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
//