ID A0A2X0MTU4_9BASI Unreviewed; 1667 AA.
AC A0A2X0MTU4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=BQ5605_C041g11978 protein {ECO:0000313|EMBL:SGZ33596.1};
GN Name=BQ5605_C041g11978 {ECO:0000313|EMBL:SGZ33596.1};
GN ORFNames=BQ5605_C041G11978 {ECO:0000313|EMBL:SGZ33596.1};
OS Microbotryum silenes-dioicae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=796604 {ECO:0000313|EMBL:SGZ33596.1, ECO:0000313|Proteomes:UP000249464};
RN [1] {ECO:0000313|EMBL:SGZ33596.1, ECO:0000313|Proteomes:UP000249464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FQNC01000119; SGZ33596.1; -; Genomic_DNA.
DR STRING; 796604.A0A2X0MTU4; -.
DR Proteomes; UP000249464; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
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; PTHR45626:SF51; SINGLE-STRANDED DNA-DEPENDENT ATPASE (EUROFUNG); 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 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; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000249464}.
FT DOMAIN 783..1153
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1505..1649
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1318..1374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..973
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1045
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1325..1343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1667 AA; 179929 MW; FC8FA79100E81BA1 CRC64;
MEFANGFEEI EVRTRPTPQS PSKVHHNEEV GTPSDLGGAT AGASMIYQSS ATQPTALTTG
VVDLTESPPS TTLLDDSWAW SDMAVSAPAA APSSAAPFRA RDAMTTATST LVSGVSSRSS
GPLAGGRFGG DTRYNKPTPL PLNVASKPLQ QPGSSSNSNP NPGAIPNPSA SHSAMDSESD
SARTAAVTFG ASSTAFATAP TSPFVSTPST SSAANPALGF GSFANPHPTR SLTLPSSFSP
TVSSASQASP MLASFAQVRS QSPAADNSGA FNSAALASTS TKPIVFASQL LPGHATSAFR
SPALAKAAST HPTPVAGPSA SRSLPGSTPK RQGSTEKNGL SSNSIQSSPD PLQAYYRMQA
ASVAAARKSA SDNMPTPTGR SGTFPGSSRP FVPLTAPHPS SSLNPNAGAG IDHPQQSRNG
RAVANSAVAS TSSSGSNTMI DLTEDDIPSD PDEMIIDDHP ICIGQITSLA LILYPIPELQ
PPAAAVDDKG RPVPAAQQLP FAQQPPPPLA VYIYRGDAQQ GHETLRLVSS RRKETFGVVE
HRVADVIGPL LGNGWSGAGI TPELGGKIWC EAHVMRKVER SPTLLPLVLL LFARPLDVPA
ISSTLERNTI YLEHPSAYNP ALHSGARYSN PHNPAAGRAS ERRRHDFQAG IYGLSGLGAT
RVVSQKDEAR SQVDEVFKSL KSVMELDEVE PRKFGCTGDP SLPTVADMCD PDLRTAPMVT
TKLYPHQKQA LSFLLDRERI HEVPEKDERG NPTILSLWSR ESNPYGQPIG WKSVVADLRI
SGPEPPPQTR GAILADDMGL GKTIAIIALV ATTLDDARKW YTAPIDRENR DDRVDSLVTK
AAAPPKLGIG DFSGRAYGFV EYGNPTASAS TGRPLSKKKQ AAAKREQKRE DAIAARHNRL
VTRSRATLIV CPLSTVQNWE SQFEEHTGYA DGRVYTVTSG LPKLESDEED EDSGGATDGS
EEYKPRPKSE RNGKKAATAQ AAAAAAEERA IKVYVYHGNH RIQDPIRLAD YDVVVTTFST
LGTEYSRQSR AEDEREAEAS REGSSDDMLE VFVLGPNGEH VETRAGDPIV KAGKPTKPKR
KRRKLEGDGA SPLQQIEWYR VVLDEAHIIK EHTTIQARAA CELATPRRIA LSGTPLQNSL
NDLFSLVRFL RLEPFTDRSV WNQHIGSLAK IGDPLGVDRL QLIMRHLALR RTKESTDKDG
KPILSLPPNK SDLVELQFSP EEHAFYQVHH QRYKHDFAKL EETDSVMKNY CSILQELLRL
RQICVHPALV RDSEDAKIGG TGVVESIKQY GISRQRAIPL LLLMRDAGGG QCSECGTEML
PVAGSNDERA DEVEDESRME KKTPAKKSRK TAKASTASAA ASDAEDNGGG PASPNELRSV
VTRCQHLFCR LCFIHHIYND WASPKAGDTA PCSVCKEMLK PVLDAVEIGA TEFLRATEKA
DKGDVKPTKG GKKSAADRVF EHSTKTFALV NDLRPFSQAN PASVNFRGDL YTSDEPREGE
TRTIGFQPHK GEVVKSVVFS QWTSYLDRLG DALSSERIKY GRLDGSMDRD ARSRAMMAFK
TDPACEVLLV SLRAGGVGLN LTAGRRVYLM EPFWNPAVEN QAVDRIHRLG QTMPVQTVRF
VIKTTIEENM RKIQKRKLDL ANMSVKKTLS KAELLQQRKE ELAILMS
//
