ID V9EVM0_PHYPR Unreviewed; 580 AA.
AC V9EVM0;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 22-FEB-2023, entry version 42.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=F443_12688 {ECO:0000313|EMBL:ETI42122.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI42122.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI42122.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI42122.1,
RC ECO:0000313|Proteomes:UP000018721};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P1569.";
RL Submitted (NOV-2013) 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:ETI42122.1}.
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DR EMBL; ANIZ01002143; ETI42122.1; -; Genomic_DNA.
DR AlphaFoldDB; V9EVM0; -.
DR EnsemblProtists; ETI42122; ETI42122; F443_12688.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_030614_0_0_1; -.
DR OrthoDB; 54298at2759; -.
DR Proteomes; UP000018721; 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 Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 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|RuleBase:RU000454};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000018721};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..580
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004774408"
FT TRANSMEM 459..483
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 36..403
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 64
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 269
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 580 AA; 62078 MW; 1A803819ACD2A2FE CRC64;
MRIHVAVATA LLRLHTTQAS DVLRQELWGL SSGLAYYVAV NIGSPVYSSG SGSSSSNSFN
LLLDTGSANT AVVTAECCSL TNENLYSCSD SSTCVDEGTS VSVSYVSGAW SGEVVRDTFS
GQGLGTVENM QFAEITAEDS FISSGYDGII GLGYKSIASP SSDPPTPYFD TVESADGLEN
IFSLQMCGAL QALSLSNFST EDSSYLYAGE FLLGGTEGPN GESYHKGDIV YTPLVQEKYF
NVIITDIGVN GESLGLDCEA INSPRSIIDS GTSNLAFPSS VYSAVIAELK TQVEKVASVT
DSFFDDDSTC CSSDCDPTNA DSFIYQLPGL TISLAVDDDK SQQMTITIPA EYIWRPIVVS
TGPGESACRV FGISEGDFTL LGDVFMDGLF TVHDRANERV GLAVADNCPN GVTSGKNITI
EAMTAEDSFC DCVGSSDRKS SLLSSYVPFS GKACFFWQWW MYVVIVAIVI IILMMVAYGY
YWWKRRKLMR QLEALQNQNQ PQVQRSLYAN DRLDRNLLHT PTQPSSVYVV GAFTPPRTAG
PIVNGGAPAT TGYVLASSPS VRFNANTNGA PATAVPGRKT
//