ID A0A094F0H8_9PEZI Unreviewed; 1215 AA.
AC A0A094F0H8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, 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=V496_08148 {ECO:0000313|EMBL:KFY52862.1};
OS Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY52862.1, ECO:0000313|Proteomes:UP000029302};
RN [1] {ECO:0000313|EMBL:KFY52862.1, ECO:0000313|Proteomes:UP000029302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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 {ECO:0000256|ARBA:ARBA00008792}.
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:KFY52862.1}.
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DR EMBL; JPJY01001563; KFY52862.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094F0H8; -.
DR STRING; 1420909.A0A094F0H8; -.
DR HOGENOM; CLU_001832_0_4_1; -.
DR OrthoDB; 5490433at2759; -.
DR Proteomes; UP000029302; 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; cd17982; DEXHc_DHX37; 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:SF99; ATP-DEPENDENT RNA HELICASE DHX37-RELATED; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000029302}.
FT DOMAIN 395..572
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 594..831
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..165
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..259
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..297
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1215 AA; 134300 MW; 76CAA8E8AD54FEEC CRC64;
MKKFVPRQRK HKVIARTKDS SKNPYDGVPD SNAVEIIPTA KAELDEKKRL LREELKKEGA
KMSGKKAKRL EKYIDTKLKK DENRILIQNL AATKTDTSLY SSSSRMGQGK ESKRQRMGRA
LREAAAGIDM DGQNDEILFE KRVLKDGPVE GDSDEEVEDD DEVSGAAMTT TEGTSNETKA
VPFTSAAGSG LKRPLELDDT GRPVIQKRQK RGGVNSKLSF KAEPKATTTA KAEPAWTGFS
ESEDSEDDNE EDSDSDSDMS DNELGPSIAV DKATSEGDEA TSDGEDGSEE SSDESDSEDN
TEDKKERSSA FKSWANQQRN EAMGFEPTNT TQLATLTPKI ENFQPRPLES DPLPAELQTA
NSIARKAFAV SFNRSAEIQE ARMQLPVVGE EQKIMEAIHN NSTVVVFGAT GSGKTTQVPQ
FLYEAGYGSP DSPTPGMIGV TQPRRVAAVS MAKRVGDELG DHGDRVAYQI RFEGTVSPKT
AIKFMTDGVL LREVALDIAL RKYSAVVIDE AHERSVNTDI LIGMMSRVVR LRDEMALEDP
SIKPLKLVIM SATLRITDFT ENKTLFTKPP PVVQAEGRQF TVTNHFARQT RHDYVEELFK
KITKAHKKLP PGGFLVFLTG QNEITHLSKK LKEAFKIGTM ASGPQVRISG QDAPAEAEDV
DFGGLMEEEL DSDDESVDFE GDDNDDAEFD VGEAEEVGPA KMHVLPLYSL LPTKEQLRVF
EPPPDGSRLV ILATNVAETS LTIPGIRYVF DCGRSKERKY DEKTGVQSFE ISWISKASAS
QRAGRAGRTA PGHCYRMYSS AVFERDFREF AEPEILRMPI EGVVLQLKAM NLQHVVNFPF
PTPPDRASLA ASEKLLTYLS AISPTGQITK VGSTMSIFPL SPRFARILLI GHLHGCLPYT
IALVAGLSTS DIFIPENQVV PALTPKDDQD EDSHFTQADR LEEDARNAIR RKYNSVQHAF
CSLDDRSDAI KLLQAVGEFA HEPTEAWCHA HYVRYKVLKE ILQLRRQITD LLRTNIPAFA
GLTFVDKLPP PSVTQIKALK QMVAAGFIDH VAIRADLAPI PPPVGRKPSR AIEVQYLTLF
PSHARRDDED KAVYIHPSSP LAHRSPKECP EYIVYSHLQR AAPSATTPER VPRARMHALV
DVSGGQLAAL AKGTPLLHYG KPIKEGKQLD KLGLEKECWV VPYLRAEGKN DMGWPLPARK
VVQKKVMGKG WVIQG
//