ID C1FZR7_PARBD Unreviewed; 843 AA.
AC C1FZR7;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Ubiquitinyl hydrolase 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PADG_00107 {ECO:0000313|EMBL:EEH43818.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH43818.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH43818.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH43818.2,
RC ECO:0000313|Proteomes:UP000001628};
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; KN275957; EEH43818.2; -; Genomic_DNA.
DR RefSeq; XP_010755695.1; XM_010757393.1.
DR AlphaFoldDB; C1FZR7; -.
DR STRING; 502780.C1FZR7; -.
DR MEROPS; C19.099; -.
DR GeneID; 22579998; -.
DR KEGG; pbn:PADG_00107; -.
DR VEuPathDB; FungiDB:PADG_00107; -.
DR eggNOG; KOG1863; Eukaryota.
DR HOGENOM; CLU_003532_2_0_1; -.
DR InParanoid; C1FZR7; -.
DR OMA; DTDWGFA; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000001628; 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:UP000001628};
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 843 AA; 96008 MW; 8C738E66A13CDC58 CRC64;
MVKWLPVDPA LETEEQTHFT WRLPNWTELE KTELSPKFEC GGSKWRILLY PHGNSHNQHL
SVYLKHGYDE GEMPGHWSAC VQFTLVLWNT ESPSSYISKN AKFRFSTDGP DWGFTKFCEL
RKLLGYLGDK PSLLGNEEAN ITAYVRTIRD HTGVLWHTFL DYDSKKATGL IGLKNLGSTG
YLNVILQIFY FTNLFRKVTK IKKTVYQLPL DNDSSKNTFL WALQRLFYSL QTDDSPVSAL
ELTRGLGWGP QHLFMQQDVQ EMARVFMERF TVESKLSDIF LGRVKSYVSV DGVQKLRIEE
FLDISLNVQN IPSLAESFQD YTRENTDEER TEHGIRKTTT GVIFGSFPTV LHLHLKRYAY
DMTQRQLLKV NDTFSYPEEF DASPYLSVDS DKSEPWIYRL TGVVVHSGGV HGGRYWVYLR
PSPNGSFYKF DDDRVTRAML RNVIEENYGA EGKATNAYML LYVRKSRIDD ILVDVKEADI
PTYIKTGLAQ DRETAERQKK EREEDPLYMG ISLITASSFR HHDGFDLANN DLDQDDKAAS
TFIRVLKETT VGDFTQQVAQ KLSLDHCHIA LWVCINRQNG TRRPHVPLLQ PEVTIEKAFL
NVAARGKIHQ LWVEVGPTVA GVRVPPPKVT TEGTTIMIFL KYFDVVNQTL RGVNTLYVQR
GSAVGPAVLT AMGWPSDVKF SVREEVKPSM ILSVDVNTTF ERAELGNGDI LCVQRRVKRN
ELPPNLRARD VTQYFDNLRN SDATTGLRHL RLYHNGSSIE NPSDIDCSSE TVHKPVNDSD
HFICCSNFDV DTVGDHDNED QGAAWDWCGS NQGGSRSQED HLYCPAPNGL GLRRGNDVTV
TER
//
