ID A0A093J736_STRCA Unreviewed; 988 AA.
AC A0A093J736;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=N308_14332 {ECO:0000313|EMBL:KFV74754.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV74754.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV74754.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV74754.1};
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|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR EMBL; KL205808; KFV74754.1; -; Genomic_DNA.
DR RefSeq; XP_009687993.1; XM_009689698.1.
DR AlphaFoldDB; A0A093J736; -.
DR STRING; 441894.ENSSCUP00000006767; -.
DR Ensembl; ENSSCUT00000008923; ENSSCUP00000006767; ENSSCUG00000005006.
DR GeneID; 104153715; -.
DR KEGG; scam:104153715; -.
DR CTD; 57695; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006275; P:regulation of DNA replication; IEA:Ensembl.
DR CDD; cd02257; Peptidase_C19; 2.
DR CDD; cd13312; PH_USP37_like; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 2.30.29.180; Ubiquitin carboxyl-terminal hydrolase 26/29/37, pleckstrin homology-like domain; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR032069; USP37-like_PH.
DR InterPro; IPR038093; USP37-like_PH_sf.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF16674; UCH_N; 1.
DR Pfam; PF02809; UIM; 3.
DR SMART; SM00726; UIM; 3.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50330; UIM; 3.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Hydrolase {ECO:0000256|RuleBase:RU366025, ECO:0000313|EMBL:KFV74754.1};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 343..960
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 132..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..704
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 988 AA; 111039 MW; F7DEC71D9E171DFB CRC64;
MAPLKVHGPV RMRSMQTGIT KWKEGSFEIV EKDNKVSLVV HYNVGGIPKT FQLSHNIKTV
TLRPNGRKLC CLMLTLKDTS FLTIDKVPFK DANEMRMYLD AVHQDRVHTA GKPSQGSGSF
GGVLGSRTTQ KEANRQFSYI ENQTPPKRAT VESKDENPFR KVLGTPARTS VKNSPGTGTP
SNRVNISASP ASSVPHRAGL LENREKRKRT QPPGSEMSED YPKENDSSTN NKALSDPAWK
YLNSSREKQL NLKQAEENRT SGVLPLQSSS FYGSRSSSKE YSTGSSTLDR SNVSSQTPSA
KRSLGFLSQP APLSVKKMRS NQDYTGWNKP RVPLSTHPQQ QLQGFSNLGN TCYMNAILQS
LFSIQSFAND LLKQGIPWKK IPLNALIRRF AHLLAKKDVC SPEVKKELLK KVKSAISATA
ERFSGYMQND AHEFLSQCLD QLKEDMEKLN KTWKSEPVPS EDNSPGRASD DLSATKVYTC
PVISNLEFEV QHSIICKMCG ETVTKREQFN DLSIDLPRRK KLLPSRSIQD SLDLFFRAEE
IEYSCEKCNG KSAVVTHKFN RLPRVLILHL KRYSFNVALS LNHKVGQQVV IPRYLTLLSH
CTESTRLPLT LGWSAHSAIS RPLKASQMVN SCTVSTSTPC RKYTFKSKSS TALYVDSDSD
DEPLKRSVAH SQRLCSIQSR DQQQLQEEPE KGSKRSKMEC DKPELGNAGF DGMSEDELLA
AVLEISKREA SLSLSHDEDK PTSSPDTGFG EDEIQELPEN LESVEVEKPK AALESGLASF
TEITKDFDEN KENKTPEGSQ GEVDWLQQYD MEREREEQEL QQALAQSLQE QEAREQKEDD
DLKRATELSL QEFNSSLLEG VGSDEDSGNE DVLDMEYSEA EAEELKRNAE TGELPHSYRL
ISIVSHIGST SSSGHYISDV YDIKKQSWFT YNDLEVSRTL EATVQCDRDR SGYIFFYMHK
DIFDELLETE KNAQPLSMEV GRSIRQPL
//
