ID A0A0F4ZF45_9PEZI Unreviewed; 1623 AA.
AC A0A0F4ZF45;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KKA29122.1};
GN ORFNames=TD95_002335 {ECO:0000313|EMBL:KKA29122.1};
OS Thielaviopsis punctulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA29122.1, ECO:0000313|Proteomes:UP000033483};
RN [1] {ECO:0000313|EMBL:KKA29122.1, ECO:0000313|Proteomes:UP000033483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA29122.1};
RA Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL Submitted (MAR-2015) 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:KKA29122.1}.
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DR EMBL; LAEV01000969; KKA29122.1; -; Genomic_DNA.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000033483; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; cd18659; CD2_tandem; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 6.10.140.1440; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
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; IPR025260; CHD1-like_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
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; PTHR45623:SF14; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF13907; CHD1-like_C; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01176; DUF4208; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 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 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:UP000033483};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 238..290
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 327..388
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 426..597
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 729..890
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1281..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1449..1479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..96
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..220
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1316..1403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1623 AA; 187936 MW; 65863B3640B83628 CRC64;
MSDSESEIMD ATGLGSGSEL SDTRPGARAY HNGTSYADDI GYSHDDSDAT RNDSDDASDD
GDYDAEERSV RSAASPSAEE EDVEEGVEED AGEDEDDVRS ASGSRRNIKR KMTADEDEYI
KNNPELYGLR RSSNTYCLVS KRSTPATNSR RVSESDSDSD VYGGAKAKLQ RKKARRARSS
QTPIIEKRFS SRAAARVQQG AYEESDFNSE DDEEPGWREQ EAEVDDSPYV GEVIGHRLLP
NKTLTLYSTK ADFEYNIKWQ GSSHMHATWQ DWETLRETRG FRKVENYFRK IVEADKRVIL
EIDVTPEQRE QFLMDKERNE EALEDYKKVE RVVAVRTDEE AKTQYYIKWK GLTYQDCTWE
AASDISPKFQ DKIDQFLDRQ SRSWVSDRRE ANPETRTRHP KLESQPEYIK GGQLRPFQLR
GLQFLALNWS RANNVILADE MGLGKTVQSV SFLSWLRNSR GQEGPFMVVA PLSVVPAWCD
TFDLWAPELN YVTYLGPENA RTVIRNNEMM VNGNAKKPKF NVLVTSYDYI MADVQFFQQF
KWQVLAVDEA HRLKNRESQL YGKLLSLNVP CKVLITGTPI QNNLGELAAL MDFLNPGKVT
INSDIESLSP IEAQEQLEQL HKNIAPYILR RTKETVESDL PPKTEKIIRV ELSDLQLECY
KAVLTKNYSA LCNATGGQKN SLLNIMMELK KVSNHPYMIN GVEKKLLNGN ESRENTMKGL
VTSSGKMMLL DQLLTKLKRD GHRVLIFSQM VAMLDLLGEY LNFRGYKYQR LDGTINASAR
RLSINHFNAE DSDDFCFLLS TRAGGLGINL MTADTVIIFD SDWNPQADLQ AMARAHRIGQ
KKPVNIYRLV SKETVEEEVL ERARNKLLLE YLTIQAGLTD DDKSVRQELD RRGLKLDGPT
TSEDIQMVLR MRSQKMFEQS GNQERLEQLD IDKILETAEV TKTAVNDKMN LSNGGIDWDS
FMQYTDVKVD ELAMDWDDII PEDQLTQLKA EEEKRKHEEY LEKMREENAP RKATLKNRVA
VDNDDRADRL AKKRQRELQK ERDLEARRAM QSDPKRPLNE REQRNLIRAL QRFGSMEDRG
DEIVQDAKLA DRDRGVIMQF VNSFIAECKR VVEDHMSRLA DDEKRHGKVI AKKDKKAILF
DFGVLKKVNA ETPVERPPQL RTLREALQNS PDWRNFRVPE ATKSAHYSCP WGAREDGMLL
VGIDRYGFGA WTQIRDDVEL EMQNKFFLEE HRIEKKEERT KGGDKIKAPG AVHLTRRAEY
LLSVVYAKFS DDVAAQKIVE NHHRTNKKLP GTNGLRRSEN TGSPAPSVSR NGSGPRARET
DSRGRPLDSK RRSVYGEERI SKRRPEDARR RSHSTERDPD SPKRKRREDD EARPSKHRRI
DDERREVRRE DRYRDERRRA EDPRLEGRRG EYRDRDRERD RERERDYRDY RDRERDRDRD
RERDRDRERE RDRDRYDRDS RKADRRDERP SRSDSEDARA RALRRLTDLR RQGDHLSDYS
NPDNDTLLWL LLKPVRQNFE RILDTTKERV RSSKDRAKIY GDELLIIGDF LEKEIQGSAV
DKATRDGFWK FLADLWPVEQ VPLNGEKLHR MYSLLASRRQ KQSADAGIGE SSSNTVDNNS
VSV
//
