ID A0A093CGD4_9AVES Unreviewed; 656 AA.
AC A0A093CGD4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
DE Flags: Fragment;
GN ORFNames=N339_02657 {ECO:0000313|EMBL:KFV14940.1};
OS Pterocles gutturalis (yellow-throated sandgrouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Ciconiiformes; Pteroclidae; Pterocles.
OX NCBI_TaxID=240206 {ECO:0000313|EMBL:KFV14940.1, ECO:0000313|Proteomes:UP000053149};
RN [1] {ECO:0000313|EMBL:KFV14940.1, ECO:0000313|Proteomes:UP000053149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N339 {ECO:0000313|EMBL:KFV14940.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL246135; KFV14940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093CGD4; -.
DR Proteomes; UP000053149; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03772; MATH_HAUSP; 1.
DR CDD; cd02659; peptidase_C19C; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF644; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7; 1.
DR Pfam; PF00917; MATH; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50144; MATH; 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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000053149};
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 42..169
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 188..495
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV14940.1"
FT NON_TER 656
FT /evidence="ECO:0000313|EMBL:KFV14940.1"
SQ SEQUENCE 656 AA; 75733 MW; FE869AA3AC8093E5 CRC64;
AGDTDDPPRI TQNPVINGNV AMADGHNNTE EDMEDDTSWR SEATFQFTVE RFNRLSESVL
SPPCFVRNLP WKIMVMPRLY PDRPHQKSVG FFLQCNAESD STSWSCHAQA VLKIINYKDD
EKSFSRRISH LFFHKENDWG FSNFMAWSEV TDPEKGFIEE DKVTFEVYVQ ADAPHGVAWD
SKKHTGYVGL KNQGATCYMN SLLQTLFFTN QLRKAVYMMP TEGDDSSKSV PLALQRVFYE
LQHSDKPVGT KKLTKSFGWE TLDSFMQHDV QELCRVLLDN VENKMKGTCV EGTIPKLFRG
KMVSYIQCKH VDYRSERIED YYDIQLSIKG KKNIFESFID YVAVEQLDGD NKYDAGEHGL
QEAEKGVKFL TLPPVLHLQL MRFMYDPQTD QNIKINDRFE FPEQLPLDEF LQKTDPKDPA
NYILHAVLVH SGDNHGGHYV VYLNPKGDGK WCKFDDDVVS RCTKEEAIEH NYGGHDDDLS
VRHCTNAYML VYIRESKLSE VLQPVTDHDI PQQLVERLQE EKRIEAQKRK ERQEAHLYMQ
VQIVAEDQFC GHQGNDMYDE EKVKYTVFKV LKNSTLTEFV QNLSQTMGFP QDQIRLWPMQ
ARSNGTKRPA MLDNEADGNK TMIELSDNEN PWTIFLETVD PEMAATGATL PKFDKD
//
