ID A0A091VTY1_OPIHO Unreviewed; 952 AA.
AC A0A091VTY1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=N306_04403 {ECO:0000313|EMBL:KFR06629.1};
OS Opisthocomus hoazin (Hoatzin) (Phasianus hoazin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Opisthocomiformes; Opisthocomidae;
OC Opisthocomus.
OX NCBI_TaxID=30419 {ECO:0000313|EMBL:KFR06629.1, ECO:0000313|Proteomes:UP000053605};
RN [1] {ECO:0000313|EMBL:KFR06629.1, ECO:0000313|Proteomes:UP000053605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N306 {ECO:0000313|EMBL:KFR06629.1};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR EMBL; KK734346; KFR06629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091VTY1; -.
DR STRING; 30419.A0A091VTY1; -.
DR MEROPS; C19.022; -.
DR PhylomeDB; A0A091VTY1; -.
DR Proteomes; UP000053605; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR028135; Ub_USP-typ.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR029346; USP_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF28; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 15; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF14836; Ubiquitin_3; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS51283; DUSP; 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|RuleBase:RU366025, ECO:0000313|EMBL:KFR06629.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000053605};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 1..88
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 258..903
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 186..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..638
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFR06629.1"
FT NON_TER 952
FT /evidence="ECO:0000313|EMBL:KFR06629.1"
SQ SEQUENCE 952 AA; 109132 MW; B89A14EF0242884B CRC64;
YLVDSRWFKQ WKKYVGFDSW DKYQMGDQNV YPGPIDNSGL LKDGDSQSLK EHLIDELDYI
LLPTEGWNRL VSWYTLMEGQ EPIARKVVEQ GMFVKHCKVE VYLTELKLCE NGNMNNVVTR
RFSKADTIDT IEKEIRKIFN IPGEKETRLW NKYMSNTFEP LNKPDSTIQD AGLYQGQVLV
IEQKNEDGTW PRGPSTPKSP GASNFSTLPK ISPSLSNNYN NMNNRNVKNS NYCLPSYTAY
KNYDYSEPGR HNEQPGLCGL SNLGNTCFMN SAIQCLSNTP PLTEYFLNDK YQEELNFDNP
LGMRGEIAKS YAELIKQMWS GKYSYVTPRA FKTQVGRFAP QFSGYQQQDC QELLAFLLDG
LHEDLNRIRK KPYIQLKDAD GRPDKVVAEE AWENHLKRND SIIVDIFHGL FKSTLVCPEC
AKISVTFDPF CYLTLPLPMK KERTLEVYLV RMDPLAKPMQ YKVVVPKIGN ILDLCTALSS
LSGVAADKMI VTDIYNHRFH RIFGMDENLS SIMERDDIYV FEIAINRTED TEQVIIPVCL
REKCRHTSYS HSGSSLFGQP FLIAVPRNNT EDKLYNLLLL RMCRYVKTCT ESEDTEGSLH
CCKDHGINGN GPNGIHEEGS PSEMETDEQD DESSQDQELP SENENSQSED SVGGDNDSEN
GLCTEDTCKG QPLTGHKKRL FTFQFNNLGN TDINYIKDDT RHIRFDDRQP RLDERSFLAL
DWDPELKKRY FDDSAAEDFE KHESVEYKPP KKPFVKLKDC IELFTTKEKL GAEDPWYCPN
CKEHQQATKK LDLWSLPPVL VVHLKRFSYS RYMRDKLDTL VEFPTNDLDM SEFLINPNAG
PCRYNLIAVS NHYGGMGGGH YTAFAKNKDD GKWYYFDDSS VSTACEDQIV ASTFPYVLFY
QRQDTISGTG FFPLDRETKQ GASAATGIPL ESDEDSNEND NDIENENCMH TN
//
