ID A0A423VLI5_9PEZI Unreviewed; 548 AA.
AC A0A423VLI5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=MPN domain-containing protein {ECO:0000259|PROSITE:PS50249};
GN ORFNames=VMCG_09167 {ECO:0000313|EMBL:ROV91856.1};
OS Valsa malicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=356882 {ECO:0000313|EMBL:ROV91856.1, ECO:0000313|Proteomes:UP000283895};
RN [1] {ECO:0000313|EMBL:ROV91856.1, ECO:0000313|Proteomes:UP000283895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-1 {ECO:0000313|EMBL:ROV91856.1,
RC ECO:0000313|Proteomes:UP000283895};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M67C family.
CC {ECO:0000256|ARBA:ARBA00010981}.
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:ROV91856.1}.
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DR EMBL; LKEA01000053; ROV91856.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423VLI5; -.
DR STRING; 356882.A0A423VLI5; -.
DR Proteomes; UP000283895; Unassembled WGS sequence.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0061578; F:K63-linked deubiquitinase activity; IEA:InterPro.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR CDD; cd08066; MPN_AMSH_like; 1.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR044098; STAMBP/STALP-like_MPN.
DR InterPro; IPR015063; USP8_dimer.
DR PANTHER; PTHR12947; AMSH-LIKE PROTEASE; 1.
DR PANTHER; PTHR12947:SF13; FI19924P1; 1.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF08969; USP8_dimer; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR SUPFAM; SSF102712; JAB1/MPN domain; 1.
DR SUPFAM; SSF140856; USP8 N-terminal domain-like; 1.
DR PROSITE; PS50249; MPN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000283895};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 369..496
FT /note="MPN"
FT /evidence="ECO:0000259|PROSITE:PS50249"
FT REGION 176..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..338
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 548 AA; 62375 MW; FB330236E5887A05 CRC64;
MDTAWTLPDR PMSITEISKE ADKFQFNALI PLKSWLRASD TLLRQGNTYV REGNLTQAYL
ILFRYSTLVL QHLPKHPDSK TPEGKKALKP LNARCIKVLE MLDKLKPQIT AAYDEWIKIH
ASQRDPSTEL EGEKSPYEKL AAKDPALSWN PKVRAKLLDA GENQDLAVNL AKQEIRRRDD
ARRATRQAGI SEEEELERRG AGLWDNWDTL GPQHGRHARD YSDDIRRNMD AARRRLDETE
QAGRPPSSES YPSRPSNYSF YDRPPSYQYP SISRSSGHQY ESSISETYDP RPLRPPSRPA
KEPIYHPEYR TEPAPPRPTK EPVYSPYNTP PPTALSQAPE LPPKTMDRKE RFTFRPAAYL
ENGTPIRPIF LPAKLREEFL RVAAPNTRKG LEMCGILCGT SVNNALFVSC LVIPQQTCTS
DTCETDNEES VIEFCMKEDL MVFGWIHTHP TQTCFMSSRD LHTQSGYQVM MPESIAIVCA
PRSDPSYGVF RLTNPPGLDH ILGCTQSTTF HQHSIDNLYT DANHPPGHVY HSSALDFSIE
DLRSSHRK
//
