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Database: UniProt
Entry: A0A225WU88_9STRA
LinkDB: A0A225WU88_9STRA
Original site: A0A225WU88_9STRA 
ID   A0A225WU88_9STRA        Unreviewed;       924 AA.
AC   A0A225WU88;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Peptidase M12A domain-containing protein {ECO:0000259|PROSITE:PS51864};
GN   ORFNames=PHMEG_0004236 {ECO:0000313|EMBL:OWZ21234.1};
OS   Phytophthora megakarya.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4795 {ECO:0000313|EMBL:OWZ21234.1, ECO:0000313|Proteomes:UP000198211};
RN   [1] {ECO:0000313|Proteomes:UP000198211}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=zdho120 {ECO:0000313|Proteomes:UP000198211};
RA   Ali S., Shao J., Larry D.J., Kronmiller B., Shen D., Strem M.D.,
RA   Melnick R.L., Guiltinan M.J., Tyler B.M., Meinhardt L.W., Bailey B.A.;
RT   "Phytopthora megakarya and P. palmivora, two closely related causual agents
RT   of cacao black pod achieved similar genome size and gene model numbers by
RT   different mechanisms.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01211};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC       ProRule:PRU01211};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01211}.
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:OWZ21234.1}.
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DR   EMBL; NBNE01000244; OWZ21234.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A225WU88; -.
DR   STRING; 4795.A0A225WU88; -.
DR   EnsemblProtists; OWZ21234; OWZ21234; PHMEG_0004236.
DR   OrthoDB; 48991at2759; -.
DR   Proteomes; UP000198211; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR   PANTHER; PTHR10127:SF850; METALLOENDOPEPTIDASE; 1.
DR   Pfam; PF01400; Astacin; 1.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198211};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU01211}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..924
FT                   /note="Peptidase M12A domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012375380"
FT   TRANSMEM        875..895
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          599..822
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   BINDING         696
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         700
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         706
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   924 AA;  102634 MW;  4264F72D1D3761D8 CRC64;
     MVFARFLPAV LCGLGFVGWG AQAAFYVCPE GCTAMLLPRD MEMIDDCVCD DGVDTTAEEA
     AADAVDNGAF SCKGRYKPKR GGVPRSVADC DCYHPYEKDS KTQECVLTEC PRAGNYEPKP
     GVREVASLAD CTCTSPYVKA ETSGQCVVGD NAQTQTRGRF QCPPNSTPTP DIFPKSFADC
     HCSWGFVRNS FDQCEREYAA YVCPVNSVKR SDLPIGERPR GFFDCECLST GEYHRDEEAH
     ACWPVSQMKA RKPKRQHDYI RGDNAEEQFT NFEVVDREAK PYQCPPFSRA VATVPHSVEQ
     CQCIPGYAWK TPEMTCVRTS GYKCPDHAYK RTKLHGSEME SSFEDCACAR GYFLDAMAER
     CVPWMLANSN SCPPFAVLTQ WPLQSNANCK CVYGLNETIS EEEDEARRKA EAEEILNGGT
     AQETPPMRRR KKECNTRPTD ISLPDFSQCP HDSMATMWPV ATADACTCLS GFEKTPLSEQ
     EISRGVGDGF HCVATPEKNL VADEAAAACH APGVIHPLSG ECRLPIEEIL DEKASKKGGK
     PEGVLFKGIE YDYELVDNTV MIIQGDVAIG ERFVWQDVDP TDPEEVTTRI EHVLHGYYNS
     GRDHRWSHER MCFQVDKSAR PFLRTLLSAT EHITHATGFK FHRCGGDNCR TDLSCRSHDF
     VAVQGVESSC YSFIGRIGGP QRLGVSADCG LGNVVHVLLH AVGLRHTVDR VDRDDHVRIA
     WECIPESKRS YFVVEDMNSA PTPTRAADRI LDPPPYDLFS IMHHPPDAFV HSVSGDGKPQ
     WCPSVVPLIA DDTKRLAVMK DMGQRERMTT TDVRSVWALY PGLKKKHHSR QKDVESGEAE
     VEELHDTFVH TEQDAVETAS ATGHGTQHRS FGQRLVSFLG AVVTLVGFGA LLAFITTELR
     RRALLSSGDD FFYEAPLIDS KNDI
//
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