ID A0A091TDG2_PHALP Unreviewed; 688 AA.
AC A0A091TDG2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, 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=N335_05675 {ECO:0000313|EMBL:KFQ72331.1};
OS Phaethon lepturus (White-tailed tropicbird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Eurypygimorphae; Phaethontiformes;
OC Phaethontidae; Phaethon.
OX NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ72331.1, ECO:0000313|Proteomes:UP000053638};
RN [1] {ECO:0000313|EMBL:KFQ72331.1, ECO:0000313|Proteomes:UP000053638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ72331.1};
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|RuleBase:RU366025}.
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DR EMBL; KK448375; KFQ72331.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091TDG2; -.
DR MEROPS; C19.073; -.
DR PhylomeDB; A0A091TDG2; -.
DR Proteomes; UP000053638; 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:UP000053638};
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 170..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 688
FT /evidence="ECO:0000313|EMBL:KFQ72331.1"
SQ SEQUENCE 688 AA; 79195 MW; 06F26804B9563A2B CRC64;
MDRCKHVGRL RLAQDHSILN PQKWHCVDCQ TTESIWACLK CSHVACGRYI EEHALKHFEE
TRHPLAMEVN DLYVFCYLCE DYVLNDNPEG DLKLLRSSLS AIRSQKHDPS TRSGRTLRSM
ALGGDMCSHQ RSPQGQSQML TALWHRRQSL LAKALRTWFD KSSRGQLKLK QKKQTEELEK
KKEAARQRRQ EMKRQLLEEL ANTPPRKSAR LLSHVHRENL IPRKFREVAT ASPTSRQMQS
SRFKQFYSIR RKPLMTPGVT GLRNLGNTCY MNSILQVLSH LQKFRECFLT LDLCETEELL
AKTVNGKSRM PGKLANGSAA NESGKTDKVG SYGMQSLPAG LNGGSSISRS LELIQPKEPS
SKHISLCHEL HTLFRVMWSG KWALVSPFAM LHSVWSLIPA FRGYDQQDAQ EFLCELLDKV
QQELESEGTK RRILIPFSQR KLTKQVLKVV NTIFHGQLLS QVTCITCNYK SNTVEPFWDL
SLEFPERYHS IEKGIIPVNQ TECMLTEMLA KFTETEALEG RIYACDQCNS KRRKSSPKPL
VLSEAKKQLM IYRLPQVLRL HLKRFRWSER NHREKIGVHV LFDQVLNMEP YCCRDSLSSL
DKETFVYDLS AVVMHHGKGF GSGHYTAYCY NTEGGFWVHC NDSKLNVCSV EEVCKTQAYI
LFYTQRTVQD KARISEKQLQ AQVPSKNN
//
