ID A0A6J1RA34_9HYME Unreviewed; 931 AA.
AC A0A6J1RA34;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 18-JUN-2025, entry version 23.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=LOC112466946 {ECO:0000313|RefSeq:XP_024891083.1};
OS Temnothorax curvispinosus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Temnothorax.
OX NCBI_TaxID=300111 {ECO:0000313|Proteomes:UP000504618, ECO:0000313|RefSeq:XP_024891083.1};
RN [1] {ECO:0000313|RefSeq:XP_024891083.1}
RP IDENTIFICATION.
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_024891083.1};
RG RefSeq;
RL Submitted (MAR-2025) 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR RefSeq; XP_024891083.1; XM_025035315.1.
DR AlphaFoldDB; A0A6J1RA34; -.
DR GeneID; 112466946; -.
DR Proteomes; UP000504618; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01795; Ubl_USP48; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.30.2230.10; DUSP-like; 2.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR050164; Peptidase_C19.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR044743; Ubl_USP48.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF722; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 48; 1.
DR Pfam; PF06337; DUSP; 2.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 2.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 2.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS51283; DUSP; 2.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000504618};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 1..193
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 389..484
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 652..763
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT REGION 225..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 931 AA; 106925 MW; F8CA047C923F95F7 CRC64;
MITCCSTCST EYPTSTTFYE LDLQLAATLK EAIDNYLSEE QLTGANQYHC VTCNDKKDAR
RFIRLESLPE TLNIQLMRFV FHRDSGQKKK LNSYIQFPED LDMSEYVGCQ PQTHLYSLVA
VLSHKGPSAH SGHYIANICN SSGEWYQFSD DKVEKMQNKR IEDGVNDKSM KRGRVPKGFL
SSNTAYMLVY KKLTADWRTN GTKKVKLKKL DTEVNVPSDT VSSEKLIVKE KSDETSDETK
QKPDIEDAPS IQEENPETIP KSDSENVIET DEDAISKKTD IPTTDKSETE KTVASTNGCK
DTHDSTLEQL QNKVHCLKQP VVKVVKLDYK RLNGDAHRAM SCGERDFYEE MEFENWQVSS
TMRELVRQEN VKHELSLLAA QQEKQKEIED QNSKRQLIID VYNIIQSTVS WDNYYWIPTD
WLSKWLNGHS SAVDVRPIDN SNLMCSHYRL DPLKVSRMKC VPEAAAQMLY DKYQGGPRLD
QTFLCEVCVK RRCKLLRFKL ALERDHKEVG ELIRTFKESP ETSYIIGTDS LRSWRRLAME
TFQEDVEQKV DDCQDTLQEE SKCTDKDGSD CPKEVEENKE NEAIINFNED LLCEHKSLKT
ADSSRKVIPQ EAWTILKKYF PDSKEYPVGS PSCSICEERM ENAQRAKKDD KIKAKQQKDE
LTDLYYGRNR NEISKCDDPE KSFYIVEKSF LDGWRSFIRY AEIYSRTPPA SIQNASLLCE
EHKGFLHTPR INNELYSIVT AEEWSKLMQF YEADYPIIIK KIADDYQTNP GPCAACMLAK
IEQERLESLK YERATIYVKC IDENEESKTD NDYEVAVKRP KMGKARPSRS RRKLKGSHEL
KVSSEITLKE LKVMTMQICG AGPYDQHIML GEHELIDDNL SLAALGIFPG ALLTLKIDAP
LENETDVESD AHNFDSLSPE KGFKGTELVP S
//
