ID A0A090L014_STRRB Unreviewed; 1588 AA.
AC A0A090L014;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=SRAE_1000128700 {ECO:0000313|EMBL:CEF63021.1,
GN ECO:0000313|WBParaSite:SRAE_1000128700.1,
GN ECO:0000313|WormBase:SRAE_1000128700};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF63021.1};
RN [1] {ECO:0000313|Proteomes:UP000035682, ECO:0000313|WBParaSite:SRAE_1000128700.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_1000128700.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CEF63021.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 Heterogonic {ECO:0000313|EMBL:CEF63021.1};
RA Aslett A.Martin.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:SRAE_1000128700.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) to UniProtKB.
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DR EMBL; LN609528; CEF63021.1; -; Genomic_DNA.
DR STRING; 34506.A0A090L014; -.
DR EnsemblMetazoa; SRAE_1000128700.1; SRAE_1000128700.1; WBGene00257891.
DR WBParaSite; SRAE_1000128700.1; SRAE_1000128700.1; WBGene00257891.
DR WormBase; SRAE_1000128700; SRP06465; WBGene00257891; -.
DR eggNOG; KOG0230; Eukaryota.
DR OMA; SNHRWSE; -.
DR OrthoDB; 5481504at2759; -.
DR Proteomes; UP000035682; Chromosome X.
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; cd17300; PIPKc_PIKfyve; 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; 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; SM00330; PIPKc; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR SUPFAM; SSF56104; SAICAR synthase-like; 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:UP000035682};
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 119..179
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1237..1571
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 329..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1588 AA; 183314 MW; 85E16872C3C1107B CRC64;
MSDFKDEDTF TFFTPLREEN DDVSKNDQSS LLVGLFNKFF KTNTQVNQTF NNTKINNSNT
SSITENSEND INNKKDSLTN VSLADDAMEV LVIDKNLEKK NDQLKKYDQS EFKRYWVPDS
TGKECYECHE KFNAFRRKHH CRICGQIFCA KCTNNTVDGA VLGYREFLRV CNYCKKNIKP
NDKHFQKNGY DSDEECILKY NDDKTFRNTN DKKIYELSQK ITESAFEPTN NVSSVSMNFP
LFKKNDDGKN NVANFSTSND ITSFQPTNIA CEKQLPTFLN IDDLARNSIE TDYTNSVVVA
TNFKNIQRKE DSLLGTSDNN EPEWVKNIEL SNSSNQSESK QTSDSNPSSF NEQKLFNTWN
VLNSSNNLNE KNNLSTNNEM PLNLKDAFDK KLNDFLDVLL EKEQIDKTKW KTLLWKLSKE
INDTVEVDVR NKGDNMSILK YVHIKKFCCN VSKPSAKLIN GIVCSKSVAH ANMATKIYNG
SVMMLSGSIE YERVTDKLSF IDHILQQERG YLSNQVDRIV SRLPSILVVE NSVAYVALDM
LLDNNICLIH NTKPKIMKRI ARIVGSDVLP AFDAQILNQR IGYVYHFSQE HILLRDGKIK
TILVFKQESG INGVSVILKA SSIRELKAAK RILKLMTLAR YSSKLEIALL EMFNTKPITI
SSSITPAKCL TCQLNLMDLD YNAKNGFLHE INYCHIGWSP FISVGPPYME TKRGQSSAIR
QYLKDNLFPI GNESDYKILA EDEDKKENDL FECKKKFKLL EEEIEDNFQH FFVKEKSLLI
EDVDDDMSSY RAVSAKIFKD RCEKKRIMEK ELMERQVHLA DDANSPLRIL QDSDVFNPEN
HQRISYLFGS FTKKSSNPFF CVLPYVLKME FYSQHDMCLG MFLSKYCFND DYKCYDQNCS
VPMIDHQRKI VHRKVRIEII SQKYVQSIED INLSKATTSA FNQENVILCW QHCPTCIVSS
AATPLPHEVW HLSFAKYIEY LANSINCVNL STSQNSKNSC NHCSFHDHQH FFAYNDYVTS
FKVYPIKPFH VQFSPIICLI EPRFVSISGL ELEYRKVDSL AKDVFEKINE NLVKLKFHPS
GIRFQLVHDT LKAFLEKIEV EVNEALQRIS TNNIFQSNNP VMSNNSDVLK INDLLNWSNH
KLYELTTLWN DEVAKINSQS KSLKKSSSSI NTNTEDNTII TTVSSGNLSV SSTDTNTPLE
LVTIYDPFPE NMHLSLPQTK DNVCIIVKDL ISKKDSVKPD YGSIIAYTLA SNEYKEERIK
LRHLKNCMDT PLSLKIPESQ NKEEVSSRNN EVHHQKNHID ITFEDINASY FVNVYYAEHF
QMLRKICFAD GEDMFIRSLS STTMWKPQGG KSGSDFYRTD DKRFVFKEMA KPEIDFFLTF
APKYFDYIYN SITEKKITCL GKIYGVYRVC YKNKKTNSQY KMDILVMEYL FYKKNIKQYW
DLKGSLRNRK AYPEKHHAKD QVLLDENFVN NLWNNQFYVH PHAKAALTQA IDNDSKFLSA
QKIMDYSLLV GVDSENDEVI LGIVDYMRPY TIEKQIESAV KKAALPGNQL PTIINPEDYR
VRFMEAINNH YIHVAPDQWT GLASISGF
//
