ID   D1ZZA3_TRICA            Unreviewed;      1241 AA.
AC   D1ZZA3;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   12-OCT-2022, entry version 73.
DE   SubName: Full=Dosage compensation regulator-like Protein {ECO:0000313|EMBL:EFA01881.1};
GN   Name=AUGUSTUS-3.0.2_07486 {ECO:0000313|EMBL:EFA01881.1};
GN   ORFNames=TcasGA2_TC007486 {ECO:0000313|EMBL:EFA01881.1};
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:EFA01881.1, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:EFA01881.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA01881.1,
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:EFA01881.1, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA01881.1,
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; KQ971338; EFA01881.1; -; Genomic_DNA.
DR   RefSeq; XP_008192026.1; XM_008193804.2.
DR   STRING; 7070.TC007486-PA; -.
DR   EnsemblMetazoa; TC007486_001; TC007486_001; TC007486.
DR   GeneID; 657645; -.
DR   KEGG; tca:657645; -.
DR   eggNOG; KOG0920; Eukaryota.
DR   HOGENOM; CLU_001832_4_1_1; -.
DR   InParanoid; D1ZZA3; -.
DR   OMA; PKCRFAH; -.
DR   OrthoDB; 278674at2759; -.
DR   PhylomeDB; D1ZZA3; -.
DR   Proteomes; UP000007266; Linkage group 4.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   Gene3D; 3.10.110.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006575; RWD-domain.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   InterPro; IPR041367; Znf-CCCH_4.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF04408; HA2; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   Pfam; PF05773; RWD; 1.
DR   Pfam; PF18044; zf-CCCH_4; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00165; UBA; 1.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   SUPFAM; SSF90229; SSF90229; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50030; UBA; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}.
FT   DOMAIN          104..149
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          226..253
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          428..597
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          691..870
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   ZN_FING         226..253
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
SQ   SEQUENCE   1241 AA;  142558 MW;  362A67ADC0041130 CRC64;
     MSGEDTINKS DFFLKDIPNV KIGNVSKAPK KNVVKEQLQF LHFNEEMQEQ ILETLRFIHG
     PDFVLKDASD YKDVKTNLGK KYWLGQSNLI IKGACDFSKI EDETYEEDRL KQFALMRLES
     YGFHLNHCIE ALKYCEGNVE DALYVLYNKY FNSGELKITD IDLSKNELLE QRMDEKSSLE
     SIYDKTFQEK VQNAVWILTL KLDYLIKIFH NKNKSKKPAK TVQNTAKKKE KCRNFITGNC
     KWGDKCRFSH EKEVIEKDPN AHLTDFNFEL EIRFPYNTKY PYEPPLILLK TNAVLPPLMN
     LHICKRLYEE AKLLAEDGIP SVYTITELLT NEEEIKSYVE TTEIDFIAPN VPLFRDEKLN
     VPKKKRPSHY IKGITNRDNQ KILTPEEIRG VDEKIVAKFK SLVKDKKYLE MLQYRKKLPA
     WGLMNDILNT IQQSQVVVIS GETGCGKSTQ VPQYILDDWL VNYANDRKHV EIVCTQPRRI
     SAISVAERVA EERVAKIGNT VGYQIRLESK VSVNTRLTFC TTGILLRRLE SEPTLPQVTH
     IIVDEVHERS EQSDFLLLIL KQILPFRPDL KVILMSATLN AQLFSDYFGE IPILTIPGRT
     FPVEQYFLET IFEKTGYVLE DGTEYARKLK DAEFIENELS LLNAGRHMTP NDNLRDENLK
     FAQLLCRYKE CSFRTCKNLL LMDPEVVNNE LIETVLTWIV SGEHNYPRKG TILVFLPGIA
     EITSLYDQLA VHPEFGTRSQ KYLVLPLHSS LSSEEQAMIF MKPKNLRKII LSTNIAETSV
     TIDDCVFVID SGRMREKHFD PNRNMESLET VWVTRANALQ RKGRAGRVMA GVCFHLYTSN
     RFRHQMLPQP IPEIHRIPLE QLILNIKILQ NFEDRDVCDV IDGLIEPPLK EHVETAIVRL
     QDVGALDTEK QLTPLGHHLA ALPVDVRIGK LLLYGAIFSC VDSALTMAAC LSNKSPFVTP
     FRKRDEANEK KKKFAVGYSD HITVLMAYKK WQSVYKKSSL AGRNFANENF LSQKTLVTIA
     DIKHQFLEYL VDIGFIAANL DGKRRSGDDD VLAITGNEFN RNGENFNVLA AILCAALYPN
     VIKVLTPPKS YVKTAGGAIP KDNEAKDFQF QTVKETVFLH PSSVNFSAKN FPSPYLVYQE
     KVKTSKVYFR DCTVIPVISL VLFSGFDLDI SVNNGCTFIS LERGWIMFQV EEHKIAEMIK
     MLRSELFMLL EEKIKDPLLN IWHHDKGERI ITTILNLINL K
//