ID H0GPM8_SACCK Unreviewed; 1837 AA.
AC H0GPM8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Mot1p {ECO:0000313|EMBL:EHN04347.1};
GN ORFNames=VIN7_4956 {ECO:0000313|EMBL:EHN04347.1};
OS Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
OS (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHN04347.1, ECO:0000313|Proteomes:UP000009009};
RN [1] {ECO:0000313|EMBL:EHN04347.1, ECO:0000313|Proteomes:UP000009009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VIN7 {ECO:0000313|EMBL:EHN04347.1,
RC ECO:0000313|Proteomes:UP000009009};
RX PubMed=22136070; DOI=10.1111/j.1567-1364.2011.00773.x;
RA Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA Pretorius I.S., Egholm M., Chambers P.J.;
RT "The genome sequence of the wine yeast VIN7 reveals an allotriploid hybrid
RT genome with Saccharomyces cerevisiae and Saccharomyces kudriavzevii
RT origins.";
RL FEMS Yeast Res. 12:88-96(2012).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:EHN04347.1}.
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DR EMBL; AGVY01000049; EHN04347.1; -; Genomic_DNA.
DR HOGENOM; CLU_000315_1_0_1; -.
DR PhylomeDB; H0GPM8; -.
DR Proteomes; UP000009009; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR CDD; cd17999; DEXHc_Mot1; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
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; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR044972; Mot1.
DR InterPro; IPR044078; Mot1_ATP-bd.
DR InterPro; IPR022707; Mot1_central_dom.
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; PTHR36498; TATA-BINDING PROTEIN-ASSOCIATED FACTOR 172; 1.
DR PANTHER; PTHR36498:SF1; TATA-BINDING PROTEIN-ASSOCIATED FACTOR 172; 1.
DR Pfam; PF12054; DUF3535; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1254..1427
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1609..1757
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 139..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1772..1792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1837 AA; 206633 MW; A2AAFF6965FB038B CRC64;
MGDLAKQHPE DILSLLSRVY PFLLVKKWET RVTAARAVGG IIAHAPSWDP NESDLVGGTN
EGSPLDNAQV KLEHEMKIKL EEATQNNQLN LLQEDHHLSS LSDWKLNEIL KSGKVLLASS
MNDYNVLGKA DDNIRKQAKT DDIKQETSML NASDKANENK SNANKKSARM LAMARRKKKM
SAKNTPKHPV DITESSVSKT LLNGKNMTNS AASLATSPTS NQLNPKLEIT EQADESKLMI
ESTVRPLLEQ HEIVAGLVWQ FQGIYELLLD NLMSENWEIR HGAALGLREL VKKHAYGVSR
VKGNTREENN LRNSRSLEDL ASRLLTVFAL DRFGDYVYDT VVAPVRESVA QTLAALLIHL
DSTLSIKIFN CLEQLVLQDP LQTGLPNKIW EATHGGLLGI RYFVSIKTNF LFAHGLLENV
VRIVLYGLNQ SDDDVQSVAA SILTPITSEF VKLNNSTIEI LVTTIWSLLA RLDDDISSSV
GSIMDLLAKL CDHQEVLDIL KNKALEHPSE WSFKSLVPKL YPFLRHSISS VRRAVLNLLI
AFLSIKDDST KNWLNGKVFR LVFQNILLEQ NPELLQLSFD VYVALLEHYK VKHTEKTLDH
VFSKHLQPIL HLLNTPVGEK GKNYAMESQY ILKPSQHYQL HPEKKRSISE TTTDSDIPIP
KNNEHINIDA PMIAGDITLL GLDVILNTRI MGAKAFALTL SMFQDSTLQS FFTNVLVRCL
ELPFSTPRML AGIIVSQFCS SWLQKHPEGE KLPSFVSEIF SPVMNKQLLN RDEFPVFREL
VPSLKALRTQ CQSLLATFVD VGMLPQYKLP NVAIVVQGET EAGPHAFGVE TAEKVYGEYY
DKMFKSMNNS YKLLAKKPLE DSKHRVLMAI NSAKESAKLR TGSILANYAS SILLFDGLPL
KLNPIIRSLM DSVKEERNEK LQTMAGESVV HLIQQLLENN KVNVSGKIVK NLCGFLCVDT
SEVPDFSVNA EYKEKILTLI KESNSIAAQD DINLAKMSEE AQLKRKGGLI TLKILFEVLG
PSILQKLPQL RSILFDSLSD HENEEASKVD NEQGQKIVDS FGVLRALFPF MSDSLRSSEV
FTRFPVLLTF LRSNLSVFRY SAARTFADLA KISSVEVMAY TIREILPLMN SAGSLSDRQG
STELIYHLSL SMETDVLPYV IFLIVPLLGR MSDSNEDVRN LATTTFASII KLVPLEAGIA
DPKGLPEELV ASRERERDFI QQMMDPSKAK PFKLPIAIKA TLRKYQQDGV NWLAFLNKYH
LHGILCDDMG LGKTLQTICI IASDQYLRKE DYEKTRSVES RALPSLIICP PSLTGHWENE
FDQYAPFLKV VVYAGGPTVR LTLRPQLSDA DIIVTSYDVA RNDLAVLNKT EYNYCVLDEG
HIIKNSQSKL AKAVKEITAN HRLILTGTPI QNNVLELWSL FDFLMPGFLG TEKMFQERFA
KPIAASRNSK TSSKEQEAGV LALEALHKQV LPFMLRRLKE DVLSDLPPKI IQDYYCELGD
LQKQLYMDFT KKQKNVVEKD IENSEIADGK QHIFQALQYM RKLCNHPALV LSPNHPQLAQ
VQDYLKQTGL DLHDIINAPK LSALRTLLFE CGIGEEDIDK KASQDQNFPI QNVISQHRAL
IFCQLKDMLD MVENDLFKKY MPSVTYMRLD GSIDPRDRQK VVRKFNEDPS IDCLLLTTKV
GGLGLNLTGA DTVIFVEHDW NPMNDLQAMD RAHRIGQKKV VNVYRIITKG TLEEKIMGLQ
KFKMNIASTV VNQQNSGLAS MDTHQLLDLF DPDNVTSQDN EEKNNGDSQA AKGMEDIANE
TGLTGKAKEA LGELKELWDP SQYEEEYNLD TFIKTLR
//
