CTSD_ASPFU
ID CTSD_ASPFU Reviewed; 474 AA.
AC Q4WNV0;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Aspartic-type endopeptidase ctsD;
DE EC=3.4.23.-;
DE Flags: Precursor;
GN Name=ctsD; ORFNames=AFUA_4G07040;
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).
RN [2]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17275325; DOI=10.1016/j.pep.2006.12.012;
RA Vickers I., Reeves E.P., Kavanagh K.A., Doyle S.;
RT "Isolation, activity and immunological characterisation of a secreted
RT aspartic protease, CtsD, from Aspergillus fumigatus.";
RL Protein Expr. Purif. 53:216-224(2007).
CC -!- FUNCTION: Secreted aspartic-type endopeptidase which is secreted and
CC contributes to virulence. {ECO:0000269|PubMed:17275325}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:17275325};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- INDUCTION: Repressed under nutrient-rich culture conditions.
CC {ECO:0000269|PubMed:17275325}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; AAHF01000005; EAL90084.1; -; Genomic_DNA.
DR RefSeq; XP_752122.1; XM_747029.1.
DR AlphaFoldDB; Q4WNV0; -.
DR SMR; Q4WNV0; -.
DR STRING; 746128.CADAFUBP00006238; -.
DR MEROPS; A01.077; -.
DR EnsemblFungi; EAL90084; EAL90084; AFUA_4G07040.
DR GeneID; 3509768; -.
DR KEGG; afm:AFUA_4G07040; -.
DR VEuPathDB; FungiDB:Afu4g07040; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_10_0_1; -.
DR InParanoid; Q4WNV0; -.
DR OMA; SSWVMGT; -.
DR OrthoDB; 753343at2759; -.
DR Proteomes; UP000002530; Chromosome 4.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:AspGD.
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; 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; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Cell membrane; Glycoprotein; GPI-anchor; Hydrolase;
KW Lipoprotein; Membrane; Protease; Reference proteome; Signal; Virulence.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..452
FT /note="Aspartic-type endopeptidase ctsD"
FT /id="PRO_0000390764"
FT PROPEP 453..474
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000390765"
FT DOMAIN 106..413
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 124
FT /evidence="ECO:0000250"
FT ACT_SITE 307
FT /evidence="ECO:0000250"
FT LIPID 452
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 474 AA; 50548 MW; C2ACC9BBC3D53066 CRC64;
MHLLQCLLST ISLASTVTAF VPYSFNLEVS TEGPPSNDVA RRFVPWKLLL DDSYNNHGSS
SNGVSLTLDL KKFPVRRDNK YKVVLADEPT TPNTAALNQE GLDYSYFATV RVGSQGQQMW
LVLDTGGPNT WVFGSDCTTV ACQRHETFGE AASKSLKLLP LNWAVGYGTG LVSGVLGTDS
LSLAGLDVNM TFGLAKNAST DFESYPVDGI LGLGRSANSN FNTPSFMETV ATQRLLKSNI
IGFSFSRNSD GARDGAANFG DLDTTRFTGD IVYTNTTGDS NNWRIPLDDA SVNGTPCRFV
NKTAVIDTGT SYAMLPPKDA TVLHNLIPGA VTTSHGQNFT LPCNSTAVVQ VSFSGLSYNI
SPKDYVGPAY GSACLSTIVG QALYGDDVWL LGDVFLKNVY SVFDYDNHRI GFANRSVPIA
SPTTTVAAAA NPSATDGAGS TLTGSMAVHT GSASIVSRFV HWPFIFALLC MVLV
