SED5_ASPFU
ID SED5_ASPFU Reviewed; 580 AA.
AC Q4WGU1;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Tripeptidyl-peptidase sed5;
DE EC=3.4.14.10;
DE AltName: Full=Sedolisin-E;
DE Flags: Precursor;
GN Name=sed5; Synonyms=sedE; ORFNames=AFUA_7G06220;
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: Secreted tripeptidyl-peptidase which degrades proteins at
CC acidic pHs and is involved in virulence. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal tripeptide from a polypeptide.;
CC EC=3.4.14.10;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
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DR EMBL; AAHF01000009; EAL86850.2; -; Genomic_DNA.
DR RefSeq; XP_748888.2; XM_743795.2.
DR AlphaFoldDB; Q4WGU1; -.
DR SMR; Q4WGU1; -.
DR STRING; 746128.CADAFUBP00008926; -.
DR EnsemblFungi; EAL86850; EAL86850; AFUA_7G06220.
DR GeneID; 3506319; -.
DR KEGG; afm:AFUA_7G06220; -.
DR VEuPathDB; FungiDB:Afu7g06220; -.
DR HOGENOM; CLU_012501_2_0_1; -.
DR InParanoid; Q4WGU1; -.
DR OMA; TFGHNDS; -.
DR OrthoDB; 616110at2759; -.
DR Proteomes; UP000002530; Chromosome 7.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008240; F:tripeptidyl-peptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd04056; Peptidases_S53; 1.
DR CDD; cd11377; Pro-peptidase_S53; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015366; S53_propep.
DR InterPro; IPR030400; Sedolisin_dom.
DR Pfam; PF09286; Pro-kuma_activ; 1.
DR SMART; SM00944; Pro-kuma_activ; 1.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51695; SEDOLISIN; 1.
PE 3: Inferred from homology;
KW Calcium; Glycoprotein; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Virulence; Zymogen.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT PROPEP ?..172
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000390754"
FT CHAIN 173..580
FT /note="Tripeptidyl-peptidase sed5"
FT /id="PRO_0000390755"
FT DOMAIN 181..567
FT /note="Peptidase S53"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 269
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 273
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 479
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 523
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 524
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 543
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 545
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 547
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 580 AA; 62768 MW; A9E643CB2AB15753 CRC64;
MYPLDGSARP HPPGTTRLNS VEPDKQIGFT VLVRPQTGAP RLPDLAQWQA IPIAERQFLS
TAGFERTYGS SEDDIVSVAS FLEKAGMTIR SRHAGAGTVE VQAKTCQIHS VFAVQLLYYR
GQLRPAARKR RDDKQPAEET YIGFEGCISL PAALHDKVIH IFGLDTRTFG ASGGYSGDPP
RAQRLIVAEL AALYGFPAGV DASQQTIGIF SGEGNDDKGQ SLSNYRPADV AAYFNNQTVG
YNRAPTVVPV SLTVADQTYR NDPDHPTQEL SQDIMTAATI AQGCTVNVYF SDLTEQGWLA
FLTRVLFPQG EEKRPTIVSI SWTMYDEQTY RDRLSFLFQR LAVVGTSVFA IAGDWGANNN
IIDGQPHVGW PGSDPWVTCV GGTVVGNVRS SGAFTEHAWS DRDNPDSQFT IDGHLGVTGG
GMSRVFATPP YQLSSGISAV TDCNGERWTG GRFIPDITGM VGFRGFIVNG KRNYFIGTSC
STPLYAGLFA ALASALGGGG EGGVLFGPLN TVLYQIDRGV YRDITFGHND SGDMPACAYF
AAGEGYDTVS GLGSVDGRRT LEELRRIYWP KTKGFGCFRN
