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Database: UniProt
Entry: A0A1A9W3D5_9MUSC
LinkDB: A0A1A9W3D5_9MUSC
Original site: A0A1A9W3D5_9MUSC 
ID   A0A1A9W3D5_9MUSC        Unreviewed;       487 AA.
AC   A0A1A9W3D5;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   18-SEP-2019, entry version 16.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
OS   Glossina brevipalpis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Hippoboscoidea; Glossinidae; Glossina.
OX   NCBI_TaxID=37001 {ECO:0000313|Proteomes:UP000091820, ECO:0000313|VectorBase:GBRI004981-PA};
RN   [1] {ECO:0000313|Proteomes:UP000091820, ECO:0000313|VectorBase:GBRI004981-PA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAEA {ECO:0000313|Proteomes:UP000091820,
RC   ECO:0000313|VectorBase:GBRI004981-PA};
RA   Aksoy S., Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|VectorBase:GBRI004981-PA}
RP   IDENTIFICATION.
RC   STRAIN=IAEA {ECO:0000313|VectorBase:GBRI004981-PA};
RG   VectorBase;
RL   Submitted (JUL-2016) to UniProtKB.
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|RuleBase:RU366025,
CC         ECO:0000256|SAAS:SAAS01117307};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|RuleBase:RU366025, ECO:0000256|SAAS:SAAS01045498}.
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DR   VectorBase; GBRI004981-RA; GBRI004981-PA; GBRI004981.
DR   Proteomes; UP000091820; Unassembled WGS sequence.
DR   GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016579; P:protein deubiquitination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
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   Complete proteome {ECO:0000313|Proteomes:UP000091820};
KW   Hydrolase {ECO:0000256|RuleBase:RU366025,
KW   ECO:0000256|SAAS:SAAS01044238};
KW   Metal-binding {ECO:0000256|SAAS:SAAS01044152};
KW   Protease {ECO:0000256|RuleBase:RU366025,
KW   ECO:0000256|SAAS:SAAS01044292};
KW   Reference proteome {ECO:0000313|Proteomes:UP000091820};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025,
KW   ECO:0000256|SAAS:SAAS01044269};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025,
KW   ECO:0000256|SAAS:SAAS01044331}; Zinc {ECO:0000256|SAAS:SAAS01044373};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS01044352}.
FT   DOMAIN       44    103       UBP-type. {ECO:0000259|PROSITE:PS50271}.
FT   DOMAIN      158    482       USP. {ECO:0000259|PROSITE:PS50235}.
FT   ZN_FING      44    103       UBP-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00502}.
SQ   SEQUENCE   487 AA;  55428 MW;  CDDC1C5E3B09CAEA CRC64;
     MAENGCKHFQ VYVKENSLDT YRIIDAYFSA CINRDAREKK ALNCCCFECG SFGLQIFACL
     HCIYFGCRGS HITSHLRAKK HSIALELSHG TLYCNSCRDF IYDSRCREIA SVNRKLEAKD
     VQKSLSWTPW IPTPKETNLM LANPRRRHVK ANETLGLRGL INLGSTCFMN CIVQALIHTP
     LLSDYFLSER HECNAKSSLK CLVCEVSRLF QEFYSGLRTP LSLHRLLHLI WNHAKHLAGY
     EQQDAHEFFI ATLDVLHRHC IKAKAETENA NKSSSSAQHT NCPTQCNCII DQIFTGMLQS
     DVVCQSCKGV STTIDPFWDI SLDLGETAHG GATPKSLIDC LERYTRAEHL GSSAKIKCST
     CKSYQESTKQ FSLRTLPSVA SFHLKRFEHS SLIDKKISTF ISFPVEFDMT PFMSDKNNAY
     GDFRYSLYAV VNHVGTIDAG HYTAYVRHHK DTWVKCDDHI ITTATLKQVL DSEGYLLFYH
     KNILEYE
//
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