ID Q6CK20_KLULA Unreviewed; 1064 AA.
AC Q6CK20;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=KLLA0_F14234g {ECO:0000313|EMBL:CAG98427.1};
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:CAG98427.1, ECO:0000313|Proteomes:UP000000598};
RN [1] {ECO:0000313|EMBL:CAG98427.1, 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 -!- 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=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034617};
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
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DR EMBL; CR382126; CAG98427.1; -; Genomic_DNA.
DR RefSeq; XP_455719.1; XM_455719.1.
DR AlphaFoldDB; Q6CK20; -.
DR STRING; 284590.Q6CK20; -.
DR PaxDb; 284590-Q6CK20; -.
DR GeneID; 2894923; -.
DR KEGG; kla:KLLA0_F14234g; -.
DR eggNOG; KOG2108; Eukaryota.
DR HOGENOM; CLU_004585_4_0_1; -.
DR InParanoid; Q6CK20; -.
DR OMA; FFVAQTR; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000000598}.
FT DOMAIN 12..313
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 314..636
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 658..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1007
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1064 AA; 121847 MW; FA04473CFF0D08CC CRC64;
MSLAASDVYL SNLNDAQRKA VIYDYTKALQ IIAGPGTGKT KVLTARFAYL VLSQKINAEE
IIMTTFTRKA AEEMKERLVP VLVSNGISPH GLKIGTFHSI CWKLLKEKGF LIGKEKIERA
TTEKIKSILE ELIVEMPDQI RDYACTKSYK NEVSLCRLKN NQWQVHPDMI LKRISELKAD
AITPEKYEQQ AIFDEALLHF YQQYQAKLSK EHLIDFDDVM LYSFELLSKH RVWKNIKHVL
VDEFQDTNLL QIHLIFQFAR GSHHSCEGVT VVGDPDQGIY GFRSALSHNF QTMIELCPIE
YDQIVLKENY RSAQAILDIS ETVIKQQKSG RDNREPLRAQ FVTDNKPVYM SFPSDDTEAY
TITKEILYLK AIPGLFKYKD FAILVRLKRS LRTFENALIA HKIPYVIQKG YTFWELKECK
AIIRYMSMIC NDDDWESLKR TINYPNRGVG ETTVGKIAAA FEKESTAEKN ETAFSFLQKI
ARDSVKINIS NSSMIGIKDY VNIIEQVRKF FSEIYSDAGK STIADAFEKF YVLTGLRGQY
KPEKKSGSIA SDDQSTEKEA HRHLNVLNVK NYFSTFKIPL GDGDGEPRIV DLIGFCHEFV
SFTDLYTFNE DNDNDVKDDH ETKDAVVLST IHASKGLEWP VVFVPQCVEG LLPSYYKDSS
DMPAPDEDSD ENMAVGDAYN EPTDSQDDNR DGKNPSSPTK KKSRTSFSEE RRMFFVALTR
AKYLLYITTV EKEATSFKSR FLKNEVIELC DDTLKCFESI EHLFKLYYTL KVQIPNQDRI
SYDQLIKDYY NYGFNSRQLL FWKDNKYSHV DLPNMTENTI GIVTKKNEIE SELCSALPRV
NKTNTTRKTV HVRPGELIIK QERGTPPLFN SPSKLSPTPN MSPTKMPPLT REETRELDVL
LSDNEFLPEA PSQAPPIKSE SDYTAAEILH NKDESIIDNR PILTSARILA SAIKQELSQS
IPNIDAPSTE TPSIKEENDT AFKGNVPKKP STKSNKKRER RQRKEQHHPR PQSSSGSVKK
TNKILSRKVK LEPKSTNDIL LKLEKAKQRK EEWDGEIIDL RSSQ
//
