ID A0A024T8M6_9STRA Unreviewed; 1330 AA.
AC A0A024T8M6;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Helicase SKI2W {ECO:0008006|Google:ProtNLM};
GN ORFNames=H310_14725 {ECO:0000313|EMBL:ETV90480.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV90480.1};
RN [1] {ECO:0000313|EMBL:ETV90480.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETV90480.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KI914034; ETV90480.1; -; Genomic_DNA.
DR RefSeq; XP_008880868.1; XM_008882646.1.
DR STRING; 157072.A0A024T8M6; -.
DR EnsemblFungi; H310_14725-t26_1; H310_14725-t26_1-p1; H310_14725.
DR EnsemblProtists; ETV90480; ETV90480; H310_14725.
DR GeneID; 20091775; -.
DR VEuPathDB; FungiDB:H310_14725; -.
DR eggNOG; KOG0947; Eukaryota.
DR OrthoDB; 1352at2759; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0006401; P:RNA catabolic process; IEA:InterPro.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.3380.30; -; 2.
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; IPR025696; MTR4_beta-barrel.
DR InterPro; IPR027417; P-loop_NTPase.
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:SF8; HELICASE SKI2W; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08148; DSHCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF13234; MTR4_beta-barrel; 1.
DR Pfam; PF17911; Ski2_N; 1.
DR PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 2.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 405..563
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 635..834
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 156..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..312
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1330 AA; 146282 MW; DA587B7081A402B4 CRC64;
MDLLDELDQL LAHERESGVL PPSSYVQHLS GYTFQEPLLT PHGKPAHPVC LPLPLLPPPQ
VDDVSVESLL AHAVLDEGSA FLWQGEPSRT LVEVQVSTNP VDIKAVKSSM VMNAMSLTYE
FASVDADGQS MAETSNLMLR KPTQLQDYAR GKIGNTPFTP GGESLVQSSS VSDTTGVSAP
TVKVRSTDSA ATLAIAADWD AHLDAFLVPA PGLGNGLTRT DILRHSSVSP ASTAAEPIAR
DTVGVNPSTL LRPYYDVIAD ADSMHALTRE IADAKALRAM DAAANPALSV QSLLGEDDDD
LEWDDEDDQP PATDSPNEVV PTAKKQTSRD DSPRGDRASD LDDDEAWWMD DIASCGNKAN
TTTTSSSSLE WASVAEIDVS NFYATIPDMA ITFPFELDSF QKQAIVHLEN HECVFIAAHT
SAGKTVVAEY AIAMSQKHMT RTIYTSPIKA LSNQKYRDFR TKFGQDNVGL ITGDVSINPE
ASCLVMTTEI LRSMLYRGAD VIRDIEWVVF DEIHYLNDSE RGVVWEEVII MLPEHVSMVF
LSATTPNTFE FSDWIGRTKQ KKIHVISTFK RPVPLGHHLY AGGEIIPIVD ANNQFLSNSH
MYANQKAKPK EAKGKPPPPP RAAGNSGRGG GDKAEWTKLV RLLQEKTLLP VVVFAFSKRL
CEESANRLAG MDLSSASERS EIHVFCAASI RRLQGSDQKL PQVLQVRDML VRGIGVHHGG
LLPILKEMVE ILFGRGLVKV LFSTETFAMG VNMPARTVVF NGTRKHDGKT FRDLLPGEYT
QMAGRAGRRG LDAIGTVIIA CWGDVPDATS LRTMLLGLPT KLESQFRLTY NMILNLLRVE
DMTVEDMIKR SFSEFRTQKA LASKNIPHAI QKAKRMLARL EDELEQTHGG HMDVDQVQLF
YELSQESKMM EKHLVQMILN SKYAATALCI GRVVVVSTAD LPDAVAIVLQ VNKGTVKSFV
ALALCPPAFS PPVAPTKRLE FQPLTRGSLG GGMSKPVGLK VGDVGSLLGK HYVVLELPES
CVDLLTQDKG STAVRNLLEA NDVSVLSRAI ELLMDVEPKI KYIVDPRADL KMNDLDAVGV
YNTIQNAYSR MQDNICFNSP FLLPVLAQFA KISKLRNYVA AMTAALSNHS LSLFPDFQQR
LQVLTRLGYI AKDNTVQVKG RVACEVNTCE ELILTEIIFE NVLASLEPEE IVSVLSALIF
QEKTQHTTTL TPRLMDAQKT VQAIATSLGL IQLEAQLEID PLEYVKSTLN FGLMEVVYEW
SRGMPFQSIC QLTDVPEGSI VRCMTRLDEV CREVRNAARV IGDPRLYRKM EIASESIKRD
VVFATSLYLS
//
