ID A0A091P167_9PASS Unreviewed; 812 AA.
AC A0A091P167;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=N310_11688 {ECO:0000313|EMBL:KFP85375.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP85375.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP85375.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP85375.1};
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.
CC {ECO:0000256|RuleBase:RU366025}.
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DR EMBL; KK843317; KFP85375.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091P167; -.
DR Proteomes; UP000053537; Unassembled WGS sequence.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02667; Peptidase_C19K; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
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:SF34; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 45; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-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|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:UP000053537};
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 35..152
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 191..811
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 812
FT /evidence="ECO:0000313|EMBL:KFP85375.1"
SQ SEQUENCE 812 AA; 90205 MW; E4470724A990FEBB CRC64;
MRVKDPSRTN PEKPKRSKRP NRPQDEDSSD DISGLTCQHV SQAVDVHHVK RAVAQSVWSI
CAECLRERRM SDGEPVAPSD IWLCLKCGFQ GCSKNSEGQH SLKHFQTART EPHCIVINLS
TWIIWCYECD EELSTHCNKK VLAQIVDFLQ KHGARAEPSS SKIIRLREEN NETSEILKGK
SSGNGASVPV KGINNLGNTC FFNAVMQNLA QTHVLNELMY EIKEKGTKLK ICHNSDSPLD
PLVVNLSSPG PLTSAMFLFL HSMREAGKGP LSPKVLFSQL CQKAPRFKGF QQQDSQELLH
YLLDAMRIEE TKRIQTGILK AFNNPTTKTA DEETRRKVKA YGREGVKMNF IDRIFVGELT
STVMCEECEN VVKEPFIDLS LPIIEERVAK PVPLGRTGKG KSVQEADLGQ YNCSSISTLN
NQPKIVKKHA LTKDKNQLNH ERRLARKASS KEEQRSPVIM QEKPKKLELE GSSGYSKDTP
ADSAVNGSQT EGSEKEASRS ESSFDADSEA SESESASKQT TFSPSSNSSA LHVSHINVKA
PHNKPSDSNE EVISSAISKL SFCDPVSEDK KLTRGDPALG LANNSVFSVD KSSLSQNPQN
AFQTLSQSYI TSSKECSVQS CLYQFTSVEL LMGNNKLLCE SCTERKQKYQ KKTNSTEKKM
EGVYTNARKQ LLISSVPAIL ILHLKRFHQA GLSLRKVNRH VDFPLILDLA PFCAASCKNV
TDGARVLYSL YGIVEHSGSM RGGHYAAYVK VRTSSKKLLE HISTTKNVLG LKEAMGAAGG
QWVYVSDTHV QMVPESRVLN AQAYLLFYER LL
//
