ID A0A1I8N765_MUSDO Unreviewed; 1127 AA.
AC A0A1I8N765;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 36 {ECO:0000256|ARBA:ARBA00039432};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE AltName: Full=Deubiquitinating enzyme 36 {ECO:0000256|ARBA:ARBA00042420};
DE AltName: Full=Protein scrawny {ECO:0000256|ARBA:ARBA00042154};
DE AltName: Full=Ubiquitin thioesterase 36 {ECO:0000256|ARBA:ARBA00041300};
DE AltName: Full=Ubiquitin-specific-processing protease 36 {ECO:0000256|ARBA:ARBA00043009};
GN Name=101899882 {ECO:0000313|EnsemblMetazoa:MDOA012268-PB};
GN Synonyms=LOC101899882 {ECO:0000313|RefSeq:XP_005189063.1};
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:MDOA012268-PB};
RN [1] {ECO:0000313|EnsemblMetazoa:MDOA012268-PB}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|EnsemblMetazoa:MDOA012268-PB};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_005189063.1}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|RefSeq:XP_005189063.1};
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};
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DR RefSeq; XP_005189063.1; XM_005189006.3.
DR EnsemblMetazoa; MDOA012268-RB; MDOA012268-PB; MDOA012268.
DR GeneID; 101899882; -.
DR VEuPathDB; VectorBase:MDOA012268; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000095301; Unassembled WGS sequence.
DR Proteomes; UP000694905; Unplaced.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
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; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF758; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 36; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|RefSeq:XP_005189063.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000694905}.
FT DOMAIN 185..489
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 34..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1049
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1127 AA; 122899 MW; D55979936AA4C613 CRC64;
MPVSVVCETT ANVNAALREE LFGSATGCSA AANNKAPDEL KTNGSSVLGT DDNDSLHDKL
VASAKRVLLS KIEYEEVTNY GQSVLESLKS KYIVLKPSTG INNGQENGRK SPATCNNNNN
GANGDDSAAG KHANGNTSAA TTTPGKRNQQ PQSPNELPAP KRVLFPRENV RIGWKATGRK
WNVGVGMMNV GNTCYLNSTL QALFHVSSMA NWLMSDSAHM ERCESTDSGC IICAMAKTLQ
ASQNSQSAIR PYFVYSKLKS ICKHLVMGRQ EDAHEFLRYL VEAMEKSYLQ RFRNYKELDQ
YSKETTPLNQ ILGGYLKTSV KCLSCQHVSV TFQHFQDLLL DIRKADTINE ALEGYFARER
LEDMGYKCEA CKKKVSATKQ FSLDRAPIAL CIQLKRFSIS GTKINKQITI KPRLDLTKFA
SRKIPGEQLT YRLVAMVTHL GASQHCGHYT AIGLTESGTY YNYDDSYVRP ISMQNVCNTN
AYIIFYEMDT QPARQVTSTQ VSGAVAQSTV TNLKDLQTTK VNGHVVNSSP QRIIGPQLPP
GYSNGTSSPL TNGGGSKLII NRNATNPSKN TTGLDSSKIM IHFKNNNGGT PSSPSVKTSL
ATSSLTSASA TSSTTSTAAS NSVFDSLKSN SNSNGLHVVG TGKFQESANT KRALGDPANK
RQVNTVKNGN ESSSDDDDDE NEVVSSSTST LPSMPKLISA EVNSTTTNNT KAPLTNGFAK
SPAPVVAIKS LVPYVWESDD ETDVATPITT NGIMSTSSTS SSSDKTPLMS NPLKRRQSSS
SWSNAAGSSS SDNDDDNDND CKPTTGTKIK KAASSTTVTS AEATGSSSVH YNGISSKKSS
ETIDEIFNKR STLATSNYLS PLKKKSQNQQ FTVTSTTPTS DTSSSDSEDI KSVPSKPQFK
RSNSTPPSPP VVKTNSGIWQ VTSLHPISAC VSPTTEKLPK NPKNPFASAK SLHNNAVGEN
SKRLKKENAG KQNFVGNGYQ RETATDTTVS ELLKQSHRGY GAPVLTWNGQ QSEIEREIIT
DAREQRQRDW EDDEENEMDR GRQKKVKAPR DPYANAPTPG YNPFQEQENQ KRWKRYHHTG
GSGGGFRQNF HRNKFKFQRF PHKFVRKNMI STGGGYNSNN THRRNDS
//
