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
//