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Database: UniProt
Entry: A0A1I8MRJ9_MUSDO
LinkDB: A0A1I8MRJ9_MUSDO
Original site: A0A1I8MRJ9_MUSDO 
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
//
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