ID   A0A1S3DNK9_DIACI        Unreviewed;       806 AA.
AC   A0A1S3DNK9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN   Name=LOC103521783 {ECO:0000313|RefSeq:XP_008485110.1};
OS   Diaphorina citri (Asian citrus psyllid).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Psylloidea; Psyllidae;
OC   Diaphorininae; Diaphorina.
OX   NCBI_TaxID=121845 {ECO:0000313|Proteomes:UP000079169, ECO:0000313|RefSeq:XP_008485110.1};
RN   [1] {ECO:0000313|RefSeq:XP_008485110.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
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DR   RefSeq; XP_008485110.1; XM_008486888.3.
DR   AlphaFoldDB; A0A1S3DNK9; -.
DR   STRING; 121845.A0A1S3DNK9; -.
DR   PaxDb; 121845-A0A1S3DNK9; -.
DR   GeneID; 103521783; -.
DR   KEGG; dci:103521783; -.
DR   OMA; RRKHALM; -.
DR   OrthoDB; 5474185at2759; -.
DR   Proteomes; UP000079169; Unplaced.
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:SF24; USP DOMAIN-CONTAINING PROTEIN; 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   ECO:0000313|RefSeq:XP_008485110.1};
KW   Protease {ECO:0000256|RuleBase:RU366025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079169};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT   DOMAIN          11..115
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   DOMAIN          244..804
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
SQ   SEQUENCE   806 AA;  92401 MW;  A203B1AD3B061904 CRC64;
     MVTNISKIVD TTPEVQKREF QDVSQANMQC GDTWYILESD WYHRFQQFIG LEDPDGMVCN
     PGPIDNSSLL DDHGDLKKGL LENDDFVFIP ENTWKKLHSW YGIVKGQSPI ARKVIPIGMF
     SQSFIVEAYP LELKIATVEN QTRTISHKFS KSDSIKKIAD FAREHFKISS DIKVQLLTEF
     KHDPLSESST VADENLIDGQ MILVQTKSDS TEWKLNGSDV DISEPSTSIV RSDINSCRYT
     PGLCGLSNLG NTCFMNSVLQ CMSNCPPITK YFLEDQHLSE LNTTNPLGMK GLVAKAFGEL
     IKTMWSGDNN HTAPSNFKIQ VSRFAPQFSG YQQHDAQELL TFLLDGLHED LNRVKKKPYI
     ELKDADGRPD EVVAKESWDN YLKRNNSVIV DYFHGLLKSH VTCPQCECVS TTFDPFCYLS
     LPLPPKKNSY IQIKYIPYDQ NKREVIYKLC IARHSLIRDI CVDFIALAKL HVNIDQLVVA
     KVVKSHIHSF FSMNDTLDDV TERDNLLYVY DLPVSHNSTD FNVIPVCTWE VSDGDSTFCK
     NELIDDPILV AFPLKELSYA EIFQIIIGQM SRHFNIPKND SLEDENNLSL VSEYVSIYQV
     SVNLSTHEKL SPDTTYILNE KNKLLAIQIE SSTKKEYHKE VTPLKQDATE QRYRLKHSLD
     ECLDLFVTNE KLGSDDAWYC PRCKKFQQAT KKFDLWSVPK VLIIHLKRFH YSRYRRDKIE
     TLVEFPVHDL DISKIVINKS EQLKKYDLVG VCNHYGTLGG GHYTAYAKND IDKNWYLFDD
     SSVRKATESE VVSSCAYVLM YIQQDD
//