ID A0A0N4VB28_ENTVE Unreviewed; 1436 AA.
AC A0A0N4VB28;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=EVEC_LOCUS7208 {ECO:0000313|EMBL:VDD92457.1};
OS Enterobius vermicularis (Human pinworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Enterobius.
OX NCBI_TaxID=51028 {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0000772401-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EVEC_0000772401-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDD92457.1, ECO:0000313|Proteomes:UP000274131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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; UXUI01008821; VDD92457.1; -; Genomic_DNA.
DR STRING; 51028.A0A0N4VB28; -.
DR WBParaSite; EVEC_0000772401-mRNA-1; EVEC_0000772401-mRNA-1; EVEC_0000772401.
DR Proteomes; UP000038041; Unplaced.
DR Proteomes; UP000274131; 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; 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:UP000274131};
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 127..182
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1091..1420
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
SQ SEQUENCE 1436 AA; 160836 MW; D066C89207977A0E CRC64;
MATSNVELTY FAQLPPEQEN DDASTSNIFT GFFGKFFKSS SGTVLEEDNG SEAAGIASSS
AVIGLEKDQE DVTVSPEVAT DREEGGDDVL ATGVRGIPGR LSSLFRSRKP SLVDYNSSSF
RRYWMPDSTG KECYECQERF TVFRRRHHCR LCGQIFCAKC CSVQVPGSLL GYMGELRVCE
YCARVVVTYL PQGLSTSDSQ QGETKEELSV RDQPVKNVAT VSAGKNTVLY GSTYNSKENG
GALTASNQLP SLLSVVELAA QKETTAKFSP LPPAEHYPSI DDYEPEWVRS IEMSNTPKML
NKPDEISSLP SNISGFDAFS NNNFDATIAK IEDRSKTLVP GLPSCVDEGP QEDIPLESAF
EERIQKLLLY LFEREMLDPT VWWDVIWPMS RQVAASVNVD VENRRDHMNV LNYVHIKKLW
VDDQKPSAAI VNGVVCSKSI THAHMPDTIA NASVLALAGG LEYERVAEKL SSIEPIVMQA
GFTQPSIVLV ENSVAQIAVR MLLQAGVTLV SNLKPQVLQR IARSTCSDVM PSLDVQILQQ
KIGFCASFKQ QTVRLASGKR KTLLIFSDCS SDLGCSIILR SNSRWQLRCA KRILRFIILT
LYSARLEVQF FSLLGTVISK RSRDCIVCAL NINEPDPDEN GFTNRLKKCT LSSSPFIEFG
VPFLETAKGR GCVLRPYFKQ PLYRHLSSDD FNRMRKRQED IEIALKNQSS KKETFYKHHD
FVENKTLCAI NDDDVASYRA FSGQIFKHHV EGSTSTEKKI SEEDFCCYED VFDPLIHQRI
AILFGSFSPK SPNAPLFCVR PWVVQMEHYG SNDMTLGEFL KRFCFNKDYQ CPSTNCEVPM
LDHARKIVYR HVCIEITTQN CVQPADESGA LSQSCNYKAD TIICWHYCLI CKASSAVVSL
PDIAVRMSFA RYIDYLANGG MGACSISAFS KVKPCHVTFS PVVCTVDAVM FTRKFVADKE
SEIRQTADTI FKLMETRIER FAQNPDSSRF SSHYIVLKEA LSETRAQFDE IILQFDPNKD
LSSKTLTIRS NDAVYIKAVD TETRCRYLIQ KLIDLWNEQC LSINQAARSF KKVVSSNLLS
NHVNASKTSS VLGDAPKDSN AVSSDTLKSS SSAVALNEVE LSPIESPFLT QLHLSLPAPN
PGMTVVVKDL MDRKGNAHPD VGSIIAYALS SVDYETKRLR DTETVSSQEH IELDFGDERA
QYFVKVYYAE SFHRLRKLLF VEGEECFIRS LSVSVGWNPQ GGKSGASFYR TQVYGVYRIG
YKNKVSGNQL KLDVLVMEYL FYKRNIKLVW DLKGSQRNRM AVEGKKTADL VLLDENLIKD
LWNNQLYVHP HSKAALNMAI SNDSHFLSAQ HVMDYSLLVG VDETNSELVL GIVDYMRTYT
LDKKLESWVK IVAIPGSLLP TVISPVMYCT RFSDAMDIYF PVAPDQWTGL GSSVSY
//
