ID A0A1G4BIX1_9PEZI Unreviewed; 795 AA.
AC A0A1G4BIX1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=CORC01_03397 {ECO:0000313|EMBL:OHF01364.1};
OS Colletotrichum orchidophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=1209926 {ECO:0000313|EMBL:OHF01364.1, ECO:0000313|Proteomes:UP000176998};
RN [1] {ECO:0000313|EMBL:OHF01364.1, ECO:0000313|Proteomes:UP000176998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 309357 {ECO:0000313|EMBL:OHF01364.1,
RC ECO:0000313|Proteomes:UP000176998};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) 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:OHF01364.1}.
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DR EMBL; MJBS01000020; OHF01364.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4BIX1; -.
DR STRING; 1209926.A0A1G4BIX1; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000176998; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000176998}.
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..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 50..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 795 AA; 87782 MW; 22C7913DA484C3EB CRC64;
MSSALDAERA PKKRKLDGKN TIKVGNKVIS LAGYLNPPAK KKEKEIQQPS TQELRPAQST
GSDATSDALA KEPKSSDHTA PSFIKHQSKK YQDRERSRSD KRGPRWREDP ALLKIRQKLP
IWAHREEIQA QLRQEDVLLL VGETGSGKST QVPQFLVREP WCRRQTVSIE GAREVSVGGV
IAVTQPRRVA ATTLAHRVSR EAGTPLGESR DGLVGYSVRF DHQVPKGTKI KFLTEGMLLQ
ELLRDPDLKQ YSAVVVDEIH ERSVDVDLVS GFLKQILLSD RKGRGGIPLK VVVMSATADV
ERIQGFFSTD SPEEKSSGDD PVGNKINSVG VLKIQGRQYS VKTIHTPKPV PDIQESLLKT
IFKIHMEEPL PGDILAFLTG QEEIESAQSL LEEYAATLAS NVPKIKVLPL YGQLSMEGQH
AAFQPVKGGF TRKIVLATNI AETSVTVPGV RYVVDGGKAK VKQFRARLGM ESLLAKPISR
SSAIQRTGRA GREGPGKCFR LYTEGTFSTL EETDLPEILR IDVLGAVLTM KARGIDDILG
FPLMDTPDVE AIERALVSLH GLGALADDGT ITEAGRKMAG FPISAAFGAV LLASAKPEFD
CVLEAIDVIS CITSGDDIFH QLQSEEQREE IEELRKELYR REGDILTYLT TMQQYAAENA
DRIQWCKQRK VNIRNMKTAL NIRRQLRSLC LKEGLLSEAP PPDPQPFTPL APEQAEALLK
CFLRGFVSKT AILAPDASYV TSQGKHVVAI HPSSVLHGQK KEAIMFLEHV FTQKNYAKKV
SIIQADWIVE AFEGH
//