ID A0A1G4JMN2_9SACH Unreviewed; 1906 AA.
AC A0A1G4JMN2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=LAMI_0E07470g1_1 {ECO:0000313|EMBL:SCU91827.1};
GN ORFNames=LAMI_0E07470G {ECO:0000313|EMBL:SCU91827.1};
OS Lachancea mirantina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1230905 {ECO:0000313|EMBL:SCU91827.1, ECO:0000313|Proteomes:UP000191024};
RN [1] {ECO:0000313|EMBL:SCU91827.1, ECO:0000313|Proteomes:UP000191024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 11717 {ECO:0000313|EMBL:SCU91827.1};
RA Devillers H.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; LT598465; SCU91827.1; -; Genomic_DNA.
DR STRING; 1230905.A0A1G4JMN2; -.
DR OrthoDB; 180798at2759; -.
DR Proteomes; UP000191024; Chromosome e.
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 Reference proteome {ECO:0000313|Proteomes:UP000191024};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1325..1498
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1679..1827
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 74..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1846..1868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1906 AA; 212981 MW; 577C5AF6680DF5C4 CRC64;
MTSQISRLDR QVILLETGST QAVRNMAADQ LGDLAKLHPE DTLSLLSRVY PFLLAKKWET
RTTAARAVGG IVSHAPAWDP NSEDGESDTD DSAVSRGGEA DAKARDNPKV TSDDGVGDGA
IGVNGEHVTG TEDDGVGQNA KVKIEQEMQL KLEELDDSDE WKSLQDDSDL FSLFDWNLGE
VLKTGKTLLA SSIHTFPASE APDPPQKLAK TEESGKLEEN VANGSLEAGA GAIPPLESKK
SARMMAMAKR KRKIQARTTT KKPVDLSQSS ISRNLLAQED SSQSPTPSPS GLANAKLEIT
EQTDKKKIMV ESMVTPLLEK HEKISGLVWQ FQGIYELLLE NLMNDAWEIR HGAALGLREI
MKKHAKSVAR IKGKLKEQND RRNQRALEDL ATRLLTVFAL DRFGDFVYDT VVAPVRESAA
QTLAALLLHL NDELSVKIFG ALEQLVLQDP RIVGLPTKIW EATHGGLLGI RYFVSIKTDF
LFRKGLLNNV VNIVLYGLKE PDDDVQSVAA AILTPITSEF VKLEASTVDL VLTTIWSSLT
HLEDDLSSSV GSVMDLLAKL CQHQEVLDVL KAKAFSQPLE WSFKSLVPKL YPFLRHSITN
VRIAVLNLLQ AFLSIKDDFS KLWINGKVFR LIFQNILLEQ NPSVLQMSFD VYVGMLSEFK
VKNPDKDLDH LFGKHLAPIL HLLITPIGEQ GKSYNMELQY ILKPSPHYQL HSERKRNSSM
TVKSDIPPPA NSERVNIDAP MLAGDITLLG TEVIVNTRTM AAKALGITLS MFQETTLKSF
FSNVLLDCLK LPYATPRLLV AVIISEFCIN VEKNFQSTHA GCPAFLAETF GPLLSEGLSD
PSTFPPFREL VPSLKALRTQ CQSLLSTFVD VGMLPPQRLP QLAIIVQGES EAGPEAFGIK
TAEKVYGEIS DKLFKHLSNS YKILTKKPLE DAKYRVLQAI ETAKEVSRAR YCSILANYAC
AILQFSGLPT KLNSFIRALM DSIKEEKYSI LRQRSGDAIK TLVVNLVQKG KSNVANKIVK
NLCGFLCVDT SEVPEFGPNF DLRTSILTLR REQNALAMQE DARAKKLAED AHIKREGAMY
TLSELLIDKG EKVLELVPQI NQSIFEPLQR CDLNFDETEN VNTKGQEVVD ALGILRALFV
YMHPSLQERE VLPRLPALLK FLRSDFAVLR YSAARTFADL ATVLPLKIIP FIIREALPLM
NNPSSVTDRQ GLTELVYHLS QYMGSDILPY VVFLIVPLLG RMSDANQDVR TLATTTFASI
IKLVPLEAGI PDPEGMPSEL LEGRERERDF LQQMMDPSKA KPFKCPVAIK TSLRKYQQDG
VNWLAFLNKY HLHGILCDDM GLGKTLQTIC IIASDQYLRH QNYEASSAVE SRPLPSLIVC
PPSLTGHWEQ EFEQYAPFLK VLIYAGGPSM RFPLRHKLDT ADIVVTSYDV ARNDIDVITK
YDFNYCVLDE GHIIKNAQSK LSKAVKLVQA NHRLILTGTP IQNNVVELWS LFDFLMPGFL
GTEKMFHERF AKPVAASRNS KTSSKEQEAG ALALDALHKQ VLPFMLRRLK EDVLSDLPPK
IIQDYYCELS DLQKQLYKDF AKKQKHNVER DIEHASDVEN KQHIFQALQY MRKLCNHPSL
VLSPSHPQWF QVQEYLKQTG LSMHDLSHAP KLGALQNLLL ECGIGTEDLE KKSKGDLPSM
DNVISQHRAL IFCQLKDMLD MVENDLFKKY MPSVTYMRLD GSVESRDRQA LVRKFNEDPS
IDCLLLTTKV GGLGLNLTGA DTVIFVEHDW NPMNDLQAMD RAHRIGQKKV VNVYRIITKG
TLEEKIMGLQ KFKMNIASTV INQQNSGLAS MDTHQLLDLF DADNVPSQEA EEGTPNAAKN
GKMDDIANES GLTGKAKEAV GELKELWDSS QYEEEYNLDN FIKTLH
//
