ID W2Q9V3_PHYPN Unreviewed; 1851 AA.
AC W2Q9V3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=CAMKK/CAMKK-META protein kinase {ECO:0000313|EMBL:ETN09651.1};
GN ORFNames=PPTG_11270 {ECO:0000313|EMBL:ETN09651.1};
OS Phytophthora parasitica (strain INRA-310).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=761204 {ECO:0000313|EMBL:ETN09651.1, ECO:0000313|Proteomes:UP000018817};
RN [1] {ECO:0000313|Proteomes:UP000018817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INRA-310 {ECO:0000313|Proteomes:UP000018817};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETN09651.1, ECO:0000313|Proteomes:UP000018817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INRA-310 {ECO:0000313|EMBL:ETN09651.1,
RC ECO:0000313|Proteomes:UP000018817};
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 INRA-310.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KI669584; ETN09651.1; -; Genomic_DNA.
DR RefSeq; XP_008904797.1; XM_008906549.1.
DR STRING; 761204.W2Q9V3; -.
DR EnsemblProtists; ETN09651; ETN09651; PPTG_11270.
DR GeneID; 20180834; -.
DR VEuPathDB; FungiDB:PPTG_11270; -.
DR OMA; MHKTFVQ; -.
DR OrthoDB; 75353at2759; -.
DR Proteomes; UP000018817; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR GO; GO:0004690; F:cyclic nucleotide-dependent protein kinase activity; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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:0000313|EMBL:ETN09651.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000018817};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 296..413
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 427..534
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 620..884
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1496..1845
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 1..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1227..1391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1667..1697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1667..1684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 649
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1851 AA; 202373 MW; 8073D8ADAD45B6BD CRC64;
MGQRFSTSRD SDVSEADGPP STALAARASD ASPTSLSSPP PTASSPPSSA DTAPRSTPGT
LSTQRPTIEN AAEQQSEREG STRLVDVVHD TLSSDQEPSA HQRRQSDEED ALSASRVSST
DSFPSSPLNV KADDAHPLTR RSSMSRTPAP PKLSRFRPSM DIPRSPQSSS DSSLDSSSSS
SDEELVGSGE ELVSDWLDEP EDAVLSPPSQ PKRTRHASAC SSVSSHTGNS VSFSAMHSSG
GRNSNSSQHS MTGWASWLSS PDDVEEEDDA DDEPVALTPF LRDNMPVYEV MRQVQLFRNL
SQMQQEQVVR ALKPAKFSDG EVIVAQGTRG SRFYMIAKGE AVVTKTVTTS SHSITGSTPS
SAGQTQERMI THLRAGHYFG ELALIYDDPR TATVRAVGDV ELLYLTQEDF QHIGQVHLSL
MLQQVPLLAR LSARDQDIVL KCLRPANFSD GEYIVHQGDE GTRFYMITRG EAIVSEKAIG
PDKKPYEKEL TRLYEGHVFG EMSLIYSEPR TASVRAVGPV KCLYLSKEDF DKCLLSDHFQ
RFIQEAYVEK ATRRAMRLRL QQRANSAATM GSSTPQARSD SSSGSTVAPP PAPSSPVKAT
ETKKLVKQRL KNGQVVVNKY VIKGDLGRGT FGRVKLCESQ EDGQMYAVKI MHKTFVQRMA
GKEDQLYDVL RREVAIMKKL NHRNVVRLVE VIDDPNSQKM YLVQEYVQHS LMEEVTQARR
LSEPVARKYM RDLLSGLQYL HFHKVIHRDI KPENILVSSD GVAKIADFGT ARMIMNETET
ISGAKGTPAF MAPEMFDIDA TYQGPAVDVW SLGATLYMMV IGHPPWMADN EIVLAERVQR
VELRFPKEVE RTMEPHLKNL LQRMLTKDPA CRISLKECFT HEWTTKEGSD PLGLITPEKN
LTVSMDESER AIENIPEQID QRLTESLAQA HQLVKTRQES VGPGVVRTNS GRYFTGTPMA
GTLGARIPST ASTTSSINTV GSSPSRASSD EVSRIICAWR HHKRVQLMDG HKELSERSRE
LLIEQKRMAF SVDRAKVTEI ILPAAKPTAR SRYPSTSSSA SLQQVREQSA LSTASSVSSM
STMCGNTPSS DSPRSRSFPA GRSNSVDNSQ LIKKNSFQIR RFKDSGNLEG FGRTSFTSVS
QLSELAATPV EESFDQRGSL SSSSESGHSN SSYSNTTEAS DADLMKRSLS RKKDFLMVTS
EVFRDEGGDY QTRKILFQAR DDDFSVASRV PTHSNSGREL LPPGRAGSTN SSSSSQKPRR
LGSTGKLGSA GSSSAMGSAM GSAMGSALGR TNTSRRSLSG SSVSSSRSVV TEDGNVEEFD
MDGIDCVQVT EIDDEDDDDL VNHGMRKGSG ASSRHFHHHS DSSRANSSHN RSHNSGLSDA
DSDSDDSDYS DVECDVDVDA TFSELIATPN QLEIISHDDE EIAPIVTQKP SLTSLHDLSS
SSLDVDNSGK VLTLGSLASM TSSSSALAMA TPSLMLDIVQ VYVSSKIREN LTLSIRSGYA
EAKGARSYME DRTTGQTTCD LSRYPAALAN NYASLAFFAV YDGHNGTETA VKLQNELHHR
FFAEGAGFVE SPVTCISSVC EAIDNEILER QNQSVLPKRK RTMAAEEMQR YLRSEGTHQS
LIEGECCEID GEIVCGEEMK QLLQPISFSG AASVFVVVAK QRKKRCRTND KEGDTDAKDS
EEVKTADEDE LDEEDQPTRL YVANVGDCRA VLCTADAIAV DLTTDHKASL PAEQERIEAS
GGFVHNGRLD GILQISRGFG DLAHKQDGHL VVTPDVVEHL VNPADQFLLL ASDGLFDVLT
SQQAVNFVLR KLQTHGDVQL AAQELVLKAQ AYFAHDNISV VIVALNQKGD A
//
