ID   A0A177DR26_ALTAL        Unreviewed;       766 AA.
AC   A0A177DR26;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=CC77DRAFT_960229 {ECO:0000313|EMBL:OAG22245.1};
OS   Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Alternaria; Alternaria alternata complex.
OX   NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG22245.1, ECO:0000313|Proteomes:UP000077248};
RN   [1] {ECO:0000313|EMBL:OAG22245.1, ECO:0000313|Proteomes:UP000077248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG22245.1,
RC   ECO:0000313|Proteomes:UP000077248};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-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   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       DDX15/PRP43 sub-subfamily. {ECO:0000256|ARBA:ARBA00024333}.
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DR   EMBL; KV441475; OAG22245.1; -; Genomic_DNA.
DR   RefSeq; XP_018387666.1; XM_018535598.1.
DR   AlphaFoldDB; A0A177DR26; -.
DR   STRING; 5599.A0A177DR26; -.
DR   GeneID; 29121192; -.
DR   KEGG; aalt:CC77DRAFT_960229; -.
DR   VEuPathDB; FungiDB:CC77DRAFT_960229; -.
DR   OMA; MKVYPLY; -.
DR   OrthoDB; 3682876at2759; -.
DR   Proteomes; UP000077248; 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   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   CDD; cd17973; DEXHc_DHX15; 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; IPR044756; DHX15_DEXHc.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
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:SF109; ATP-DEPENDENT RNA HELICASE DHX15 HOMOLOG; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:OAG22245.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077248}.
FT   DOMAIN          111..276
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          301..483
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   766 AA;  86343 MW;  7C5F315557DED135 CRC64;
     MTAMTKREYG DDDSARVKRV KTESNGEGKM DAAANPYLAH WNDEKPVKSE YSGAGTGLQG
     FKRHATTTAQ ANAAEDGPNN AFTGRPLSSK YMSILKKRRD LPVHQQRDEF LKLYQESQIL
     VFVGETGSGK TTQIPQFVLF DDLPQENAKM VACTQPRRVA AMSVAQRVAE EMDVELGEEV
     GYSIRFEDKT GPNTILKYMT DGMLLREAMN DHNLTRYSTI ILDEAHERTL ATDILMGLLK
     EVVLRRPDLK LIIMSATLDA TKFQKYFHNA PLLAVPGRTH PVEVFYTPAP ERDYVEAALR
     TVLQIHATEG EGDILLFLTG EEEIEDACRK INLEAQDLSR EGGAGPLVVY PLYGTLPPAQ
     QQKIFNPAPP PSTPGGRPGR KVIVSTNIAE TSLTIDGIVY VVDPGFSKQK VYNPRIRVES
     LLVSPISKAS AQQRAGRAGR TRPGKCFRLY TEQAFKKELI EQTYPEILRS NLASTVLELK
     KLGVDDLVHF DLMDPPAPET LMRALEELNY LACLDDEGEL TTLGGLASQF PLDPALAVML
     ITSPEFYCSN EILSLTALLS VPQIFVRPAN NRKRADEMKE LFAHPKGDQL TMLNVYHAFK
     SEEAQANPKQ WCHDHFLSYR ALQQADNVRL QLKRIMEREE LELMSTPFEN KKYYENIQRA
     LVAGFFMQVA KRDGNGKSYI TVKDEQNVLL HPSTVLAEDS EWVIYNEFVL TTKNYIRTVT
     SVKPEWLLDI SPNYYDLSQF KKGEIKTALQ RVVTKLQRKE AEKPRR
//