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Database: UniProt
Entry: A0A139WFJ1_TRICA
LinkDB: A0A139WFJ1_TRICA
Original site: A0A139WFJ1_TRICA 
ID   A0A139WFJ1_TRICA        Unreviewed;      1209 AA.
AC   A0A139WFJ1;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Helicase SKI2W-like Protein {ECO:0000313|EMBL:KYB26733.1};
GN   Name=AUGUSTUS-3.0.2_33645 {ECO:0000313|EMBL:KYB26733.1};
GN   ORFNames=TcasGA2_TC033645 {ECO:0000313|EMBL:KYB26733.1};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:KYB26733.1, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:KYB26733.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:KYB26733.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=18362917; DOI=10.1038/nature06784;
RG   Tribolium Genome Sequencing Consortium;
RA   Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA   Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA   Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA   Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA   Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA   Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA   Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA   Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA   Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA   Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA   Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA   Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA   Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA   Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA   Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA   Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA   Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA   Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA   Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA   Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA   Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA   Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA   Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA   Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA   Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA   Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA   Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA   Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA   Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA   Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA   Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA   Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA   Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA   Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA   Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA   Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA   Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA   Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA   Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA   Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA   Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT   "The genome of the model beetle and pest Tribolium castaneum.";
RL   Nature 452:949-955(2008).
RN   [2] {ECO:0000313|EMBL:KYB26733.1, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:KYB26733.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=19820115; DOI=10.1093/nar/gkp807;
RA   Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA   Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT   "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT   for Tribolium castaneum.";
RL   Nucleic Acids Res. 38:D437-D442(2010).
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DR   EMBL; KQ971352; KYB26733.1; -; Genomic_DNA.
DR   RefSeq; XP_008195520.1; XM_008197298.2.
DR   AlphaFoldDB; A0A139WFJ1; -.
DR   STRING; 7070.A0A139WFJ1; -.
DR   EnsemblMetazoa; TC033645_001; TC033645_001; TC033645.
DR   GeneID; 659256; -.
DR   KEGG; tca:659256; -.
DR   eggNOG; KOG0947; Eukaryota.
DR   InParanoid; A0A139WFJ1; -.
DR   OMA; CGSDITR; -.
DR   OrthoDB; 1352at2759; -.
DR   Proteomes; UP000007266; Linkage group 7.
DR   GO; GO:0055087; C:Ski complex; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0070478; P:nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay; IBA:GO_Central.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 1.10.3380.30; -; 1.
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; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KYB26733.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          279..435
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          543..716
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   COILED          730..757
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1094..1121
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1209 AA;  138215 MW;  C95535D85B3EA5C3 CRC64;
     MSDVNIDIEP PPILPDITDE LRDYLICPER LPIHRYETNQ EFWPRTPDLK ELLFFEESPL
     CTTLKVQRDP NTGEIIEFRE IPIQSAGANA TNSMSLTRQP APPSEATRGN ASFIPFWPAS
     FPDPVSQLPK QELLDTELLT VPPGFTRGIV FASDGRTVLS KETPREKESV EVPANVVNLF
     EIIQEDPNFF GTLENANIKK PDDISEHKQR ETLPEEEEVL PNDPPILKIS TVPPPTEFKS
     TEWAILLDTS KPVKDFKERI PEMAYEFPFE LDTFQKLAIL QLEQHNHVFV AAHTSAGKTV
     VAEYAIALSQ KHMTRTIYTS PIKALSNQKY RDFKKEFKDV GLITGDFQIN QTASCLIMTT
     EILRSMLYCG SDITRDLEYV IFDEVHYIND RERGHVWEQV LILLPAHVCV VLLSATVPNT
     IEFADWLGRT HQRKVYVITT YKRPVPLLHF LYTGTGGASR DNRYLVLNSE GWKMGGYAAA
     VASLPKVDPK SAYPQAKSQY YNFTPKQEKV LWNGLVDHLN RKNLLPIVAF TFSRAKCDQN
     AENLMSLDLT TQKEKAQIHM FFEKCVRSLK EPDRNIPQIL RMRNILHKGI GVHHSGVLPI
     IKEIVEMLFQ KGLIKLLFAT ETFAMGVNMP ARTVVFDSIT KHDGQERRNL KPAEYIQMAG
     RAGRRGLDSE GTVIILCKNK IPKVEELQAM MLGTPNVLQS QFRLTYGMVL SLLRVESLSV
     EGMMSRSFRE ADHQKKMVDK QNELLEVEKE IRDLCTQELS SYLQPLVKFY NCASSYLEAR
     KKCLDNVMSS PKLIKVLTPG RIILITHKSH VNKLALLLSI VRGKKPTYKV LVLTDSKPEI
     KEEKNDLWYK MIGLASDNIY APGSSPGHAI LTIPTEDIFE ITHKTVKVDT DLVIKDWEKR
     QIERFRNDPV GQTCQQAIQE LHKFTISVNE AKNQEKLSYL HLIQDLKVNE HQIHDDLQVV
     YKFKDILIDH LPSTQIPNFE QQFASVFTRT FLERKRDDLK HYLSSASLSL YPDYENRIEL
     LRTLKYVDLQ NRVQLKGRVA CEMGMNELLI TELVLRNILT KLQPAEVAAL LSALVFSPKK
     DNREEETVHI TDDLTKAMKE MQNIHQEIAK LEMNLDIKTD EFQNDLNFAL IEIVYEWASA
     KPFADIMCLT DIQEGIIVRC IQQLNDTICD VRNAARIIGD PELQNKMEEA SAAIKRDIVF
     AASLYTNDL
//
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