ID A0A2B7ZTE3_9EURO Unreviewed; 740 AA.
AC A0A2B7ZTE3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Ubiquitinyl hydrolase 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=GX50_00638 {ECO:0000313|EMBL:PGH36453.1};
OS Emmonsia crescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=73230 {ECO:0000313|EMBL:PGH36453.1, ECO:0000313|Proteomes:UP000226031};
RN [1] {ECO:0000313|EMBL:PGH36453.1, ECO:0000313|Proteomes:UP000226031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH4076 {ECO:0000313|EMBL:PGH36453.1,
RC ECO:0000313|Proteomes:UP000226031};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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 -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PGH36453.1}.
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; PDND01000007; PGH36453.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7ZTE3; -.
DR STRING; 73230.A0A2B7ZTE3; -.
DR VEuPathDB; FungiDB:EMCG_06855; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000226031; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF644; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7; 1.
DR Pfam; PF00917; MATH; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50144; MATH; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000226031};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 17..146
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 172..460
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 740 AA; 85279 MW; 2F72DCEC4F044CB0 CRC64;
MMARLLPADP NLETADQTYF TWRLPNWTEL EKTELSPKFE CGGSKWRILL YPRGNSNSQH
LSIYLKHGFD DGEVPDHWNA SVQFSLVLWN TNSPEAYISH KINFRFSVED PDWGFTRFCE
LRKLLGHLGD KPSLLGNDEA NVTAYVRVIR DHTGTLWHTF QDYDSKKMTG LVGLKNLGST
GYLNVILQCF YFTNIFRKAT YQLPLGDESS KNTFLWALQR LFYSLQSDDK SVSTLELTKA
LGWGPQHLYM QQDVQEMARL LLDRFLNEPK LPDIFRGKSN SYVSIDGVQH SKIEDFLDLS
INVQNIRSLE DSLAEYIRER VDEERTQHDI QKTKIGIIFE SFPDVFHVHL KRYTYDMAQR
QLLKVNDFFT YPEEFDASPY LSADADKSEP WIYRLTGVVV HSGGVQGGRY WAFLRPGANV
PFYKFDDERV TRAMLKNAME DNYGGEGQVT NAYMLIYIRK SRINNIFANV TAADVPAYIK
NGLVEDREMA ERLKKEKEEQ HLYLQINLIS ATHFRFHSGF DLTSADLGNG DMTALRVRKE
TLVRDFTQKA AEKMGLEPGC ITLWIFISRQ NGTRRPHEPL LRANIKIQQA FLDAGFTGTN
PQIWVEVIRA ETGVPVPVPR ATSGEDTILI FVKNFDVVKQ TLRGVTSLCV RKDSTVRPHL
LTLMEWSEDT RFSVHEEVKP AMILNVDPNT TFERAELGNG DILCVQKLVK RSEYPPNLLA
KDVTQYFDNL RNERNKKKYT
//
