ID W2PNF8_PHYPN Unreviewed; 1920 AA.
AC W2PNF8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=1-phosphatidylinositol-3-phosphate 5-kinase {ECO:0000256|ARBA:ARBA00012009};
DE EC=2.7.1.150 {ECO:0000256|ARBA:ARBA00012009};
GN ORFNames=PPTG_16612 {ECO:0000313|EMBL:ETN02397.1};
OS Phytophthora parasitica (strain INRA-310).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=761204 {ECO:0000313|EMBL:ETN02397.1, 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:ETN02397.1, ECO:0000313|Proteomes:UP000018817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INRA-310 {ECO:0000313|EMBL:ETN02397.1,
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; KI669618; ETN02397.1; -; Genomic_DNA.
DR RefSeq; XP_008912434.1; XM_008914186.1.
DR STRING; 761204.W2PNF8; -.
DR EnsemblProtists; ETN02397; ETN02397; PPTG_16612.
DR GeneID; 20185689; -.
DR VEuPathDB; FungiDB:PPTG_16612; -.
DR OMA; SNHRWSE; -.
DR OrthoDB; 5481504at2759; -.
DR Proteomes; UP000018817; Unassembled WGS sequence.
DR GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd15725; FYVE_PIKfyve_Fab1; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd17300; PIPKc_PIKfyve; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.810.10; 2-Layer Sandwich; 1.
DR Gene3D; 3.50.7.10; GroEL; 1.
DR Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR044769; PIKfyve_PIPKc.
DR InterPro; IPR027483; PInositol-4-P-4/5-kinase_C_sf.
DR InterPro; IPR002498; PInositol-4-P-4/5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45748; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE-RELATED; 1.
DR PANTHER; PTHR45748:SF7; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE-RELATED; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF01504; PIP5K; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00330; PIPKc; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS51455; PIPK; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE-
KW ProRule:PRU00781}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Reference proteome {ECO:0000313|Proteomes:UP000018817};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00781}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 96..167
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 264..331
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1523..1852
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 230..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1391..1418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1873..1903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1404..1418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1920 AA; 214602 MW; E72145521256733E CRC64;
MATVCGAFRQ LTSACVSAPE SPARLKAGRA SSLSSSRELA LFSVPNGAPL TFTGPATRIA
RNSRTGLGGY TSLEQFTRSV EKISTLPVAR LRSDERVGTM FSSMDAFLGV QLVASSRRDF
RVCVNFVLPG SDAETLGIHP AALVVAINGK SMRGVSLQRV LSTIRRALCA NENRSDGTAI
EVPDLGDHIE IDLAQREHEM NVDRNPFALT QFPSPQGHHL PGVKQFRDNQ AEDQRQEPMQ
IQEQNSPTLG RQRSRSFKHF WMSDRSSKAC YECEQLFTFF RRRHHCRSCG QIFCANCCAR
LPQSFGGNKV DESIERLRKQ LVCHTCHRQL REGLQMELTG ANFEEDPQKP ASSPPAPTLL
LMPQHIAEAM ERSTSDASNY KQLDKSELFD KDEISDDMRV SEPPEKSRPP VLFSMFPKVQ
IVASAQHLAH QPHLHELTKE VKQTGHGTGR RLRTFSEPLI LFGRKDAQHT SRKLKRSNSQ
ADLCNPSNHR WSAAEFKRLV AESNAQARLA GAYPPTSNAL TTRPKAMSVS FETPRFGNAV
QWSPFGPNKL ASKDSGILAM VGLSKDVHNE AEDPKCVSRR EAAMEQMSKD ARDRIEERIF
HLLDSSPAVS QLLMVEQHRW MQIISLFAHR AALTVSCEPD KGDLLDIMHY VRVQCLDGGR
VQDSFFIDGV LVHKSLARKG MRSDILNPRI LLIASALDYQ RKKEAISSLE SVAGQEVEYM
HIVTEKILTL NPDIVMFEGH VHRVAEELLF KASVSVVKNV RLIDLQRIAR CTGASVLTSY
DHIDKMSDVG VIGTCKRFYV LLSDQEPKSA KKIAFRANAD GFYVAEDGSA ISRQRKKRTQ
RQNIVFEGGI TSKGCTLCLR GGTPGVFTEI TNVLTAIIRA AYNMRLQRSM LAAYGYIAPS
QNHERSVAEE WFAKSSTSLY ISLKSNSLSM RAALKETQAM CKWCKAHTRF NNISSLRVVR
GADDDDSIPS STTVVQSGHP HWCTCGAKSS SSLRDRILFS TCWSTLEGKT ASKADMMCID
FYSSNDMSVG QFFDNFCFSS SKTEFKRAFS TSKLSFSHDT GRVIVRVKDL TDFKDSSDQL
PPAEFLREFN YRAVLQRVRS EDVLMWSRNM SGGNHLSSEY TVVPSDLWNY SFGKFLEDMF
YGKAMDIDCA RFPHLAGVSG SRDSSLVHYF SRRGRVVSVH VEPLEPVLHV ALQPALWQEH
IDHQVQLDAI HDLCDLVREV YGVTTSKVAE SMADLVTPLH AKQNLKILRN EVQQWYSCFG
AKIESNPPQD VFAYNAHFRE IYEYAVGWSL RITRAVQATV KPTMASLVNS PKSALPKAWF
DQLAQQAEFS DRYSEPATPS ELEATPVNIN FQEPGNLAHL ASFARSLAAA KSASPAGGMA
EVANEVANTL RQNGTTSSRQ SEPWDTDESY DRYDESSHSF PADYKAETES YPAAPVFKQS
VSALGVPGHV SSTMGALASK KALENFRLTQ QAKKPDGLGY LALPKRLLEW HPSLPLGANK
ATVLVNAKQP TSVVAYSLFS NEYSQCISEN MRKEATRYAL EAKTNGTSPP IDCVQSDEIR
SMLRILRSTT RNNVDHSFVD ENQFQSAMRF SCKSYYAMQF HALRKLYYGG DRNYVESLCN
CQQWNAAGGK SGAGFLKTRD ERFIAKAIPE IELQMFLSMA NEYFCYMAKT FENDLSSMLS
KVLGIYKVSI SNTTQSGDSD PNVRMCVIVM ENLMYGREVD FSFDLKGKME GRYKEDHNGD
SRSVLWDRNF VELAGGIPLP LQESALSLLL SAIMNDTTFL ASVQATDYSM LVGYDVNKQE
LVACIIDYIH KYDFMKMMEH AGKRLIQEEG EITVLNPKHY RKRFCLAMNK YFVTIPSRYT
KVTTVIRNTA SNTTTVGSTG TTAQEDEKDR DYAQPPYSTS TTASSVSTIA SVVGTHRRQL
//
