GenomeNet

Database: UniProt
Entry: W3XD84_PESFW
LinkDB: W3XD84_PESFW
Original site: W3XD84_PESFW 
ID   W3XD84_PESFW            Unreviewed;      1886 AA.
AC   W3XD84;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Helicase mot1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PFICI_05248 {ECO:0000313|EMBL:ETS83372.1};
OS   Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX   NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS83372.1, ECO:0000313|Proteomes:UP000030651};
RN   [1] {ECO:0000313|Proteomes:UP000030651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX   PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA   Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA   Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT   "Genomic and transcriptomic analysis of the endophytic fungus
RT   Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT   of natural products.";
RL   BMC Genomics 16:28-28(2015).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KI912111; ETS83372.1; -; Genomic_DNA.
DR   RefSeq; XP_007832020.1; XM_007833829.1.
DR   STRING; 1229662.W3XD84; -.
DR   GeneID; 19270261; -.
DR   KEGG; pfy:PFICI_05248; -.
DR   eggNOG; KOG0392; Eukaryota.
DR   HOGENOM; CLU_000315_1_1_1; -.
DR   InParanoid; W3XD84; -.
DR   OMA; WYSDIAC; -.
DR   OrthoDB; 180798at2759; -.
DR   Proteomes; UP000030651; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR   CDD; cd17999; DEXHc_Mot1; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
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; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR044972; Mot1.
DR   InterPro; IPR044078; Mot1_ATP-bd.
DR   InterPro; IPR022707; Mot1_central_dom.
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; PTHR36498; TATA-BINDING PROTEIN-ASSOCIATED FACTOR 172; 1.
DR   PANTHER; PTHR36498:SF1; TATA-BINDING PROTEIN-ASSOCIATED FACTOR 172; 1.
DR   Pfam; PF12054; DUF3535; 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; SSF48371; ARM repeat; 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.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
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:UP000030651};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1309..1482
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1654..1805
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          75..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          175..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          693..732
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..102
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..273
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        701..732
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1886 AA;  210011 MW;  F293167A7CB2A96B CRC64;
     MASRLDRLVT ILETGSTKLI KDTAVNQLAD WQKQHPEELF NLLSRVVPYL RHKDWDTRAT
     AAKAIGKIVE NAACYDPNED EDPSSAKKEE SAENGHIKKE EEPAVAVSSE LFSLDTLDVS
     MILKYGRELL RTGSVDLGLA SLEPQARLVH QKKTLLGRLG LLGRPFEDDE IPIQIEKSAS
     PMTPQDAPPN GNGLGRQESI GGPAQLGEDS GLSARQLNQL RRKRKRDAQN AAKGKGGFGD
     LSIRRSFTDK SDIDDTPMAD TDSKKNGKAD YFSLERPDDV DEESKVVSEY KGPVIPIKSE
     IETKDELQGS EWPYERLCDF LKIDIFDPQW ETRHGAALGL REILRVHGAG AGRLRGKSRS
     DNDALNRGWL DDMACRLCSV LMLDRFTDYA SDTSVAPIRE TVGQTLGSFL KHIPPESVYS
     IYRILHRMVM QQEDLGLDRQ IWSVCHGGMV GLRYVVAVRK DLLLQHNDLI DGIIQAVMKG
     LGDLDDDVRS VSAATLIPMA QEFVAMRPAV LDELINIVWE SLSSLGDDLS ASTGKIMDLL
     ATLCGFPEVL EAMKKSALED EERSFKQLVP RLYPFLRHTI TSVRLAVLKA LMTFVHLGEE
     SLGWLDGKTL RLIFQNLLVE RDSATLNVSM DLWLALVQCL AKNPEHLAQE FLPHIDALMQ
     LTLHPVGVSR NPIPMNGALF QKPSGGTYSI TGFVSQTPRK GSETEGERAA KRRRKSTKVD
     EAPTTAHSHD LDGHMMHGDV DLVGMDTLIR SRIFAGRAMG FIMSLVPTSR LEAFDATLMP
     GFTSSYSSTQ LSACMIVDEY STNSANASSE QRYVDELQKI IESERPSHYR DLVSYVQRVR
     SQCAQLVNLF RDHGKVSQSK LPTLPVVVQG EAEAGPTAFS ISIAEKCVGD DFERLRKAMA
     PAQRLITTND LMDARKSTST AIQEAKSAKD GRDIRIRAAA ACALIAMKVL PKKPSPLIKG
     IMDSIKLEES HLLQTRSSET ISRLVQLFTE KGRRGPADKV VANLVKFSCV EVAETPEFPV
     HVNKTDVVLS MQKEEDRVDH DDPEKWAREA KAARVTRRGA KEALEILARV FGADIFNIVP
     SLRKYMEEPL TVAFSGDLPA DAKDPECELG QEIVDALSVI RTMAPTLDNA LHPFIMQQVP
     LIIKALHSEL SVYRYMAAKC IATICSVLPV EGMTALVEKV LPSISNPIDL HFRQGAIETI
     YHLIAVMGDG ILPYVIFLIV PVLGRMSDSD NDIRLIATTS FATLVKLVPL EAGIPDPPGL
     SEELLKGRDR ERTFMGQLLD PKKVESFQIP VAINAELRSY QQDGVNWLNF LNKYHLHGIL
     CDDMGLGKTL QTICMVASDH YNRAEEFKKT GASDVRKLPT LIVCPPTLSG HWQQELKTYA
     PFLSVTAFVG PPAERRAKAS QFASSDIVVT SYEVCRNDTE YLEKQSWNYI VLDEGHLIKN
     PKAKITIAVK RLPSNHRLIL TGTPIQNNVL ELWSLFDFLM PGFLGTEKVF LDRFAKPIAA
     SRFSKASSKE QEAGALAIEA LHKQVLPFLL RRLKEEVLDD LPPKILQNYY CDLSDLQRKL
     FEDFNKKQGK KISETAGRED KEAKQHIFQA LQYMRKLCNS PALVMTPANN MYDETQRFLA
     KQGTSIDDIV HAPKLTALKD LLIDCGIGVE GTDSNDPLYQ PIKPHRALIF CQMKEMLDMV
     QNTVLKRMLP SVSHLRLDGS VEANKRQDIV NKFNSDPSYD VLLLTTSVGG LGLNLTGADT
     VIFVEHDWNP QRDLQAMDRA HRIGQKKVVN VYRLITRGTL EEKILSLQAF KIDVASTVVN
     QQNAGLGTMD TDQILDLFSL GDAGPNLITD KPKDGIDGRE EDMVDVETGD VRAPGKKAWI
     DDLGELWDNR QYEESFDLDG FMKTMQ
//
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