ID A0A068YBX3_ECHMU Unreviewed; 755 AA.
AC A0A068YBX3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=EmuJ_000837800 {ECO:0000313|EMBL:CDS40779.1};
OS Echinococcus multilocularis (Fox tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX NCBI_TaxID=6211 {ECO:0000313|EMBL:CDS40779.1};
RN [1] {ECO:0000313|EMBL:CDS40779.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23485966; DOI=10.1038/nature12031;
RA Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL Nature 496:57-63(2013).
RN [2] {ECO:0000313|EMBL:CDS40779.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707,
CC ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
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DR EMBL; LN902841; CDS40779.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068YBX3; -.
DR STRING; 6211.A0A068YBX3; -.
DR eggNOG; KOG1870; Eukaryota.
DR OMA; MCIPEAL; -.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF24; USP DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025, ECO:0000313|EMBL:CDS40779.1};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 9..126
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 246..743
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 755 AA; 86020 MW; B2E3D672A298BABD CRC64;
MRKMDDCFHN IGEQQQKYDE YFYDGDIPKL EAVDDERCVI ISKDWFDKWK TYIRRSQTES
DNKVDITGKG DPPGPLDISS ITSDGKLKIN LALRVDVMCI PEALFEKLTN WYGFEGDERA
IPYRKVYVTN DKEPSFDLYP PLLHLRPRRE HKELDLECDS KETIGYVKSY IRNQNNLKSD
VDIHLFDAKN GDKLPDDEKA TLKECSLDGE KDIEYAVVSK SMANGNGLHG LYSCKNFDSF
YPVGVCGLSN LGNTCFMNSA IQCIASVAPL RSYVIANHFE DHINSENKLG SGGNIARAFA
CLMRQMWSEC NRGGTCVPRE LKIQIAKIAP QFAGYQQQDA QELMNFLLDF LHEDLNKVKK
KPPIEAKDAD GRPDKVLAEE AWSNFKKCND SIIVDLFYGL LKSTVTCPEC KLVSITFDPF
NSLSLPLTNV DVVVRFWPSK KYHLPVVPSC RAKDILTSFE RHLPHQDECE YVVTTVYGNR
LKVIPLTSEK SLRFEEVCIF NLTKSSYVQI FLHVDGEAEL PPFLANLRIS QRQFTKKDLI
LAVKVVLSSI SAKYSEMFER FANLEKLKFS PDSEVFDLDD ESCILIGLPE SLEIELNGSP
ARLDVKLDDC IDLFLASEQL GDQDLWYCKK CQQHRQAFKK FDIWSLPQVL VIHLKRYRSV
YRMVKNKAFV DYPETNLKVT CVEGTKVYDL VAVSNHMGFV GGGHYTAYAK NGKTWYSFND
SFVDVLRSSV VTGDAYILVY MLSSISTSPE TINGY
//
