ID   A0A2G5DZ11_AQUCA        Unreviewed;       944 AA.
AC   A0A2G5DZ11;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN   ORFNames=AQUCO_01300006v1 {ECO:0000313|EMBL:PIA48762.1};
OS   Aquilegia coerulea (Rocky mountain columbine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC   Aquilegia.
OX   NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA48762.1, ECO:0000313|Proteomes:UP000230069};
RN   [1] {ECO:0000313|EMBL:PIA48762.1, ECO:0000313|Proteomes:UP000230069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA   Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA   Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT   "WGS assembly of Aquilegia coerulea Goldsmith.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-terminal
CC       Gly of ubiquitin. Involved in the processing of poly-ubiquitin
CC       precursors as well as that of ubiquitinated proteins.
CC       {ECO:0000256|RuleBase:RU366025}.
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|RuleBase:RU366025};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
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; KZ305030; PIA48762.1; -; Genomic_DNA.
DR   EMBL; KZ305030; PIA48763.1; -; Genomic_DNA.
DR   EMBL; KZ305030; PIA48769.1; -; Genomic_DNA.
DR   Proteomes; UP000230069; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
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; 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   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF46; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 10-RELATED; 1.
DR   Pfam; PF06337; DUSP; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00695; DUSP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 1.
DR   PROSITE; PS51283; DUSP; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU366025};
KW   Protease {ECO:0000256|RuleBase:RU366025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230069};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT   DOMAIN          47..162
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   DOMAIN          336..928
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          31..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   944 AA;  106446 MW;  289697DA0269E3C2 CRC64;
     MTMIPTTSVT LGSSHEEEEV EEELLSLMMD NDVAPPTTTT TTTSSSFTPD QEKQIINDLI
     HVSGSNAKPG DLFYLLSNRW YMEWLRYTGQ DSDENSTVST VCRPGQIDNH HLVIGGSDSY
     GDDLELLKTL QEGHDYVLVS QDVWKILYDW YKGGPALPRK MISQGVANKT LLVEVYPLCL
     QLIDARDDKQ YAIRISKKAT VRDLYNQVSV LLKLDEEKFR IWDYFNKKKS SVLAVADQDL
     EDANLQMDQD ILVEVEQHLW PSGLGLDSTG NGLALVPVEP ARSSITIAGG PTQSNGYSSG
     YISNFYEGNA LGSPLTGAED GYNLSKMAKG DRGGLSGLQN LGNTCFMNSS IQCLVHTPSL
     VEYFLHDYSA EINKQNPIGM QGELAIAFGE LLRKLWSSGR APIAPREFKT KLARFAPQFS
     GYNQHDSHEL LAFLLDGLHE DLNRVKFKPY IEIKDATGRP DEEVADECWE IHKARNDSVI
     VDVCQGQYKS TLVCPVCGKV SVTFDPFMYL SLPLPSTVTR SMTITVFYGD GSALPMPYIV
     TVPKHGLYKD LFQALGTACC LNSDELLLLA EVYDHGIFRY LVNPLEQLFT IKDEEHIVAY
     RLPKKQEGFT RLEIVHESKE NGVRKRLGTP LVTFIAEAAQ KSEDVQNAVQ MVLSPLLKVK
     VCHPSNCIHT SMEDGFASEN DIDGLFNAGN SGCRLRNQSV DKMELDQLSN GMDSFILSLT
     DEKGMHCSSI ENDFHFRQDQ FMRVILDWSD REYGMYNISF LEDLPVVHKT TTKKIRSEAI
     SLFSCLEAFL KEEPLGPDDM WYCPTCKEHR QATKKLDLWR LPEILVVHLK RFSYSRYLKN
     KLDTFVNFPT HNLDLRNYVK SNVAARSHTY ELYAISNHYG GLGGGHYSAY AKLSKENRWY
     HFDDSHVSSI NEDEIKTSAA YVLFYQRVQE KRVDESSQVH SSSG
//