ID A0A0F4G801_9PEZI Unreviewed; 1974 AA.
AC A0A0F4G801;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Helicase ATP-binding domain-containing protein {ECO:0000259|PROSITE:PS51192};
GN ORFNames=TI39_contig4316g00002 {ECO:0000313|EMBL:KJX93444.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX93444.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJX93444.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJX93444.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KJX93444.1}.
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DR EMBL; LAFY01004275; KJX93444.1; -; Genomic_DNA.
DR STRING; 1047168.A0A0F4G801; -.
DR OrthoDB; 1877777at2759; -.
DR Proteomes; UP000033647; Unassembled WGS sequence.
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 Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45626:SF17; HELICASE-LIKE TRANSCRIPTION FACTOR; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000033647}.
FT DOMAIN 834..1063
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 27..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1538..1574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1588..1613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1753..1974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..54
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1598..1613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1795..1817
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1818..1836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1837..1851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1902..1916
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1952..1968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1974 AA; 222646 MW; 91526CCC845E27EF CRC64;
MKIAEDRKPV IQTPASEAQI EAVVDMLRDL EVVDDEGDEA EDDNDEEEAH EDQEGSEDGG
NTAQNASERR GPNRNQRRAM NRYAAKLARA TQARERDART VRRASAYPPP QSKPQGVPQT
IAYLGFHNYR HAWLWLMSPP VLKAMETYRM LGFPTEVTNL QMAASIARTM EDQWVEKYGD
NWPHPDDFRK EFPINLYNSK DSKNPMPGPP EKIKMNTGQW KCVGDGYSEN NQAHVYAYLL
CWLPRETARF DSLSGKEQRK EYRRLTIPKN FSYLLPKWSE LNIAPDTKFP SPQWNHPNDI
AKILEPLNRV ATTLAFMGTR FAYTAKPTAH FTVGWNTHCR NKSIFKDKQF NSEICRPQWM
TKDFLCTKAP PQPTVVQLPS ETRPRKIMVH ISGRGEYGDT KKKLWRLEDH EKDAFNKAWH
DNEPEEDEDR ELPTKYDLRD TNHLGKGLDR LREYLKLPEE CKAIVRGIAL DNTEQPEKKS
LILYDRAGGR TDVTWAEAQA YIDQEGRTTV LKIAVQFPDL DDPDDPVKFN ERDTGMDLWT
SANTMRVAVN GEIVTGDVVA ELDPTLNDLS ADNVDASSSP QEQEARRKEE QDRDDNVHRI
LNFNHQTIRD LPHPNQLHLA GDTVDSPLNI AALEKYYGCP YKDIPELDSE AWRKMVGQLI
EKLLQRHPRT KPAKEHVEFH DAVDLSQVTK LKNESKKVFV SEKNTAQTKL AGLSSNADTT
DPQDQARAAL LGAQREAREA NGGTGVQRGH RLDDVLKIMK AWVPDGDAGR HQHDPEIKKY
VVGLFPESVR PDINFFGTQL TGALWMMLRM GLSNLPLEEA HLKEASLKEA LDRLGPMVPT
YGGYVADDAG VGKTFLILLA LAFFAQWGES EKKGNRKETY RPTLYLAPSQ SVANQTFQAI
RKHFPNLTPL MCSGNNFSKE KQGGDRKYFV PKDQLRLGRN SKHDLLKRAL NQGKKEARSF
VLISTYRANM WRSQDSNPTA KQLKDQSRNS PGGKPDKKPL KNVQAGWYGR TIFDECQEIK
NPNTKTNKIA QLRNCPVNFM VSATPALNDE GDIRGSLKIL WPRIFKHLHD DKKAWAWHRS
KTTSEDDSWK VFEALNDLEK DGKLPVHDNK RLSTFNPTVM KSLLDTKIGA QFGLGEAGKY
YHLFMDTGTL LRNSSTRIPL NDTDTLSLEM LVPQPDITAE TLFPSDRERV NMETRGMFVA
QRFYKAWVNS SGNTSYSATA TADGDGSLHL DRDGEPKFPQ TTREARLSSI MASSSVLGDL
HLQLGGKSWA HLFDNRRHSS HNAQLVHNIV TKWKEATPDT QLEMMAYLVE GSPKARRMLE
FFHRKILFNP DKKLLVCEEI PFCAWFWELI FITLNIPARV FHGKLTDEER TELVVQFNTA
KDPLKVMICE YGVTVAGLNF QECCSDVFVC TSAANLQTEH QLQFRCCRAD QREKKITILR
VCVRNTDDEI REQRVARKAL SMANIAIGGP DKMALLARWA SVMIPLIVLA WRNQRALALV
RSMDPVLAKY AERHPFVMPD VGDESSNPLS KMEAQVQAMR DEVKKTNKQS ASGKKLSAKE
QEEKQQEVKD SLAHLDNVER EAEEMMRKLD AQDSTYVDDK PRNTSNTPKM SSKEKITSAV
VMPGIGLDGR LVKAGEKKPP VNDANAMRQA KGDDRLLRYF LKFNPKIVAF TAKHVEMFPQ
VAHLALTTLN KYHYGIADDT HRASCHIRYS AVPPVMAALV KKYEENHADA VADTPWAADK
SVDDATKMVE LGRSEPSYGM NQADDPCEDT GDLESDDDDQ QQQGSSSGLS ATRKPRKAAP
RDLRERPQLE AEEHYNLLTN RRSASAMQSG GEDNTPARPQ KRQKTNRDAE QVDNGDGAAG
SSSARKPAAR RGGRRIQTEG DVDSILQNVR NGKKRAMDAE SEDDELGSDG PLEELSSEED
PQPNPKRQKT NAATAKKPTG KAKAPAKKAS AKTTAAKNTS TAGTTRTLRS GKPK
//
