ID A0A135TLW3_9PEZI Unreviewed; 795 AA.
AC A0A135TLW3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=CSIM01_09228 {ECO:0000313|EMBL:KXH49097.1};
OS Colletotrichum simmondsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=703756 {ECO:0000313|EMBL:KXH49097.1, ECO:0000313|Proteomes:UP000070328};
RN [1] {ECO:0000313|EMBL:KXH49097.1, ECO:0000313|Proteomes:UP000070328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS122122 {ECO:0000313|EMBL:KXH49097.1,
RC ECO:0000313|Proteomes:UP000070328};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum simmondsii CBS122122.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
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:KXH49097.1}.
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DR EMBL; JFBX01000121; KXH49097.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135TLW3; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000070328; 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: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; 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 PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF118; ATP-DEPENDENT RNA HELICASE DHX33; 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 PROSITE; PS00690; DEAH_ATP_HELICASE; 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:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 129..316
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 357..534
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 34..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 795 AA; 88094 MW; 9B305472DA1C3DA0 CRC64;
MSSVLDAERA PKKRKLDGKN TIKVGNKVIS LEGYLNPPAK KKEAEVQQRP TEELRSVQET
ENDATSDALV KDPKDSHQTA PTFIKRSSKT SQDRDRPKFD KRGPRWREDP ALLKIRQKLP
IWAHREEIQA RVRQNDVLLL VGETGSGKST QIPQFLVREP WCRRQVVSIA GAREVSVGGM
IAVTQPRRVA ATTLAHRVSR EAGTPLGESR DGLVGYSVRF DHQVPKGTKI KFLTEGMLLQ
ELLRDPDLKQ YSAVIVDEIH ERSVDVDLVS GFLKQILLSS RKGRGGIPLK VVVMSATADI
ERIQSFFSAN SPEEKSGGDD LVNKKSNSVG VLKIQGRQYP VKTIHTPQPV PDIQESLLKT
IFKIHMEEPL PGDILAFLTG QEEIESAQSL LEEYAATLAS NVPKIKVLPL YGQLSMEGQH
AAFQPVKGGF TRKIVLATNI AETSVTVPGV RYVVDGGKAK VKQFRARLGM ESLLAKPISR
SSAIQRTGRA GREGPGKCFR LYTEGTFSTL EETDLPEILR IDVLGAVLTM KARGIDDILG
FPLMDTPDVE AIERALVNLH GLGALADDGT ITEAGRKMAG FPISAAFGAV LLASAKPEFD
CVLETIDVIS CITSGDDIFH QLQSEEQREE IEELRKELYR REGDILTYLT TMQQYAAENA
DRIQWCKQRK VNIRNMKTAL NIRRQLRSLC LKEGLLTEAP PPDPQPFTPL APEQAEALLK
CFLRGFVSKT AILAPDASYV TSQGKHVVAI HPSSVLHGQK KEAIMFLEHV FTQKNYAKKV
SIIQADWIVE AFEGH
//
