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Database: UniProt
Entry: A0A0D1ZZ21_9PEZI
LinkDB: A0A0D1ZZ21_9PEZI
Original site: A0A0D1ZZ21_9PEZI 
ID   A0A0D1ZZ21_9PEZI        Unreviewed;      1804 AA.
AC   A0A0D1ZZ21;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIV99677.1};
GN   ORFNames=PV09_08731 {ECO:0000313|EMBL:KIV99677.1};
OS   Verruconis gallopava.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX   NCBI_TaxID=253628 {ECO:0000313|EMBL:KIV99677.1, ECO:0000313|Proteomes:UP000053259};
RN   [1] {ECO:0000313|EMBL:KIV99677.1, ECO:0000313|Proteomes:UP000053259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 43764 {ECO:0000313|EMBL:KIV99677.1,
RC   ECO:0000313|Proteomes:UP000053259};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KN847574; KIV99677.1; -; Genomic_DNA.
DR   EMBL; KN847574; KIV99678.1; -; Genomic_DNA.
DR   RefSeq; XP_016209547.1; XM_016362680.1.
DR   RefSeq; XP_016209548.1; XM_016362681.1.
DR   STRING; 253628.A0A0D1ZZ21; -.
DR   GeneID; 27316704; -.
DR   VEuPathDB; FungiDB:PV09_08731; -.
DR   HOGENOM; CLU_001161_1_0_1; -.
DR   OrthoDB; 2787289at2759; -.
DR   Proteomes; UP000053259; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   CDD; cd18007; DEXHc_ATRX-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; IPR044574; ARIP4-like.
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; PTHR45797:SF1; HELICASE ARIP4; 1.
DR   PANTHER; PTHR45797; RAD54-LIKE; 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.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000053259}.
FT   DOMAIN          1057..1263
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1481..1645
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          168..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          229..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          649..709
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          754..780
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          952..992
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1394..1447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1757..1804
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          457..484
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        170..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        654..675
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        676..690
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1394..1411
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1427..1442
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1774..1804
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1804 AA;  202829 MW;  743B16031024FCDF CRC64;
     MAEDIDPYDW TLDQVVDAFC YKRTLWQEEQ PNAILPDPVT LERLLRLNHI YGAALLTEVT
     PQVLKDDLSL KSLGQRSSIS WAIRRLQARS RKFIAQQSAA ALSLHGNLSA QAQINQYSTP
     LPFTPFTPHQ SERNVLQSPF SIQSDAHASV GTSPGFVQPA LLAHPDHHLA QSPSRSNPFQ
     PMLGTGTSVG EGETDAVSLK RRAGETVIED GAGRKKRRLD LSAMMTRTTT TMNEASQSNN
     DADLPSSEAT ATFTAAQASQ PTSPSPVYLP ANTLLQKCGL EPGITSFLGK KKFSFETMFF
     GSTRYGKELN IDVDCKPLIK EGSSVGETLI YHGSANTAVY GLQMVMNRKM MSFLRRDPYL
     NVNTKDESMA FYPYSATPSQ STESRALIHI MEESGIVIAK RTKLDQVLYA DSGLNFDDTT
     SNHDWDFLSH WQRERGEKED AILPAYGDSE SEDDVELDSL VEELERDEEE DAEETRKLDA
     AQVEKIIEDT IADQVTAWRE KRLPVLQDRA LATWKKGRSG HHREKLARLA EQEIARLDAS
     VAKLSRSIAN DTWTRGRDVR AQCESIEPTV HWREEEKFKL SVWRNPKAPP PPSGQLLTCK
     KRNSYVSSNP GEHVLDSDEE VVDNRPGLDT FIDVDELVPL DLTAFKAQDE TESHGADTNQ
     PVQSEQAQLT SLDELGERTR SQDENRSELD SATEMLSQTK PKDDSTVDAH VDETVKVEPF
     SGPVFPELDK TCLPDKYMID LTFDSDTELP LITAQAGPSS RRTRAQSANK DFSDHPEDDP
     DESVALWDWV VLQENTDRVR VIIKLIREMP AFEYKRLREH VLEDYGTGQR PKIYELGENI
     EKVLRTRLGL AANFEMAEFA FDRAVELLHL YVCWLESSPV HFREGYDLNE QNFKLVDLEH
     QLLQNAFAQT RQDESEDLGE CLQYIYSTFF RHEHPLQSAK EDDNSDIELQ EIDSHEADGA
     IPRKQRKRHV EESQAALSKR QKSKQKAADW KDRTDTFLQQ SHHQSSQLGT SAGDIVVNTG
     KEEDDPEIFI SPHIAPALKP HQIDGIRFMW REIVGTADDS DEPQGCLLAH NMGLGKTLQV
     IAFIDTLARA ARSEDKRVKR QVPKKLRAMR VLILSPAGLI SNWVDEFMKW NKAESAIGEP
     FVLTAQTTTM QRLELLKDWY NAERGSVLLM SYELFRNWEG NKKAGKNYSS PFSEKEHEEV
     KKQLLGGPSL VVADEAHKLK NHTSAVTIAA QKLSTKSRIA LTGTPLSNNL LEYYAMVDWI
     SKDYLGGLVE FKANYIEPIE NGLYLGSSRG EYRRARIRMA ALIAMLEPKI DRREIDVLAG
     SLKPKVQFVL KVPLTPLQFD VYDGFVQEAI GEIGDSVSNA RLWGFMSYLQ LLCGHPSLFR
     GAIVEARKKQ KALDEKRAKD ASKKQAKSPL SRVVDERPGN SPQSNDDEET DNSDDTKDDV
     DDDGNAPADS ISLQIAERLF NKLVDKFEPI LAAFHDAQFS YKVSLLLKIV EKSRAVGDKL
     LIFSHRIPTL DFLGQVLKKS NVRCERLDGS TSMNKRLQMT KNFNKGNEYD VCLISTRAGG
     VGFNLYGANR VILFDFSFNP TWEEQAIGRA FRLGQEKPVF VYRFISTGTF EEKLFDKTIF
     KLQLSYNVVE KKHTKSRAVR VQDYIETPKK SKLQDFSSCR GNDGVLDAIL DEMEEGKELV
     HHIALDTTFK EEIKENLDEE GRKEMEMLVQ QNQLRITDPQ AYASQQLKQQ QGATAARFNM
     PSSAARPDHV TGIPSRLAQD ATLAPPASAP VAGTSDRNPA TLSPSLTAQE QPTGSKAPAT
     NRMD
//
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