ID A0A135STX7_9PEZI Unreviewed; 1892 AA.
AC A0A135STX7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=SNF2 family domain-containing protein {ECO:0000313|EMBL:KXH39372.1};
GN ORFNames=CNYM01_06462 {ECO:0000313|EMBL:KXH39372.1};
OS Colletotrichum nymphaeae SA-01.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH39372.1, ECO:0000313|Proteomes:UP000070054};
RN [1] {ECO:0000313|EMBL:KXH39372.1, ECO:0000313|Proteomes:UP000070054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA-01 {ECO:0000313|EMBL:KXH39372.1,
RC ECO:0000313|Proteomes:UP000070054};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:KXH39372.1}.
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DR EMBL; JEMN01001354; KXH39372.1; -; Genomic_DNA.
DR Proteomes; UP000070054; 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; 3.
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 1312..1485
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1657..1808
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 72..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1892 AA; 209682 MW; 0B3D1702963BEF13 CRC64;
MASRLDRLVT ILETGSTRLI RDTAVNQLAD WQKQHPDELF NLLSRVVPYL RHKDWETRST
AAKAIGKITE NAPLYDPNED EDFAPVKKDE PEENGHVKKE EEKDATSFSS SELLKLGSLN
VEHIIKFGRQ LLRGGNIEYA LASLDPPARL AHQKKTLNGR LGLLGRVFED AEMPVLVEKE
PSPLTPQESA NGHNGTKEST TSHGQSQPAE EAGLSSRQLN VLKRKRKREL QKAAQGKGGF
GDLTMRRTTT AGSEGFDETP AADADAKQKN GKVNDYFNLD RPADVDEESK VVSEFKGQVI
PIKSEIEVDE TMEGAEWPYD RLCDFLKVDL FDPSWETRHG AAMGIREVIR VHGGGAGRVR
SKAQAENDRL NQAWLDDLAC RLCCVLMLDR FTDYSSDTSV APIRETIGQS LGSVLRHIPA
ESVHGIYKIL YQMVMQDDLQ LDMLQWSVCH GGMVGLRYVV AVRKDLLLED SEMIDGVVRL
VMKGLEEHDD DVRAVSAATL LPMTKEFVTL RPGSIDSLIN IMWGSLADLG DDLSASTGKI
MDLLATLCSY PEVLQAMETS AAQDEERSFT LLVPRLYPFL RHTITSVRLA VLKALMTFAN
LGAENSRGWL NGRILRLIFQ NVLVERDRET LAMSLDVWTA LVRSLLQTPE ILADEFAAHV
EPLMRLTLHP IGVSRHPLPM PAHLFQKPSG GTYAPVAVTP ARKASSPDGL ERANKRRRKS
AKTDDVPVTS HTHDVDGHMI QGDVDLVGMD TLIRSRVSAA KAMGLIMSFI PVASLAEYDQ
LLLAGISDRA SSTQLSACMI IDEYATNGPA EGATRYAAPL QKIIETERPA HYGDLVSFMH
RVRSQCQQLL NMFRDHGKVS SGRLPTLAVL VQGDEQAGPG AFSIAVADKV VGEDFDKLKK
AMSPGQRLVA SQMLSEAREV AVSAITDAKA AKDSRDVRIK AGAACALVAI KALPKKPSPL
IKGIMDSIKT EDNQVLQSRA SATIARLVQV FNEMGRRGPA DKVVSNLIKF SCVEVAETPE
FPVHATKTDC VLSMQKEEDR VDHADAAKWA KEVKAARITR RGAKEALEIL SKTYGAELLT
AVPTIRVFME DPLVKAFSGA LPAEAKDPEN TFGQEIVDAL SLIRTLMPTL DKAMHPFIME
KVPLVIKALH SELSVFRYMA AKCMATICSV ITVEGMTALV ENVLPSISNP IDLNFRQGAI
EAIYHLIAVM GDAILPYVIF LIVPVLGRMS DSDNEIRLIA TTSFATLVKL VPLEAGIPDP
PGLSEELLKG RDRERTFISQ LLDPKKVESF PIPVAIKAEL RSYQQDGVNW LHFLNKYHLH
GILCDDMGLG KTLQTICMVA SDHHQRAEEY AKTGAPDVRR LPSLVVCPPT LSGHWQQEIK
TYAPFLSVTA YVGPPAERKS MKDSLDKTDI VVTSYDVCRN DADVLAKYNW NYVILDEGHL
IKNPKAKITI SVKKLASNHR LILTGTPIQN NVLELWSLFD FLMPGFLGAE KVFLDRFAKP
IAASRFSKAS SKEQEAGALA IEALHKQVLP FLLRRLKEEV LDDLPPKILQ NYYCDLSDLQ
KKLFDDFTRK QGKKLQEEAG REDKDAKSHI FQALQYMRKL CNSPAMVMKP GHGMYEETQR
ILNKQGTSLE DPVHAPKLTA LRDLLVDCGI GVEEAESNDP LYQPIKPHRA LIFCQMKEML
DMVQNTVLKT MLPGVTHLRL DGGVEANKRQ DIVNKFNSDP SYDVLLLTTS VGGLGLNLTG
ADTVIFVEHD WNPQKDMQAM DRAHRIGQKK VVNVYRLVTR GTLEEKILSL QRFKIDVAST
VVNQQNAGLA TMDTDQILDL FNLGDTGPSL ISDKPQNSME GREEDMVDIE TGDVVTGKQP
GKKAWLDDLG DLWDNRQYEE SFDLDGFLKT MQ
//
