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Database: UniProt
Entry: Q6CUF0_KLULA
LinkDB: Q6CUF0_KLULA
Original site: Q6CUF0_KLULA 
ID   Q6CUF0_KLULA            Unreviewed;      1605 AA.
AC   Q6CUF0;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   SubName: Full=KLLA0C05368p {ECO:0000313|EMBL:CAH01290.1};
GN   ORFNames=KLLA0_C05368g {ECO:0000313|EMBL:CAH01290.1};
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:CAH01290.1, ECO:0000313|Proteomes:UP000000598};
RN   [1] {ECO:0000313|EMBL:CAH01290.1, 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.
CC       {ECO:0000256|ARBA:ARBA00007025}.
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DR   EMBL; CR382123; CAH01290.1; -; Genomic_DNA.
DR   RefSeq; XP_452439.1; XM_452439.1.
DR   STRING; 284590.Q6CUF0; -.
DR   PaxDb; 284590-Q6CUF0; -.
DR   GeneID; 2892355; -.
DR   KEGG; kla:KLLA0_C05368g; -.
DR   eggNOG; KOG1001; Eukaryota.
DR   HOGENOM; CLU_244107_0_0_1; -.
DR   InParanoid; Q6CUF0; -.
DR   Proteomes; UP000000598; Chromosome C.
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; cd18008; DEXDc_SHPRH-like; 1.
DR   CDD; cd18793; SF2_C_SNF; 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   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45626:SF24; ATP-DEPENDENT HELICASE ULS1; 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50089; ZF_RING_2; 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   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000598};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   DOMAIN          932..1137
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1313..1371
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          1432..1588
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   COILED          143..198
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1605 AA;  184434 MW;  B306BEE02258AB65 CRC64;
     MTENGAEIPV VNLTLDAEEE EENEVVSELK RQETPKLFVK REIDEIEAEH LQPLVKHFKP
     MEQDSQVIVV SSEEEADVKP AEGAHVALQH LQERLLVLTK KLRAKKSMTD VLTNKLARRK
     DAEDTLQVKY RSLLNLYGED PNMPSQRKLL TDLRQQIRAA EERTVATRTK LHSVKRDHHD
     LENEIKQLYE RIRAISSHNG KEMSLQLQSV SKDIIKDVRK HNLFVETINK VKELLRNTSR
     SEDNKIYINT LCDRLLAFES EIFYEQPSSV FLKATIYQIL TELTSQGIKM PYIFQRFQEL
     KLYDEDLPKS EESLSTDSKF KSHIDQVFSL ADKIHRPDKE KHQIKHYASI VLDGYRNRSQ
     YPLQHPGKYN KITHALLRLV QLGVRIPFVL EEMKKLHYNI NSAIDSTKVF QEIHAVKSSI
     LEKSLSSDRA SKLFKDLDLL IGFLEFTLEG EEVYDPEIVK NIFKLMVHIE RLNINIPYTK
     EAMHKLGLNW DDFIDTEYFL QSITKMKRRL HELKSSRSPA DMSRILQSLD CLVFFIEKYH
     EDKQYKVPTM HSKEREEVCH SAHILHSSGI LLLYCYESLT KLGFDWQYYP EESLKVIELA
     KDMLQKDSSK TIHEKANILT LIQTLEKGII RAMDMSTFSE MKIESFRLTL STLQRTGCKM
     PSVELTYQSI MKGTYLNCLL NAERQAALVD NARDSQSSTS HSLSSGLKYE KDDKALIGNP
     PYESKKSTSK LEGHSQLLSL RKLQDEIEEA ILTLSTNHSL DKMAQDTIVS ALSNILSLLK
     ISEEFNSTTV PSMWRSTVQM SIDVLDRFLY IGTIPGVLDR LFQLGFSIPE QYANDDDLAV
     IGGKTIKNEE FVTYDSDEDD DIDEVIENYK TRIDHSLRMT NIYNTADASS LRDLLEGLKE
     IETEVEGEDL TPNELTVNLL KHQRQGLRWL VSMEKSSKRG GLLADDMGLG KTVQSLALLM
     ANKPEPKSAI KTTLVVAPVA VLRVWKDEVA VKIKKDVNVK VVIFGGGENN SSKFRSWKDL
     AEYDIVLVSY QTLASEFKKH WPLSWKNGEH QPDVHAVDLK LMNQVKSSDE YFSPFYRNDS
     EFYRVILDEA QNIKNKKTQA AKACCTISST FRWALSGTPI QNNIGELYSL IRFLRIPPYN
     KEAKFHSDIG AVLNTKKPYD YNDSERQRAM KKVQVLLRAI MLRRTKTSQI DGKPILQLPE
     KHLKESANKL EGDELEFYQA LESKSRDKAK KMLESKQKQG AYSSILTLLL RLRQACLHSE
     LVKIGESNAK SSKIINGKDF EKDWRPLYFV SKRMGQNQAT LNAVNACLDD MTCPVCMEQM
     DIDSMLVLNS CGHCLCAQCF EPYVDNAKLE PTASFGPKGT NSVNIPCLVC RKMNNDKEAI
     SYQLFDQVNN LNYSIDDLRL EYDKMVAEQK ARLKNGYTID YKSLKESKKV EMCLDIIKKV
     TDSNTDEKLV IFSQFTMFFE ILGHFIKKNL GLNFLRYDGS MSSSQRSACI ESFYQDNNYR
     VMLISMKAGN SGLTLTCANH VILADPFWNP FVEEQAMDRC HRISQEREVY VHRLLIKMSV
     EDRIVELQNK KKTLVNLAMD PTQIREVNKL GRKELGFLFG LNSLD
//
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