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
//