ID Q6CL05_KLULA Unreviewed; 1096 AA.
AC Q6CL05;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 24-JAN-2024, entry version 122.
DE SubName: Full=KLLA0F06710p {ECO:0000313|EMBL:CAG98092.1};
GN ORFNames=KLLA0_F06710g {ECO:0000313|EMBL:CAG98092.1};
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590 {ECO:0000313|EMBL:CAG98092.1, ECO:0000313|Proteomes:UP000000598};
RN [1] {ECO:0000313|EMBL:CAG98092.1, ECO:0000313|Proteomes:UP000000598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
RC WM37 {ECO:0000313|Proteomes:UP000000598};
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; CR382126; CAG98092.1; -; Genomic_DNA.
DR RefSeq; XP_455384.1; XM_455384.1.
DR AlphaFoldDB; Q6CL05; -.
DR STRING; 284590.Q6CL05; -.
DR PaxDb; 284590-Q6CL05; -.
DR GeneID; 2894771; -.
DR KEGG; kla:KLLA0_F06710g; -.
DR eggNOG; KOG0385; Eukaryota.
DR HOGENOM; CLU_000315_0_2_1; -.
DR InParanoid; Q6CL05; -.
DR OMA; EFQFRES; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProt.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 1.20.5.1190; iswi atpase; 1.
DR Gene3D; 1.10.1040.30; ISWI, HAND domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; ISW-1; 1.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51293; SANT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000000598}.
FT DOMAIN 153..318
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 451..602
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 834..887
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 87..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 892..919
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1020..1048
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1077
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1096 AA; 127742 MW; 42F0D14498FD3619 CRC64;
MDSPEYLEKL KPFQEGIPNS IAEKKERYLL PLRDLASGKR KFDEQGTVKR FEHLLGLSTL
FRHFIERKAA KDPRFREVLD TIDNVNGKAN GKGKKHTDAR RRKTEKEEDA ELMKDEEEEE
EELADVDFQF RESPAYVNGQ LRPYQIQGLN WLVALHKNQL AGILADEMGL GKTLQTIAFL
GYLRYIEKKN GPFLVIAPKS TLNNWLREIN RWTPEVSAFI LQGDKEERSK LCHDKLLACD
FDICVASYEI IIREKASFKK IDWEYVVIDE AHRIKNEESM LSQVLREFSS RNRLLITGTP
LQNNLHELWA LLNFLLPDIF ADSATFDEWF SSESSEEDKE KVVKQLHTVL SPFLLRRIKN
DVEGSLLPKK ELNVYVGMSS MQKKWYKQIL EKDIDAVNGS NGQKESKTRL LNIVMQLRKC
CNHPYLFDGA EPGPPYTTDE HLVYNSAKLK VLDKLLKKFK EQGSRVLIFS QMSRVLDILE
DYCYFREYEY CRIDGSTAHE DRINAIDDYN APDSKKFIFL LTTRAGGLGI NLTTADIVVL
YDSDWNPQAD LQAMDRAHRI GQKKQVRVFR FVTDNSVEEK ILERATQKLK LDQLVIQQGR
VTNKKKENKN DSKEGLLSMI QHGAVDVFKS NDSSAMTSQT GTPHPDDGKD KDEDVDLDAL
LAQSEDKTRS LNAKYATLGL DELQRFNQDS AYEWDGQNFK KKVEKDIINP LFIPPTKRER
STNANYSVDN YYKDVLNPGR NNQYTVPPKM PKLQPLNSHQ LLRPQLKAIY EKERMWIAKK
NNYVPNLDDV VTTYGDVKDE AEKKDKLELL KLSIANAEPL TEEETNNKIE WEKEGFHNWN
KLDFRKFITA SGKHGRNSIQ AIAAEFGGSK TEEEVRAYAK AFWANLERVE DYERYVKNIE
TEEERVRRVK MNQEALRRKI SQCANPLFEL KLKFPPSTNN KRTFSEEEDR FILLMLFKYG
LDRENVYEMI RDEIKHHPLF ELDFFFQSRT PIELQRRTIT LLQCLEKEFN TGIQKTDELN
DRLKKEDEEG ERLREKLKEE NKARRQEEEE QEEEEEEKEE EVNGTATQRK DEATEVDTEV
NGNSLNEPEQ KKVKTE
//