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
//