ID A0A0A0ABS0_CHAVO Unreviewed; 1078 AA.
AC A0A0A0ABS0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 7 {ECO:0000256|ARBA:ARBA00021393};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE AltName: Full=Ubiquitin thioesterase 7 {ECO:0000256|ARBA:ARBA00031508};
DE AltName: Full=Ubiquitin-specific-processing protease 7 {ECO:0000256|ARBA:ARBA00031500};
DE Flags: Fragment;
GN ORFNames=N301_14895 {ECO:0000313|EMBL:KGL91541.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL91541.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL91541.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL91541.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-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 -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; KL871254; KGL91541.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0ABS0; -.
DR STRING; 50402.A0A0A0ABS0; -.
DR MEROPS; C19.016; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
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; IPR029346; USP_C.
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; PF14533; USP7_C2; 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:0000313|EMBL:KGL91541.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000053858};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
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:KGL91541.1"
FT NON_TER 1078
FT /evidence="ECO:0000313|EMBL:KGL91541.1"
SQ SEQUENCE 1078 AA; 125682 MW; 20C5FA3A135AB78C 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 PKFDKDHDVM
LFLKMYDPKT RSLNYCGHIY TPISCKIRDL LPVMCERAGF PQETNLILYE EVKPNLTERI
QDYDVSLDKA LDELMDGDII VFQKDDPEND SSELPTAKEY FRDLYHRVDV IFCDKTIPND
PGFVVTLSNR MNYFQARVAK TVAQRLNTDP MLLQFFKSQG YRDGPGNPLR HNYEGTLRDL
LQFFKPRQPK KLYYQQLKMK ITDFENRRSF KCIWLNSQFR EEEITVYPDK HGCVRDLLEE
CKKVVELSEK GSGKLRLLEI VSYKIIGVHQ EDELLECLSP ATSRTFRIEE IPLDQVDIDK
ENEMLITVAH FHKEVFGTFG IPFLLRIHQG EHFREVMKRI QTMLDIQEKE FEKFKFAIVM
MGRHQYLNED EYEVNLKDFE PQPGNMSHPR PWLGLDHFNK APKRSRYTYL EKAIKIHN
//
