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
//