ID A0A091F155_CORBR Unreviewed; 748 AA.
AC A0A091F155;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=N302_06897 {ECO:0000313|EMBL:KFO62986.1};
OS Corvus brachyrhynchos (American crow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC Corvus.
OX NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO62986.1, ECO:0000313|Proteomes:UP000052976};
RN [1] {ECO:0000313|EMBL:KFO62986.1, ECO:0000313|Proteomes:UP000052976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO62986.1};
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 C19 family. USP10 subfamily.
CC {ECO:0000256|ARBA:ARBA00005427}.
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DR EMBL; KK719362; KFO62986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091F155; -.
DR STRING; 85066.A0A091F155; -.
DR Proteomes; UP000052976; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR CDD; cd02257; Peptidase_C19; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR009818; Ataxin-2_C.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF687; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 10; 1.
DR Pfam; PF07145; PAM2; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KFO62986.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052976}.
FT DOMAIN 401..748
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 117..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO62986.1"
FT NON_TER 748
FT /evidence="ECO:0000313|EMBL:KFO62986.1"
SQ SEQUENCE 748 AA; 81659 MW; 11E53C3E2B6030EB CRC64;
YIFGEFSPDE FNQFFVTPRC SVELPPYNET VSCGIKSTGK FHDGEEYQRI EFGVNEVIET
QSSVLNNTDY SISSTLNPQA PEFILSCAPA QKTPDDALSD TNYNSIDCQF SDPTLALDSG
SNAENDSLAG GLGQRERKKK KKRPPGYYSY LEDVPDGVAA PEALVNGHAT AAGLNSLSTE
DTELAGDLPS LATPRTCSSP ASSLDFLAGA ACAEPGAAAP GRTAGQPEVC RLPNSEQFCL
PSEAIRDSPL RTAVVQSYAG TDTTETLGVT NGQTLESSGE DTAANGVELH TVESTDSDQA
KPEEASPTTE ATVPLAGSVP VNQPAKSWAS LFHNSKPSAS TSVVYVETKY TPPATSPLVP
EKQVEVKEGP VPVSEDPVAI KIAEILENVR LIHKPVSLQP RGLINKGNWC YINAVSFPGK
KINALKLIFT LQALVACPPM YHLMKSIPMY SKSQRPCTST PMLDSFVRLM NEFTNMPVPP
KAKQALGDKI VRDIRPGAAF EPTYIYRLLT VIKSSLSEKG RQEDAEEYLG FILNGLHEEM
LTLKKLLSPH NEKLSVSNGP EAQSVPKEEE QEEQGEGSED EWEQVGPRNK SSVTRQADFV
QTPITDIFGG HIRSVVYQQS SKESATLQLF FTLQLDIQSD KIRTVQDALE SLVARESVQG
YTTKTKQEVE ISRRLTLEKL PPVLVLHLKR FVYEKTGGCQ KLIKNIEYTV DLEISKELLS
PGVKSKISKG QRTYRLFAVV YHHGNSAT
//
