ID A0A2U9R8B1_PICKU Unreviewed; 836 AA.
AC A0A2U9R8B1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=ATP-dependent DNA helicase CHL1 {ECO:0000256|ARBA:ARBA00017386};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE AltName: Full=ATP-dependent DNA helicase chl1 {ECO:0000256|ARBA:ARBA00016387};
DE AltName: Full=Chromosome loss protein 1 {ECO:0000256|ARBA:ARBA00029709};
GN ORFNames=C5L36_0D03460 {ECO:0000313|EMBL:AWU77612.1};
OS Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=4909 {ECO:0000313|EMBL:AWU77612.1, ECO:0000313|Proteomes:UP000249293};
RN [1] {ECO:0000313|EMBL:AWU77612.1, ECO:0000313|Proteomes:UP000249293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS573 {ECO:0000313|EMBL:AWU77612.1,
RC ECO:0000313|Proteomes:UP000249293};
RA Douglass A.P., Offei B., Braun-Galleani S., Coughlan A.Y., Martos A.,
RA Ortiz-Merino R.A., Byrne K.P., Wolfe K.H.;
RT "Population genomics shows no distinction between pathogenic Candida krusei
RT and environmental Pichia kudriavzevii: One species, four names.";
RL Submitted (JUN-2018) 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX11/CHL1 sub-subfamily. {ECO:0000256|ARBA:ARBA00008435}.
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DR EMBL; CP028776; AWU77612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9R8B1; -.
DR STRING; 4909.A0A2U9R8B1; -.
DR VEuPathDB; FungiDB:C5L36_0D03460; -.
DR OrthoDB; 124793at2759; -.
DR Proteomes; UP000249293; Chromosome 4.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:DNA damage response; IEA:UniProt.
DR GO; GO:0090304; P:nucleic acid metabolic process; IEA:UniProt.
DR CDD; cd18788; SF2_C_XPD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
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 NCBIfam; TIGR00604; rad3; 1.
DR PANTHER; PTHR11472:SF41; ATP-DEPENDENT DNA HELICASE DDX11-RELATED; 1.
DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
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:UP000249293}.
FT DOMAIN 4..426
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
SQ SEQUENCE 836 AA; 96460 MW; 6A085807A60AE3C4 CRC64;
MAQINTFNHP FEHPYQVQLD LMQEIYDTLK NGYKVGIFES PTGTGKTLSL ICSTMTWLRE
YKKMHNEGLI KDKLKSAEED DDEEDEPEWV RQSFIDKIMS EYVGEAKKYE EHLARVHDQG
TSVIIDGNIG KKGNVKIYKK RKTEKLQNDE TIDDLAPDDF DILDDTTSKS GISRDVEFLL
ERFENKSKKY ENKIHSTQIN ESKVKIFFVS RTHSQLSQFS SQLKLTTFPS SIDQLPGERI
KYLPLGSRKQ LCINESVSKL VDSQAINKAC QNLQQSTDEN KKCQYMPNPF NEEHLHLKDK
MNDLVMSDIR DIEDIHELGE QLRICPYYST RADIPIAEII SMPYQLLLHK DTRHILGLDL
QNSVVVIDEA HNLLDTISRI YSTSVSLNDL KMVRKALKLY TRKFMLKMSA GNRINIAKLN
KIISKLYKFI EASNEKGIVT SGKTVDRDDI FGDDVSELLN IYELETYLIK SKLAFKLESY
MEKVVKVDGD ELYKSSGQPI LFGIKSFLYS LSNPLKSGKF FWDKSENDLS LKYLLLDPSE
DFKEIVEEAK CVILAGGTME PVSEFTDFLV PYLEKDKIHQ FSCDHVIPDE NLIVFPIGRY
RNTEFEFSFQ RRNNDFMITK LGESFCELLR EIPAGCVAFF PSYSYLSQVL ESWRKSGVYE
TLDTVKKIFT ESKDKSVDET LSEFKQTIEL DDNRKGAFLL SVVGGKLSEG INFSDDLARA
VFMIGLPYPN AFSSDLIAKR EYIEQKYLTN GKTESYAKRK SQEFYENLCM KAVNQSVGRA
IRNINDYATI YLFDSRYGNP RIVNKLSQWV KKRVLPMNTT NPVLETRAFF EKHAQR
//
