ID A0A091FZN1_9AVES Unreviewed; 813 AA.
AC A0A091FZN1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=N303_00293 {ECO:0000313|EMBL:KFO74671.1};
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:KFO74671.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO74671.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO74671.1};
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm,
CC perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP20/USP33 subfamily.
CC {ECO:0000256|ARBA:ARBA00008269}.
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DR EMBL; KL447531; KFO74671.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091FZN1; -.
DR STRING; 55661.A0A091FZN1; -.
DR MEROPS; C19.037; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
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:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
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:SF32; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 33; 1.
DR Pfam; PF06337; DUSP; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00695; DUSP; 2.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51283; DUSP; 2.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
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:UP000053760};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 1..62
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 106..637
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 639..732
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 741..813
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO74671.1"
FT NON_TER 813
FT /evidence="ECO:0000313|EMBL:KFO74671.1"
SQ SEQUENCE 813 AA; 91808 MW; E04FE67C6E7D0C0A CRC64;
CTYVGCGESH VDHSTTHSQE TKHCLTVNLT TLRVWCYACS KEVFLDRKLG SQSPLPQSRL
SHQAQENSVQ DFKIPSNPTL KIPLAAVFDD LDIEVEEDEL KTRGLTGLKN IGNTCYMNAA
LQALSNCPPL THFFLDCGGL ARTDKKPAIC KSYLKLMTEL WHKSRPGSVV PTGLFQGIKT
VNPTFRGYSQ QDAQEFLRCL MDLLHEELKE PVVELEDAQP MSVEESIEED KNQSDVGFQP
CESCGTCDKT ESDAIFKPVL EDPAETTMLI QDDDNNSITS KDWQKEKIPN NKLKRANSMD
DLEKDTNTAS ETTEFLNNQG TVKVQIHSRF SEYISDAHVN DISAAQIPSA NEGMNTRLSN
SPPKSYASCS SLASVHKKVS TVSSPKRKKR KKYRSVISDI FDGTIISSVQ CLTCDRLSVT
LETFQDLSLP IPGKEDLAKL HSASHQTSLV KAGSCGEAYA PQGWIAFFME YFKRFVVSCV
PSWFWGPVVT LQDCLAAFFA RDELKGDNMY SCGRCKKLRN GVKFCKVQKF PEILCIHLKR
FRHELMFSTK IGTHVSFPLE GLDLQPFLAK DSPAQIVTYD LLSVICHHGT ASSGHYIAYC
RNNLNNLWYE FDDQSVTEVS ESTVQNAEAY VLFYRKSSEE AQRERRRISS LLNMMEPSLL
QFYVSRQWLN KFKTFAEPGP ISNNDFLCMH GGVPPHKANF IEDLVVMLPQ NIWDNLYSRY
GGGPAVNHLY VCHTCQIESE RIEKRRKNEL EMFIRLNRAF QEEESPSTFY CISMQWFREW
EGFVKGKDSD PPGPIDNAKI AVTKCGNAVL KQG
//
