ID A0A0A2V747_PARBA Unreviewed; 656 AA.
AC A0A0A2V747;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PAAG_11336 {ECO:0000313|EMBL:KGQ01945.1};
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779 {ECO:0000313|EMBL:KGQ01945.1, ECO:0000313|Proteomes:UP000002059};
RN [1] {ECO:0000313|EMBL:KGQ01945.1, ECO:0000313|Proteomes:UP000002059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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}.
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DR EMBL; KN293994; KGQ01945.1; -; Genomic_DNA.
DR RefSeq; XP_015703426.1; XM_015847004.1.
DR AlphaFoldDB; A0A0A2V747; -.
DR STRING; 502779.A0A0A2V747; -.
DR MEROPS; C19.099; -.
DR GeneID; 9099967; -.
DR KEGG; pbl:PAAG_11336; -.
DR VEuPathDB; FungiDB:PAAG_11336; -.
DR eggNOG; KOG1863; Eukaryota.
DR HOGENOM; CLU_003532_2_0_1; -.
DR OMA; ISCYEIT; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000002059; Partially assembled 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:UP000002059};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 16..145
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 171..465
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 656 AA; 74752 MW; 519D8C60D17A2047 CRC64;
MAKWLPVDPA LETEEQTHFT WRLPNWTELE KTELSPKFEC GGSKWRILLY PHGNRHNQHL
SVYLKHGYDE GEMPGHWSAC VQFALVLWNT ESPSSYISKN AKFRFSTDGP DWGFTKFCEL
RKLLGYLGDK PSLLGNEEAN ITVYVRIIRD HTGVLWHTFL DYDSKKATGL IGLKNLGSTG
YLNVILQSFY FTNIFRKVTK IKETVYQLPL DNDSSKNTFL WALQRLFYSL QTDDSPVSAL
ELTRGLGWGP QHLFMQQDAQ EMARVFMERF AVESKLSDIF LGRVKSYISV DGVQKLRIEK
FLDISLNVQN IPSLAESFQD YIRENTDEER TEHGIRKTAT GVIFGSFPTV LHLHLKRYAY
DMAQRQLLKV NDTFSYPEEF DASPYLSADS DMSEPWIYRL TGVVVHSGGV HGGRYWVYLR
PSPNGSFYKF DDDKVTRAML RNVMEENYGA EGKATNAYML LYVRKSRIDD ILVDVIEADI
PTYIKTGLAQ DRETAERQKK EKEEDPLYMG ISLITASSPH VPLLQPEVTI EKAFLNVAAR
GKIHQLWVEV GPTVAGVPVP PPKVTTEGTT IMIFLKYFDV VNQTLGGVNT LYVQQGSAVG
PTVLTAMGWP RDVKFSVHEE VKPSMILSVD VNTTFERAEL GNGDILCVQR RVKRNE
//
