ID S8ANX7_DACHA Unreviewed; 1262 AA.
AC S8ANX7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=H072_1345 {ECO:0000313|EMBL:EPS44650.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS44650.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS44650.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS44650.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) 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 -!- 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:EPS44650.1}.
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DR EMBL; AQGS01000040; EPS44650.1; -; Genomic_DNA.
DR RefSeq; XP_011107337.1; XM_011109035.1.
DR AlphaFoldDB; S8ANX7; -.
DR STRING; 1284197.S8ANX7; -.
DR eggNOG; KOG0924; Eukaryota.
DR HOGENOM; CLU_001832_6_1_1; -.
DR OMA; VDVMFHR; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000015100; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000015100}.
FT DOMAIN 572..735
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 757..932
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 77..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1262 AA; 141525 MW; 483E8B5BA13F80DD CRC64;
MPDATIPPGL NDQYTKHLAA LIGKELGRDP NDYLARNIIQ IAKGQPGPKS FVAACSAFGR
YRDEFLQEVF QEVKRRVEEG GDSGSNAQNA SSKGGFTKPE RLERQSELPG GLLVLASTRN
RDEVDHDGKR ESRLGLDRKR IKLDFKVDGE DEEKTQADAE KSSGSSSSVD AKKSRQQTSR
SNDDNSVEFK KPSLPIQRHP VKAQRRMETP SHGGGLSREA AERLAAYRGR RDRDRERQND
DRGNGDRRLQ YNDRDRDRGL YSDRDQRWRD DGRDGYRARQ DYGNRRHDPT PLRQDRFAGG
RVTTARTSKY PAATPRSNAA IRDSEEGFYD AEGTQAMDRD WYAGDEMGHT FGDETHNPFG
SLDNSWADQQ REQALAERKT GKRMSARAQQ KQRDVDAWET NRMLTSGVAQ RADIGMDDLD
DEEETRVHIL VHDIRPPFLD GKTIFTKQLD PVPAVRDPQS DMAIFSKKGS VLVRERRQQR
ERAKQAQEAT NLAGTNLGNV LGIRDEEGDS ALGAAEPTKQ KADGPDDGDI RVENKFADHL
KKNEGASEFS RSRTLREQRE YLPAFAVREE LLRVIRDNQV IIVIGETGSG KTTQLTQFLY
EDGYGKLGMI GCTQPRRVAA MSVAKRVSEE MEVKLGGTVG YAIRFEDCTS DETVIKYMTD
GVLLRESLVD PRLEKYSCII MDEAHERALN TDVLMGLIKK ILARRRDLKL IVTSATMNAE
RFSRFFGGAP EYTIPGRTFP VDVLWSKSPC EDYVDAAVKQ VLSIHLGQSA GDILVFMTGQ
EDIEATCDVI AERLAQLIDP PKLAILPIYS QMPADLQAKI FDKAEGGARK VIVATNIAET
SLTVDGIMYV VDAGYSKLKV YNPRMGMDTL QITPISQANS GQRSGRAGRT GPGKAYRLYT
EQAFQNEMYI QTIPEIQRTN LSNTVLLLKS LGVQDLLEFD FMDPPPQDTM TTSLFDLWAL
GALDNIGELT SLGKSMASFP MEPALSKLLI MSVEYGCSEE MLTIISMLSV PSVFYRPKER
QEESDAAREK FFVPESDHLT LLHVYQQWKS NGYADGWCIK HFLHPKALRR AREIRQQLND
IMKFQKMELT SCGTDWDVAR KCICSGYFAQ AAKVKGIGEY INLRTSVTVQ LHPTSALYGL
GFLPDYVVYH ELILTSKEYM STVTAVDPHW LAELGGVFYS VKEKGYSAKD RRVTENEINK
KMEIEAKIAE DRQKAEAAKA AARDAAPIKR AATAVNPVVK RVATQQGAVK RPTTPLARRR
AF
//
