ID A0A0W8D129_PHYNI Unreviewed; 3195 AA.
AC A0A0W8D129;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=AM587_10017013 {ECO:0000313|EMBL:KUF90109.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF90109.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|EMBL:KUF90109.1, ECO:0000313|Proteomes:UP000052943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUF90109.1}.
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; LNFO01001581; KUF90109.1; -; Genomic_DNA.
DR STRING; 4790.A0A0W8D129; -.
DR EnsemblProtists; KUF90109; KUF90109; AM587_10017013.
DR Proteomes; UP000052943; 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:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 1.
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; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.50.7.10; GroEL; 1.
DR Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_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; PF13855; LRR_8; 2.
DR Pfam; PF01504; PIP5K; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00054; EFh; 3.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00364; LRR_BAC; 13.
DR SMART; SM00369; LRR_TYP; 14.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00330; PIPKc; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51450; LRR; 5.
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 Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE-
KW ProRule:PRU00781}; Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Reference proteome {ECO:0000313|Proteomes:UP000052943};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 DOMAIN 2146..2181
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 2182..2217
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
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 1872..1910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2366..2388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3166..3195
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"
FT COMPBIAS 1894..1910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3169..3184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3195 AA; 360709 MW; 417953F8427E5F1E 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 SVVGTHRRRS
KLDGGQEGME TIVLLEAVLH DYSPRTTVMN PFKPKENRLL SALRSVKAAP AREIVGRIQL
IRRRHPISFG SSNPVLTYWL RFEDVRIRNE RDLLLYVMLS RGNEPALDDE RSVHKMEASG
QTVLLDCGPD GQWKGSHMPR LFEQELLVFD PLVFASVAIG KPASAKPPTA QMLVFAYGAF
ETYVPPAKSA EQVAQEMEAL SSRFLQTVME VEQDQLQGEE ELSLDALQRN ARQLFRMFDQ
DKSDSIDFEE YKQMLAYMKV NLLESKAKRF FQLVDDQNKG YIDEREFVIA MYITNYLRAQ
QKQKRDDNKT TNSQTLSPID VFRQLDGDRD ELLNAFEYEK ALELLGVPLK TKRACKLARV
KLPRSATMSL EQFKRAWVEL VDARAELQKR NVEGFGGQKK GKKMMEKMQN ALLDEIHREE
QEELRAALEA KEVVVRLEKE RRAAEQEESR RLFQQQRQAA TSTRTKEALR ERQYKINRKK
ERTIKDRQAR EERRLLDRAE AEGGKRVIHE REVVQELMMS KMERIIRRKA RCGDDVVDLR
GHGLKEFPHD LYHGRDALSS LSSLLILDLS RNQLQSLPGA IFTHLFSLQS LDISNNALSA
LPEEIGEARD LQLLDVRINR LTTTPKGLTH LHELRVLHLA YNRIARFGDN CQGLYSLEEL
NLVNNVLEVL SDDIGDNLVK LVRLNLRGNP TLKRLPNSLQ QLRELSIWDL SACDQKRLGK
DVFGSQLQSL RSLNLSFNAL STLPDSIGAM PKLQELNFKS NALGSLPSAV GNLSELVMLN
GENNELQCLP SGCGEHWGLL EELRLPHNRL VALPVTLGLL RSLRRLYLSN NRLTTLPLEL
GALTSLRELD VSWNQLASIP DELGCLESLT TLDLSHNQLV TFPQTTAMLK RLIHLCCSYN
ALTTPLEPGL GDLKALRYVD LAENRLVELE PCLYELPQVE VLNLYGNRIT MLPREMAQRC
SSLHKLDLYN NGLQALPLEL ADGLLAQLDV LSIGRNPLTL LPEKTSSTWK LRDQYQTSFT
NGYTPTETKA WVADSRVCYP VFVRVWEELM FEISASLTLP MLDENPGNHR EVSALTSDEF
CKRVKETMKA VTGEDAEGAW QPRYERLARH YFYEFKYVGH TIVFDESTQR KIGNENSEVE
MNLHRLRQER VDAAIKGCSQ IRAHLKAVYR ADEDVLVPAM KYAHERRVVH EKQLLNHARH
DAQETNAGIK EQIEIVQRRH NEAQKLQRTK FADEMKRLAR ERLQMKQQRS SLRKINSRKV
LAATQDCSDT PEREH
//
