ID A0A151WIJ7_9HYME Unreviewed; 921 AA.
AC A0A151WIJ7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, 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 ORFNames=ALC60_13376 {ECO:0000313|EMBL:KYQ47620.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ47620.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ47620.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ47620.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ47620.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-2015) 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 -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR EMBL; KQ983089; KYQ47620.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151WIJ7; -.
DR STRING; 64791.A0A151WIJ7; -.
DR Proteomes; UP000075809; Unassembled WGS sequence.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02667; Peptidase_C19K; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
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:SF39; UBIQUITINYL HYDROLASE 1; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
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 Hydrolase {ECO:0000256|RuleBase:RU366025, ECO:0000313|EMBL:KYQ47620.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000075809};
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 31..154
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 188..920
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..879
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 921 AA; 103717 MW; 8DDF96A4B6554D37 CRC64;
MSKKRNRQPD ANPDVSEAST ESCEETSSAG AKCLHIAKAI NLNKVKKNLK KTGILSKCSM
CKKLEMDLNA AEKCDISKPL WICLQCGEQG CSKEQKQHAF EHYRKPHSDC HCMVMDSHHW
SVWCYQCEIE VHPNSRKKLL ETVEFIKKYV NIPQISQSKM QAIQCQKETI IDVQVKEHKI
LNNLPKVGGL ANLGNTCFFN AVLQCLSQTP YLVKVLDDLR VPGQKFVLPG GKHKPPPIEG
TLERWGSFTS ILCETLSKMQ NTNGHQTYTP LNLLCKLRKK TTQCVDGGQH DSHEFLRHLL
EIVRNEDLRR YQSIILKEVG LSEKTKPDCV EKSLKSRVKF YGNQASTRLL GPEAVFRGVL
VSTLECLDCH HSSQRTEPFL DLSLPVTADK PQPPLLKRKN SEFEDAFDMM NIQRHDCQTE
IWKSEDTPWK QLKKEKKAAR KNRKNKRHEN YNNSNALMDL NNPAEENTDN ILKSEESDAD
VEDNIEMDNS HPEIGESGYS SEKASAVTSP VSPADHHHHH HHHYHHHLNN DFNGTISPEN
SNLDNRNLDP AQVRHPVNIN ALTSPSPTDV SMTDLTEIRM PFEKTDRNIG TISSENEVSA
TALTSPIIVN SNVTSPEIPT ASLSSSAASK ESPTSPVNNE EIAERLDGVE TWMATTLSRY
GRRKYNNGTS NGDDPEEQDV YNELGDIVTG MSRLGIAGHQ SPGRYTTKEG ECSVESCLNQ
FTALELMTGS NKVVCEACTA REKKLFFPQN QEGSSKMVCT SSTKQYLISQ VPPILILHLK
RFQTQRVGFR KVFKHVSFPI LLDLAPVCTD RKKSRLYALY GVVEHSGTVH GGHYVAYVKT
RLPLSPDDPR WKFLPKDKDP KANNESSSSD SDEEEASAKG ISIVEPPPGK WYYVSDSRVS
EVDENTVLQS QAYLLFYERI L
//
