ID Q6CSV4_KLULA Unreviewed; 1525 AA.
AC Q6CSV4;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE SubName: Full=KLLA0C17578p {ECO:0000313|EMBL:CAH01836.1};
GN ORFNames=KLLA0_C17578g {ECO:0000313|EMBL:CAH01836.1};
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:CAH01836.1, ECO:0000313|Proteomes:UP000000598};
RN [1] {ECO:0000313|EMBL:CAH01836.1, 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}.
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DR EMBL; CR382123; CAH01836.1; -; Genomic_DNA.
DR RefSeq; XP_452985.1; XM_452985.1.
DR STRING; 284590.Q6CSV4; -.
DR PaxDb; 284590-Q6CSV4; -.
DR GeneID; 2892053; -.
DR KEGG; kla:KLLA0_C17578g; -.
DR eggNOG; KOG0384; Eukaryota.
DR HOGENOM; CLU_000315_29_2_1; -.
DR InParanoid; Q6CSV4; -.
DR OMA; WVQIRDD; -.
DR Proteomes; UP000000598; Chromosome C.
DR GO; GO:0000123; C:histone acetyltransferase complex; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd17993; DEXHc_CHD1_2; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 6.10.140.1440; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 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; IPR041150; Cdh1_DBD.
DR InterPro; IPR025260; CHD1-like_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623:SF14; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF18196; Cdh1_DBD_1; 1.
DR Pfam; PF13907; CHD1-like_C; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01176; DUF4208; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000000598};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 184..266
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 294..361
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 400..574
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 711..874
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 23..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 994..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1234..1291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1310..1419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1057..1106
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 61..76
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..105
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..164
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1015
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1317..1375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1405..1419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1525 AA; 174287 MW; 372C314E4E2E69B4 CRC64;
MVQDLPDEVL ANPELYGLRR SHRAAITHNT YAGLDSDSDE EVIRPRRGKQ KRKAVKQEHN
YDEEEEEEEE IDDFSDTDDF GSKRKPTRAP SAKRGRKRVS AGNSKSKRQA KRVEESDEEN
VVLPTRFSSR NNNKVINYTL NDDSNDEDLM ESSEEQDEGH NLDSEDMDLQ DGYSASPSPQ
QETHSIDIVV DHRLKEGVDN SGSTKNRRWD VDSIRANFEF LIKWADQSHL HNSWESYEDL
KENGTKGLKR IENYYKQFII LDQEVRADPY TTREDIEVMD LEHERRIDEF EEFKVPERII
DSERFENEDG SGSSQLKYLV KWRRLNYDEC TWEVASEIVK MAPEQVKEFQ NRTNSKIMPQ
NSSNYPANQR PKFEKLDAQP SFIKGGELRD FQLTGINWMA FLWSKNDNGI LADEMGLGKT
VQTVSFISWL IYARRQNGPH LVVVPLSTMP AWQETFDKWA PGLNCVYYMG NQASRDLIQD
YEFYTNPQAK GKKHLKFNVL LTTYEYILKD RSTLGSIKWQ FLAVDEAHRL KNAESSLYES
LNSFKVANRL LITGTPLQNN IKELAALVNF LMPGRFTIDQ EIDFENQDEQ QEEYIRDLHK
RLQPFILRRL KKDVEKSLPS KTERILRVEL SDVQTEYYKN ILTKNYSALT SGIKGGHVSL
LNVMNELKKA SNHPYLFDNA EERVLSKFGD GHKSRENILR GLIMSSGKMV LLDKLLTRLK
KDGHRVLIFS QMVRILDILG DYLSIKGINF QRLDGTVPSA QRRISIDHFN AEDSNDFVFL
LSTRAGGLGI NLMTADTVII FDSDWNPQAD LQAMARAHRI GQKNHVMVYR FVSKDTVEEE
VLERARKKMI LEYAIISLGV TDGNKISSTK KNEPSAGELS EILKFGAGNM FKPNDNQQKL
EDLNLDEVLN HAEDHITTPE LGESNLGGEE FLRQFEVTDY KADVDWDDII PEDELKKLKD
EEQRRIDEEY VREQLDIMNR KTAAIDKIKR SVNGETFGSD SEDEGNSKSR KRSKANNLDA
FGEREIRALY KCILRFGDIE NKFEELIADG SLPVKSIDRY KELYHEMITE AETLMRDEEA
KRHEIFSKLE KDAAEYRQKI KNLEIKPEDD AGKETPITLL SAKRREKRAI LFEFHDTKAL
NADTLVNRRD NLKFLSNFVE RNYKDDPLQF KFVNKNPKPV SAWNCVWGKE DDEKLLIGIY
KYGYGAWMQI RDDPFLGLTE KLFLNNEVTQ KAATPAAPSL TPSAPGASVA GSSTPGADAV
KTETPDTTAN TPIVTASSEN TNKKTVKKAP GAVHLGRRVD YLFTVLRDEA KGPQTDPSHP
AGSSSTGTTT PQQNKRKPKK SATTAGNSNG NENAHTAGTP SDGNSVNLTG KDSTPDNSSE
TKRGKAHHHQ QPSSRSGTPV VGSKKQQRKG KDIPLAPKAD IRLPDKEYDS MDEEECKKTM
TNVRSSLKRL RSGGDGLERK QWANLLKKEL KRVGDYIESH KKDSSKTSPE KYKRHLWSFT
AYYWPRDVPS SKLLAMYDKI KASEH
//
