ID H0ES71_GLAL7 Unreviewed; 1268 AA.
AC H0ES71;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Putative Chromodomain helicase hrp3 {ECO:0000313|EMBL:EHK98608.1};
GN ORFNames=M7I_5549 {ECO:0000313|EMBL:EHK98608.1};
OS Glarea lozoyensis (strain ATCC 74030 / MF5533).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1104152 {ECO:0000313|EMBL:EHK98608.1, ECO:0000313|Proteomes:UP000005446};
RN [1] {ECO:0000313|EMBL:EHK98608.1, ECO:0000313|Proteomes:UP000005446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 74030 / MF5533 {ECO:0000313|Proteomes:UP000005446};
RX PubMed=22302591; DOI=10.1128/EC.05302-11;
RA Youssar L., Gruening B.A., Erxleben A., Guenther S., Huettel W.;
RT "Genome sequence of the fungus Glarea lozoyensis: the first genome sequence
RT of a species from the Helotiaceae family.";
RL Eukaryot. Cell 11:250-250(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:EHK98608.1}.
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DR EMBL; AGUE01000141; EHK98608.1; -; Genomic_DNA.
DR HOGENOM; CLU_000315_29_2_1; -.
DR InParanoid; H0ES71; -.
DR Proteomes; UP000005446; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
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; IPR041150; Cdh1_DBD.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
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; PF18196; Cdh1_DBD_1; 1.
DR Pfam; PF00385; Chromo; 2.
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; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00598; CHROMO_1; 1.
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, ECO:0000313|EMBL:EHK98608.1};
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:UP000005446};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 237..300
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 337..397
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 435..606
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 737..895
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 116..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1238..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1053
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1268 AA; 145978 MW; C51DC8219AC8AB66 CRC64;
MASWPIRTFV AFNRSDSHHQ PYHQDTTHTM AMRQRPLKTS QTFSGCYRDE IWVACFFAIQ
PSQHGEFSLS ERGAFHIYIA NITVSSPTID DNINRRESLA ISFQWGQWQL GREVQHRPII
ESDDDNDSDS DVVSARRPKR RKQERSRPVS KRNTPALPSG SASESDSDNY GGARAKKSKK
NRRQVNDSAG EAVVRWSSRR AAQVTAGAYQ ESDADMDDES EMMTPNQWAG DTEDNTPYVD
TVLEHRLKES ESMAKEDLGR DDFEYYVKWQ GKSHYHASWE TTTTLTGVRG FRRVENYYKK
IVLDDIYMSR GDDIQPEEKE KWMLDRERAS DALLDYTKVE RVIGTREGEE GTEYFVKWKG
LYYDSCTWES ASLISEISQE AIDSFLDRGS RTLSSDRHES NPNTRSAHVP IREQPSYIMN
GQLRAFQMTG LNFLAYNWTK NKNVILADEM GLGKTVQTVA FTNWLRNDRN QQGPFLIVVP
LTTIPAWADT FDNWAPDLNY VIYNGKEAAR ATIREYELLI DGNPKRPKFN VLLTSYEYIL
ADSSFLAQIK WQFMAVDEAH RLKNRESQLY VKLLDFKAPS RLLITGTPVQ NTLGELSALM
DFLMPGELQI EEDMDLSAEA AGEKIAALTK DIEPYILRRT KQKVENDLPP KTEKIIRVEL
SDVQLEYYKN ILTRNYKALN EGSKGQKQSL LNIMMELKKA SNHPYMFPNA EDKIIKGSTR
RDDQLKGLIA SSGKMMLLDR LLAKLKRDGH RVLIFSQMVK MLDILGDYLQ LRSYQFQRLD
GTIAAAPRRL AIDHFNAEGS NDFCFLLSTR AGGLGINLMT ADTVIIFDSD WNPQADLQAM
ARAHRIGQKK PVSIYRLVSK ETVEEEILER ARNKLMLEFV TIQRGVTDKE RKELREKAFK
KGVMVDDPKS SDDISRILKK RGQKMFSDQS GNQKKLEELD IDAVLEDAEE HNTEVPEGMV
ADGGEDFLKS FEYTDVKIDN LEWDDIIPKD QLEAIKKEEE ERAEQEFLQN AIDQSKPRKA
AMKNTAEWER EQRLQKKRER DQYQQEEADK ESAALLADPK RELNEKEARN LFRAFLRYGS
LEERQEELIT EARLVGRDVE VLRAAIKAIT DESVRLKAEY DLKIDEIQKT ENKSLTKKDK
KAVLFDYLGV KRLNADTIID RPVEMRILKN LISNYSDYKN FRVTNAPKTA NYSCQWGPRE
DGMLLVGIHR HGYGAWVEIR DDPDLGLSDK LFLEEHRVEK KDERSKGEEK AAKSPGAVHL
VRRSDYXI
//
