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Database: UniProt
Entry: A0A074S018_9AGAM
LinkDB: A0A074S018_9AGAM
Original site: A0A074S018_9AGAM 
ID   A0A074S018_9AGAM        Unreviewed;      1692 AA.
AC   A0A074S018;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=V565_071190 {ECO:0000313|EMBL:KEP50900.1};
OS   Rhizoctonia solani 123E.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX   NCBI_TaxID=1423351 {ECO:0000313|EMBL:KEP50900.1, ECO:0000313|Proteomes:UP000027456};
RN   [1] {ECO:0000313|EMBL:KEP50900.1, ECO:0000313|Proteomes:UP000027456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=123E {ECO:0000313|EMBL:KEP50900.1,
RC   ECO:0000313|Proteomes:UP000027456};
RA   Cubeta M., Pakala S., Fedorova N., Thomas E., Dean R., Jabaji S., Neate S.,
RA   Toda T., Tavantzis S., Vilgalys R., Bharathan N., Pakala S., Losada L.S.,
RA   Zafar N., Nierman W.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DeSI family.
CC       {ECO:0000256|ARBA:ARBA00008140}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KEP50900.1}.
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DR   EMBL; AZST01000210; KEP50900.1; -; Genomic_DNA.
DR   STRING; 1423351.A0A074S018; -.
DR   HOGENOM; CLU_002988_0_0_1; -.
DR   OrthoDB; 3682876at2759; -.
DR   Proteomes; UP000027456; 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:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   CDD; cd02947; TRX_family; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 3.90.1720.30; PPPDE domains; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
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; IPR008580; PPPDE_dom.
DR   InterPro; IPR042266; PPPDE_sf.
DR   InterPro; IPR013535; PUL_dom.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF83; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE DHX16; 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   Pfam; PF05903; Peptidase_C97; 1.
DR   Pfam; PF08324; PUL; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01179; DUF862; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51858; PPPDE; 1.
DR   PROSITE; PS51396; PUL; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:KEP50900.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027456}.
FT   DOMAIN          2..142
FT                   /note="PPPDE"
FT                   /evidence="ECO:0000259|PROSITE:PS51858"
FT   DOMAIN          154..329
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          309..607
FT                   /note="PUL"
FT                   /evidence="ECO:0000259|PROSITE:PS51396"
FT   DOMAIN          1036..1200
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1225..1398
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          140..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          652..674
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          689..824
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        702..766
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        777..812
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1692 AA;  189271 MW;  136A204823B29486 CRC64;
     MSLVQLYVYD LSGGLARALS MQMTGKQIDG IWHTSVVVFG KEIFYGQGIS ITAPGRSHHG
     KPLQIIDFGE TAIDEETFNE YLSEIREHYT ADKYHLLDFN CNSFTNDVIG FLTGQHIPSW
     IRDLPADFLS TPFGASLRPT IDNMFRRPTP GATPPPGTPQ MAAPAPDISN LLLQAVAQRA
     SSSSSYPPST PNPASSTVAA PVHIATNPPS LDSLIKSHKT SIIFFTSSTC GPCRMIEPAF
     EDLAREKAGP DVVFVKVNLD VPGTAEVAGR WEVRVTPTFI MCLDGEKTDE LKGADRGELK
     TRVDLLLYQA FPPHPHLSLK LSALKGLSTQ ATVYDQLPDL SKLLAKLQTT TTSLGLANYP
     NIATMVNATR IQGADSINDQ VASAFAKASD AFVAVAPAQD LFPLLDLWRI TLLNPNFATK
     CALRDYGLAN VITKVSEHLE KLKGASPKAL ALTSLRLQSN ISSNPALLRH LMSDRALRSS
     FTQVAVSGLL HEDIGVRTAA ATLVFNLGTH LQRSRRENPT RPDPAEDGDW EVEVITAILE
     SLSRESDPGV VRRLVAAFGF FVMLSPSFSE QTGPLLEVLE ARSTLEVVAS ASHVEDVTKL
     ARDDRSLSLF GLSDQTTTDF VIASASRAKS ADALHAVLSL PDTPDGHRFA EEVFSRAPRK
     SKAKHAVADS RRDAEQKIKE MRNKNFGFLL EEDTASAPLP NKKSSKRKEE PTKVEMKSTG
     RKERHTRKRD ADGRDWESDE EEKERKRRRE EEEEDYYSRT QAMSDDEGEE LVDEETRQEE
     ERLRDAKERD EFAKRVRDRD KDKTKKVVED KSSRTSGAAA EAAQRRALAD DAAARVAAMP
     NLRERSRQEY LSKREIQQIE LLRKEIADDE ALFRGMKITK REQRDLDYKK QVLALAESRL
     KIKDKYEGYQ LPDDYETEQG KIDKKKKENV LYQRYEEAKE GQFVTDVDQW EEAQAKNSAF
     KSGAMDKPEL VDEYDYVFDE SQTIQFVMDK AMRGEGLLND KDSALRAQIE EAERKAQSMD
     QTRKSLPIYA YREQLLEAIE AHQVLIVVAE TGSGKTTQLP QYLHEAGYTK GGVKVGCTQP
     RRVAAMSVAA RVAEEMGTKV GYEVGYSIRF EDCTSDKTVL KYMTDGMLLR EFLTEPDLAG
     YAALIIDEAH ERTLSTDILF ALVKDIARFR PELRLLISSA TMDAKKFSEY FDDAPIFYVP
     GRRYPVDIHY TPQPEANYLH AAITTVFQIH TTQPKGDILV FFTGQDEIDA AMENLQETAR
     ALGNKVAELI VCPIYANLPS EMQAKIFEPT PEGARKVVLA TNIAETSITI DGVVFVIDPG
     FVKQNSYNPR SGMASLVVVP CSRASANQRA GRAGRIGPGK AFRLYTKWAY SNELEENTVP
     EIQRTNLGMV VLLLKSLGIN NLIEFEFMDP PPGETLMRAL ELLYALGALN DRGELTKLGR
     RMAEFPVDPM LSKTIIASEQ YACTDEILSI ISMLSESSSL FYRPKDKKMH ADKARQNFVK
     NGGDHFTLLN IWDQWSETNY SQQWCYENFV QFKSLSRVRD IRDQLAGLCD RVEVVIQSNV
     NSNDITPIQK ALTSGYFYNT ARLQKSGDSY RTLKTNQTVY IHPSSSLFQA QPPIKFALYY
     ELVMTSKSYM RQIMEIKPAW LLEVAPHFFK YAYSFGFGYL LLTSKLRPAD LEQLGGTDKK
     MPKAIGSIAA TQ
//
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