GenomeNet

Database: UniProt
Entry: D6WG65_TRICA
LinkDB: D6WG65_TRICA
Original site: D6WG65_TRICA 
ID   D6WG65_TRICA            Unreviewed;       794 AA.
AC   D6WG65;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 68.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|PIRNR:PIRNR016308};
DE            EC=3.4.19.12 {ECO:0000256|PIRNR:PIRNR016308};
GN   ORFNames=TcasGA2_TC003401 {ECO:0000313|EMBL:EFA00536.1};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Coleoptera; Polyphaga;
OC   Cucujiformia; Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:EFA00536.1, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:EFA00536.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA00536.1,
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.,
RA   Friedrich M., Grimmelikhuijzen C.J., Klingler M., Lorenzen M.,
RA   Richards S., Roth S., Schroder R., Tautz D., Zdobnov E.M., Muzny D.,
RA   Gibbs R.A., Weinstock G.M., Attaway T., Bell S., Buhay C.J.,
RA   Chandrabose M.N., Chavez D., Clerk-Blankenburg K.P., Cree A., Dao M.,
RA   Davis C., Chacko J., Dinh H., Dugan-Rocha S., Fowler G., Garner T.T.,
RA   Garnes J., Gnirke A., Hawes A., Hernandez J., Hines S., Holder M.,
RA   Hume J., Jhangiani S.N., Joshi V., Khan Z.M., Jackson L., Kovar C.,
RA   Kowis A., Lee S., Lewis L.R., Margolis J., Morgan M., Nazareth L.V.,
RA   Nguyen N., Okwuonu G., Parker D., Richards S., Ruiz S.J.,
RA   Santibanez J., Savard J., Scherer S.E., Schneider B., Sodergren E.,
RA   Tautz D., Vattahil S., Villasana D., White C.S., Wright R., Park Y.,
RA   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.,
RA   Brown S.J., Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H.,
RA   Lorenzen M., Maselli V., Osanai M., Park Y., Robertson H.M., Tu Z.,
RA   Wang J.J., Wang S., Richards S., Song H., Zhang L., Sodergren E.,
RA   Werner D., Stanke M., Morgenstern B., Solovyev V., Kosarev P.,
RA   Brown G., Chen H.C., Ermolaeva O., Hlavina W., Kapustin Y.,
RA   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.,
RA   Aranda M., Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F.,
RA   Bopp D., Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E.,
RA   Ferrier D.E., Friedrich M., Gordon C.M., Jindra M., Klingler M.,
RA   Lan Q., Lattorff H.M., Laudet V., von Levetsow C., Liu Z., Lutz R.,
RA   Lynch J.A., da Fonseca R.N., Posnien N., Reuter R., Roth S.,
RA   Savard J., Schinko J.B., Schmitt C., Schoppmeier M., Schroder R.,
RA   Shippy T.D., Simonnet F., Marques-Souza H., Tautz D., Tomoyasu Y.,
RA   Trauner J., Van der Zee M., Vervoort M., Wittkopp N., Wimmer E.A.,
RA   Yang X., Jones A.K., Sattelle D.B., Ebert P.R., Nelson D., Scott J.G.,
RA   Beeman R.W., Muthukrishnan S., Kramer K.J., Arakane Y., Beeman R.W.,
RA   Zhu Q., Hogenkamp D., Dixit R., Oppert B., Jiang H., Zou Z.,
RA   Marshall J., Elpidina E., Vinokurov K., Oppert C., Zou Z., Evans J.,
RA   Lu Z., Zhao P., Sumathipala N., Altincicek B., Vilcinskas A.,
RA   Williams M., Hultmark D., Hetru C., Jiang H., Grimmelikhuijzen C.J.,
RA   Hauser F., Cazzamali G., Williamson M., Park Y., Li B., Tanaka Y.,
RA   Predel R., Neupert S., Schachtner J., Verleyen P., Raible F., Bork P.,
RA   Friedrich M., Walden K.K., Robertson H.M., Angeli S., Foret S.,
RA   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:EFA00536.1, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA00536.1,
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
RT   information for Tribolium castaneum.";
RL   Nucleic Acids Res. 38:D437-D442(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide,
CC         peptide and isopeptide bonds formed by the C-terminal Gly of
CC         ubiquitin (a 76-residue protein attached to proteins as an
CC         intracellular targeting signal).; EC=3.4.19.12;
CC         Evidence={ECO:0000256|PIRNR:PIRNR016308,
CC         ECO:0000256|SAAS:SAAS01117307};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|SAAS:SAAS01045498}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; KQ971320; EFA00536.1; -; Genomic_DNA.
DR   RefSeq; XP_967156.1; XM_962063.3.
DR   STRING; 7070.TC003401-PA; -.
DR   MEROPS; C19.084; -.
DR   EnsemblMetazoa; TC003401_001; TC003401_001; TC003401.
DR   GeneID; 655510; -.
DR   KEGG; tca:655510; -.
DR   eggNOG; KOG0944; Eukaryota.
DR   eggNOG; COG5207; LUCA.
DR   InParanoid; D6WG65; -.
DR   KO; K11836; -.
DR   OMA; QYVERHY; -.
DR   OrthoDB; 556111at2759; -.
DR   PhylomeDB; D6WG65; -.
DR   Proteomes; UP000007266; Linkage group 3.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 2.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR016652; Ubiquitinyl_hydrolase.
DR   InterPro; IPR041432; UBP13_Znf-UBP_var.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   Pfam; PF00627; UBA; 2.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   Pfam; PF17807; zf-UBP_var; 1.
DR   PIRSF; PIRSF016308; UBP; 1.
DR   SMART; SM00165; UBA; 2.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS50030; UBA; 2.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007266};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR016308,
KW   ECO:0000256|SAAS:SAAS01044238, ECO:0000313|EMBL:EFA00536.1};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR016308,
KW   ECO:0000256|PIRSR:PIRSR016308-3, ECO:0000256|SAAS:SAAS01044152};
KW   Protease {ECO:0000256|PIRNR:PIRNR016308,
KW   ECO:0000256|SAAS:SAAS01044292};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW   Thiol protease {ECO:0000256|PIRNR:PIRNR016308,
KW   ECO:0000256|SAAS:SAAS01044269};
KW   Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR016308,
KW   ECO:0000256|SAAS:SAAS01044331};
KW   Zinc {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|PIRSR:PIRSR016308-3,
KW   ECO:0000256|SAAS:SAAS01044373};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS01044352}.
FT   DOMAIN      190    263       UBP-type. {ECO:0000259|PROSITE:PS50271}.
FT   DOMAIN      320    794       USP. {ECO:0000259|PROSITE:PS50235}.
FT   DOMAIN      615    656       UBA. {ECO:0000259|PROSITE:PS50030}.
FT   DOMAIN      677    717       UBA. {ECO:0000259|PROSITE:PS50030}.
FT   ZN_FING     190    263       UBP-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00502}.
FT   COILED      280    307       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    329    329       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR016308-1}.
FT   ACT_SITE    756    756       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR016308-1}.
FT   METAL       192    192       Zinc. {ECO:0000256|PIRSR:PIRSR016308-3}.
FT   METAL       195    195       Zinc. {ECO:0000256|PIRSR:PIRSR016308-3}.
FT   METAL       212    212       Zinc. {ECO:0000256|PIRSR:PIRSR016308-3}.
FT   METAL       225    225       Zinc. {ECO:0000256|PIRSR:PIRSR016308-3}.
SQ   SEQUENCE   794 AA;  88512 MW;  0BB2FE85DF14F8FB CRC64;
     MELLTPHLSS VRVPTATSKV YKDECVFSFD NPETETGLYV GLKSFFGLGR DYVEKHFHKT
     GEAVYLHIRR VRHEVSSPPQ GDGPEKKITR LAIGVDGGFD PEAMSKKFEF EDSYNIVVLP
     GFSTIPWPNT ELPQIVKSSI EGILEAPSAS KVAEMEALTG TWDGEARVVS QFAHNLPQLD
     NGKKIPPSGW QCEKCDKTDN LWLNLTDGSI LCGRRFYDGS GGNNHAIEHY NATGHPLAVK
     LGTITKEGKG DVFSYKEDDM VEDPNLVQHL AHWGINIANM EKTEKSMVEL ELELNQKSNE
     WSALQESDGQ LKPIYGPGYT GMTNMGNSCY LNSVMQMVFS IPDFIQRYYH DAELFFNNVV
     GDPCEDFNAQ MAKLAVGLHS GKYSVPPPAG SPVDADPPGI CPLMFKALVG RGHPEFSTKK
     QQDAQEFFLH ILTLLERNSK NKVNPGDCFK FKVEEKFQCS ASKKVKYLTR SDVLLPLIIP
     MDAAINKDEV AAYETKKLEA EKTGKKLLAN TIVRPKINFL SCLELFTQSE VINNFYSSAV
     NANVTARKTT RLATFPDYLC IQLKKFMLRE DWVPIKLDVS IEMPDILDIS SLRGTGPQSD
     EELLPEPKVQ PPAPVMDEGV LAQLADMGFP PEACKRAVFF THNSGLEAAT AWIMEHITDS
     DFSDPFVPPG TESSHFTPNA EALASIVAMG FTQHQATKAL KATDNNVERA MDWIFSHQDE
     LDNVTSPPPP EFRDGDGRYK LVAFVSHMGT STMVGHYVVH ILKNGQWVIF NDNKVALSER
     PPKDLGYMYL YERL
//
DBGET integrated database retrieval system