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Database: UniProt/TrEMBL
Entry: B4PCV0_DROYA
LinkDB: B4PCV0_DROYA
Original site: B4PCV0_DROYA 
ID   B4PCV0_DROYA            Unreviewed;       828 AA.
AC   B4PCV0;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   03-APR-2013, entry version 32.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase;
DE            EC=3.4.19.12;
GN   Name=GE21667; Synonyms=Dyak\GE21667; ORFNames=Dyak_GE21667;
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01;
RX   PubMed=17550304; DOI=10.1371/journal.pbio.0050152;
RA   Ranz J.M., Maurin D., Chan Y.S., von Grotthuss M., Hillier L.W.,
RA   Roote J., Ashburner M., Bergman C.M.;
RT   "Principles of genome evolution in the Drosophila melanogaster species
RT   group.";
RL   PLoS Biol. 5:E152-E152(2007).
CC   -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC       thioester, amide, peptide and isopeptide bonds formed by the C-
CC       terminal Gly of ubiquitin (a 76-residue protein attached to
CC       proteins as an intracellular targeting signal).
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
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DR   EMBL; CM000159; EDW93854.1; -; Genomic_DNA.
DR   RefSeq; XP_002094142.1; XM_002094106.1.
DR   STRING; 7245.FBpp0266677; -.
DR   EnsemblMetazoa; FBtr0268185; FBpp0266677; FBgn0238916.
DR   GeneID; 6533424; -.
DR   KEGG; dya:Dyak_GE21667; -.
DR   FlyBase; FBgn0238916; Dyak\GE21667.
DR   eggNOG; COG5207; -.
DR   KO; K11836; -.
DR   OrthoDB; EOG4NGF2M; -.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR   InterPro; IPR001394; Peptidase_C19.
DR   InterPro; IPR009060; UBA-like.
DR   InterPro; IPR000449; UBA/transl_elong_EF1B_N.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   InterPro; IPR016652; Ubiquitinyl_hydrolase.
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   PIRSF; PIRSF016308; UBP; 1.
DR   SMART; SM00165; UBA; 2.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   SUPFAM; SSF46934; UBA_like; 1.
DR   PROSITE; PS50030; UBA; 2.
DR   PROSITE; PS00972; UCH_2_1; 1.
DR   PROSITE; PS00973; UCH_2_2; 1.
DR   PROSITE; PS50235; UCH_2_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Metal-binding; Protease; Thiol protease;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
SQ   SEQUENCE   828 AA;  92099 MW;  CDAAECD847CB9D7C CRC64;
     MEELRKHLSK VNVPCASGAG SPPIYKDECV YSYDNPETPT GLYVCLHSFL GFGEAYVREY
     ADKTGNRVFL HIQRVKTPKE GADTEAECDP ESEAGPERKI TRLAIGVEGG YNESDMAKKY
     EIKDTYSIVV APQLDKKLPY PDPELPMRVT QAVEAILAAD SAIAKLEKAT LMGTWDGEVR
     QASKYAENLQ QLDNGKKIPP SGWQCEKCDL TNNLWLNLTD GSIMCGRKFF DGSGGNDHAV
     EHYRVTGFPL AVKLGTITAD GKSDVFSYPE DDMVLDPHLE RHLSHFGINM AAMKKSEKSM
     VELELDINQR IGEWSALTES ESELQPLAGP GYTGMRNLGN SCYINSVMQV LFVIPDFQQR
     FVGTGAERYF SEFPSDPAND FNIQMAKLGT GLQSGKYSSI AENTLDTDHS TGISPAMFKN
     IVGKNHPDFS TKQQQDANDF YLHLLTLLDR NSRNQTNPAD ALKFLLEDRV ECLASRKVKY
     KTREEYSFRL PVPLDKATNL DEVREFQERE KAARETGQRL LDRDIVRHKV PLQACLERFF
     GPELIEQFYS TAIDGKTNAR KITRLATMPD CLMIHVGKFT LGDDWVPKKL DVSVDMPDEL
     DLSNWRSTGG LQPGEEALPE PAAEEVKFTF DEAVMSELLT MGFPPEACKR ACFHTKNSGL
     EAASNWLMEH IADEDISEPF VVPNNSIGDS AANQFVANPE SLAMLMSMGF DERQAVAALK
     ATDGNVERAT DWIFSHADSI GVEEVAPASN SSAAAASSAP NKTDYRDGGG KYRLVAFISH
     MGTSAQVGHY VCHIRKKGEW VIFNDSKVAK SQNPPKDLGY LYLYMREQ
//
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