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Database: UniProt
Entry: A0A0D2IXJ5_9EURO
LinkDB: A0A0D2IXJ5_9EURO
Original site: A0A0D2IXJ5_9EURO 
ID   A0A0D2IXJ5_9EURO        Unreviewed;      1096 AA.
AC   A0A0D2IXJ5;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Peptidase M16 N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Z520_01905 {ECO:0000313|EMBL:KIY01767.1};
OS   Fonsecaea multimorphosa CBS 102226.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIY01767.1, ECO:0000313|Proteomes:UP000053411};
RN   [1] {ECO:0000313|EMBL:KIY01767.1, ECO:0000313|Proteomes:UP000053411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 102226 {ECO:0000313|EMBL:KIY01767.1,
RC   ECO:0000313|Proteomes:UP000053411};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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DR   EMBL; KN848064; KIY01767.1; -; Genomic_DNA.
DR   RefSeq; XP_016635889.1; XM_016772419.1.
DR   AlphaFoldDB; A0A0D2IXJ5; -.
DR   STRING; 1442371.A0A0D2IXJ5; -.
DR   MEROPS; M16.020; -.
DR   GeneID; 27707651; -.
DR   VEuPathDB; FungiDB:Z520_01905; -.
DR   OrthoDB; 129328at2759; -.
DR   Proteomes; UP000053411; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR032632; Peptidase_M16_M.
DR   PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   Pfam; PF16187; Peptidase_M16_M; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053411};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          33..195
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          221..400
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          406..695
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          700..881
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   1096 AA;  125973 MW;  E5D139A27478F13C CRC64;
     MNSVRRITDE LEKPDLDDRS YRVIELPNKL EALLVHDAET DKASASLNVN VGNFSDEEDM
     PGMAHAVEHL LFMGTEKYPI ENEYSSYLSS NSGHSNAYTA ATQTNYFFEC AARHESNDKL
     TNGVVNGTAH DTVNGTSRGP LYGALDRFAQ FFVKPLFLEN TLDRELRAVD SENKKNLQSD
     GWRLSQLAKS LSNPKHPFHH FSTGNLQTLR DEPEKKGVKI RDEFIRFYER HYSANRMKLV
     VLGRESLDEL ENWVVELFSE VKNKDLPLNR WDDIEVLSKD QLSTEIYAKP VMESRSLEIS
     FPWQDEEDMF ETQPARYISH LIGHEGPGSI LAYLKDRGLA QTLSAGYHPV CPGSAFFEID
     IGLTPDGLKN YHEIVKIVFR YIGMMKATPP VAWMHEEMKN MAEVDFRFRQ KSPASRFTSA
     ISCVLQKPEL PRNWLLSSTS KFRKFDAQAI AQAMQYLRED NFRLMLVAQD YPGDWDQKEK
     WYGTEYKVER IPTDVLSDIR RALSDSKSDR IPELHLPHKN EFIPTKLDVE KLDVKVPAKA
     PKLLRNDDKV RLWWKKDDAF WVPKANLYIK VRNTVTSANI ANYVKTNLFI DLVKDALSSY
     SYDAEISGLS YAIGPNMVGF DISVHGYNDK MAVLLEKILT TIRTIEIRTD RFEIIKERTA
     RRYKNWAYQQ PYYQIGDYTR WLLNERSWMN DAYAKELPHV TVDDIRTFVP ELLQQSHIEV
     LAHGNLYKEE AKKIGNLIES TLKSRAFPSS EWLLRRNVIL PEGSNFVYKH VLGDPANINH
     AIEYYLDVGH VMDLDLRAKT QLFSQMTDEP AFDQLRTKEQ LGYVVWSGIR PAAVTMGYRV
     LIQSERDPDY LETRINAFLL KFKSDLESMS DEEFEGHKRS LVNKRLEKLK NLDFETGRLW
     AYISAEYLNF YQVDRDVASI RQLTKDDMKR FYAQYIDPES PKRRKLSIHL EAQASSPVPE
     VSPAQQKDQF VGLIGQVLGS LSIDVDEEKL KVQFENVDPS SLPQVSNAVK EYIGTSTSPA
     KSNETLEQMK QAIPQMQVAL KIKPVEPPKD VTEVAAQIPT PVIIKDVARW RAGLEVTKGP
     VPVEDVHNFE DLEPKL
//
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