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Database: UniProt
Entry: A0A1Z5TV71_HORWE
LinkDB: A0A1Z5TV71_HORWE
Original site: A0A1Z5TV71_HORWE 
ID   A0A1Z5TV71_HORWE        Unreviewed;       530 AA.
AC   A0A1Z5TV71;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=MPN domain-containing protein {ECO:0000259|PROSITE:PS50249};
GN   ORFNames=BTJ68_00178 {ECO:0000313|EMBL:OTA39920.1};
OS   Hortaea werneckii EXF-2000.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX   NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA39920.1, ECO:0000313|Proteomes:UP000194280};
RN   [1] {ECO:0000313|EMBL:OTA39920.1, ECO:0000313|Proteomes:UP000194280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA39920.1,
RC   ECO:0000313|Proteomes:UP000194280};
RA   Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA   Nislow C.E.;
RT   "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT   insights from long-read sequencing.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Endosome {ECO:0000256|ARBA:ARBA00004177}.
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:OTA39920.1}.
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DR   EMBL; MUNK01000001; OTA39920.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5TV71; -.
DR   STRING; 1157616.A0A1Z5TV71; -.
DR   VEuPathDB; FungiDB:BTJ68_00178; -.
DR   InParanoid; A0A1Z5TV71; -.
DR   OrthoDB; 5490729at2759; -.
DR   Proteomes; UP000194280; Unassembled WGS sequence.
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   PROSITE; PS50249; MPN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000194280};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          352..482
FT                   /note="MPN"
FT                   /evidence="ECO:0000259|PROSITE:PS50249"
FT   REGION          132..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..248
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..292
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..333
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..348
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   530 AA;  58558 MW;  7255A0259AAAA6C0 CRC64;
     MAVSRHHAAL TRPLSIPEIV AQAQDFEFSA QRTLQQWLKA AKMLLTEAAI CEQDGNIQMA
     YLYLYRHAEL VLDKLPKHPN YKDPSAREEL AQARKALQKN IRKLEDWKPK IESEFSKYAK
     ALEKREAERQ RVLEERQRDE RAGILPAGGA SRKRQSDDGM LGDGSQIINA TENSQLAVDL
     ARREIRRRDA NKQTTRRACL SPSEVANRRR GIVVDDSHAA EPGYDQADGV REVGRQLYGH
     RRRESASSQK TANRGSDGHA YHYPSVPSRE NAMDWNSPPL QPAPPLPEKF RQPPARPAKE
     AFEASAPPLP PKPHDSHPST PSLKPPSPPS PAASKYTFQP SATTEGGSPL RTMLLPPDLR
     TTFLKLAAPN TALNLETCGI LCGTIISNAL IISHLILPDQ TSTPETCDTT AAGDNALFDY
     CSSADLLVMG WIHTHPSQTC FLSSRDCHTN AGYQVMMPEA IAIVCAPRHE PGWGVFRLTD
     PPGLPHVLAC TQTGTFHPHS ERELYTDALR PGHVVEGPGL GFEIVDLRKG
//
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