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Database: UniProt
Entry: A0A0L6V952_9BASI
LinkDB: A0A0L6V952_9BASI
Original site: A0A0L6V952_9BASI 
ID   A0A0L6V952_9BASI        Unreviewed;       513 AA.
AC   A0A0L6V952;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=VP01_2356g1 {ECO:0000313|EMBL:KNZ56645.1};
OS   Puccinia sorghi.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ56645.1, ECO:0000313|Proteomes:UP000037035};
RN   [1] {ECO:0000313|EMBL:KNZ56645.1, ECO:0000313|Proteomes:UP000037035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ56645.1,
RC   ECO:0000313|Proteomes:UP000037035};
RA   Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA   Sacco F.;
RT   "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT   Schw, the Causal Agent of Maize Common Rust.";
RL   Submitted (AUG-2015) 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:KNZ56645.1}.
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DR   EMBL; LAVV01007232; KNZ56645.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6V952; -.
DR   STRING; 27349.A0A0L6V952; -.
DR   VEuPathDB; FungiDB:VP01_2356g1; -.
DR   OrthoDB; 1203010at2759; -.
DR   Proteomes; UP000037035; Unassembled WGS sequence.
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:SF6; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037035};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..513
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005567898"
FT   DOMAIN          109..453
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          76..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          142..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        329
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   513 AA;  52862 MW;  AE11D158857CF1EE CRC64;
     MLNPSSVVLS LLVLGLAPLT IGRNTFNLGT EASAPRAIPL VRRHGQQLLR KRSPIHVQDY
     ALRQADLLIN KYPNLSRGGT HPSLPGRPTL RARDPSAAAL SNGYADSEYY GMIFVGTPPQ
     TFNVILDTGS SDLWLVGQGA SSSSTSRAGE GMSIGSPTAS STSATGVPFA PSSSSSFKSN
     SNTFQITYGS GSASGTVGTD TITQGSYTVT NQAFAVVNKA TSGLLSGDVS GIMGMAFQSL
     ASTNSAPFWQ SAKIDTFAFG ITRFVNISSA TDVEPGGVMT LGGINNTLFQ GDVNYIPLKS
     QSYWLIAMDS VSINGQVLIG SQSNAVAIDT GTSLIGAPTS VVAAVYAQIP GARAASGSYQ
     GYYEFPCSAN PVMALTFGGK AYPIAADDFN VGAVDSDGKM CLGSIFAVES SSTNTSGSKS
     SNSPAWIIGD SFLKNVYTVF RASGDGGAAV GFAVPAPGYQ SLLRSVGTAN GGGVTTNGGT
     TTNARHSSAN PLPSLPTLLF LSFSLLYTLL FFL
//
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