GenomeNet

Database: UniProt
Entry: A0A087RGJ9_APTFO
LinkDB: A0A087RGJ9_APTFO
Original site: A0A087RGJ9_APTFO 
ID   A0A087RGJ9_APTFO        Unreviewed;       684 AA.
AC   A0A087RGJ9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=AS27_09637 {ECO:0000313|EMBL:KFM12603.1};
OS   Aptenodytes forsteri (Emperor penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC   Aptenodytes.
OX   NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM12603.1, ECO:0000313|Proteomes:UP000053286};
RN   [1] {ECO:0000313|EMBL:KFM12603.1, ECO:0000313|Proteomes:UP000053286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM12603.1};
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   -!- SIMILARITY: Belongs to the peptidase C19 family. USP44 subfamily.
CC       {ECO:0000256|ARBA:ARBA00038113}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KL226356; KFM12603.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087RGJ9; -.
DR   STRING; 9233.A0A087RGJ9; -.
DR   MEROPS; C19.057; -.
DR   Proteomes; UP000053286; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
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:SF15; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 44; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
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   Hydrolase {ECO:0000256|RuleBase:RU366025, ECO:0000313|EMBL:KFM12603.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|RuleBase:RU366025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053286};
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          2..99
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   DOMAIN          272..681
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          176..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..210
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         684
FT                   /evidence="ECO:0000313|EMBL:KFM12603.1"
SQ   SEQUENCE   684 AA;  78575 MW;  399BC57B466C31DA CRC64;
     MDKCKHIGRL RLAQDHSILN PQKWHCMDCN TTESVWACLS CSHVACGRYI EEHALKHFQE
     SSHPVALEVN ELYVFCYLCD DYVLNDNATG DLKLLRSTLS AIKSQNYECT TRSGRTLRSM
     GASDDSYLSH GGAQALLRNE DRMFTALWHR RRAFLGKIFR SWLELTPTGK KILEEERRRE
     EAEERKDKAR KRRQERKREL KAEMEKMPPR KSSRLQNQIR MSSETAPCLQ KPSQNMESVA
     ELKKTYTSDE VRLKKISDSP IKRRPTVTPG VTGLRNLGNT CYMNSILQVL SHLPIFRECF
     LKLDLNQTQE LLATATNGKT RSSSKHLSIA ASTLHVNENQ EKVKGSSSVR RPSVSSGLSG
     GASKSRNMEL IQPREPSSKH ISLCHELHTL FQVMWSGKWA LVSPFAMLHS VWRLIPAFRG
     YAQQDAQEFL CELLDKVQQE LETTGTRYPA LIPASQRKLI KQVLNVVNNI FHGQLLSQVT
     CLACDNKSNT IEPFWDLSLE FPERYHCNGK EMSSQYPCLL TEMLAKFTET EALEGKIYAC
     DQCNTKRRKF SSKPVILTEA QKQLMVCRLP QVLRLHLKRF RWSGRNHREK IGVHVNFDQM
     LNMEPYCCRE SLKSLLPDCF IYDLSAVVMH HGKGFGSGHY TAYCYNSEGG FWVHCNDSKL
     NMCTMEEVCK AQAYILFYSQ RLTQ
//
DBGET integrated database retrieval system