ID A0A180GDW1_PUCT1 Unreviewed; 521 AA.
AC A0A180GDW1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=PTTG_01942 {ECO:0000313|EMBL:OAV90133.1};
OS Puccinia triticina (isolate 1-1 / race 1 (BBBD)) (Brown leaf rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=630390 {ECO:0000313|EMBL:OAV90133.1};
RN [1] {ECO:0000313|EMBL:OAV90133.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV90133.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAV90133.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV90133.1};
RA Cuomo C.A., Bakkeren G., Szabo L., Khalil H., Joly D., Goldberg J.,
RA Young S., Zeng Q., Fellers J.;
RT "Comparative analysis highlights variable genome content of wheat rusts and
RT divergence of the mating loci.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAV90133.1}.
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DR EMBL; ADAS02000108; OAV90133.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A180GDW1; -.
DR VEuPathDB; FungiDB:PTTG_01942; -.
DR OrthoDB; 2900143at2759; -.
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:SF51; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454}.
FT DOMAIN 143..512
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 161
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 354
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 521 AA; 55737 MW; 363E30726B619384 CRC64;
MSIVRTPVFY QAPSGNFRQV LGHGIARYGF FGFLNSDRAT SDIGPYVQSN LPPQMQALSV
DYLAKKKSKS KRGLKKQLFT RLLQLFPSAL GTIESGTKLI ISPVVSTADV ISGHLPGKNE
LAQDSSWGTS TVKTDSLQGD LLWSTTVNLG SSSQPLRINI DTGSADFFVF DPKCQSCALN
THAAFFYAQS RTFTPLVNLT FNAQYADGGG VNGYLAQDSL NFGGGVSVPQ QLFGLATDVS
GYWQSLGVDG LMGLGPDVLS SFPPPNNLGV FTQLVNNKAL SQPVIGIALT KSSVNSSGEF
SFGKVNEQWV RGGASQMFWK NVSSQNFWGT ELSGIFVNGQ NVMATEDPPR AIVDTGTSLM
LVSDTAAAGI HKQIPGAVVD PSNGIWRLPC STANVATTPK RPTFASIFGF MPRPQRRASL
RNAFSKAYPA PPNIFVELGS GAPKLGIPVT DLAYQAIPSD EANSLALDGR TKMCYSGIQA
GADGFFVLGG TFIKNHYIAL RRDGAKRSIG FGNRKDLPEI Q
//