ID H3GM21_PHYRM Unreviewed; 636 AA.
AC H3GM21;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
OS Phytophthora ramorum (Sudden oak death agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra77495, ECO:0000313|Proteomes:UP000005238};
RN [1] {ECO:0000313|Proteomes:UP000005238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pr102 {ECO:0000313|Proteomes:UP000005238};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
RN [2] {ECO:0000313|EnsemblProtists:Phyra77495}
RP IDENTIFICATION.
RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra77495};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; DS566022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3GM21; -.
DR STRING; 164328.H3GM21; -.
DR EnsemblProtists; Phyra77495; Phyra77495; Phyra77495.
DR VEuPathDB; FungiDB:PSURA_74839; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_025981_0_0_1; -.
DR InParanoid; H3GM21; -.
DR OMA; RYGTHFQ; -.
DR Proteomes; UP000005238; 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:InterPro.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR032799; TAXi_C.
DR InterPro; IPR032861; TAXi_N.
DR PANTHER; PTHR13683; ASPARTYL PROTEASES; 1.
DR PANTHER; PTHR13683:SF375; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF14541; TAXi_C; 1.
DR Pfam; PF14543; TAXi_N; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005238};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..636
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003587439"
FT TRANSMEM 530..551
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 56..400
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 409..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 74
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 285
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 319..365
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 636 AA; 68503 MW; 57701BB0057EFEF3 CRC64;
MVHVYAGFPV LLAAISTITT LAEAAQSAGM TMELHRLPQH EIHPERYARR LNIEEDAPEL
VPLHLGLGAS VIADTGSGLM AFPCSGCDGC GSHTDQPFMA DNSSTLVHVT CSQQSFFQCK
ECKQTSDTCG ISQSYMEGSS WKASVVEDVV YLGGETSFQD EEMRNRYGTH FQFGCQSSET
GLFVTQVADG IMGLSNADNH IVAKLHRENK IPSNLFSLCF TDQGGTMSVG QANTNAHRGE
ISYAKVISDR SASHFYNVHM KDIRIGGKSI NAKEEAYTRG HYIVDSGTTD SYLPRALKTE
FLQMFKEVAG RDYQVGTSCH GFTNEDMASL PTIQLVMEAY GDENAEVVLD VPPEQYLLNA
NGAFCGSIYL SENSGGVIGA NLMMNRDVIF DLGNQRVGFV DADCAYQSNS STTASPSISN
DSTSSTDGET NNVVPIVTNA ATVPSATEAT VESSPKPTSA AAASEPTVTA ASTPEATVAN
ISTLDLASST ADLNIQPLSE EGTTKTQSSS SGVAADPKAK EKSSGGAHPM VLTIVGAVLV
VGFLLMMLIS VSRRRQKTGK DQLWSRVKGS EEDEDDDDEE EFGMVRNDKK GSAKHQRLDA
DDDDDDQSSS DEEDEVFDRK SLQEETKVDN RTLERL
//
