ID A0A437A298_ARTFL Unreviewed; 1244 AA.
AC A0A437A298;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JAN-2026, entry version 28.
DE RecName: Full=Antiviral helicase {ECO:0008006|Google:ProtNLM};
GN ORFNames=DFL_003577 {ECO:0000313|EMBL:RVD85251.1};
OS Arthrobotrys flagrans (Nematode-trapping fungus) (Trichothecium flagrans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Arthrobotrys.
OX NCBI_TaxID=97331 {ECO:0000313|EMBL:RVD85251.1, ECO:0000313|Proteomes:UP000283090};
RN [1] {ECO:0000313|EMBL:RVD85251.1, ECO:0000313|Proteomes:UP000283090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS H-5679 {ECO:0000313|EMBL:RVD85251.1,
RC ECO:0000313|Proteomes:UP000283090};
RA Youssar L., Wernet V., Hensel N., Hildebrandt H.-G., Fischer R.;
RT "Intercellular communication is required for trap formation in the
RT nematode-trapping fungus Duddingtonia flagrans.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010140}.
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:RVD85251.1}.
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DR EMBL; SAEB01000006; RVD85251.1; -; Genomic_DNA.
DR RefSeq; XP_067490795.1; XM_067632535.1.
DR AlphaFoldDB; A0A437A298; -.
DR STRING; 97331.A0A437A298; -.
DR GeneID; 93585888; -.
DR VEuPathDB; FungiDB:DFL_003577; -.
DR OrthoDB; 64767at2759; -.
DR Proteomes; UP000283090; Unassembled WGS sequence.
DR GO; GO:0055087; C:Ski complex; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0070478; P:nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay; IEA:TreeGrafter.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR FunFam; 3.40.50.300:FF:000354; ATP-dependent RNA helicase SKI2; 1.
DR FunFam; 3.40.50.300:FF:000987; DEAD/DEAH box RNA helicase; 1.
DR FunFam; 1.10.3380.30:FF:000001; Ski2 ATP-dependent RNA helicase; 1.
DR Gene3D; 1.10.3380.30; -; 1.
DR Gene3D; 1.20.1500.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR025696; Beta-barrel_MTR4.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C-like.
DR InterPro; IPR048392; MTR4-like_stalk.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR050699; RNA-DNA_Helicase.
DR InterPro; IPR016438; SKI2-like.
DR InterPro; IPR012961; Ski2/MTR4_C.
DR InterPro; IPR040801; Ski2_N.
DR PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR PANTHER; PTHR12131:SF1; ATP-DEPENDENT RNA HELICASE SUPV3L1, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08148; DSHCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF21408; MTR4-like_stalk; 1.
DR Pfam; PF13234; MTR4_beta-barrel; 1.
DR Pfam; PF17911; Ski2_N; 1.
DR PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01142; DSHCT; 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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000283090};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 297..453
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 571..771
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 495..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1244 AA; 139739 MW; 6C09F8F192D987DD CRC64;
MATIHNFGIE RADEIDIDAT LTSPKPRPPV KRHREELLGE LENGFLTPLD QFPVEWLNNL
QERWEDPPDY YSLFALSSTM TRTVIRFTRE GLEGRVTGYK EVSVPAQSTN AKNSTSLLRK
PGTRADFVRG KAGFFPFTPG GLEAGSASER SEDLAAVEFA QDSLYGKDGM LQVAPGLLRG
LNIEGDEELE DEEDNDGFQF GDVEPIRQLK DKIESNEQGP QPTGQISELE GIDDLLSVEF
PLLAPRGQLA PSSTISRGKE WAHMVDINQD LTNFKELVPN MAREWPFELD NFQKEAIYHL
ENGDSVFVAA HTSAGKTVVA EYAIALAAKH MTKAIYTSPI KALSNQKFRD FRTIFDDVGI
LTGDVQINPE ASCLIMTTEI LRSMLYRGAD LIRDVEFVIF DEVHYVNDQE RGVVWEEVII
MLPDHVNLIL LSATVPNTKE FASWVGRTKK KDIYVISTPK RPVPLEHYLW AGKKMHKIVD
QNKKFLEAGL KDANEAMSGK KDERPSQSAP TRGNISQRGG QRGGPNHRGS QSARGGRGGN
VMRGASGAAS FNRGGRGGRT TANQDKNLWV HLVQHLKKED LLPGCIFVFS KKRCEENADA
LSNLDYCTAN EKSAIHMIVE KSIARLRIED RQLPQIRRLR DLLARGIAVH HGGLLPIVKE
MVEILFAKSL VKVLFATETF AMGLNLPTRT VVFSGIRKHD GRSFRDLLSG EYIQMAGRAG
RRGLDSSGTV IIVGNGDEAP PAGTLKTMIL GQPTKLQSQF RLTYNMILNL LRVEALKIEE
MIKRSFSENA TQTLLPEHQK MVTANEEGLK NLIREDCVHC NEDLDSLHEA AITYKKLTQE
LHILALKNPQ GKRMYCSGRV VVLQDEDNTR TIGALIRPSQ TTGPNPVIQI LKLTGGNDQK
IPNDSIPFNP IFASVIRQVA GDKIKIKETA VPPSHIEYIS KTVVESRITE ARTGKATVVK
QLLQELKDLG QSLDGSAWAE NDWTKIRDMR FQEVMKGRKA ELQKIKKCKS LSCPNFPKHF
RARNEEYKLQ EKIKNLKQLI SDQNLQLLPD YEQRVRVLKQ LDFIDESSRV QLKGRVACEI
NSANELVLTE LILENTLADF EPEEMVALLS AFVFQEKTDT VPVVPPKLER GKEKILEIAK
RVNEIQSEHQ VLINAETDDF EGRPRFGLME VVYEWAKGMS FERITDLTDV LEGTIVRVIT
RLDETCREVR NAARIIGDPA LYQKAEKCQE MIRRDIISCG SLYF
//
