ID A0A091FKM6_9AVES Unreviewed; 988 AA.
AC A0A091FKM6;
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=N303_03692 {ECO:0000313|EMBL:KFO69704.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO69704.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO69704.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO69704.1};
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; KL447081; KFO69704.1; -; Genomic_DNA.
DR RefSeq; XP_009555909.1; XM_009557614.1.
DR AlphaFoldDB; A0A091FKM6; -.
DR STRING; 55661.A0A091FKM6; -.
DR KEGG; cuca:104056360; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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:KFO69704.1};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000053760};
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..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..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 168..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; 111149 MW; A668BCCD80768FDD CRC64;
MAPLKVHGPV RMRSMQTGIT KWKEGSFEIV EKDNKVSLVV HYNVGGIPKT FQLSHNIKTV
TLRPNGRKLC CLMLTLKDTS FLTIDKVPFK DANEMRMYLD AVHQDRIHTA GRPSQGSGSF
GGVLGSRTTQ KEANRQFSYM ENQTPPRRVT AESKEETPFR KVLGTPARAS AKNSTGNGTP
GNRVNIPASP ASSGPHRNGL LENREKRKRT QPPGSEMSED YPKENDSSTN NKALSDPTWK
YLNSSREKQL NLKQAEENRT SGILPLQSSS FYGSRSSTKE YSTGSSTLDR STVSSQTTSA
KRSLGFLSQP APLSVKKMRS NQDYTGWNKP RVPLSTHPQQ QLQGFSNLGN TCYMNAILQS
LFSIQSFAND LLKQGIPWKK IPLNALIRRF AHLLAKKDVC SPEVKKELLK KVKSAISATA
ERFSGYMQND AHEFLSQCLD QLKEDMEKLN KTWKSEPIPS EDNSPGRASD DLSATKVYTC
PVISNLEFEV QHSIICKTCG ETVTKREQFN DLSIDLPRRK KLLPSRSIQD SLDLFFRAEE
IEYSCEKCNG KSAVVTHKFN RLPRVLILHL KRYSFNVALS LNHKVGQQVV IPRYLTLLSH
CTESTRLPLT LGWSVHSAMS RPLKASQMVN SCTVSTSTPC RKYTFKSKSS TALYVDSDSD
DEPLKRSVAH SQRLCNIQSR DQQQLQEEPE KGSKRSKMEG DKPELGNAGF DGMSEDELLA
AVLEISKREA SLSLSHDEDK PTSSPDTGFG DDEIQELPEN LESMEMEKPK ASLDSGPANF
AEITKDFDEN KENKTPEGSQ GEVDWLQQYD MEREREEQEL QQALAQSLQE QEAREQKEDD
DLKRATELSL QEFNSSLLDS VGSDEDSGNE DVLDMEYSEA EAEELKRNAE TGELPHSYRL
ISIVSHIGST SSSGHYISDV YDIKKQSWFT YNDLEVSRTL EATVQCDRDR SGYIFFYMHK
DIFDELVETE KNAQPLSMEV GRSVRQPL
//
