ID A0A165IP98_EXIGL Unreviewed; 1358 AA.
AC A0A165IP98;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=p-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:KZV93681.1};
GN ORFNames=EXIGLDRAFT_767789 {ECO:0000313|EMBL:KZV93681.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV93681.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV93681.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV93681.1,
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).
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DR EMBL; KV425985; KZV93681.1; -; Genomic_DNA.
DR STRING; 1314781.A0A165IP98; -.
DR InParanoid; A0A165IP98; -.
DR OrthoDB; 53793at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006575; RWD_dom.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF145; ATP-DEPENDENT RNA HELICASE DHX29; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 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 SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50908; RWD; 1.
DR PROSITE; PS50030; UBA; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:KZV93681.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT DOMAIN 256..296
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 405..504
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 594..760
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 830..992
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 784..811
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 530..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1358 AA; 149056 MW; E6F5470E72995DE2 CRC64;
MPPKKGIVKS GNAGNSSADP KPQKTHKKGK GAAPEPPQAQ PAAAPKPAQS SQQPLFPAFS
KTPLSLLNER CQKNDWHKPI VDTRQAKDDQ GFSFVVTLSR RNNKTSLTES VRMEPHPPYY
MPTALEARHW GATYALHRIA NHLQLDRVLP PGPREYWKQL DAERKLAPQH LSWMYEPDPW
AAKRSVEDRQ AKAAVRKEEV AATPVLSPAE RKAAREFEGA VEVRMAPAMR DIVERCIKDA
SAEHPEIEGP EGQDFTSDTK LVTDLEKLGF KTHHVRRTLE TLSGSSPLAA SLLREGSPLD
AAIQHLVLSC PECDLPQRFL PANNSSVPFV ASAHSGKEDL RVRWMEERAI KEAGFPAAAV
KECSADPRVD GTFAHLISKL NSALLGVEWT FDPDTGDVET SARDDEIDAL QAVYPDAHYD
ASTLELQVPL PDLDTDLTLH VLFSAAHPYP AGDSLPAMYI TSSDLPPYVR LHLLAQTLQA
DLGEPDEGRL FGAVEAVLAA YEIVRTQGPP EMSEVMTNLL PRAARKAKKI SSNEASNGRT
AGKAGTRSRS SPTDDRTNEQ VRSAWASVVK SDKYMKLLET RQNLPSYAMK NEIVEAVEKN
RVLVLVGSTG CGKTTQVPQF VLDALIDSGA GAGAQILVTQ PRRVAAMSVA ARVSAERAED
GSVGYAVRGE SKVTKRTKIL FCTTGVALRR LGPGGDGLEG LTHIIVDEVH ERSVDGDFLL
LELKDLLQRN DKLKIILMSA TINQETFSKY FGNAPVLSIP GRTFPVQDVY IEEIIADIAY
KPSFVRWNKQ IEELKNAIER ENSKLNDESV RTLAAISAAT SVDPQLVAAV LGYVLKKTPT
GAVLIFMSGV QEIRQTIEAI KSSTYGNQVD VLPLHANLTP EEQRLCFGRT NRQKIVVSTN
TSVTIDDVVC VIDSGIAKEM RYDAEAGLSR LVETRISQSS GGQRRGRAGR TKPGTCYKLY
SRRTEENMRK FVQPEILRVP LESLSLSVKA MREDEDVKSF LSRAIDPPSI TAMDRAWVNL
KALGAVGEDD ELTALGKHMA TMPLDLQLAK ILVMGAIFSC VGPVLTIAAC LSSKPLFLNP
VDKRKEAGSA RQKFLTANSD LLTLVAAYEA AADEVAAGGM RNARDFFEDN FISHTAFREI
ASLREDFWQC LVDIGFAPQH ADPDDRAFNA NSDNQNVVKA IIAAGLWPRI CRVKTPRAQF
QQTQGGTVEK ENEAHELRFF DVRSDQRVFV HPGSSLFSAT AFKSEFVAYF TKTLTSKLYI
REVSEVPLYS ILLFGGPISV NHVGGGLIIR TRVADDDQGV DIKLKAWPRI GVLVNFLRRL
LEAHLAAAIF DPSVLATFSE QPVATTMVQL LDRDGMSA
//
