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Database: UniProt
Entry: E3L1T6_PUCGT
LinkDB: E3L1T6_PUCGT
Original site: E3L1T6_PUCGT 
ID   E3L1T6_PUCGT            Unreviewed;       421 AA.
AC   E3L1T6;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 2.
DT   08-NOV-2023, entry version 63.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=PGTG_16098 {ECO:0000313|EMBL:EFP90511.2};
OS   Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS   (Black stem rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=418459 {ECO:0000313|EMBL:EFP90511.2, ECO:0000313|Proteomes:UP000008783};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CRL 75-36-700-3;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C., Jaffe D.,
RA   Butler J., Alvarez P., Gnerre S., Grabherr M., Mauceli E., Brockman W.,
RA   Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA   Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA   Zeng Q., Kodira C., Yandava C., Alvarado L., O'Leary S., Szabo L., Dean R.,
RA   Schein J.;
RT   "The Genome Sequence of Puccinia graminis f. sp. tritici Strain CRL 75-36-
RT   700-3.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000008783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRL 75-36-700-3 / race SCCL
RC   {ECO:0000313|Proteomes:UP000008783};
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA   Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA   Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA   Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA   Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA   Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA   Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA   Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; DS178333; EFP90511.2; -; Genomic_DNA.
DR   RefSeq; XP_003334930.2; XM_003334882.2.
DR   AlphaFoldDB; E3L1T6; -.
DR   EnsemblFungi; EFP90511; EFP90511; PGTG_16098.
DR   GeneID; 10530408; -.
DR   KEGG; pgr:PGTG_16098; -.
DR   VEuPathDB; FungiDB:PGTG_16098; -.
DR   HOGENOM; CLU_013253_1_4_1; -.
DR   InParanoid; E3L1T6; -.
DR   OrthoDB; 4946at2759; -.
DR   Proteomes; UP000008783; Unassembled WGS sequence.
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; 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; NAPSIN-A; 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   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008783};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..421
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003172390"
FT   DOMAIN          110..418
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        306
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        141..146
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   421 AA;  45836 MW;  7B9A267FE347B7CD CRC64;
     MWKFFSVIAI LVSLPLSSIT ISSSIGADLN NAHPLRIPLE KKLFVRGGDG IFNFTAAQLS
     HQHTLRKYRG TCEKYKHARS FWPSLSKLSR PYRHHRRQIE RLTNQGNQMW TGLVKIGTPS
     QTFSVDFDTG SGDFWVPSID CKDNPCGSKN IYNASASSTS TRLPDSFKVN YGDGSTTSGN
     QYRDSVKLAG ITIANQTFAG VSKLSDEFQH DPTDGVLGLA YPAISHLKSP SFIENAFNQG
     LIPSKTFSFK LANEGGELYL GGVNPSRFVG TLEAHPVIRQ AYWEIGNGSV NVNSINISQN
     GRMILDSGTT IIYGPKLAVE KLYSSVDGAK KYEKRDGLWK FPCVSAPSVS FSWNGGGQWA
     IDPKRMSLGK VEANSAECIG AISSQAVGLN DSWLLGDTFM SNVYSVFNPV GGGTVSFATP
     V
//
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