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Database: UniProt
Entry: D7GYM9_TRICA
LinkDB: D7GYM9_TRICA
Original site: D7GYM9_TRICA 
ID   D7GYM9_TRICA            Unreviewed;      1048 AA.
AC   D7GYM9;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 2.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE            EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
GN   Name=AUGUSTUS-3.0.2_16332 {ECO:0000313|EMBL:EFA13472.2};
GN   ORFNames=TcasGA2_TC016332 {ECO:0000313|EMBL:EFA13472.2};
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:EFA13472.2, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:EFA13472.2, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA13472.2,
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:EFA13472.2, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA13472.2,
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; KQ973093; EFA13472.2; -; Genomic_DNA.
DR   AlphaFoldDB; D7GYM9; -.
DR   STRING; 7070.D7GYM9; -.
DR   EnsemblMetazoa; TC016332_001; TC016332_001; TC016332.
DR   eggNOG; KOG0017; Eukaryota.
DR   HOGENOM; CLU_000384_9_3_1; -.
DR   InParanoid; D7GYM9; -.
DR   OMA; AIMCHEN; -.
DR   Proteomes; UP000007266; Unassembled WGS sequence.
DR   GO; GO:0042575; C:DNA polymerase complex; IEA:UniProt.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd09274; RNase_HI_RT_Ty3; 1.
DR   CDD; cd06094; RP_Saci_like; 1.
DR   CDD; cd01647; RT_LTR; 1.
DR   Gene3D; 1.10.340.70; -; 1.
DR   Gene3D; 3.30.70.270; -; 2.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR041588; Integrase_H2C2.
DR   InterPro; IPR001995; Peptidase_A2_cat.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR034132; RP_Saci-like.
DR   InterPro; IPR000477; RT_dom.
DR   InterPro; IPR041577; RT_RNaseH_2.
DR   PANTHER; PTHR37984:SF7; INTEGRASE CATALYTIC DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR37984; PROTEIN CBG26694; 1.
DR   Pfam; PF17921; Integrase_H2C2; 1.
DR   Pfam; PF17919; RT_RNaseH_2; 1.
DR   Pfam; PF00665; rve; 1.
DR   Pfam; PF00078; RVT_1; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW   RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022918};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transposable element {ECO:0000256|ARBA:ARBA00022464}.
FT   DOMAIN          41..114
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000259|PROSITE:PS50175"
FT   DOMAIN          744..911
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
FT   REGION          1014..1048
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1027..1048
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1048 AA;  119188 MW;  06191FAE0BD6D4D3 CRC64;
     MSAPLQFPAG KLIAPSPIEA MGDGLEHRTH RLFITDPPSN IRFLIDTGAE VSVLPKCFAT
     NSATPGENVL FAANNTPIRT YGTRRLTLSL GLRRAFRWEF VVAGIAKPIL GADFLNFHNL
     LPDLRNRKLV DATTQLHTRG VVAAGQSEVI TTVARTTPYH ELLAAYPEIT RPHTPKPKSQ
     STVRHHIFTQ GPPVAETPRR LSPEKMKVAR AEFEFMSEQG WCRPSNSPWA SPLHLVPKKV
     PGQWRACGDY RKLNSITVPD RYPIPHVQDF AYKLQGKKVF STIDLVRAYQ QIAVADEDIP
     KTAVCTPFGL FEFTVMCFGL RNAAQTFQRH VNAVLGDLDF CHAYIDDILI ASESPEEHKQ
     HLKEVFERLR QHNLVVNPAK CVFGVEEVEY LGHRITPSGC QPLPKKVEAV TNFPKPNTVK
     ELRQFLGMIN FYRRFVKNAA QIQTPLLEYL KNATKNDKRK IEWTPQAEAA FSLCKLELAN
     AALLAHPMEA GALTLTTDAS DNAVGAVLEQ KTEGTWQPLG FFSKKLNQAQ RNYSTYDREL
     LAIYEAIKHF RYMVEGRQFV IRTDHKPLIY AFQQKPDKAS PRQLRHLDFI GQFSTEVVHI
     AGESNAVADA LSRIDEIVTP TALSPEELQA EQETDPELKD LLKSTTTSLR LKKCTPVGTT
     ASFYCDTSTQ FVRPYVPFRL RKAAFKLFHE PAHSGVRATS RAIRQKFVWP RMDDDVKRWT
     RVCIPCQRSK VTKHTRTELK KFNVTGTRFE HVHIDIVGPL PEAEGHRYCL TMTDRFTRWP
     EVTPMRDMSA ETVARTFYST WIARFGCPLR ITTDQGRQFE SHLMTAVSNL FGIKRCRTTA
     YRPQCNGIIE RWHRTIKAAI MCHENPNWLT ILPTILLGLR TALKQDLQCS PAEMTYGSQL
     RIPGEFFFSA QTDDGYEDPA TFVGLLKEHM RKLQPVPATA HDKRKVFVHQ ELQRCSHVFL
     REDAVKRPLQ QPYTGPYEVL ERRENNVKID VNGKAVLVHL DRLKPAFLAQ DVAEPQPPQT
     VPFSASRASR EDKRSTRPPI RFRDYIPH
//
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