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Database: UniProt
Entry: A0A421JKA8_9ASCO
LinkDB: A0A421JKA8_9ASCO
Original site: A0A421JKA8_9ASCO 
ID   A0A421JKA8_9ASCO        Unreviewed;       835 AA.
AC   A0A421JKA8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=JA1_004239 {ECO:0000313|EMBL:RLV90925.1};
OS   Spathaspora sp. JA1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX   NCBI_TaxID=2028339 {ECO:0000313|EMBL:RLV90925.1, ECO:0000313|Proteomes:UP000285775};
RN   [1] {ECO:0000313|EMBL:RLV90925.1, ECO:0000313|Proteomes:UP000285775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA1 {ECO:0000313|EMBL:RLV90925.1,
RC   ECO:0000313|Proteomes:UP000285775};
RA   Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT   "Physiological and comparative genomic analysis of newly identified yeasts
RT   Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT   production.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC       {ECO:0000256|ARBA:ARBA00006637}.
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:RLV90925.1}.
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DR   EMBL; NSGQ01000043; RLV90925.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A421JKA8; -.
DR   STRING; 2028339.A0A421JKA8; -.
DR   Proteomes; UP000285775; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:InterPro.
DR   CDD; cd18029; DEXHc_XPB; 1.
DR   CDD; cd18789; SF2_C_XPB; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR032438; ERCC3_RAD25_C.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001161; XPB/Ssl2.
DR   InterPro; IPR032830; XPB/Ssl2_N.
DR   NCBIfam; TIGR00603; rad25; 1.
DR   PANTHER; PTHR11274:SF0; GENERAL TRANSCRIPTION AND DNA REPAIR FACTOR IIH HELICASE SUBUNIT XPB; 1.
DR   PANTHER; PTHR11274; RAD25/XP-B DNA REPAIR HELICASE; 1.
DR   Pfam; PF16203; ERCC3_RAD25_C; 1.
DR   Pfam; PF13625; Helicase_C_3; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   PRINTS; PR00851; XRODRMPGMNTB.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:RLV90925.1};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:RLV90925.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022806,
KW   ECO:0000313|EMBL:RLV90925.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000285775}.
FT   DOMAIN          362..524
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          578..732
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          812..835
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..50
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   835 AA;  94953 MW;  519B1FE0322A7E73 CRC64;
     MASSRRTGQV NYAELNNGND DDYLSDDKIS DEDDYGTKPK KRKMKNQTVD NQVKRKQVQS
     TVDYIRNEVD DTNFSDEELI ELTPEIPADY VPDAVSRAFG KADFSYLKLK PDHFSRPIWI
     SPNDGRIILE SFSPLAEQAQ DFLITIAEPI SRPSHIHEYR ITAYSLYAAV SVGLETDDII
     SVLNRLSKVP VAESIINFIK GATISYGKVK LVLKHNRYFV ESTQADILQM LLKDPVIGPL
     RIQSSENTVT SNGLVQSAPP TNDIVIPGTK KTDQSNTEAE DIFASVVGTK EDDENDDDLD
     TVHSFEISND SVEIVKKRCQ EIEYPVLEEY DFRNDSRNAD LEIDLKPSTQ IRPYQEKSLS
     KMFGNGRARS GIIVLPCGAG KTLVGITAAC TIRKSVIVLC TSSVSVMQWR QQFLQWCTIQ
     PENVAVFTSE NKEMFTSDSG LVVSTYSMVA NTRNRSHDSQ KVMDFLKSRE WGFIILDEVH
     VVPAAMFRRV VTTIAAHAKL GLTATLVRED DKIDDLNFLI GPKLYEANWM DLASKGHIAN
     VQCAEVWCPM TSEFYQEYLR ESARKRMLLY IMNPTKFQAC QFLIHYHEKR GDKIIVFSDN
     VYALQEYALK LGKPFIYGST PQSERMKILQ NFQHNDEINT IFLSKVGDTS IDLPEATCLI
     QISSHYGSRR QEAQRLGRIL RAKRRNDEGF NAFFYSLVSK DTQEMYYSTK RQAFLVDQGY
     AFKVITHLSG MEQLNDLAYS SARERRELLQ QVLLKNEDAA GLEIGDDVDT NFISKERRMK
     YEKEQANRTA GSLAGLAGGE DMAYIEYSKN KNKELREQSH HPLIQKMYYP KQGKK
//
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