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Database: UniProt
Entry: A0A074WC30_9PEZI
LinkDB: A0A074WC30_9PEZI
Original site: A0A074WC30_9PEZI 
ID   A0A074WC30_9PEZI        Unreviewed;       467 AA.
AC   A0A074WC30;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=MPN domain-containing protein {ECO:0000259|PROSITE:PS50249};
GN   ORFNames=M437DRAFT_80137 {ECO:0000313|EMBL:KEQ67492.1};
OS   Aureobasidium melanogenum CBS 110374.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ67492.1, ECO:0000313|Proteomes:UP000030672};
RN   [1] {ECO:0000313|EMBL:KEQ67492.1, ECO:0000313|Proteomes:UP000030672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ67492.1,
RC   ECO:0000313|Proteomes:UP000030672};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
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}.
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DR   EMBL; KL584824; KEQ67492.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A074WC30; -.
DR   STRING; 1043003.A0A074WC30; -.
DR   MEROPS; M67.A14; -.
DR   HOGENOM; CLU_023304_4_0_1; -.
DR   OrthoDB; 5490729at2759; -.
DR   Proteomes; UP000030672; 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:UP000030672};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          287..419
FT                   /note="MPN"
FT                   /evidence="ECO:0000259|PROSITE:PS50249"
FT   REGION          176..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..215
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..256
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   467 AA;  51553 MW;  7B0FCAA86B47B933 CRC64;
     MTAPKSVEQI VAEASNFDHA ANIPLNMALR TAQNMTSQAA NYERDANLQE AYYFLYRHAD
     FFFTHISKHP DAKKPEYKAQ MARTRDHVKA DLSRMEALKP EITSRYQKYQ DVVKRRNQLK
     SQTDTPAASQ ESFVLSAAEH KDVALQLANR ELRRRAKDSR DDNAVMDDLS RGIQDLGRCI
     DTPRDSSRNT STSQTSSPYH YPSVPSHASI VPSSPSLAPS RPPKDELSSH KAPPPLPSKP
     VQSLNSPPPL PSKAGGPARP PKQDISPTQS YQFQPAAYTE NGTPLRTLFL PTSLRTSFVS
     LAATNTSSNL ETCGILCGTL ISNALFISHL VIPDQTATSD TCETTDQGET DLFDYVDHEG
     LMVCGWIHTH PTQTCFLSSR DLHTSVGYQV MLPESVAIVC APSKSPDHGI FRLTDPPGKQ
     AILNCHKPGL FHPHDVDNLY TDATRPGHVS ELSGLQFQVV DLRKGKK
//
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