ID A0A0A0AN65_CHAVO Unreviewed; 683 AA.
AC A0A0A0AN65;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=N301_06625 {ECO:0000313|EMBL:KGL95949.1};
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:KGL95949.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL95949.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL95949.1};
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 ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR EMBL; KL872519; KGL95949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0AN65; -.
DR STRING; 50402.A0A0A0AN65; -.
DR MEROPS; C19.073; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF7; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 49; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000053858};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 2..99
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 260..666
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 172..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 683
FT /evidence="ECO:0000313|EMBL:KGL95949.1"
SQ SEQUENCE 683 AA; 78708 MW; 03E30C8F1E3B7C1C CRC64;
MDRCKHVGRL RLAQDHSILN PQKWHCVDCQ TTESIWACLK CSHVACGRYI EEHALKHFEE
TRHPLAMEVN DLYVFCYLCE DYVLNDNPEG DLKLLRSSLS AIKSQKHDPS TRSGRTLRSM
ALGEDMCSHQ RSPQGQSQML TALWHRRQSL LAKALRTWFD KSSRGQLKLK QKKQMEELEK
KKEAARQRRQ EMKRQLLEEL ANTPPRKSAR LLSHVHRENL IPRKFREVAT ASPTSRQMQS
SRFKQFYSIR RKPLMTPGVT GLRNLGNTCY MNSILQVLSH LQKFRECFLT LDLCETEELL
AKTVNGKSRM PGKLANGSAA NESGKTDKVG SYGTQSLPAG LNGGSSISRS LELIQPKEPS
SKHISLCHEL HTLFRVMWSG KWALVSPFAM LHSVWSLIPA FRGYDQQDAQ EFLCELLDKV
QQELESEGTK RRILIPFSQR KLTKQVLKVV NTIFHGQLLS QVTCITCNYK SNTVEPFWDL
SLEFPERYHS IEKGIVPVHQ TECMLTEMLA KFTETEALEG RIYACDQCNS KRRKSSPKPL
VLSEAKKQLM IYRLPQVLRL HLKRFRWSER NHREKIGVHV LFDQVLNMEP YCCRDSLSSL
DKETFVYDLS AVVMHHGKGF GSGHYTAYCY NTEGGFWVHC NDSKLNVCSV EEVCKTQAYI
LFYTQRTVQD KARISEKQLQ AQV
//
