ID D0ERU8_PHYIN Unreviewed; 675 AA.
AC D0ERU8;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 22-FEB-2023, entry version 53.
DE SubName: Full=Putative RXLR effector PEXRD17_MK88_4 {ECO:0000313|EMBL:ACX46546.1};
DE Flags: Fragment;
OS Phytophthora infestans (Potato late blight agent) (Botrytis infestans).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4787 {ECO:0000313|EMBL:ACX46546.1};
RN [1] {ECO:0000313|EMBL:ACX46546.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=88069 {ECO:0000313|EMBL:ACX46546.1};
RX PubMed=19794118; DOI=10.1105/tpc.109.068247;
RA Oh S.K., Young C., Lee M., Oliva R., Bozkurt T.O., Cano L.M., Win J.,
RA Bos J.I., Liu H.Y., van Damme M., Morgan W., Choi D., Van der Vossen E.A.,
RA Vleeshouwers V.G., Kamoun S.;
RT "In planta expression screens of Phytophthora infestans RXLR effectors
RT reveal diverse phenotypes, including activation of the Solanum
RT bulbocastanum disease resistance protein Rpi-blb2.";
RL Plant Cell 21:2928-2947(2009).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR EMBL; GQ869436; ACX46546.1; -; Genomic_DNA.
DR AlphaFoldDB; D0ERU8; -.
DR VEuPathDB; FungiDB:PITG_08599; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06455; M3A_TOP; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR024080; Neurolysin/TOP_N.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11804:SF82; THIMET OLIGOPEPTIDASE-RELATED; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 220..667
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACX46546.1"
FT NON_TER 675
FT /evidence="ECO:0000313|EMBL:ACX46546.1"
SQ SEQUENCE 675 AA; 77265 MW; 50689F1E13827BBA CRC64;
KKQQRTRVLR KQLTNLRFDL SVAEIEAETE RILAQMKRVD DEIAALSPSA VTFESTAQKI
IDLDHEMLSR VTNVTFLGQV AADKETRDAC TKADEVIEDF SVQRSMRADV YKAVNTLYKS
AAYQKLNTVT QRYVHRLVQD FERNGLQLPG EKQKEVQAWK QKLSKLGIQF QQNLSEETIE
VQFLHDELKG LSNDFIAALE KGDDGKYKIA LSYPTVFPIL NTCTVESTRK AVEYAFNRRC
ISTNVAILEE MLEIRHKVAL ALGYENHAAY VLEQRMAETP ANVKKFLSDL DNKLVPLAKK
DLDDLLKLKE ADCEQNEWKF DGKINMWDFR FYMDQYVKKH CSIDSEKLRE YFPLTHVTTE
LLSMYQELLS LKFVEISQPH VWHKDVRMFA VYDARPGKAG NLVGHFYLDL FPRAGKYGHA
ACFTLQQSCI NSAGVREYPA AAMVANFNAP TKSKPSLLGH QEVVTYFHEF GHVMHCLCSE
VDIPRFAGTR VERDFVEAPS QMLENWCWEK EPLQRLSSHY ETGEKLSDDL ITRLISTKNV
NTGLLNKRQL LFAIFDQTIH SKPKANTAQL LKQLQTEIML IDMTPETNFA GSFGHLAGGY
DAQYYGYMWS EVFSMDMFVS RFKKEGLMNP KTGLAYRELI LARGGSVDAS VMLKDFLGRA
PNQDAFLLSK LMPRV
//
