ID A0A433SL33_ELYCH Unreviewed; 528 AA.
AC A0A433SL33;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=EGW08_022389 {ECO:0000313|EMBL:RUS69850.1};
OS Elysia chlorotica (Eastern emerald elysia) (Sea slug).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Sacoglossa; Placobranchoidea;
OC Plakobranchidae; Elysia.
OX NCBI_TaxID=188477 {ECO:0000313|EMBL:RUS69850.1, ECO:0000313|Proteomes:UP000271974};
RN [1] {ECO:0000313|EMBL:RUS69850.1, ECO:0000313|Proteomes:UP000271974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC2010 {ECO:0000313|EMBL:RUS69850.1};
RC TISSUE=Whole organism of an adult {ECO:0000313|EMBL:RUS69850.1};
RA Cai H., Li Q., Fang X., Li J., Curtis N.E., Altenburger A., Shibata T.,
RA Feng M., Maeda T., Schwartz J.A., Shigenobu S., Lundholm N., Nishiyama T.,
RA Yang H., Hasebe M., Li S., Pierce S.K., Wang J.;
RT "A draft genome assembly of the solar-powered sea slug Elysia chlorotica.";
RL Submitted (JAN-2019) 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. USP14/UBP6 subfamily.
CC {ECO:0000256|ARBA:ARBA00008739}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RUS69850.1}.
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DR EMBL; RQTK01001556; RUS69850.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A433SL33; -.
DR STRING; 188477.A0A433SL33; -.
DR Proteomes; UP000271974; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd02657; Peptidase_C19A; 1.
DR CDD; cd16104; Ubl_USP14_like; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR044635; UBP14-like.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR43982; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR43982:SF1; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 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};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000271974};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 107..499
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 503..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 528 AA; 58443 MW; A2DA96376B1A3704 CRC64;
MPVHKVNVKW GKERFTDVEC NTDEPPELFK AQLFALSGVQ PARQKVMVTG AILKDDDWGP
VKNKLKDGIT LLMMGTADAL PSEPAEKPVF VEDMSEQQLA SALDVPAGLT NLGNTCYMNA
TVQCLKAVPE LKNALKQFTG GLTVAGAIAP ADSITAALRD LYAAMDKTSN PIPPIIFLQI
LHMVFPRFAE KGENGGYQQQ DANECWTEIV RSLQQKLKPI EAPSTPHEPM DTSSSASSAC
VGATASSGFI DQYFGGEFET TMKCNEAPDE GEIHGSEKFL QLSCFIEKEV KYMHTGLQSR
LSETITKNSP TLGRDAIYTK SSKISRLPGY LTIQFVRFFY KEKQSTNAKI LKDIKFPLML
DVFDLCSSNL QQKLVPMREK FKALEDKKVE LAQGSKSSLQ DKGKKVVIKK DDKDVKYEPY
SFPDDVGSNN SGYYELSAVL THKGRSSSSG HYVGWVRKKG DEWLMFDDDR VTAVPAEDIL
KLSGGGDWHC AYVLLYAPRR LEEDSTVDQQ ADTKPVAAEP TQQTQQQS
//
