ID A0A1A6ACK8_9TREE Unreviewed; 758 AA.
AC A0A1A6ACK8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=I303_02004 {ECO:0000313|EMBL:OBR87791.1};
OS Kwoniella dejecticola CBS 10117.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296121 {ECO:0000313|EMBL:OBR87791.1, ECO:0000313|Proteomes:UP000078595};
RN [1] {ECO:0000313|EMBL:OBR87791.1, ECO:0000313|Proteomes:UP000078595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10117 {ECO:0000313|EMBL:OBR87791.1,
RC ECO:0000313|Proteomes:UP000078595};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus dejecticola CBS10117.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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|RuleBase:RU365068};
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC {ECO:0000256|RuleBase:RU365068}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC {ECO:0000256|RuleBase:RU365068}.
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DR EMBL; KI894028; OBR87791.1; -; Genomic_DNA.
DR RefSeq; XP_018265633.1; XM_018405352.1.
DR AlphaFoldDB; A0A1A6ACK8; -.
DR STRING; 1296121.A0A1A6ACK8; -.
DR GeneID; 28965703; -.
DR VEuPathDB; FungiDB:I303_02004; -.
DR OrthoDB; 276261at2759; -.
DR Proteomes; UP000078595; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24031:SF384; DEAD-BOX ATP-DEPENDENT RNA HELICASE 31; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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, ECO:0000256|RuleBase:RU365068};
KW Helicase {ECO:0000256|RuleBase:RU365068, ECO:0000313|EMBL:OBR87791.1};
KW Hydrolase {ECO:0000256|RuleBase:RU365068};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365068};
KW Reference proteome {ECO:0000313|Proteomes:UP000078595};
KW RNA-binding {ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 199..401
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 429..597
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 62..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 758 AA; 83030 MW; E0C4400142576393 CRC64;
MIPRSSIMRA SSALGNLASR RSVLVSRSIA RPAPIAPIQS TRSQSLQSIL LSRGYSAAAQ
RKSEDDFFVS EPSQSPTSSS SRSSSSTSPS SSSPRSPKAE DDGFFAPSLT ESSRSQASSA
SSAVPPEGSS RTGPAVDIVP FESLKGKIDH DTLKALTFKP FQLKAMSEVQ KRVLGLMPSL
GGGRLKGQAR EDAEAVGQVE EAKEREDLLV KAKTGTGKTI AFLVPAIDAR INKINELIKT
PYPDGTLPDR AAQGRNERAI TRSHVGTLII SPTRELATQI ANEALKLCTW HKEMQVRLLV
GGESRHRQLK DWKRGRKDII VATPGRLKDL LSEEEVKSAI EFTDQLILDE ADTLLDMGFS
QDLNHIISHL PKERQTFLFS ATVSREIAAI ARKSLKQGHK VIDCVPKNES NVHLHIPQHY
TIVPSAADQI PHILRLIAHD QFINPHSKVI VFLNTTKLTM LTATLVRELK SSLPKDINVY
EIHSRLDQNQ RSRASERYRR DTKPSVLITS DVSARGVDYP GVTRVIQVGI PASAEQYIHR
VGRTGRGGKE GGRGDLVLLP FEEGFVDRLN KIPIKPVPTS ALEREVTEMA SSEDERYIEK
LEGIKDAITQ LMPSLDSEAI EEVFTSMIGY YMGKSDQLNV NNHEILQGLK DWSVEAAGLP
EPPYLSPGFL QKLGLGGGNR RSGGFGNRSG GGGNRSGGFG MNRRSGSGSG GFGGDRDQRD
REPRVRSGSF SYGGDRDRDS NRSSGFSNRD RDRSSKRW
//
