ID A0A0D2AFA5_9EURO Unreviewed; 990 AA.
AC A0A0D2AFA5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=PV07_11737 {ECO:0000313|EMBL:KIW23547.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW23547.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW23547.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW23547.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) 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 PRP16 sub-subfamily. {ECO:0000256|ARBA:ARBA00038040}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN847046; KIW23547.1; -; Genomic_DNA.
DR RefSeq; XP_016243763.1; XM_016399201.1.
DR AlphaFoldDB; A0A0D2AFA5; -.
DR STRING; 569365.A0A0D2AFA5; -.
DR GeneID; 27350931; -.
DR VEuPathDB; FungiDB:PV07_11737; -.
DR HOGENOM; CLU_001832_6_1_1; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000054466; 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; 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:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054466}.
FT DOMAIN 299..462
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 484..659
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 928..955
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 16..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 990 AA; 111387 MW; 3B138F5460EDCAF7 CRC64;
MERSYSPKRR KLAGGFQSAQ TDSSDDLGPS LKPQYASKGR SARPSDRSHS RLRHSKPHQQ
EFDGPEPFFN DEDTAAMDRD WYTGDEFGHT FGDETHNPFG GADATWADKQ REQALLDKKL
GKRMTAKAAQ KQKEVDAWEA NRMLTSGVAQ RRDQVQDFDD DDTVRVHLLV HDLKPPFLDG
KTVFTKQLEP VPAVRDPQSD MAVFSRKGSK VVREKRQQKE RQKQAQEATN VAGTALGNIM
GVREDEGDSA AAVPGEDSGK SKFSAHLKKS TGSSAFSKSK TLKEQREYLP AFAVREELMR
VIRDNQVIIV VGQTGSGKTT QLTQFLHEEG YGKQGLIGCT QPRRVAAMSV AKRVSEEMEV
ELGGLVGYAI RFEDCTSDET VIKYMTDGVL LRESLTQRDL DKYSCIIMDE AHERALNTDV
LMGLIKKVLA RRRDLKLIVT SATMNSERFS RFYGGAPEFI IPGRTFPVDI QFSRSPCEDY
VDSAVKQVLA IHVSQGAGDI LVFMTGQEDI EVTCELIEER LRLLVNPPKL MVLPIYSQMP
ADLQAKIFDP APPGVRKVIV ATNIAETSLT VDGIMYVVDS GFSKLKVYNA KMGMDTLQIT
PISQANASQR AGRAGRTGPG KAFHLYTEQA FKNELYIQTI PEIQRTNLAN TVLLLKSLGV
KDLLDFDFMD PPPQDTITTS LFDLWALGAL DHVGDLTSIG RTMTAFPMDP SLAKMLITSS
IEYDCSEEML TIVSMLSVPS VFYRPKERQE ESDAAREKFF VHESDHLTLL HVYTQWKSNG
YSDGWCVRHF LHPKALRRAK EIREQLHDIM VGQQKMELVS CGTDWDIIRK CICSGYYHQA
ARRRGVGEYI NLRTSVTVQL HPTSALYGLG DPPDYVVYHE LILTSKEYMS CVTAVDPHWL
ADLGGVFYSL KSKEYSAKDK RIIESEFNRK MEIERQMAED RAKEERRRQE DEEKERLFIG
RAKGSGTVVK KMGSNGVVKK PIVPRRRMGF
//
