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Database: UniProt
Entry: A0A2R6RW36_9APHY
LinkDB: A0A2R6RW36_9APHY
Original site: A0A2R6RW36_9APHY 
ID   A0A2R6RW36_9APHY        Unreviewed;       662 AA.
AC   A0A2R6RW36;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=MPN domain-containing protein {ECO:0000259|PROSITE:PS50249};
DE   Flags: Fragment;
GN   ORFNames=PHLCEN_2v1755 {ECO:0000313|EMBL:PSS34205.1};
OS   Hermanssonia centrifuga.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Meruliaceae; Hermanssonia.
OX   NCBI_TaxID=98765 {ECO:0000313|EMBL:PSS34205.1, ECO:0000313|Proteomes:UP000186601};
RN   [1] {ECO:0000313|EMBL:PSS34205.1, ECO:0000313|Proteomes:UP000186601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FBCC195 {ECO:0000313|EMBL:PSS34205.1,
RC   ECO:0000313|Proteomes:UP000186601};
RA   Granchi Z., Peng M., de Vries R.P., Hilden K., Makela M.R., Grigoriev I.,
RA   Riley R.;
RT   "Genome sequence of the basidiomycete white-rot fungus Phlebia
RT   centrifuga.";
RL   Submitted (FEB-2018) 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:PSS34205.1}.
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DR   EMBL; MLYV02000141; PSS34205.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R6RW36; -.
DR   STRING; 98765.A0A2R6RW36; -.
DR   Proteomes; UP000186601; 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   PANTHER; PTHR12947; AMSH-LIKE PROTEASE; 1.
DR   PANTHER; PTHR12947:SF13; FI19924P1; 1.
DR   Pfam; PF01398; JAB; 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:UP000186601};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          511..640
FT                   /note="MPN"
FT                   /evidence="ECO:0000259|PROSITE:PS50249"
FT   REGION          120..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          395..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..272
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..305
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..347
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..417
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..445
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..466
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..490
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         662
FT                   /evidence="ECO:0000313|EMBL:PSS34205.1"
SQ   SEQUENCE   662 AA;  74475 MW;  A343AD02A5DB7837 CRC64;
     MNSSYTPGDH PATIAELASI AQQDIWDASR PLKHWLRTAE KARKVGQAEA EAQNYEAAFV
     EFAKAATIVL ERLPKHSEYQ LLLNADQRHN LGLNGQDILD HLSQLKPILV DRYERWRSGA
     DSRASSSLSS DPRSREDSAR RKREAQEQER AMHAKEAVQR EEEWKRQDLA KRQAEELERR
     VREESSWARQ PSEVRYREAS EARRAADARE AAEHERIAQA ARLKREEDVR RQQSDDERRE
     EERSRRRADE RRRQEQDGIL RRQQEAEASA RAARREIVAA SGSVTTPQPS RPASSSQNTS
     FTDPYGRAPP TMPLESPSRY DDDTDVEGTY DRNMPWQRSR HADQTPTKAK HLNAGAMYPP
     SITTTSPAPP ELGSIRYPTL MSQHQLKQGY VPSLQSMFSH PSSDPPSNSS LLFDAKPSTP
     LYSNILPKPS APAGPPIPPY APGMPMPDTN SYQYDSHYSS SEPRGHSPSG ARPPLPPLPS
     KEPQPPPSSS TAPRIVRGAS AEPDIHELKS VKLPRECLPR FLSIARVNTL QNRETCGLLL
     GKDKGSKFVV TTLLIPKQHS TSDTCTMDEE ELVLQFTEER HLITLGWIHT HPTQSCFMSS
     VDLHTHSGFQ RMLPESFAVV CAPHSTPTFG IFRLTDPDGL QTVLKCTAKE AFHPHPEVPI
     YT
//
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