ID A0A0A0AQ93_CHAVO Unreviewed; 906 AA.
AC A0A0A0AQ93;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=N301_12711 {ECO:0000313|EMBL:KGL95738.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL95738.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL95738.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL95738.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-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, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm,
CC perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP20/USP33 subfamily.
CC {ECO:0000256|ARBA:ARBA00008269}.
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DR EMBL; KL872462; KGL95738.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0AQ93; -.
DR STRING; 50402.A0A0A0AQ93; -.
DR MEROPS; C19.025; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
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:0006897; P:endocytosis; IEA:UniProtKB-KW.
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; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; 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:SF13; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 20; 1.
DR Pfam; PF06337; DUSP; 2.
DR Pfam; PF00443; UCH; 2.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00695; DUSP; 2.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51283; DUSP; 2.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
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:UP000053858};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 1..104
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 140..677
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 679..772
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 781..884
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT REGION 245..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL95738.1"
FT NON_TER 906
FT /evidence="ECO:0000313|EMBL:KGL95738.1"
SQ SEQUENCE 906 AA; 101661 MW; 9BFEC16DE29E0A1D CRC64;
DICPHLDSIG EVTRDDLLLK SKGTCQSCGA AGPNLWACLQ IGCPYVGCGE SFADHSTLHA
QAKKHNLTVN LTTFRVWCYA CEKEVFLDQR LAMHTQTRRV KFSEPVSTLL APPLKAVPIA
VADEGESESE DDDLKTRGLT GMKNLGNSCY MNAALQALSN CPPLTQFFLE CGGLVRTDKK
PALCKSYQKL VSEVWHKKRP SYVVPSSLSH GIKLVNPMFR GYAQQDTQEF LRCLMDQLHE
ELKEPIVAET RDLDTSDQDD KREGDQSPSE DEFLSCDSSS DRGEGDGQSR TTAGMGSSSL
AETELLIQDE AGRGISEKER MKDRKFSCGH RRSNSEQVDE DADVDTTMMP VDGRASPEML
PAPRPASPCR TPEPDNDAYV RCSSRPCSPV HHEMHSKLSS SPPRSSPARL GPSYVLKKAQ
MQASGKKKKE LRYRSVISDI FDGSILSLVQ CLTCDRVSTT VETFQDLSLP IPGKEDLAKL
HSAIYQNVPA KTGACGDNYA SQGWIAFIME YIRRFVVSCI PSWFWGPVVT LEDCLAAFFA
ADELKGDNMY SCERCKKLRN GVKYCKVLRL PEILCIHLKR FRHEVMYSFK INSHVSFPLE
GLDLRPFLAK ECVSQITTYD LLSVICHHGT ASSGHYTAYC QNVINGQWYE FDDQYVTEVH
ETVVQNAEAY VLFYRKSSEE AVRERQKVVS LASMKEHSLL QFYISREWLN KFNTFAEPGP
ITNHTFLCSH GGIPPNKYHY IDDLAVILPQ NVWEYLYNRF GGGPAVNHLY VCSICQVEIE
ALAKRRRIEI DTFIKLNKAF QAEESPSVIY CISMQWFREW EAFVKGKDNE PPGPIDNSKI
ALTKAGGHMQ VKQGADYGQI SEETWICFST LYGGGPEIAI RQNVAQVQEL ENLHGEQKIE
AETRAV
//
