ID Q6CSU4_KLULA Unreviewed; 2149 AA.
AC Q6CSU4;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 133.
DE SubName: Full=KLLA0C17798p {ECO:0000313|EMBL:CAH01846.1};
GN ORFNames=KLLA0_C17798g {ECO:0000313|EMBL:CAH01846.1};
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:CAH01846.1, ECO:0000313|Proteomes:UP000000598};
RN [1] {ECO:0000313|EMBL:CAH01846.1, 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).
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DR EMBL; CR382123; CAH01846.1; -; Genomic_DNA.
DR RefSeq; XP_452995.1; XM_452995.1.
DR STRING; 284590.Q6CSU4; -.
DR PaxDb; 284590-Q6CSU4; -.
DR GeneID; 2892165; -.
DR KEGG; kla:KLLA0_C17798g; -.
DR eggNOG; KOG0951; Eukaryota.
DR HOGENOM; CLU_000335_1_0_1; -.
DR InParanoid; Q6CSU4; -.
DR OMA; QTEIQYY; -.
DR Proteomes; UP000000598; Chromosome C.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProt.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR InterPro; IPR041094; Brr2_helicase_PWI.
DR InterPro; IPR048863; BRR2_plug.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR PANTHER; PTHR47961:SF4; U5 SMALL NUCLEAR RIBONUCLEOPROTEIN HELICASE; 1.
DR Pfam; PF21188; BRR2_plug; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF18149; Helicase_PWI; 1.
DR Pfam; PF02889; Sec63; 2.
DR PIRSF; PIRSF039073; BRR2; 1.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000598}.
FT DOMAIN 501..684
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 718..932
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1349..1511
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 39..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2149 AA; 243889 MW; 2B08B637718A3988 CRC64;
MTEDAKERKQ KIKEIYRYDE MSNQVLRADR SLIENRTDVH RDAEISQPKS MSGRIRLTEM
GSAVKENGLE DNERATAEKE FEKRMKSSSP QQTNSSRLDR TTVLDDITSL NYIPTDDRNT
EIYDEITTWC SEILGDDIPH SIIVDATDLI IVTLKQDESV DLESKKKTIE VALDTELDNA
SFNSLVKLVK SISDYYAESA DTGRTVNVAI NPNEDDDEAE EEEEPNALLE AVDDVAGEEA
DEEAGYNEKT DNSNDNFSVR SDIMNNSESL QIQSAAVMEE IIDIKDIDGF YLQRKIRKQL
KNIEETKVQE MANNVYDLLA NDISEEELTQ NLHDIFGPDA KQLIRLIVSN RETLYWGHNL
QRSANENIDE ILGEMAQRNL SHLVEAYKAK PDSAKRKLNS EPEVGTKKQK IEAEDEPKVI
ALDDLKLSQN TKFLSDVKIS LPENSFKRVK DSYEEIHVPP PKKVDDNFPL VQIESLPKWA
RSAFPTSETT SLNRIQSEVY PTAFNTDANV LLCAPTGAGK TNVAMLTVLR AMSHYYREER
NAFDLKKFKV VYIAPLKALV QEQVREFQRR LHHFGVKVAE LTGDSNLSKQ QIEETQLLVA
TPEKWDVITR KSTDTSFHKL VRLIIIDEVH LLHDERGPVI ESIVARVLRD TTAEIPTRLV
ALSATLPNYI DVAKFLHVPD NGLFYFDSTF RPCPLAQQYC GITEKNALKK KNAMNQACYD
KLLEAAKEGH QVIIFVHSRK DTARTARWLI QKLINEDKIS AFQGTDKGSL EILKTESSNA
TDRSLSDLIP YGFGIHHAGL TKDDRSLSED LFADGLLKVL VSTATLAWGV NLPAHTVIIK
GTEMYSPEKS DWVMLPPQDI LQMLGRAGRP RYDVNGEGII ITNQSDVRYY LAVLNQQLPI
ESQMISKVVD NLNAEIVLGN VTSLDEAVNW LGYSYLSVRM KQSPHLYNLQ GSSGDMSDAE
LIRVNRNIVH TALNLLQNNG LVNYDSLSKS VQPTELGRIS SHFYISYSSI AKYNRELTIN
STLIDILRIF AMSEEFKNIT VRQEEKTELE KLVERCPIPI KEKATDSLAK ANILLQVYIS
KLRLEGFALN ADMIYISQSA GRLFRALFEM CLRKGWPRLT KLLLTICKCV DSRMWPTNSP
FRQFKRCPQE IIRRAEASGL PWNDFLLLKN AHEVGEALRS PKNGKVAFDL LQRFPKIGIH
CAMQPVTNSL LRFELELQPT WIWDLDSSSY SETFLVLVED TDGEQTIYHE TLHVGRNAIN
SIVYLDFVVF LKQKMLPPNY FVSVISEKWL NCEYKIPVIL SEIKLPKPFP PAISVSDSIK
KSTKELQIDE FEALYNFHSF NKVQTEVFDT LYHETENALI CATKGSGKTI MAELSLLNHW
REGRGRAIYI CPFKTKITEL LKNWKKRFSH LAGGKLINAF SGNLQHDQKQ LAQSHLILAT
PNEFEYLSRR WPERKNIQRI ELIICDDIHE IGNEIIGPMY EIIITRMIFI ATQLEKNIRI
VGLGTPLANA KDFGEWLGAK KSSIFNFTAL ERQTPLTVDI ETSILVKSPT SNRMALTEIV
ESSNRVASPD ETITVFVTDR YECVSFATEL VGLAVAKGID LLRAEESSLH SYLNKVQDSN
LKTLLQSGIG ILYQGMHYSD RNVVRKLHEY KVISILVASR DCCFDAPSSS FVFVTTTQYF
EGRENRYIDY PVNTILEMMG TAFTASNKQQ AHAKLITTMQ RKEYYKKFLC DGLPTESSLP
YHVIDLLTTE FANQTLETKQ DCIDLLTYTY LYRRIHANPS FYGIQDVTAD EISSYLTELV
EEAVTTMKET ELISVEGEAN DSTEIAEEVI SPNNACLISA IHAVSCLTIC NFSRAASRSL
RMSGILEILS SSEEFKTLPL RLHDIKPLRK LYDISPLKLS SEFDPRSTTA KVFVLLQAHF
SGLHLPMDLS LDLSEILSKA PSLAGTMVDI LSMNGYLNAT TAMDLSQMIV QGVWDTDSPL
KQIPFFDTDI LEKCKNHNVE TVYDVMALED EEREDIITLP ENKLNKVAEF VNSYPNIELK
YALDMSAPMK PHDKKMVTVT VSRDEEPETL NVSSKSLPHE KTEAWWIFIG EKSSRQLYAI
RKIALTKMTQ DYELEIELED PGDHELTIWC VCDSYLDADK EVTFNVNIA
//
