ID A0A0A8L1E4_9SACH Unreviewed; 1959 AA.
AC A0A0A8L1E4;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 08-NOV-2023, entry version 35.
DE SubName: Full=WGS project CCBQ000000000 data, contig 00107 {ECO:0000313|EMBL:CDO91952.1};
GN ORFNames=KLDO_g282 {ECO:0000313|EMBL:CDO91952.1};
OS Kluyveromyces dobzhanskii CBS 2104.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=1427455 {ECO:0000313|EMBL:CDO91952.1, ECO:0000313|Proteomes:UP000031516};
RN [1] {ECO:0000313|EMBL:CDO91952.1, ECO:0000313|Proteomes:UP000031516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS2104 {ECO:0000313|Proteomes:UP000031516};
RA Nystedt B., Astrom S.;
RT "The genome of Kluyveromyces dobzhanskii.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDO91952.1}.
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DR EMBL; CCBQ010000004; CDO91952.1; -; Genomic_DNA.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000031516; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0010467; P:gene expression; IEA:UniProt.
DR CDD; cd18020; DEXHc_ASCC3_1; 1.
DR CDD; cd18022; DEXHc_ASCC3_2; 1.
DR CDD; cd18795; SF2_C_Ski2; 2.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
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; IPR003593; AAA+_ATPase.
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; 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:SF13; SEC63 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 2.
DR Pfam; PF02889; Sec63; 2.
DR PIRSF; PIRSF039073; BRR2; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 2.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
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; 2.
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}.
FT DOMAIN 292..480
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 511..726
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1144..1319
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1357..1545
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1959 AA; 222577 MW; 4E21480A72EF256C CRC64;
MSTTYSVHSV GSYMKAMDVM VSSVEQMSSR FTDSAVPEVD QELKTGYKND DKGKLLVTSQ
DRNDWDDIFD EFSNLSSERL LSLVTTNYSN SNGQPQIFKE LFRLLENVDS DFSQDQLLQQ
LVELLRSNEK TGTAEQDLFD YLGAENVELI SFLIENQDLL KQTPTADMSN SSMHDGNGFM
TEEDIKRQVM MNVENGKNIK LAPAQRKVRY PHVFRQSEDA GSSMLSFAGQ KFALPSGSSR
STFQTHEEIT IPCAEPKTRF NIPLIKVSDL DDYCRKVFEY EYLNKVQSLV YPVAYNTNGN
MLICAPTGAG KTDIALLTIL NTIKQYSVIN EDGDFDIEYD DFKIIYVAPL KALAAEITDK
FARKLSVFDV KVRELTGDMQ LTKKEILDTQ VIVTTPEKWD VVTRKASGDN DLTSKVKLLI
LDEVHLLHED RGSVIESLVA RTLRQVESSQ TMIRILGLSA TLPNFVDVAD FLGVNRNVGM
FYFDQSFRPK ALEQHLIGCR GKAGSKQCRE NTDKVAYEKA SEMMKRGNQV MIFVHSRKDT
VRTARTLINM ARENHEIDSF KGDEVAMSSF QKDLSKHKDK DLKELSQSGF GVHHAGMSRS
DRNITEKMFK SGAINLLVCT ATLAWGVNLP ADCVIIKGTQ IYDSKKGGYN DLGISDVIQI
FGRAGRPGFG ADYGTAYLCT SGDRLDHYVD LISQQHPIES RLGAKIVDNL NAEISLGTVT
NVEEGVKWLG YTYMFVRMKQ NPFTYGIDWE EILNDPQLYD KRRQIIITAA RRLHSLQMIV
FDEVSMHFIS KDLGRIASEF YLLNESVEIF NQIANPRATE ADVLAMISMS SEFDSIKFRE
EESGELKKLL ENAVECQISG DLDSSAGKTN ILLQAYVTQS RINDSALNSD ANYIAQNSAR
ICRALLLIGI NRRWGTFSMV MLDICKSIEK RMWAFDHPLC QFDLPDTILR NIKAKNPSME
LLLDMDSSEL ADLVHNQKMG GKLYRIISRF PRVDIDAEIF PITTNVMRIH ISLSPDFEWD
YRVHGDAQFF WVFVEESNQS SILHFEKFIL NKKQLSNPHE MDFMIPLSDP LPPQVVVKVV
SDTWIGCESM HAISFQHLIR PHNETLQTRL QKLNPLPTNA LKNPLLESIY NFKYFNPMQT
MVFHTLYHSN VSTFVGSPTG SGKTVVAELA IWHAFRDFPG SKVVYIAPMK ALVRERVDDW
RKRITPATGD RIVELTGDSV PDPQDIKDAT IVITTPEKFD GISRNWQTRK FVQNVSLIIM
DEIHLLASDR GPILEMIVSR MNYVSSQTKK PVRLLGMSTA VSNAFDMASW LGVKENGLYN
FPSSVRPVPL KMYIDGFPDN LNFCPLMKTM NKPAFMAIKQ HSPEKPVLIF VASRRQTRLT
ALDLIHLCGM EDNPRRFLHI DDEEELQYYI SKVSDDTLKL SLQFGIGLHH AGLIESDRAI
SHELFQRSKI QILVATSTLA WGVNLPAHLV IIKGTQFFDA KIEGYRDMDL TDILQMMGRA
GRPAYDTSGT AIVYTKESKK MFYKHFLNVG FPVESSLHKV LDDHIGAEIS SGTITTKQEA
LDFLNWTFLF RRAHHNPTYY GITEDTSTSG VNKYLSDLVN TTLDNLKEST CVEIFGTNIY
STPFLSISSY YYISHKTIRS LLKQITPHAS FQEVLRWLSL AVEYDELPVR NGEIIMNVEM
SAQSRYSIES SFAEELYLPM WDPHVKAFLL LQAYLSRAEL PIVDYHQDTI SVLDQSLRIL
QAYVDVAAEK GYFKTVMTLI KAMQCVKQGH WYEDDPISSL PGARLKRDDT LEFGEDGWPL
SGKGYKMSLD TLGRLDSTNN RNKLKSILNK QYHVKPEQQK QMLKEVSKLP ILDNIEFVPQ
TSNESLILKA THHNKTAKDF SIYCAKYPKT QRELWFAIAY RNDELLMLKR CQPRSGPNGM
GVLKFDFIVP ESIRGEELNF MLINDALDIK YDLKHTLIV
//