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Database: UniProt
Entry: X0B431_FUSOX
LinkDB: X0B431_FUSOX
Original site: X0B431_FUSOX 
ID   X0B431_FUSOX            Unreviewed;       859 AA.
AC   X0B431;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Insulysin {ECO:0000313|EMBL:EXK76516.1};
GN   ORFNames=FOQG_18745 {ECO:0000313|EMBL:EXK76516.1};
OS   Fusarium oxysporum f. sp. raphani 54005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK76516.1, ECO:0000313|Proteomes:UP000030663};
RN   [1] {ECO:0000313|EMBL:EXK76516.1, ECO:0000313|Proteomes:UP000030663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54005 {ECO:0000313|EMBL:EXK76516.1,
RC   ECO:0000313|Proteomes:UP000030663};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum PHW815.";
RL   Submitted (NOV-2011) 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; JH658707; EXK76516.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0B431; -.
DR   eggNOG; KOG0959; Eukaryota.
DR   HOGENOM; CLU_004639_1_2_1; -.
DR   Proteomes; UP000030663; 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; 3.
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; 1.
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:UP000030663};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          49..194
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          259..529
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          535..717
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          793..820
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        793..815
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   859 AA;  98459 MW;  318A617E8AE8B639 CRC64;
     MPHSECEEDA PTVAGNAHIP VTLVTDSLEK PLQDDRIYRV IRLGNELEVT LVHDPKTDKA
     SAALDVNVGY FSDEPDIPGM AHALLFMGTK KFPIENEYGQ YISANAGDSN AYTGPTSTTF
     FFDISAKPDN DQEPSDTNPS PLREALDRFA QFFIEPLFLA ETLDRELKAV DSEHKKNLQD
     DILRLHQLGK SLSNSEHPFS YFGTGNFDVL KTLPEARGVN VRDKFIEFHA RHYSANRMKL
     VVLGREPLDV LQKWVAEFSA MQKPLPREWL LSGHSRLREF APDEIQKALA TIHPDNFRMT
     IVSREYPGNW DQKEKWYGTE YRHEKIPDDL MKECKKAYAV SPKDRLSALH LPHKNPFIPE
     DLKVEKEEVS EPAPKPWILR NDSIARTWWK KDDTFWIPRA NVFVSLKTPL IHASAANNVL
     ARLFSDLVHD ALEEYSYDAD LAGLHYYVKL DARGLLLAVS GYNDKLPVLF EHIVTTMRDM
     DIKEGRFEIL KDSLTREYRN WELASPHGQV GHYLDWLNAP ERNFIAPELA AELSSVTLEG
     VRLFQKQMLG QVFIEVYVHG NMYKEDALKA TDVVESILKP RVLPKAQWPI LRSLILTKGS
     NYVFRKTLKD PKNVNHCVET WFYVGSREDR DVRTKTLLLE QMLSEPAFDQ LRTKEQLGYI
     VWRGTRDFKT TCGFRFLIQS EMTAEFLDSR IEAFLMRYAD TLEKMSETEF EGHKQSLIVQ
     RLEMFQTLDA ESVHHFTQIT NEYYDFESAQ RDAAQIKLLT KPEVIEFFNQ RLNPASTQRA
     RLSIHLQAQV KAEGVDKRQE EAQKKADEEP SPGDAVKTAE EITDVSLYRV GLTASSGARP
     VKDIHEYEDM NVALEGVSG
//
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