Y1220_ASPFU
ID Y1220_ASPFU Reviewed; 439 AA.
AC Q4WFS2;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable aspartic-type endopeptidase AFUA_3G01220;
DE EC=3.4.23.-;
DE Flags: Precursor;
GN ORFNames=AFUA_3G01220;
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 aspartic-type endopeptidase which contributes to
CC virulence. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; AAHF01000010; EAL86405.2; -; Genomic_DNA.
DR RefSeq; XP_748443.2; XM_743350.2.
DR AlphaFoldDB; Q4WFS2; -.
DR SMR; Q4WFS2; -.
DR MEROPS; A01.081; -.
DR EnsemblFungi; EAL86405; EAL86405; AFUA_3G01220.
DR GeneID; 3506170; -.
DR KEGG; afm:AFUA_3G01220; -.
DR VEuPathDB; FungiDB:Afu3g01220; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_035052_1_0_1; -.
DR InParanoid; Q4WFS2; -.
DR OMA; WEGDGTT; -.
DR OrthoDB; 753343at2759; -.
DR Proteomes; UP000002530; Chromosome 3.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; PTHR47966; 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; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Secreted; Signal; Virulence.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..439
FT /note="Probable aspartic-type endopeptidase AFUA_3G01220"
FT /id="PRO_0000406417"
FT DOMAIN 95..436
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT REGION 31..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 439 AA; 46364 MW; A3C182A75E508170 CRC64;
MHFSIGSLFL YLIASASCTA ASPQYIQRSR RTPFTTSTSK PSAFTNPSTD TATTPYVLEL
TKINNKGNAR SAVELNSQVR SGSANLVSFA EGVGFATSIN IGNQTFEVVI DTGSSDLWVV
RDGFICIDPV SRKEVAQSEC RFGPAYAPNT TFHEVVGEFV DIKYADGEIL SGVIGTENVT
LAGITVNQTI GVMDYAGWYG DGVTSGLMGL AYSSLASAYT TNNRQPRLYN PIFATMYEQG
LIDPIFSMVM NRNASNGTAA GYLTLGGLPP VDINGNFSTT PILITNIKGY PKDYDFYAVN
IDGVALGNRS LPEAAGGIQY IIDSGTTLNY YPTPVADSVN AAFIPPAVYN DYDGAYVVDC
NATASVHGVM IGGSTFYINP TDMILPGGMD NSGNKTCISG INAGGDVGQG IFVLGGTFLR
NVVAVFDVGA AEMRFAASA
