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Database: UniProt
Entry: A0A1G4BIX1_9PEZI
LinkDB: A0A1G4BIX1_9PEZI
Original site: A0A1G4BIX1_9PEZI 
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
//
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