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Database: UniProt
Entry: A0A0L6US13_9BASI
LinkDB: A0A0L6US13_9BASI
Original site: A0A0L6US13_9BASI 
ID   A0A0L6US13_9BASI        Unreviewed;       510 AA.
AC   A0A0L6US13;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=VP01_39g5 {ECO:0000313|EMBL:KNZ51326.1};
OS   Puccinia sorghi.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ51326.1, ECO:0000313|Proteomes:UP000037035};
RN   [1] {ECO:0000313|EMBL:KNZ51326.1, ECO:0000313|Proteomes:UP000037035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ51326.1,
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:KNZ51326.1}.
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DR   EMBL; LAVV01009057; KNZ51326.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6US13; -.
DR   STRING; 27349.A0A0L6US13; -.
DR   VEuPathDB; FungiDB:VP01_39g5; -.
DR   OrthoDB; 1203010at2759; -.
DR   Proteomes; UP000037035; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037035};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..510
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005568059"
FT   TRANSMEM        483..505
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          110..438
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        316
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   510 AA;  55724 MW;  09688AE08FAD7A81 CRC64;
     MNTLASFRVC LVLVLSWEVL SRETPSTVST LAIPLYRRHG VQKARKTDPK ALQVFALRNT
     RAFQAKYRHS NPRVCPNCCS EEVIKTWRRS VPEELKSIVA LQNEWSDTDY YSQVEIGTPP
     QSFNVVLDTG SADLWVAGTA VLGRREDGEG SKASFYSSSF SSTFRNSSEN FHITYGSGTA
     SGIVGIDHVR QGSYSSLEQK FAIVHNISSH LLADQISGIM GMAFQQISTM RSSPFWESAN
     ISTFSFGMTR FCDVPFPREV EPGGVVMLGA TDRSLYTGEI SYTNVLNEGY WEIKMDAVSV
     NGKTLDGSQG NSAAIDTGTS LIGGPAELVK TLFDKVTGAR PGSGAYQGYY TYPCDSSFSL
     SLFFEGEAYN IDPVDINLGS IDENHRECLA GIFSIDHGRK NSKGRPKNGL PDWILGAVFL
     KNVYTVFQRG PPAAVGFGKP SSDYQVLLGG LGVSDHQGSP GEVTNRANQM PPTSGTSTVQ
     YSVLFKIFFL LSLLHILFFL NSLVLGCSLF
//
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