ID A0A194VRF9_9PEZI Unreviewed; 1679 AA.
AC A0A194VRF9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Chromodomain helicase hrp3 {ECO:0000313|EMBL:KUI66400.1};
GN ORFNames=VM1G_01871 {ECO:0000313|EMBL:KUI66400.1};
OS Valsa mali.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=105487 {ECO:0000313|EMBL:KUI66400.1};
RN [1] {ECO:0000313|EMBL:KUI66400.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-8 {ECO:0000313|EMBL:KUI66400.1};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CM003099; KUI66400.1; -; Genomic_DNA.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000078559; Chromosome 2.
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; cd18660; CD1_tandem; 1.
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; 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; PF13907; CHD1-like_C; 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; 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; 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:KUI66400.1};
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 269..340
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 369..429
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 467..638
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 786..950
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1338..1445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1578..1679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1373..1445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1578..1660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1679 AA; 192993 MW; A1E7EA52062D74AB CRC64;
MSASPESSPV NGHVSPVANP VAVQLLDPDP SDSDLSDVQA PDVASPSSDS ANNLNSTALD
GPADISDEAS SPSENDASDD GDFDDVADSP ASPRSNDGHN EAAASASDDS RTASKRKAGG
PSLEEEYIRE NPELYGLRRS SRPQQRKMIV DDDDDDSESD SVVVNRRAVK KRRVDRSLPS
SKRDTPLRQM SMNDSDSDTY GGARARALQK KARRQAESQP ALAFEKRWNN RRAAQVSAGA
YQESDAEQDD DSETTPAYWA GAEAEDNSPY IEKILRHDLQ EGVEWSPDVT RHDFNYLIKW
QGKSHMHNTW ETTESVAGFR GFRRLENYYR KSIEFELGMK FDDEDITPEQ KEQYILDRER
EKEAVEDYTK VERVVAVRDG DDGTEYLIKW KGLQYDECTW ESAYEISERA QDQIDQFLDR
SSRNWQSDRK ESNLDSRGRM TKLEHQPDYI QNGELREFQL KGLNFLALNW TRGNNVILAD
EMGLGKTVQT VSFLSWLRNA RDQEGPFLVV APLSVIPAWC DTFNNWAPDI NYVTYLGPEA
ARSTIREHEL LINNNPRKTK FNVLVTSYDY ILLDADFLKT IKWQVLAVDE AHRLKNRESQ
LYGKLVGFNV PCKVLITGTP IQNNLAELSA LLDFLNPGKV IIDEELELLG QSDKKDEVLD
EERDEEQRRQ TQEKLRHLHT AIAPFILRRT KETVESDLPP KTEKIIRVEL SDVQLDYYKN
ILTRNYAALK DASGQKQSLL NIMMELKKIS NHPYMFQGAE ERVLNGSTRR EDQIKGLIAS
SGKMMLLDQL LTKLKRDNHR VLIFSQMVKM LDILGDYLRI RGYPFQRLDG TIPAGPRRLA
INHFNAEGSD DFCFLLSTRA GGLGINLMTA DTVIIYDSDW NPQADLQAMA RAHRIGQKKP
VSVYRLVAKQ TIEEEVVKRA RNKLFLEYLT IQAGVTDEGK ALREQFQDRG LKVDEAKTAE
DIQMILKMRS QNLFEQSGNQ EKLEQLDIDA ILEQAEETKT AVDDKLNLSS GGIDWDNWMQ
VTDVKVDEMA LDWDQIIPSD QLAVIKADED KKKHDAYLAK AMEENAPRKV TLKNVKKGAE
ADRAERMAKK REREQQELEE LEEQRALLSD PRRPLNEKET RNLIRAFFRY GSMDDRGDEV
VHEARLSDRN RDFLHAIIDD LINISQTAVD ASNEKVREEE ERTGKTLAKK DKKAVLVDFG
EVRKVNAETV LERPPQLRLL RNILAEQDNP LNFRLPEAAK AAHYTCEWGA REDGMLLIGI
DKYGFGAWTQ IRDDTSLQMQ EKFFLEEHRV DKKEERKKTD DKSIQSPGAV HLVRRAEYLL
SVLMAKYSDD IAAKKAVENH HRSKKNLVLN GHRRSDVNSA SGSPAPQLVK KAAQNRDRNR
ERLHNDHHRS RSIADERGTP RPEHKRKHTD DHEDRHIKHR RMEHGHGDTR HGSHDKHAKD
NRTKLDSEAL DRLNRRREEA VQRFNRLMEL DDNKLDIRDN EQLIWSLLKP VRVNFKRIMY
TTQDHIASAK ERAKIMGSEL RQIGNHLTGL KDAGLPAEQL DGLMPQFWDF LSTVWPIGEI
EVTGDKLAKM YRTLAEKDKG KDKKDGGEKK QSKKRDDLED GEIDDEEEAR RRARREMRRE
SSEDVRRDYR RDDYRHRAYE NGDRLSFRRD RDRPLNDRSL ADRGRPSWSP DNQHRQSPY
//
