ID A0A0V1NJI7_9BILA Unreviewed; 845 AA.
AC A0A0V1NJI7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
DE Flags: Fragment;
GN Name=Rrm1 {ECO:0000313|EMBL:KRZ84169.1};
GN ORFNames=T08_12676 {ECO:0000313|EMBL:KRZ84169.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ84169.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ84169.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ84169.1};
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|ARBA:ARBA00000206,
CC 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:KRZ84169.1}.
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DR EMBL; JYDM01000183; KRZ84169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1NJI7; -.
DR STRING; 92180.A0A0V1NJI7; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000054924; 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:UP000054924}.
FT DOMAIN 7..100
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 793..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..809
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 845
FT /evidence="ECO:0000313|EMBL:KRZ84169.1"
SQ SEQUENCE 845 AA; 95719 MW; B5949215156E5F15 CRC64;
MPGAFSLVII AFFAHGRREA VHFDKITSRI KKLCYGLNME HVEPILISQK VIAGLYQGVT
TVELDNLAAE ISATMTTKHP DYATLAARIA VSNLHKETKK VFSDVIDDLY QWINPNTNKH
SPMISPKVHQ IIQANSQRLN STIVYDRDFS YSYFGFKTLE KSYLLKINGK VAERPQHLLM
RVAIGIHEDD IDAAIETYNL MSEKWFTHAS PTLFNAGTCR PQLSSCFLIT MKSDSIEGIY
DTLKECAIIS KSAGGIGLNV HCIRASGTYI AGTNGYSNGL LPMLRVFNNT ARYVDQGGNK
RPGAFAVYLE PWHADIFDFL DAKKNTGVEE NRARDLFYAL WIPDLFMKRI EADGDWSLMC
PHECPGLADL WGDEFEKLYE KYEAQGKHKR RIKAQQLWYA IIESQIETGT PFMVYKDACN
RKSNQQNLGT IKCSNLCTEI VQYSSPDETS VCNLASIALN KFVNVAKREF DFAKLAEVTK
VVTVNLNKII DRNYYPVAVV FLFSNAKDSL FLVLSIELDP FQAEKSNKRH RPIGIGVQGL
ADAFILMRYP FESEEARLLN KKIFETIYYA ALESSCDLAK QFGPYETYQG SPASKGILQY
DMWNVQPTDL WDWESLKCRI EKYGLRNSLL LAPMPTASTA QILGNNESVE AYTSNVYTRR
VLSGEFQIVN HHLMKDLVEL GLWDESLKNE IIANKGSIQS IESIPAEIRE LYKTVWEISQ
KCVIDMAAER GAFIDQSQSL NIHIAEPNYA KLTSMHFYGW KKGLKTGMYY LRTKPAVTAI
QFTVDKLALK QKKTKEEEEG QRHNGGYVDK GRKFPTSGDN WSNNVNTLLQ QCRLENGDEC
MLCSS
//
