ID H3GSR0_PHYRM Unreviewed; 1847 AA.
AC H3GSR0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblProtists:Phyra80068};
OS Phytophthora ramorum (Sudden oak death agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra80068, 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:Phyra80068}
RP IDENTIFICATION.
RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra80068};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS566042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 164328.H3GSR0; -.
DR EnsemblProtists; Phyra80068; Phyra80068; Phyra80068.
DR VEuPathDB; FungiDB:PSURA_80068; -.
DR eggNOG; KOG0585; Eukaryota.
DR eggNOG; KOG0698; Eukaryota.
DR eggNOG; KOG1113; Eukaryota.
DR HOGENOM; CLU_003057_0_0_1; -.
DR InParanoid; H3GSR0; -.
DR OMA; MHKTFVQ; -.
DR Proteomes; UP000005238; Unassembled WGS sequence.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00038; CAP_ED; 2.
DR CDD; cd00143; PP2Cc; 1.
DR CDD; cd14008; STKc_LKB1_CaMKK; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24353:SF37; CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT PRKX; 1.
DR PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00481; PP2C; 1.
DR PRINTS; PR00103; CAMPKINASE.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00332; PP2Cc; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 2.
DR PROSITE; PS00889; CNMP_BINDING_2; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
DR PROSITE; PS51746; PPM_2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; cGMP {ECO:0000256|ARBA:ARBA00022535};
KW cGMP-binding {ECO:0000256|ARBA:ARBA00022992};
KW Kinase {ECO:0000256|ARBA:ARBA00022527};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000005238};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 240..357
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 371..478
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 565..829
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1484..1841
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 1..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 996..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1180..1290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1315..1379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1657..1689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1065
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1666..1689
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 594
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1847 AA; 201080 MW; 528F3A6D6C4BB52B CRC64;
MGQRFSTSRE SDVSEEGGLP SPPASPIPLS SDRPLLPVQQ DEHMRLGDVV HDTLSVSQEP
PYQPQSDSFP SDNALPLTRR SSMAKPPKLS RFRPSMDLPK PAGSPQSGYL SSSDSRSLDS
SSSSSDEDLV GSGEELVNDW LDEPEDAVLS PLAQPKRTRH ASACSSVSSH TGNSVSFSAM
HSSGGRNSNS SQHSLTGWAS WLSSPDDVEE EEEADEEPVA LTPFLRDNMP VYEIMRQVQL
FRNLSQMQQE QVVRALKPAK FSDGEVIVAQ GTRGSRFYMI AKGEAVVTKT VIASSHSITG
STPSSAAKTQ ERMMTHLRAG HYFGELALIY DDPRTATVRA VGDVELLYLT QEDFQHIGQV
HLSLMLQQVP LLARLSARDQ DIVLKCLRPA NFSDGEYIVH QGDEGTRFYM ITRGEAIVSE
KAVGPDKKPY EKELTRLYEG HVFGEMSLIY SEPRTASVRA VGPVKCLYLS KEDFDKCLLS
DHFQRFIQEA YVEKATRRAM RLRLQQRANS AATMASTPQT SSGADSSSGS IVAPPPAPTS
PVKATETKKL VKQRLKNGEV VVNKYVIKGD LGRGTFGRVK LCESQKDGQM YAVKIMHKTF
VQRMAGKEDQ LYDVLRREVA IMKKLNHRNV VRLVEVIDDP NSQKMYLVQE YVQHSLMEEV
TQARRLNEPV ARKYMRDLLT GLQYLHFHKV IHRDIKPENI LVSSDGVAKI ADFGTARMIM
NETETISGAK GTPAFMAPEM FDIDATYQGP AVDVWSLGAT LYMMVIGHPP WMADNEIVLA
ERVQRMELRF PKDVERTMEP HLKNLLQRML TKDPALRISL KECFIHEWTT KEGSEPLGML
TSEKSLTVSM DESERAIENI PERIDQRLTE SLAQAHQLVK TRQESVGPGV VRTNSGRYFT
GTPVSGTLGS RIPSSASTTS SITTVSSSTS ISPSRASSEE VSRIICAWRH HKRVQLMDGH
KELSERSREL LIEQKRMAFS VDRAKVTEII LPAAKPTSRS RYPSAASSSS LRQVREQSVL
SSSSSVSSMS TVGGDTPSSV DSPRTRSFPT GRSNSVDNSL LAKKNSFRSR SHKDSGNLEG
FGRTSFTSVS QLSELAAIPV EDNLDQRGSL SSSSEAGSIG HSSSSNLSNT SSSDADLMKR
SLSRKKDFLM VTSEVFRDDA GDYQTRKILF QARDDDFSVA SRVPTHSNSG RELLPPGRAG
STNSSSSSQK PRRLGSAGKL GSTSKLGSLS KLGSAGSGSA MSSAMGSAMG SAMGSAMGSA
MGSAFSKGAT SRRSSHGSAG SISSSSRSVV TDDGNIEEFD MEGIDCVQVT EIDDEDDDEP
MHRGSMHKNS GASSRHFHLH ASDSSRANSS HNRSHSSQGT GMDGLSDADS DSDDSDYSDV
ECDVDVDATF SELIASPNQL DLISHDDEEI APIVTAKPSL TSLLGSSSSS LDVDNSGNVL
TLGSLASMAS GASALSMATP ATLPDIVQVY VSSKIRENLT LSIRSGYAEA KGARSYMEDR
STGQTTCDLS RYPVALADTY ASLAFFAVYD GHNGTDTAVK LQNELHHRFF AEGAGFVESP
VSCISSVCEA VDNEILEQQN RSVLPKRKRT MAPDELRRYL RSEAADETDP SLLEGECCEI
DGEIVCGEEM KAQLQPISFS GAASVFAVAV KQRKKRRRTA GDKEGDAESE EGEDDEDVKV
VEDEEDLEGE DQPTLVYVAN VGDCRAVLCT ADAQAIDLTT DHKASLPAEQ ERIEASGGFV
HNGRLDGILQ ISRGFGDLAH KQDGHLVVTP DVVEHVVHPS DQFLLLASDG LFDVLTSQQA
VNFVLRKLQT HGDVQLAAQE LVLKSQAYFA HDNVSVVIVA LNQKGDA
//
