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Database: UniProt
Entry: A0A0B1PAN1_UNCNE
LinkDB: A0A0B1PAN1_UNCNE
Original site: A0A0B1PAN1_UNCNE 
ID   A0A0B1PAN1_UNCNE        Unreviewed;       779 AA.
AC   A0A0B1PAN1;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=General transcription and DNA repair factor IIH helicase subunit XPD {ECO:0000256|ARBA:ARBA00014344};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=EV44_g2756 {ECO:0000313|EMBL:KHJ33719.1};
OS   Uncinula necator (Grape powdery mildew).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Erysiphe.
OX   NCBI_TaxID=52586 {ECO:0000313|EMBL:KHJ33719.1, ECO:0000313|Proteomes:UP000030854};
RN   [1] {ECO:0000313|EMBL:KHJ33719.1, ECO:0000313|Proteomes:UP000030854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=c {ECO:0000313|Proteomes:UP000030854};
RX   PubMed=25487071;
RA   Jones L., Riaz S., Morales-Cruz A., Amrine K.C., McGuire B., Gubler W.D.,
RA   Walker M.A., Cantu D.;
RT   "Adaptive genomic structural variation in the grape powdery mildew
RT   pathogen, Erysiphe necator.";
RL   BMC Genomics 15:1081-1081(2014).
CC   -!- FUNCTION: ATP-dependent DNA helicase important for chromosome
CC       transmission and normal cell cycle progression in G(2)/M (By
CC       similarity). May have a role in changing DNA topology to allow the
CC       loading of proteins involved in maintaining sister chromatid cohesion
CC       in the vicinity of the centromeres (By similarity). Has a specific role
CC       in chromosome segregation during meiosis II.
CC       {ECO:0000256|ARBA:ARBA00025396}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009146}.
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:KHJ33719.1}.
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DR   EMBL; JNVN01001269; KHJ33719.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B1PAN1; -.
DR   STRING; 52586.A0A0B1PAN1; -.
DR   HOGENOM; CLU_011312_1_0_1; -.
DR   OMA; IREQFFR; -.
DR   OrthoDB; 124793at2759; -.
DR   Proteomes; UP000030854; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   CDD; cd18788; SF2_C_XPD; 1.
DR   Gene3D; 1.10.275.40; -; 1.
DR   Gene3D; 1.10.30.20; Bacterial XPD DNA helicase, FeS cluster domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
DR   InterPro; IPR045028; DinG/Rad3-like.
DR   InterPro; IPR010643; HBB.
DR   InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR   InterPro; IPR006554; Helicase-like_DEXD_c2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR   InterPro; IPR013020; Rad3/Chl1-like.
DR   InterPro; IPR001945; RAD3/XPD.
DR   InterPro; IPR042493; XPD_DNA_FeS.
DR   NCBIfam; TIGR00604; rad3; 1.
DR   PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR   PANTHER; PTHR11472:SF1; GENERAL TRANSCRIPTION AND DNA REPAIR FACTOR IIH HELICASE SUBUNIT XPD; 1.
DR   Pfam; PF06733; DEAD_2; 1.
DR   Pfam; PF06777; HBB; 1.
DR   Pfam; PF13307; Helicase_C_2; 1.
DR   PRINTS; PR00852; XRODRMPGMNTD.
DR   SMART; SM00488; DEXDc2; 1.
DR   SMART; SM00491; HELICc2; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KHJ33719.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030854}.
FT   DOMAIN          1..268
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51193"
FT   COILED          239..281
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   779 AA;  88919 MW;  2F9A47CC46698B66 CRC64;
     MKFNIDSSGL ILLETLDAGG HCVLEMPSGT GKTVSLLSLI VAYQQYYPEH RKLIYCSRTM
     SEIEKALAEL RALMKYRAEQ LGYEEEFRGL GLTSRKNLCL HPTVKREKSG AIVDAKCRSL
     TARFVKEKKE RGENVPICIY HDNLDLKEPH NLVDPGVYTL ESLMRYCEQE KICPYFASRR
     MMSFCNVIIY SYHYLLDPKI AERVSKELSK DCIVVFDEAH NIDNVCIESL STDITNDSLR
     KATRGAQNLE MKISEMKEKD KEKLVNEYAK LVEGLKDASE AQAEDAFMSN PALPDDLLTE
     AVPGNIRRAE HFVAFLKRFI EYLKTRMKVR QVISETPPSF LAHLKEYTFI EKKPLRFCAE
     RLSSLVRTLE LANIEDYQPL QEVATFATLV ATYEKGFLLI LEPYESDTAE VPNPVLHFTC
     LDAAIAIKPV FDRFSSVIIT SGTISPLEMY PKILGFSTVV QESYSMTLAR RSFLPMIVTR
     GSDQVAISSG FQVRNEPSVV RNYGHLLTEF SKLTPDGMVV FFPSYLYMES IISMWQGMGI
     LDEVWKYKLI LVETPDAQET SLALETYRTA CCNGRGAILL CVARGKVSEG IDFDHQYGRT
     VLCIGVPFQY TESRILKARL EFLRETYRIR ENDFLSFDAM RHAAQCLGRV LRGKDDYGIM
     VLADRRFLRK RNQLPRWINQ ALLDSEVNLS TDMAFGIAKK FLRNMAQPFR SSDQEGISTW
     SLEDLERFKE KEEEEAIKKL MTADGGSKEE SLPQKELLTA NITDILDDDE LEVCMMDLN
//
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