ID A0A091HAF5_BUCRH Unreviewed; 952 AA.
AC A0A091HAF5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=N320_07428 {ECO:0000313|EMBL:KFO91670.1};
OS Buceros rhinoceros silvestris.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Bucerotiformes; Bucerotidae; Buceros.
OX NCBI_TaxID=175836 {ECO:0000313|EMBL:KFO91670.1, ECO:0000313|Proteomes:UP000054064};
RN [1] {ECO:0000313|EMBL:KFO91670.1, ECO:0000313|Proteomes:UP000054064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N320 {ECO:0000313|EMBL:KFO91670.1};
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; KL527427; KFO91670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091HAF5; -.
DR MEROPS; C19.022; -.
DR Proteomes; UP000054064; 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; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
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; SSF55205; EPT/RTPC-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:KFO91670.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000054064};
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..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..670
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 623..638
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO91670.1"
FT NON_TER 952
FT /evidence="ECO:0000313|EMBL:KFO91670.1"
SQ SEQUENCE 952 AA; 109090 MW; 14C7C9CD1D35DE5A CRC64;
YLVDSRWFKQ WKKYVGFDSW DKYQMGDQNV YPGPIDNSGL LKDGDSQSLK EHLIDELDYI
LLPTEGWNRL VSWYTLMEGQ EPIARKVVEQ GMFVKHCKVE VYLTELKLCE NGNMNNVVTR
RFSKADTIDT IEKEIRKIFN IPCEKETRLW NKYMSNTFEP LNKPDSTIQD AGLYQGQVLV
IEQKNEDGTW PRGPSAPKSP 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 RMDPDAKPMQ YKVVVPKIGN ILDLCTALSA
LSGVPADKMI VTDIYNHRFH RIFGMDENLS SIMERDDIYV FEIAINRTED TEQVIIPVCL
REKCRHTSYS HSGSSLFGQP FLIAVPRNNT EDKLYNLLLL RMCRYVKTCA ESEDTEGSLH
SCKDHSINGN GPNGIHEEGS PSEMETDEQD DESSQDQELP SENENSQSED SVGGDNDFEN
GLSTADTCKG PPLMGHKKRL FTFQFNNLGN TDINYIKDDT RHIRFDDRQP RLDERSFLAL
DWDPELKKRY FDDNAAEDFE KHESVEYKPP KKSFVKLKDC IELFTTKEKL GAEDPWYCPN
CKEHQQATKK LDLWSLPPVL VVHLKRFSYS RYMRDKLDTL VDFPVNDLDM SEFLINPNAG
PCRYNLIAVS NHYGGMGGGH YTAFAKNKDD GKWYYFDDSS VSAACEDQIV ASTFSYVLFY
QRQDTISGTG FFPLDRETKQ GASAATGIPL ESDEDSNEND NDIENENCMH TN
//
