ID A0A2H3INV4_9EURO Unreviewed; 1116 AA.
AC A0A2H3INV4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=PENO1_018810 {ECO:0000313|EMBL:PCH06188.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH06188.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCH06188.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCH06188.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
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 -!- 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:PCH06188.1}.
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DR EMBL; NPFK01000031; PCH06188.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3INV4; -.
DR STRING; 290292.A0A2H3INV4; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF23; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE USP2; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:PCH06188.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381}.
FT DOMAIN 417..549
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 741..1113
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..346
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1116 AA; 123956 MW; 8E7767E5BFA119BF CRC64;
MSSGPTVLPS AFGSPATTPD QGGAIPGMQP SGARSSWATS TQNGRPVSYN SRGGRAPLPY
IKDLQDQAAH LEVDETSPIS RLLSTAAASV QQCQILLDGD QVGQAYVQYL RASEIVVNLV
PRHADYRTLH AQHPGLYAQF QKLMMSISQQ QSAMDTIKQQ IIEDNLAHSL PRNDAAGTNN
TASSSTYIAY KPSNGAIRMP SPTDFQRGST SQQDSALKLK SMSSPEDVLA QRFARLRASQ
GLVSTNGSAV ADQNTSATSR PSAGVVTDYP PRPSPNSIPT TMSMSPGPGS PRPLGPRAMG
TSQYGSGVTA RKPLDTANVS LPRAPDPAYS PIWSIPSQPP QPNPPRKSTD SIQATNTRYS
QLAGSRVSSP SRFGDDDNPY RSRTPNGIHL AQENKATSAD IPHNTTIRAQ QLLEYMRKYN
VLVIDVRPRD TYDSGHIYAR SIICIEPVVL KENVSAEELE ERLIVSPEHE QSLFEQRNEF
DLVVYYDQNT DSVSYLAGSP VGTSAPHLRA LYDTLYEFNA YKPLKDGRPP ALLVGGLDAW
EDLVGSQSLA TSSTAAIMGS LQTKRVQQRP GRAFGRVPSA SANSSLEIRK RRLREFTPLN
HEELTAWMER AKNEEIKPGA YQGDEAGIPE EGADDDAVTE EPPSPFVHTY EDFLRRFPEP
QAIQQSMVVP EPRVLVSSTP NYASPVPVAP SRPPPAIPRP SYGGVADGRQ IQPTLARQNS
ATKTALYTSN SFMTRLKLPR TGLTNFGVTC YMNSTLQCLS STAVMSKFFI DDRFRYYVQK
NWKGSQGVMP GLYANLIRSL WKNDVEVIIP TSFRNFCGRL NREWAIDRQQ DAKEFFDFLV
DCLHEDLNIN WQRTQLRPLT LEEEMQRERM PVPKVSKIEW DRYCHREESF ISSLFAGQHA
SRLKCTTCKR TSTTYEAFYS ISVEIPHTGT GDIYQCLRSY CQEEMLSGDE VWKCPYCKCE
RVATKQIIIT RAPQILVIHL KRFSASKTQS ARKIHTPVDF PLHGLRMDKF VIPYPAANPE
SGDHVNGNAG APAPSSMTLS PTTPPFTYDA YGVLRHLGST LSGGHYISLV RDAQRQCWRK
FDDERVSDFN PRDLRFSDRL QNEQAYILFY ERVPAK
//
