ID Q6BM64_DEBHA Unreviewed; 1151 AA.
AC Q6BM64;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 2.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN OrderedLocusNames=DEHA2F07986g {ECO:0000313|EMBL:CAG89047.2};
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG89047.2, ECO:0000313|Proteomes:UP000000599};
RN [1] {ECO:0000313|EMBL:CAG89047.2, ECO:0000313|Proteomes:UP000000599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC 2968 {ECO:0000313|Proteomes:UP000000599};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382138; CAG89047.2; -; Genomic_DNA.
DR RefSeq; XP_460707.2; XM_460707.2.
DR AlphaFoldDB; Q6BM64; -.
DR STRING; 284592.Q6BM64; -.
DR GeneID; 2903510; -.
DR KEGG; dha:DEHA2F07986g; -.
DR VEuPathDB; FungiDB:DEHA2F07986g; -.
DR eggNOG; KOG0952; Eukaryota.
DR HOGENOM; CLU_000335_0_1_1; -.
DR InParanoid; Q6BM64; -.
DR OMA; VYGYQSH; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000000599; Chromosome F.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase 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; IPR003593; AAA+_ATPase.
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; SM00382; AAA; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000599}.
FT DOMAIN 162..335
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 377..557
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1105..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1151 AA; 131304 MW; ABB913DF602C2322 CRC64;
MPFTPPRFMS NTGNSGIQEF ALGLSTPLSG INSNNSALSG SRCHTYRSGT LGIGRIREPV
FNFDTSHIFG DHYSLNCPPV RRKPSIPIRS VKRFDLRKQA DKGINFSDFS SSSEGNETLD
VSQKSTLMST NQPVLSTSIL PEKYRSIFSF SHFNKMQSES FETIYNSDHN CVINAPTGSG
KTVLFELAML RLFYFSNTNN KVLYLAPSKA LCAEKYNDWV GKFSFLSITI GVLTSETSLE
EAEDVKRSNI IISTPEKLDL LTRRLSNYDK LLNDVKLIVI DEIHILKDTR GSTLEVVTTR
INKMCSKVRI IGASASAPNL YDMSIWLRKK DDLNPAITLN FDDTYRSVQL DKIVLGYASQ
KDKDFHFDQF LHSKLVGVIR HYGKNKPTLI FCPTRNSCIE TAKYLNDNFD RNLCSQNSRI
QFDEKELLVY AAHGIAFHHA GLSSDDRKKI ELLFIEGKLN ILCSTSTLSS GVNLPTYLVI
IKGTKRWYSG SFHEYKETDV LQMIGRAGRP QFETRGKAVI MTTENQKDKY QRLLKGILKD
GSEKIESCLH LNLAQHLVAE ISLGTIGSID DTLQWLKSTF FFIRFTSNPS YYKEISSFHA
SEPNKRLHHF CQKYLDSLVN ERIVSPISSG GFRCTEYGDV MTKYYILYPT MRNIIRSKAG
NTLLDVLTIF SRSSEFSEFS IKYNEKKLYK AINSSPYIRF PLHSTEFQDS DKVMLLLQYE
LCGLDFPNSP ELMKLYYSFE GDKCYVFKQA SRIIRCMIDV FRYKKDCVSL LNTLRFSRCV
AGRCWENSVT ELKQLDGIDE ECIKKLRKNN ISGFAEAKYL SQSQLEYFLG IEPGTGKNIA
QSLQSLPKFK INATLASNKV RTDLETLEIS LIVSIGIDNM ERGNSKIKHN FINTIIGLST
GELLDFRRIA ILELVEGNIN SFRLTANVTD RQQKIHCHIL SEDMVNIDAR YVLSLDIIEE
WKFDNLMNQK SRYESEYNST TIKEIDNVLT QYSKSDSESD LDSEDLILDP VKSIRSTVEV
SKEKCNLRDK PYRLNAIRKL RLDGNYECNH LCKDKTKCRH FCCRDGIPKV KKQRNTNKHV
EIESNNCDSR LTASCSSFDI SQIARSQTSR PNGPSFQSQD YLSSPNHKRK KIRLGQRVGI
FNSNNGGLFD Y
//
