ID E6ZZQ2_SPORE Unreviewed; 452 AA.
AC E6ZZQ2;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 08-NOV-2023, entry version 53.
DE SubName: Full=Related to aspartic protease {ECO:0000313|EMBL:CBQ72732.1};
GN ORFNames=sr10744 {ECO:0000313|EMBL:CBQ72732.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ72732.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ72732.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQ311470; CBQ72732.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZZQ2; -.
DR MEROPS; A01.078; -.
DR EnsemblFungi; CBQ72732; CBQ72732; sr10744.
DR VEuPathDB; FungiDB:sr10744; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_1_2_1; -.
DR OrthoDB; 1203010at2759; -.
DR Proteomes; UP000008867; Chromosome 5.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_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; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF57; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 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 Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:CBQ72732.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..452
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003215209"
FT DOMAIN 91..395
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 109
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 281
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 452 AA; 46585 MW; B7C6FF4ED6C02FD2 CRC64;
MKLTGATLVS SGLLAASAAS TALAAPAPSS SSPAVHIPIQ KRSVVRRSGN ELLSWAYDQK
AILQSKYKLA PANQRRAGST SLTNVQYDSS WVAPLYGGTP SKQYEVVLDT GSADLWISSQ
YYSPSASSSF QNYSTPFDIQ YGSGDVAGYE ATDTFTLAGT TVNNLHFAVA QSVSSGLTSA
AMEGIMGMGF QRLASSGEPP LWVAAGVNTF SFYLERASLT SSDQTQAGGL FTLGGSNSSL
YQGDISYNAL IEELYWMVRL GAAGTKGSNV NLNSLTRAAI DTGTTLIGGP DSVVQALYSQ
IPNSRSQGNG YYSFPCSSSV DATLTFGGMQ YTIPDSDFIA GTLDQSGSEC LGAFFGLGSS
SQTDLQWIVG DAFLKNVYSI FTTNGNNGGA AVGFASLASG LNSGTNSKSV SSSTSSSTSS
GTSSPAPRTA ARWSLSALAA AVAVPVLAAV LA
//
