OPSB_ASPFU
ID OPSB_ASPFU Reviewed; 485 AA.
AC Q4WDN4;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable aspartic-type endopeptidase opsB;
DE EC=3.4.23.-;
DE Flags: Precursor;
GN Name=opsB; ORFNames=AFUA_6G05350;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- FUNCTION: Probable GPI-anchored aspartic-type endopeptidase which
CC contributes to virulence. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; AAHF01000012; EAL85504.1; -; Genomic_DNA.
DR RefSeq; XP_747542.1; XM_742449.1.
DR AlphaFoldDB; Q4WDN4; -.
DR SMR; Q4WDN4; -.
DR STRING; 746128.CADAFUBP00009030; -.
DR MEROPS; A01.081; -.
DR EnsemblFungi; EAL85504; EAL85504; AFUA_6G05350.
DR GeneID; 3505349; -.
DR KEGG; afm:AFUA_6G05350; -.
DR VEuPathDB; FungiDB:Afu6g05350; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_3_1; -.
DR InParanoid; Q4WDN4; -.
DR OMA; LYFMGGV; -.
DR OrthoDB; 753343at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd05474; SAP_like; 1.
DR Gene3D; 2.40.70.10; -; 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; PTHR47965; PTHR47965; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; Cell membrane; Glycoprotein; GPI-anchor; Hydrolase;
KW Lipoprotein; Membrane; Protease; Reference proteome; Signal; Virulence;
KW Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..461
FT /note="Probable aspartic-type endopeptidase opsB"
FT /id="PRO_0000397704"
FT PROPEP 462..485
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000397705"
FT DOMAIN 69..397
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 285
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT LIPID 461
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 485 AA; 51337 MW; 368E316BAE0BFCE2 CRC64;
MRHIFSLLSI VCLMVKHGAC LTLHQRDVPA VVSLDIKRSI VSDPVVRDRV RRKRDKTIGQ
TLDNAETLYF CNVTLGTPGQ ALRLVLDTGS SDLWCNAANS TLCSDSNDSC NISGSYDPSS
SSTYAYVSSD FNISYADGTG AVGDYATDIL HIGGSTLRNL QFGIGYSSTS SEGVLGIGYP
SNEVQVGQYG KDTYPNLPRA MVDQGLINSN AYSLWLNDLE SNTGSILFGG VNTGKYLGEL
QTLPIQKVNG RYSEFVIALT GVAFDSESHH KTYSSDALPA AVLLDSGSSL TYLPDSIVEN
IYRDLNVAYE PSSGVGYLPC KLAGNNINIT YTFSSPNITV MIDELLLDAG DLRFRDGARA
CIFGIVPAGD STAVLGDTFL RSAYVVYDIA NNEISIANTN FNSTEDNILE IGVGPDSVPS
ATQVSHPVTS VVADGSGARI GAPTGASSTT VPSISSAGAL SAGVARADKQ YLAIALIAVW
FVLGL
