ID A0A1I8ALD6_9BILA Unreviewed; 2376 AA.
AC A0A1I8ALD6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
OS Steinernema glaseri.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC Steinernema.
OX NCBI_TaxID=37863 {ECO:0000313|Proteomes:UP000095287, ECO:0000313|WBParaSite:L893_g6916.t1};
RN [1] {ECO:0000313|WBParaSite:L893_g6916.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406,
CC ECO:0000256|RuleBase:RU003410}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000256|ARBA:ARBA00009303}.
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DR WBParaSite; L893_g6916.t1; L893_g6916.t1; L893_g6916.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000095287; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd02205; CBS_pair_SF; 1.
DR CDD; cd17920; DEXHc_RecQ; 1.
DR CDD; cd01049; RNRR2; 1.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR CDD; cd00400; Voltage_gated_ClC; 1.
DR Gene3D; 1.10.1650.20; -; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 1.10.3080.10; Clc chloride channel; 1.
DR Gene3D; 1.10.150.80; HRDC domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR014743; Cl-channel_core.
DR InterPro; IPR001807; Cl-channel_volt-gated.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR012348; RNR-like.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR033909; RNR_small.
DR InterPro; IPR030475; RNR_small_AS.
DR InterPro; IPR000358; RNR_small_fam.
DR InterPro; IPR018982; RQC_domain.
DR InterPro; IPR039718; Rrm1.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00570; HRDC; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR Pfam; PF00268; Ribonuc_red_sm; 1.
DR Pfam; PF09382; RQC; 1.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SMART; SM00116; CBS; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00341; HRDC; 1.
DR SMART; SM00956; RQC; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF81340; Clc chloride channel; 1.
DR SUPFAM; SSF47240; Ferritin-like; 1.
DR SUPFAM; SSF47819; HRDC-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50967; HRDC; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
DR PROSITE; PS00368; RIBORED_SMALL; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 29..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 66..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 220..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 251..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 303..360
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 368..431
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 700..907
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 928..1076
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1245..1328
FT /note="HRDC"
FT /evidence="ECO:0000259|PROSITE:PS50967"
SQ SEQUENCE 2376 AA; 265074 MW; 5127D309CAEB28F9 CRC64;
XVAAAYGAPI AGAVFVAEIV LGTMTMSSFG PLLMAAVSAH LTMRVLGGYH APYEMTNVQA
VAGWDILPFL VLGVLIGLAA PAFLKLLNLF RTLFKRTGLG LPLRLALGGL LLGLLLIAMP
RVAGNGFSVV SSMLHSDWAW YSVLLILAFK VLATGLTVGS GAVGGVFTPA IFVGAAFGTL
FGQLTLWVLP GXXXXXXXXX XXXXXXXXXX XXXXXXDLPL YLFTLVGMGA FLGAATSAPF
MAILMLFEMT LSYQLVLPLI VACVMAYFVS RGVAEVAMYE VTLVRERDAL LRHKLRHTTL
AELVRPADTV VSTTTQMRDA LQMFLDYPVR YLYVVNEEQV YQGVIAQPDL TRMLLDDNAA
QERVVGDILR MDFVKTLYPN MSLDEAQEHF VSFAGERLPV LNGDGSGRLI GVVYKSAVLE
KYSAIKRSLD ASGERGLAGG LIVGLAMLFA VPLATAQNRV GLENLSATRV ARWLSSAPDQ
VWQFGERNWR YVNEDGLQLT LGNDTVTAPD WARPVELGGI NITQQFEQGP AGPWRYALAV
GALDMTGKQD NGDLVYGSSA GSLMLSTDVT SRTSIDTQME SARDFGLTGL GATYRSPDFG
VWQASVAKAS HSVGQGWRYQ AAYGLDVLDD LHLQWQGERY QDNFLDLSRY QGMKVDAASS
RQVVGLSMPL RRWGEVKTQY EVQQEVFGYD SFRGSQHEII ETLIQGGDAL VLMPTGGGKS
LCYQIPALVR PGTGVVVSPL IALMQDQVDA LNELGVNAAY LNSTQDWQTA XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
ARGQISLFAI DEAHCVSQWG HDFRPEYLGL DLLAQRWPGV PRVALTATAT QLTRVEIAQR
LKLEEARHFV ASFDRPNICY RIIEKNEVRK QLLSFIQEEH SGDAGIVYCL SRSRVEDTAE
FLCKNGIHAL PYHAGLDAQQ RAINQARFLR EEGVVMVATI AFGMGVNKPD VRFVAHIDLP
KSVEGYYQET GRAGRDGEAA TAWLAYGLQD VVQLYRMINQ SQGDAAHRRQ QGQALDAMLG
LCETISCRRQ RLLAYFDQQI EPCGNCDTCL EAPEAWDGTV AAQKMLSTIY RLWRERGQRF
GAGHLIDILL GKLTDRVKEH EHDKLTVFGV GKELTDQAWR GVLRQLLAHS LVTVDPEGYG
TLLLTDASRE VLKGERTLML RRETVTRGPA AHRVKGQAPA GPALEPDQQR RFEALRAWRA
ATAREHGVPA YVIFHDATLR EVAIRCPSSE ADLEPITGIG FYNGIRTSDI HETIIKSAAD
LISEDTPDYQ YLAARLAIFH LRKIAFGQFE PPSLFDHVTL QTKEGRYDPH LLQDYTRAEF
DELDAHLDHW RDMNFSYGAV KQLEGKYLIQ NRVTKRIYES PQFLYMLVAM CLFARYPADT
RLSFIKRFYD AVSQFKISLP TPIMAGVRTP TRQFSSCVLI ECDDSLDSIN ATTSAIVRYV
SQRAGIGING GRIRAVGSEI RGGEAQHTGC LPFFKMFQAA VKSCSQGGVR GGAATLFYPM
WHLEVETLLV LKNNRGVEEN RIRHLDYGVQ INRLLYQRLI KGSHITLFSP HDVPGLYEAF
FADQDEFERL YEMYEQDPAI RKRSLPAVEL FSLLMQERAS TGRIYIQNVD HCNTHSPFQA
DRAPVRQSNL CMEIALPTKP LNDLNDPEGE IALCTLSAFN LGALESLDEL DGLAELIVRA
LDALLDYQDY PVKAALNATN KRRSLGVGVI NYAYYLAKNG TRYSDPAALG LTHRTFEAIQ
YYLLKASVQL SREYGPCDAF DETTYAAGLL PTDTYKKDVD GICNEPLHLD WEALRADIVK
HGLRNSTLTA LMPSETSSQI ANATNGIEPP RGLVSVKQSK DGILRQVVPE FEKYKDQYEL
LWQMPGNDDY LKLVGVMQKF VDQSISANTN YDPQRFEGGR VPMKQLLKDL LLAYKYGVKT
LYYHNTRDGA DDSHGESIMT TYSTFSKTDN DQLKEPMFFG QPVNVARYDQ QKYPIFEKLI
EKQLSFFWRP EEVDITQDRI DYQNLPDHEK HIFISNLKYQ TLLDSIQGRS PNVAFLPLVS
IPELETWIET WAFSETIHSR SYTHIIRNIA NDPSVIFDDI VRNENIQLRA ADISSYYDDL
ISDTMLYAQL GAGEHEINGE TRTLSVYELK KKLYLCMMSV NILEAIRFYV SFACSFAFAE
RKLMEGNAKI IRLIARDEAL HLTGTQHIIN ILRSGSDDPE FAQIARELEP VCFDMFKDAA
EQEKQWADYL FRDGSMIGLN KDILGQYVEY ITNIRMGAVG LKPAFESVKH NPIPWINTWL
SSDTVQVAPQ EVELSSYLVG QIDSAVSAGD FDGIEL
//
