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
//