ID A0A091MF28_9PASS Unreviewed; 908 AA.
AC A0A091MF28;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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_06131 {ECO:0000313|EMBL:KFP71721.1};
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:KFP71721.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP71721.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP71721.1};
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; KK823924; KFP71721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091MF28; -.
DR MEROPS; C19.025; -.
DR Proteomes; UP000053537; 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:SF13; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 20; 1.
DR Pfam; PF06337; DUSP; 2.
DR Pfam; PF00443; UCH; 2.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00695; DUSP; 2.
DR SMART; SM00290; ZnF_UBP; 1.
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:UP000053537};
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..104
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 140..673
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 681..774
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 783..886
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT REGION 245..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP71721.1"
FT NON_TER 908
FT /evidence="ECO:0000313|EMBL:KFP71721.1"
SQ SEQUENCE 908 AA; 101805 MW; 9CA8335F2F810990 CRC64;
DICPHLDSIG EVTRDDLLLK SKGTCQSCGA VGPNLWACLQ IGCPYVGCGE SFADHSTLHA
QAKKHNLTVN LTTFRVWCYA CEKEVFLDQR LAAHPPSPPA KFTEPDSPLP THPLKAVPIA
VADEGESESE DDDLKPRGLT GMKNLGNSCY MNAALQALSN CPPLTQFFLE CGGLVRTDKK
PALCKSYQKL VSEVWHKKRP SYVVPSSLSH GIKLVNPMFR GYAQQDTQEF LRCLMDQLHE
ELKEPVVAET RDLDPSDQED KREGDRSPSE DDESSSDRGE GEGQSRSTGS MSSGSLAETE
LLIQDEAGRG ISEKERMKDR KFSCGHRRSN SEQVDEDADV DTTMMPVDGR ASPEMLPAPR
PASPCRTPEP DNDAYVRCSS RPCSPVHHEM HSKLSSSPPR SSPARLGPSY ILKKAQMQAS
GKKKKELRYR SVISDIFDGS ILSLVQCLTC DRVSTTVETF QDLSLPIPGK EDLAKLHSAI
YQNVPAKTGA CGDNYASQGW IAFIMEYIRR FVVSCIPSWF WGPVVTLEDC LAAFFAADEL
KGDNMYSCER CKKLRNGVKY CKVLRLPEIL CIHLKRFRHE VMYSFKINSH VSFPLEGLDL
RPFLAKECVS QITTYDLLSV ICHHGTAGSG HYIAYCQNVI NGQWYEFDDQ YVTEVHETVV
QNAEAYVFVF WSFPSLRKSS EEAVRERQKV VSLASMKEHS LLQFYISREW LNKFNTFAEP
GPITNHTFLC SHGGIPPNKY HYIDDLVVIL PQNVWEYLYN RFGGGPAVNH LYVCSICQVE
IEALAKRRRI EIDTFIKLNK AFQAEESPSV IYCISMQWFR EWEAFVKGKD NEPPGPIDNS
KIALTKAGGH VQVKQGADYG QISEETWIYL STLYGGGPEI AIRQNVAQVQ ELENLHGEQK
IEAETRAV
//
