ID N1RCY0_FUSC4 Unreviewed; 495 AA.
AC N1RCY0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 28-JUN-2023, entry version 47.
DE SubName: Full=Putative aspartic-type endopeptidase opsB {ECO:0000313|EMBL:EMT64418.1};
GN ORFNames=FOC4_g10007090 {ECO:0000313|EMBL:EMT64418.1};
OS Fusarium oxysporum f. sp. cubense (strain race 4) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=2502994 {ECO:0000313|EMBL:EMT64418.1, ECO:0000313|Proteomes:UP000016929};
RN [1] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
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:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
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, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; KB726991; EMT64418.1; -; Genomic_DNA.
DR AlphaFoldDB; N1RCY0; -.
DR STRING; 1229665.N1RCY0; -.
DR HOGENOM; CLU_013253_9_3_1; -.
DR Proteomes; UP000016929; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05474; SAP_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033876; SAP-like.
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; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000016929};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..495
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004111900"
FT TRANSMEM 473..494
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 56..398
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 423..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 74
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 274
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 495 AA; 53094 MW; 1A1E4D432FF25582 CRC64;
MKSSLVGASL VSTLGLVQAQ TIQWNIEGRH PQPHLARRAK TTYEEIISND RSEGGYFTEV
TIGNPPQNIT LQLDTGSSDV WVPWNCADIC EDDKNGKSGC PLGSFDPDKS KTFKHVAPGM
FGITFVDDSY VKGDYFEDHF ELDGAVINNL TMGLAIKTNI SYGLIGVGYA KNEASGSTTD
VIYPNLPVAM YQAGYINTIA YSVWLNDLDA KAGSILFGGV DTAKYVGDMH RIDIQKLDGH
YYHFVVALTS LVATSSSGSD VLTSDSFPIQ AVLDSGTTLS YLPQDLAHEI WEEVGAVWSP
YYGVAVLPCA YGRNQGNFTF GFAGPDGPSI SVGMDELVLS MTSDAANMPA FESGAYKGEN
ICTFGIQNDT NDLYLLGNTF LRSAYVVYDL VNNEVGIAAT DFNSTKSKRV PFKSYGATIP
SATAASNQHR ATEKPTVPGN NFTAAEGFQE SDSNGNDDED NAGSLLDPPT TPLALVVTTM
SFMLAGGGIF SSIFL
//