ID A0A423XFC7_9PEZI Unreviewed; 1137 AA.
AC A0A423XFC7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ROW14668.1};
GN ORFNames=VPNG_03255 {ECO:0000313|EMBL:ROW14668.1};
OS Cytospora leucostoma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Cytospora.
OX NCBI_TaxID=1230097 {ECO:0000313|EMBL:ROW14668.1, ECO:0000313|Proteomes:UP000285146};
RN [1] {ECO:0000313|EMBL:ROW14668.1, ECO:0000313|Proteomes:UP000285146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYLt {ECO:0000313|EMBL:ROW14668.1,
RC ECO:0000313|Proteomes:UP000285146};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-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:ROW14668.1}.
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DR EMBL; LKEB01000013; ROW14668.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423XFC7; -.
DR STRING; 1230097.A0A423XFC7; -.
DR InParanoid; A0A423XFC7; -.
DR Proteomes; UP000285146; 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 GO; GO:0046872; F:metal ion binding; 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; 1.
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 InterPro; IPR017907; Znf_RING_CS.
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.
DR PROSITE; PS00518; ZF_RING_1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000285146};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 486..697
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 953..1114
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..940
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1137 AA; 126498 MW; C00920AA3F5F9BFD CRC64;
MASRNLNNGT SPLPSPHSRP PPQQQALNPF LDHVLEPSQD HSSAQLTHIE SEGDTTSRQV
AAWPAAALLN PKAAMTSQKP SPVSSPKHSR TPSNVPKNTN NIAAQVAFSF STPNDTPAFG
AYTPRPSVTP DPTGTPRSST PNGMSYMIER VNNIQDRGSA PVPKRRRIEE DLDGQGSQNG
FSNGSSGMLS EYVKQKQQMG QAAPSATLQT VDLTGGDDDD EVVEIKDPRD QEVCFGMIGG
ASVNCHTVPS PKPGSRTLTP GSWPQVKVVL RRLAEDRSST IEVYDHTRKI IGKLDSRTSH
GLAPLLDARL LGLRTDVMIG IRRRLPEEEA GKPISKSYPL QLMVYGKFKF AKTVGMHLEK
AHLNLLSPTR VDKGVMVFNP LAKENRAVAA PRVYSQPAPP PIARTEEEIR SDVLSVFDSL
QETDSLPERE PGSSIVTPLL KHQKQALHFM LEREDPSKMV DELWQQRTDA YGQVCFYNVI
TNQQSRQPPA KAQGGILADM MGLGKTLSVL SLVACTVPES QQWMGLDPVQ RTPPETERKQ
HPSQFAPPKP DSLALTRVKR NSKATLLICP LSTVTNWEEQ IKQHVQPNTL SYHIYHGPHR
IKDAERLAQY DLVITTYGSV SSELSARFSN KRGPHPLEDI GWFRVVLDEA HMIREQSTLQ
FKAICRLQAN RRWAVTGTPV QNKLEDLAAL LAFLRIQPFD DRSRFNHYII APFKVCDENV
VPKLRILVDT ITLRRMKDKI NLPNRRDQTI RLQFSPEERR MYDAFEKDAQ VRVNVLTGQR
ERMVGGRTYI HILQAILRLR LFCSGGKDLM NDDDLRLLEG LSSDAPIDID SDGEEQNPAL
AENQAYDMFN LMKDTNGDNC IACNQKLGPK EGADIESERQ EDIIGHMTPC FHLICTSCIK
DLGAICPCGT PTENGLVPLR LSRAGQEHDA HAEGRGGSKA SKALKDWGGP NTKVRYLVEQ
LKKWRDMSEA NPGEPPYKSV VFSQWTTNLD LITMALEAEG IIWTRLDGKM TRTARTRAMD
RFREDPAVQV ILVSITAGGL GLNLTAGNSV YIMEPLFNPA AEAQAIDRVH RLGQKREVDC
VRLLMAGSFE EKMRELQDKK TKLASLSMDR QKGEGGGFLS KSEAAKQRLM DLRSLFK
//
