ID A0A1I8MRJ9_MUSDO Unreviewed; 493 AA.
AC A0A1I8MRJ9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=101897220 {ECO:0000313|EnsemblMetazoa:MDOA007716-PA};
GN Synonyms=LOC101897220 {ECO:0000313|RefSeq:XP_005181587.1};
OS Musca domestica (House fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Musca.
OX NCBI_TaxID=7370 {ECO:0000313|EnsemblMetazoa:MDOA007716-PA};
RN [1] {ECO:0000313|EnsemblMetazoa:MDOA007716-PA}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|EnsemblMetazoa:MDOA007716-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_005181587.1}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|RefSeq:XP_005181587.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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|RuleBase:RU366025}.
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DR RefSeq; XP_005181587.1; XM_005181530.3.
DR STRING; 7370.A0A1I8MRJ9; -.
DR EnsemblMetazoa; MDOA007716-RA; MDOA007716-PA; MDOA007716.
DR GeneID; 101897220; -.
DR KEGG; mde:101897220; -.
DR VEuPathDB; VectorBase:MDOA007716; -.
DR eggNOG; KOG1872; Eukaryota.
DR OrthoDB; 160664at2759; -.
DR Proteomes; UP000095301; Unassembled WGS sequence.
DR Proteomes; UP000694905; Unplaced.
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; IPR029071; Ubiquitin-like_domsf.
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 SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 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 ECO:0000313|RefSeq:XP_005181587.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000694905};
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 104..481
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 493 AA; 55935 MW; C4F0056B908E4C40 CRC64;
MPQFKVKVKW GRELFPDIEV NTDEEPILFK AQLFALTGVA PDRQKVMCKG GILKDDQWNL
QIKEGATILL LGTKEQVPEK PVEQVKFIED MNEAEMATAM EVPAGLTNLG NTCYMNATLQ
CLRAIPELRE ALDNFRVETA DADSMPLAIT SAMKFLFKQM ERTGSTVTPF VLLGTLHRAF
PQFAQTGENG TYRQQDANEC WSELLKMLQQ KLPSSNKKEA EGGEGEKQVK KYNSFIEQYF
GGSFEVKMSC SEAPEEETTT SKENFLQLSC FISPEVKYMH SGLKSKLNET LVKRSESLGR
DANYTRSYLI SRLPAYLTIN FVRFQYKGKE GINAKVLKDI KFPLEFDAFD LCTPDLQNKL
CPVRAKFKEL EDKKLEKQIK DPLAEVKSKE GDEKPKIEYE PYYFEDDVGS NNSGFYTLQA
VLTHKGRSST SGHYVAWVKH TDEVWFKFDD DVVSSVTSEE ILRLSGGGDW HCAYVLLYGP
KLLPKTIEPM DST
//