ID A0A074VUB0_9PEZI Unreviewed; 682 AA.
AC A0A074VUB0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=M437DRAFT_75363 {ECO:0000313|EMBL:KEQ62839.1};
OS Aureobasidium melanogenum CBS 110374.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ62839.1, ECO:0000313|Proteomes:UP000030672};
RN [1] {ECO:0000313|EMBL:KEQ62839.1, ECO:0000313|Proteomes:UP000030672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ62839.1,
RC ECO:0000313|Proteomes:UP000030672};
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:ARBA00000600};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000256|ARBA:ARBA00000600};
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC {ECO:0000256|ARBA:ARBA00007913}.
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DR EMBL; KL584833; KEQ62839.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074VUB0; -.
DR HOGENOM; CLU_001666_8_2_1; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000030672; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR CDD; cd18044; DEXXQc_SMUBP2; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 2.40.30.270; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047187; SF1_C_Upf1.
DR InterPro; IPR004483; SMUBP-2/Hcs1-like.
DR InterPro; IPR048761; SMUBP-2_HCS1_1B.
DR NCBIfam; TIGR00376; IGHMBP2 family helicase; 1.
DR PANTHER; PTHR43788:SF19; DNA-BINDING PROTEIN SMUBP-2; 1.
DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF21138; SMUBP-2_HCS1_1B; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KEQ62839.1};
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:UP000030672}.
FT DOMAIN 201..465
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|SMART:SM00487"
FT DOMAIN 219..455
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 418..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 682 AA; 75127 MW; 25AE9D67AC233373 CRC64;
MAPIDIPSFA DKQLKLLAAE LNAELEETAL LTATHAPSTL ARAGLAVLNL SVSAQRTGLG
GKSLIELSLD PAIAGTETQL PEHGLRVGDI VGVSEQPKGA EKKKERQDME KKQIQGVVVK
VLREIIVVAL DKDEVDIPGG KLWLLVNSAS VFWKRMLMNQ TMTKLLKMPE SEHSTLTRVL
FGQSSAVSVQ PRDMAEELEW LDPSLNDSQK EAIKFALASP EVALIHGPPG TGKTHTLIEL
IRQCLKKGLR LLVCGPSNIS VDNIVERLSP HKVPMVRLGH PARLLPGVLN HSLDILTRTS
DAAALVKDIR NEMDAKQASI RKTRKGRERK AIYGEIKELR KDYRQREAAC VSSLVRESKV
VLATLHGAGG FHLKSQEFDV VIVDEASQAL EAQCWVPLLS SGASKLILAG DHLQLPPTIK
SSNSKSTKQN TKTGQGGVDL ETTLFDRMLD LYGESIKRML TIQYRMHEKI NAFPSAALYE
SKLIAAETVK ARLLKDLPYD VEETEDTTEP VVFWDTQGGE FHEKTDDDDE PKSKSSLLGE
SKSNELEAAI VKKHVQSLVD AGVKAEDIAV VTPYNGQLAV LSQLLKERFV GIELGSIDGF
QGREKEAVVV SLVRSNSEHE VGFLAEKRRL NVAMTRPKRH LCVVGDSETV GRGSKFLKSW
MEFLEENADL RYPDLDDVLR SE
//
