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Database: UniProt
Entry: A0A165IRW9_EXIGL
LinkDB: A0A165IRW9_EXIGL
Original site: A0A165IRW9_EXIGL 
ID   A0A165IRW9_EXIGL        Unreviewed;      1888 AA.
AC   A0A165IRW9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KZV93790.1};
GN   ORFNames=EXIGLDRAFT_645875 {ECO:0000313|EMBL:KZV93790.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV93790.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV93790.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV93790.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KV425984; KZV93790.1; -; Genomic_DNA.
DR   STRING; 1314781.A0A165IRW9; -.
DR   InParanoid; A0A165IRW9; -.
DR   OrthoDB; 1384108at2759; -.
DR   Proteomes; UP000077266; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
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; IPR000330; SNF2_N.
DR   PANTHER; PTHR45623:SF17; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED; 1.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00298; CHROMO; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          857..1034
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1165..1321
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          454..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          623..668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          691..753
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1421..1493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1627..1683
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1743..1765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1830..1888
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..188
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..239
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..296
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..327
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        712..726
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..753
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1422..1466
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1830..1866
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1873..1888
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1888 AA;  209878 MW;  C7C0AF4365DDEC9F CRC64;
     MVRERDTTPP SRARGEVIEI EDTPERPTRA TRRSGRVLDV VVPRLSDGDK NDYAALNTPP
     DDSDSEEDGD DDAGPVPATI LGEIRRKSEM FYFVLHDDDV IRRYSARDVK AHYPKLVDEY
     ETSKDDDSLE PFNYNDSRIE AKSRDSHVSL PIAKKKAQSK ADAKSKSKSK SKAADSKDAT
     HDYRDTDEES SDPSSEENSG GSDYEHEEEA PAPRRSTRSA VVAPKAKQKA KEKAPSPKKA
     TRTSGRARNA VTYGGMQAPS DVESDVDMSD EEAPAPTAKD KKAPRPRKKH VSRPAYGNIR
     HTKELSDDED DDRDRLHVHR EGCEKCGEPP AHVQVLDQRR KKRRKKGKRK AAHSSDEDDE
     LSDDEMDFDA LGGWIRCLKC CVVSHWKCLS AEQRNEILRA VKEKDTAVDE DGKPLPKRKK
     LEVFETTEFV CASCSKGGIC FMCNAVAVEK FQPQTTSAAA PPTSTGEPAS EDVEMKDNTA
     QTPDAPKTDD ASDKPLLFRC ITCKRAAHYD HLLVPDASDV QEIAMYYQDD QDWTCDDCKS
     FVYGVENILA WRPYPADAVE PPLDAGEVPN HKNMLPREYL VKWEGRSYKR VQWVPHMWLL
     ATAPAKLKGF ITRGSLVKLL APTAASGAPS KRSTPFLEEA SGRPSPAPSD DIGEREFGPP
     ASSSDAFDRI PRQWYTIERV LDVQLWCPPG CGQKQKQKQK RRDSGKRVVD DDEDVEMDDD
     SDSDAPEGLA EALATARAEG DEPESKKTQT VAGWEKRHGR ELTERDIGLV VWGYFKYTDL
     SYDQGTWDAP PSEDDDGYVA FKRAFKGFIA ARSVLVKEKG TGRKLGKFEP LEGQPKLCED
     DSFALRDFQL DGLNWLYYNW HKGHSSILAD EMGLGKTVQM TTLLGLLVKH HDAFPLLVIV
     PNSTLSNWLR EFERWAPNVR VVPFYGEGKS RDIIKKYELY HDYVPKGYTS SKFHVLLSTY
     ESFTNVKDGY AVFTAVKYWE AIVVDEGQRL KSDASLLFRR LTSLNARHRI LMTGTPLNNN
     IRELFNLMNF LDPKEWADLP ALEEKYSELT EESVKELHER LKPYFLRRTK ADVLKLPPKN
     ELIVPVSMSA LQKTVYKSVI GQNAELLQAL LQGKNGAKNN KAKKLNNILM QLRKCIQHPY
     LVDRELEPSG LDKKDTHRNL VDASSKLQLL KVMLPQLKQR GHRVLLFSQF RIALDIIEDF
     LVAEGHTFRR LDGETKQADR QKYMDEFNAE DSDVFIFILS TRAGGVGINL FTADTVIVFD
     PDYNPHQDPQ AIARAHRFGQ KKTVLVFKLM MKDSAEEKIM QAGKKKLALD HLIVQSMDDE
     NAADNDVQTL LSYGAKALFE EDGAAQTITY SASDVEQLIV RTETAVDVEQ DETTKGSLSF
     DFTKIWLPEK GGVEELQEDT GTTSQDEHDF WAKTLALASA EQEAAKERER QQMGRGARRR
     KEVNYAMPVS PEKDKRGKGR KRNIDDDDDD EDVDFTMQDG VSSDDDTASF YGGDVEDRLS
     LDEPAAHAVS GLAASGPNQH TAPGAFAGVA AHVDVPVLKK KVKKRKLVDQ ENVSGLDDMC
     GLCHQRHPAK SCYMTNNPLN LIEYRKILFD DQNDEPYETR AAAVQAIDRE LNARGMSSML
     KSLPAFPAEP IPLPTDHKAK KRKTDPGPLT TALPKPPVLS DAAVNSRPTT VSGPVPPLPS
     PFTSAPLPTT SHAKSAVTDP AAVKATSSPA PVVLPKVKAP VAAPVPPKVS PPAPMVASDR
     VSTPAADVGR AGTPGMRQTT LSFGRKDSKT SVARCPVCNQ SAHPVLQCPD AQDGTSIRAA
     IERLKGKPEH QGTVDNLRQL FADRFIISSS HKPAASSSSQ TEKTASRHSY GGTAAPSESS
     ASLMRRKSNP KPVKSRPVVD EDVIEISD
//
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