ID A0A091M5J4_CARIC Unreviewed; 427 AA.
AC A0A091M5J4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE Flags: Fragment;
GN ORFNames=N322_01510 {ECO:0000313|EMBL:KFP65992.1};
OS Cariama cristata (Red-legged seriema).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cariamiformes; Cariamidae; Cariama.
OX NCBI_TaxID=54380 {ECO:0000313|EMBL:KFP65992.1, ECO:0000313|Proteomes:UP000054116};
RN [1] {ECO:0000313|EMBL:KFP65992.1, ECO:0000313|Proteomes:UP000054116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N322 {ECO:0000313|EMBL:KFP65992.1};
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 -!- SIMILARITY: Belongs to the peptidase C64 family.
CC {ECO:0000256|ARBA:ARBA00005865}.
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DR EMBL; KK519745; KFP65992.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091M5J4; -.
DR Proteomes; UP000054116; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd22767; OTU_ZRANB1; 1.
DR Gene3D; 1.25.40.560; -; 1.
DR InterPro; IPR041294; AnkUBD.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR049768; ZRANB1_OTU.
DR PANTHER; PTHR13367; UBIQUITIN THIOESTERASE; 1.
DR PANTHER; PTHR13367:SF28; UBIQUITIN THIOESTERASE ZRANB1; 1.
DR Pfam; PF18418; AnkUBD; 1.
DR Pfam; PF02338; OTU; 1.
DR PROSITE; PS50802; OTU; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054116};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 159..311
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP65992.1"
FT NON_TER 427
FT /evidence="ECO:0000313|EMBL:KFP65992.1"
SQ SEQUENCE 427 AA; 48905 MW; AAA5133735E4D0B6 CRC64;
GVVEGDLAAV EAYKSSGGDI ARQLTADEVR LLNRPSAFDV GYTLVHLAIR FQRQDMLAIL
LTEVSQHAAN PAMVCPEVTE QIRREIAASL HQRKGDFACY FLTDLVTFTL PADIEDLPPT
VQEKLFDEVL DRDVQKELEE ESPIINWSLE LGTRLDSRLY ALWNRTAGDC LLDSVLQATW
GIYDKDSVLR KALHDSLHDC SHWFYTRWQD FGLHFSLREE QWQEDWAFIL SLASQPGASL
EQTHIFVLAH ILRRPIIVYG VKYYKSFRGE TLGYTRFQGV YLPLLWEQSF CWKSPIALGY
TRGHFSALVA MENDGYGNRG AGANLNTDDD VTVTFLPLVD SERKLLHIHF LSAQEIGNEE
QQEKLLREWL DCCVTEGGVL VAMQKSSRRR NHPLVTQMVE KWLDRYRQIR PCTSLSDGEE
DEDDDDE
//