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}.
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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
//