ID   A0A0B4I3I7_METMF        Unreviewed;       538 AA.
AC   A0A0B4I3I7;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Endosome-associated ubiquitin isopeptidase (AmsH) {ECO:0000313|EMBL:KID99662.1};
DE   Flags: Fragment;
GN   ORFNames=MAJ_04492 {ECO:0000313|EMBL:KID99662.1};
OS   Metarhizium majus (strain ARSEF 297).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium;
OC   Metarhizium majus.
OX   NCBI_TaxID=1276143 {ECO:0000313|EMBL:KID99662.1, ECO:0000313|Proteomes:UP000031176};
RN   [1] {ECO:0000313|EMBL:KID99662.1, ECO:0000313|Proteomes:UP000031176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 297 {ECO:0000313|EMBL:KID99662.1,
RC   ECO:0000313|Proteomes:UP000031176};
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT   adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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:KID99662.1}.
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DR   EMBL; AZNE01000016; KID99662.1; -; Genomic_DNA.
DR   RefSeq; XP_014578656.1; XM_014723170.1.
DR   AlphaFoldDB; A0A0B4I3I7; -.
DR   MEROPS; M67.A14; -.
DR   HOGENOM; CLU_023304_4_0_1; -.
DR   OrthoDB; 5490729at2759; -.
DR   Proteomes; UP000031176; 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   PROSITE; PS50249; MPN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000031176};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          362..492
FT                   /note="MPN"
FT                   /evidence="ECO:0000259|PROSITE:PS50249"
FT   REGION          125..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          217..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          322..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..233
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        263..286
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KID99662.1"
SQ   SEQUENCE   538 AA;  60550 MW;  2F0265383F6CD6A0 CRC64;
     MDAGSGMRPT RPQSVKELVA QAENFTFNAN IPFKHWTRAA ETLYQEASFA LSDGDYGRAY
     MMLYRHSVLV LKCLQTHPQF KDPESRKAFR PLSKRIDRVI ADLEEIKPII NDEYAEWERV
     RPAGSKLEEQ GPIKSPSSYG EFAARDPSLS GNATVLDASE NQELAVELAQ KELARRDTVR
     QANRRTRVYG DTILTSRSGD GQKLDFSLQS QMEAVRRATE SSQQDLYESQ THKPTATPHR
     DAVPQSYVYP SISKSRPLQL DEAPRTPPRP PSLSPPSRPP KEYIHAPPGD PSYISRRELP
     VVPNKVPVAD SLSARYPSYE VARKNQPPLP PKTLDGPSLP KKERLAFKPG AYLENGDPIR
     SVFLPSKLRA AFLDVAAPNT NKGLEMCGIL CGTPVNNALF VRSLLIPDQK CTSDTCETEN
     ESAIFDYCAG EDLMVLGWIH THPTQTCFMS SRDLHTHAGY QVMMPESIAI VCAPRFTPSY
     GIFRLTHPPG LDHILDCRQS ETFHQHSVDN LYRETEYPNG HVYESEKMPF EIKDLRRK
//