ID N4TSL0_FUSC1 Unreviewed; 743 AA.
AC N4TSL0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Putative aspartic-type endopeptidase opsB {ECO:0000313|EMBL:ENH65819.1};
GN ORFNames=FOC1_g10003444 {ECO:0000313|EMBL:ENH65819.1};
OS Fusarium oxysporum f. sp. cubense (strain race 1) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1229664 {ECO:0000313|EMBL:ENH65819.1, ECO:0000313|Proteomes:UP000016928};
RN [1] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; KB730470; ENH65819.1; -; Genomic_DNA.
DR AlphaFoldDB; N4TSL0; -.
DR STRING; 1229664.N4TSL0; -.
DR VEuPathDB; FungiDB:FOC1_g10003444; -.
DR HOGENOM; CLU_013253_9_4_1; -.
DR OMA; FGCKEAT; -.
DR Proteomes; UP000016928; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000016928};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..743
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004119892"
FT DOMAIN 60..373
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 398..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 78
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 270
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 305..338
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 743 AA; 78074 MW; 826464E8BD4CD7FF CRC64;
MLSALFLAIA APALAHAAAP QEDGLIRFPL KVSTGAPVVK GVTKRQNEVA LESQQNGFFY
SIDVELGTPG QKVTVNLDTG SAELWVNPVC SKAQQPAFCE SFGHFGESST WVNLNTTGGV
VYGTGYAYWN YGYDHVVVGS ANIRNQVFGV AYDSSFTSVG IMGAAPDLNG WDAPYPLVID
SMVRQGLIKS RALSLDIRTL DSDRGAVIFG GLDTKKYTGH LEKRPIIPAE SSPDGLTRYW
VHLDGISIIQ DDGSEDAIFS QTNGQPVLLD SGYTVSALPG PIFNKIVAAF PTAQRTPGAY
VDVDCSVADL KGTVDFKFGN TVIKVPYADF IWHNDDRCVL GVFQDDEFPV LGDTFLRAAY
VVYDWDNRNV WLANNEDCGT NLVAIGTGPN AVPDLVGECG SDSTTPSGAP TSTETASESV
TESVSSAETT ADTTLSFSTT RYSNTTFTTS KPGSTSTGGS GNTYVLPTAS APSTTITSTV
TTSKVYTVTA CPPSVTDCPV GHVTTEIITS LTTYCPGSEA TGVAPQPTKG PVKSTLTSTR
VYTITSCPGS GSCNKGDVTT EIVHNTQIIN PEQPTGVYTI PEAIQCGFGN FGCKEATTKG
YRTVTITSVV KAPKPTPVPG YCTTCGPPGS NHHNNGTFTG HYTKPGYEQP TKGHATQDYP
EPTGTASKPT GGNPLEELHT YKPTHVYAQP PNTVATVVKP TGTPVDSTPS EPTGTSPAIV
NGASAWNVPA LAAFIVGAFV AAL
//
