ID W2LPS2_PHYPR Unreviewed; 1335 AA.
AC W2LPS2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Atypical/PI3K/PI4K protein kinase {ECO:0000313|EMBL:ETL99442.1};
GN ORFNames=L917_03717 {ECO:0000313|EMBL:ETL99442.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL99442.1};
RN [1] {ECO:0000313|EMBL:ETL99442.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL99442.1};
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 CHvinca01.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KI678359; ETL99442.1; -; Genomic_DNA.
DR EnsemblProtists; ETL99442; ETL99442; L917_03717.
DR VEuPathDB; FungiDB:PPTG_08029; -.
DR Proteomes; UP000054423; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05168; PI4Kc_III_beta; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF22; PHOSPHATIDYLINOSITOL 4-KINASE BETA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ETL99442.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1039..1320
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 820..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..850
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..894
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..988
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1335 AA; 148507 MW; BAC4A1CF5BF0CAD6 CRC64;
MEVTTMPEGS TPVAAAALKR LQINEDSSDD NRSEDWGADE SDWRTSSSSE PAARFSLIAL
PSKVRDSVFR RDRKPQRKTK DRSSTADTTV TSSANSTPRD SELITKTQQE LENVEKFRIF
WDEKLRNTMD RLAGTKTKQT DVEDDVFHLL LKLYAHQDVV AQLYSSYEAN AAEFEFYIPQ
LCTFLIHGNY AKQHQLECFL MSRSGDSLPF AHRLTWFLRS FCDDAKEYQS EYLSVTSSQD
QENSDLLTAI GMRAGVPALL MNRGLCVEEV SAAKPHNLEK RRSIIFPTDN DLDSSTLETD
ETFAGHLLSK RNSIQDEARA EEGNSQQILL FKQTPKFVEA LTDLADQLIP TPRPQRNSEL
RKGLAEIEEQ MLPSDVIYLP IGNSCHRVKG IRIDECFTFS TKERVPYFLC VEVLDYSVPS
ASKKQRKRRR SKTSRNQSRV FSLRLPFKKT DSDLMVPVDD SPMSSSTSPE SELSFVPSPS
VSSPLPEIEE EKSLETMLDE PLDGEDGDDE KEESKRKSRK SFQEDEGLQR AGEEQQERLG
QWNTSRPRRR SIKEYSSSAS ARSGGQFDSF YSSWFSKKAQ QEAEDEFSAP HASSMQPTQT
IRNDEEDAEA MELAPVETDC TDDNTASTES SEGVLNDIEV EQTQASDVIE DTTKAEAETY
DAVATESATP AANGGIFLSL FSRKPKLEVV NVTSNQHENQ PDDAKEDVPA ESKPAEIEAP
KTTTPETACV AAAPAQSAGI FSALFAKKPT DVSVPASIPT ETSVVDKEPS KEEATASSSE
ECNEAKPIVA PAAPVGIFAS IFAKKPAEAT AVAADITVAS VSSLEPSEED VSDDLDAEDA
DGEESESNEA LSSDNDPADR TEASVSSLDR SESGISDSIE AEEADSEDTD SNGGFFSDEE
YAHEPEPSPM TLPAEKPASF VSWFSRKPTA VVVEPAPEKE ENATAVTDTT TSSESPPDSE
TAEASAPVVD DEKDSQDDAL FQQRKRDLSE SLDFADPTAW KKKFDLEDGL TEEEPDLEMT
DVDAVEEDAD EEENDASEDE KPMIVFRERW SEKEARIRRE SPFGGHPGWR LLSVIVKSND
DLRQEQFAAQ LIAQCDRIFR EYSLPLSLRP YNVIATSAKT GLIEAVPDTV SLDSLKRNDP
GYTTLLDFYT RLHGEQGTTG FIRAQRNFAE SLAAYSIVCY VFQIKDRHNG NILVDTDGHV
IHIDFGFLLT NSPGSNWNFE RAPFKLTDEF VELMGGPRSS TFRYFRSLCI RAYLALRRNM
DQIVLLVEMM LVGNADLPCF AGGKKAVIEG LRARLKPGAR TSTCQVFVNQ LIDQSINNWR
TRWYDKYQRA CLGIL
//
