ID A0A074X4N9_AURPU Unreviewed; 1049 AA.
AC A0A074X4N9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=M438DRAFT_107933 {ECO:0000313|EMBL:KEQ80475.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ80475.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ80475.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ80475.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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};
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DR EMBL; KL584997; KEQ80475.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074X4N9; -.
DR STRING; 1043002.A0A074X4N9; -.
DR HOGENOM; CLU_000335_0_1_1; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000030706; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR47835; HFM1, ATP DEPENDENT DNA HELICASE HOMOLOG; 1.
DR PANTHER; PTHR47835:SF2; SEC63 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF02889; Sec63; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00973; Sec63; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KEQ80475.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000030706}.
FT DOMAIN 256..430
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 470..658
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 167..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1049 AA; 117972 MW; 0E038AEA77D69E4E CRC64;
MTRLPTAQKA RPCSERLWLS APSAFLGVLN FLTTVDPAIE TSVTMEPNDP YSYYLPYEQY
ANNNVDDYIL NAGYQDDQVD YELSRPHRPD TVTRQSQAAF GRARLSLPPP APVPIEVNDY
LGYNYASTPS DDYTRAYLEN QSEDIRPSIQ AVHALAPTES RPYQHIFRRQ ESSSSPTNAV
PSSPTYQASQ RQQNPEASMP IRSYAFPTAQ QGKPEIDRGP PTVQGIQLVP VHTLPDRFRT
IFPFAMFNAV QSACFQSIYE SDDNCVFSSP TGSGKTVLFE IAICRMLRGW TNGTFKVVYM
APTKSLCSER ARDWKAKFGP LNLKCEEMTG DSDITSLHHV QRADIIVTTP EKWDSMTRKW
KDHEKLVRLI KLLLIDEVHI LNKDRGAALE VVVSRMKSVG AGTRFVALSA TVPNSQDIAT
WLGRNDDTPN VPATHKRFGE EFRPVELTRY VCGYQSNANA FGFDTVLTKK LSDVVVKYSQ
KKPIMVFCFT RKSCSEAAKF LAEWWKHSAP KNRYWHAPTR QIRVEDKGLQ STVSAGVAVH
HAGLGLDDRG AVESAYLAGE LSVICCTSTL AVGVNLPCHM VIIKNTVSYE AGAIKEYSDL
EIMQMIGRAG RPQFDTSALA VIMTKMQQVK HYEQLLSGQE RLESCLHLNL VEHLNAEIGL
GMVPDLCAAK KWLAGTFLRV RLEDNPTHYQ IKGDTPDRDL GARLEQICDS AISQLQELGL
IECTPSFKTT DYGEAMARYY MNITTMETIL SLPRKPKISE ILAVISQAHE FRELRFRSGE
KPVYKELNDM PDIRFPIKVD LSAYAHKVSL IVQSVLGGVR HVADQPNHRV QNSIDQSLIF
QHIHRLIRCI VDCQSFDKDA IGIRNALMLS RSLAARVWDD SPMVLQQIEQ IGPVALRKLV
GAKITTMDEF ASTEPGRLEY VLNKAPPFGL NMHNRIQAFP KLRVALQMIG QPFVKAQEHV
AVKLKIDLGF LNQKTPVYYR TKPVFVIVLV GTSDGQKITF FRISAQKLER INPINATAYL
TSPTQLIECY VMCDDLGQCH NMFHLKLLH
//
