8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE            EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN   ORFNames=T09_2283 {ECO:0000313|EMBL:KRX56633.1};
OS   Trichinella sp. T9.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX56633.1, ECO:0000313|Proteomes:UP000054681};
RN   [1] {ECO:0000313|EMBL:KRX56633.1, ECO:0000313|Proteomes:UP000054681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS409 {ECO:0000313|EMBL:KRX56633.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-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   -!- PATHWAY: Genetic information processing; DNA replication.
CC       {ECO:0000256|ARBA:ARBA00005160, 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:KRX56633.1}.
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DR   EMBL; JYDN01000118; KRX56633.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0UZA8; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000054681; 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:UniProtKB-UniPathway.
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:UP000054681}.
FT   DOMAIN          1..92
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
FT   REGION          760..782
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        760..775
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   814 AA;  92386 MW;  436B9D108C114039 CRC64;
     MYVVKRDGRR EAVHFDKITS RIKKLCYGLN MEHVEPILIS QKVIAGLYQG VTTVELDNLA
     AEISATMTTK HPDYATLAAR IAVSNLHKET KKVFSDVIDD LYQWINPNTN KHSPMISPKV
     HQIIQANSQR LNSTIVYDRD FSYSYFGFKT LEKSYLLKIN GKVAERPQHL LMRVAIGIHE
     DDIDAAIETY NLMSEKWFTH ASPTLFNAGT CRPQLSSCFL ITMKSDSIEG IYDTLKECAI
     ISKSAGGIGL NVHCIRASGT YIAGTNGYSN GLLPMLRVFN NTARYVDQGG NKRPGAFAVY
     LEPWHADIFD FLDAKKNTGV EENRARDLFY ALWIPDLFMK RIEADGDWSL MCPHECPGLA
     DLWGDEFEKL YEKYEAQGKH KRRIKAQQLW YAIIESQIET GTPFMVYKDA CNRKSNQQNL
     GTIKCSNLCT EIVQYSSPDE TSVCNLASIA LNKFVNVAKR EFDFAKLAEV TKVVTVNLNK
     IIDRNYYPVA VAEKSNKRHR PIGIGVQGLA DAFILMRYPF ESEEARLLNK KIFETIYYAA
     LESSCDLAKQ FGPYETYQGS PASKGILQYD MWNVQPTDLW DWESLKCRIE KYGLRNSLLL
     APMPTASTAQ ILGNNESVEA YTSNVYTRRV LSGEFQIVNH HLMKDLVELG LWDESLKNEI
     IANKGSIQSI ESIPAEIREL YKTVWEISQK CVIDMAAERG AFIDQSQSLN IHIAEPNYAK
     LTSMHFYGWK KGLKTGMYYL RTKPAVTAIQ FTVDKLALKQ KKTKEEEEGQ RHNGGYVDTS
     RKFPTSGDNW SNNVNTLLQQ CRLENGDECM LCSS
//
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