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Database: UniProt
Entry: A0A165UDR6_9APHY
LinkDB: A0A165UDR6_9APHY
Original site: A0A165UDR6_9APHY 
ID   A0A165UDR6_9APHY        Unreviewed;      1494 AA.
AC   A0A165UDR6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=p-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:KZT74762.1};
GN   ORFNames=DAEQUDRAFT_748014 {ECO:0000313|EMBL:KZT74762.1};
OS   Daedalea quercina L-15889.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Daedalea.
OX   NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT74762.1, ECO:0000313|Proteomes:UP000076727};
RN   [1] {ECO:0000313|EMBL:KZT74762.1, ECO:0000313|Proteomes:UP000076727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-15889 {ECO:0000313|EMBL:KZT74762.1,
RC   ECO:0000313|Proteomes:UP000076727};
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).
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DR   EMBL; KV429032; KZT74762.1; -; Genomic_DNA.
DR   STRING; 1314783.A0A165UDR6; -.
DR   OrthoDB; 1095660at2759; -.
DR   Proteomes; UP000076727; Unassembled WGS sequence.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd17917; DEXHc_RHA-like; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF197; DEPENDENT RNA HELICASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G07950)-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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   Hydrolase {ECO:0000313|EMBL:KZT74762.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076727}.
FT   DOMAIN          673..851
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          941..1121
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          208..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          385..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..415
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1494 AA;  165554 MW;  59CA967AD8B134AF CRC64;
     MGTKKKKTQL KPVARGFATT SVPKKIVPVA DAISEDNGSQ SDAMAVKIAE TASATPSDVS
     PRPGDASGLV HAAEDVDPIL QGLVDKLQDR TEKDIIRTIK AIEQERRFAE TMTSLEFDTN
     AVHRVLDPQL DYECREVEPT IDGPSEKALA RMGVTYGVLR RLGFSEGRVE ECLRSIKGVD
     LEEAVDWLHL HCTEEELDVE KGMYSLDVGS AEGSNSKPTS VPSTPRTVQH PLSVRSRPVT
     PPLYSPQTPD RTGFSGRLDA NAPAFVPSGI TSPLNHSQDE ASNNPPVSGT ESPIAGTSRH
     SANSSGNWSP TDDPNAAFVQ LKMQISELTT HRQPGETRGA SFLRDLQRRL EEVKNDYMFD
     EAEAESQYRI ERERADARIL QSKLRGTTPT SPLVPTTPAT PRRAETHQKQ PSASANAAIV
     DVFENDEEEE SGGGMFELLE EIPTTEVTQN GTTVNVRNMS LPKNWSGRTP KSVLAERVHK
     VDRFAAIAYA DISGTSRAKR ASVDIRWTGG KTDSWSMGDV ACHDMSQAEQ FIATVALHAI
     SFRQSEAFAL GATAGTGSQT VFRLLPAIHR DLWDELEKQR LAQDNATNRN IWAKLRGILE
     PKLKTEREAA EKLAKPAMDV IPRDNNRSNN YGSDLNPEQI IAGFQARQAS PAYQHMLRQR
     EQLPIAEYRN DIVEALETYQ VLVLSGETGC GKSTQVPSFI LEDHLSRGKH CKIYCTEPRR
     ISAISLAQRV SRELGEPAGA VGTVGSVVGY SIRLESNISF RTRLAYVTNG IALRMLEGGS
     GQGGQGTAFD EITHIIIDEV HERTIESDFL LIVLKSLLRE RPDLKVILMS ATVEAEKISD
     YFGGAPVFYV PGRTFPVDVR YLEDAVELTQ WKITEGSPYA RRGNDKFSWS RARNEWSEDI
     APADDDDDET TQENVKLEKR YSALTTNTIN LLDERLVPFD LIVRLLERVC HEDAAYASYS
     SAVLVFMPGM AEIRRLTDLL LEHPVFGSED HFWVYPLHST ISSEQQGAVF DIPPAGIRKI
     VIATNIAETG ITIPDITCVI DTGKHREMRF DEKRQISRLV ETFIAKSNAA QRRGRAGRVQ
     AGLCFHLFTK IRHDTKLAPH PDPEMMRLSL SDLALRIKIM KVRLGTSIED VLSRALDPPL
     PVNIQRAVSA LVEVRALTPS EEITPMGRLL SKLPTDVHLG KFLLIATLFR CLDPALTIAA
     ALNAKSPFVT PMGLEQAADR AKMSFRVENS DFLTIHNAFA SWRRACANGQ LQARKFCKEC
     FLSYQNLQQI EEIRQQFLGY LVDSSFLQVD VAFVRELSRA RYSRNRTRFV TVPPEHDAYS
     GNAYLLNAAL AAGLYPKILS IDPSNGALKT VANNASVAFH PTSVNFGKRA TDFGVNHLCY
     FTLMQSKKLY ARETGPVDDL AVVLLCGEPE FKLIANIVYI DKKIKFRISP KAGIALKLLR
     SQLSSLLSAQ MRAKPLTETQ ALWNELAMMI LGKVKPEQPG RQLDSITLVV NKQL
//
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