ID A0A016UWA0_9BILA Unreviewed; 1469 AA.
AC A0A016UWA0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=1-phosphatidylinositol-3-phosphate 5-kinase {ECO:0000256|ARBA:ARBA00012009};
DE EC=2.7.1.150 {ECO:0000256|ARBA:ARBA00012009};
GN Name=Acey_s0023.g671 {ECO:0000313|EMBL:EYC19699.1};
GN Synonyms=Acey-ppk-3 {ECO:0000313|EMBL:EYC19699.1};
GN ORFNames=Y032_0023g671 {ECO:0000313|EMBL:EYC19699.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC19699.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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:EYC19699.1}.
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DR EMBL; JARK01001359; EYC19699.1; -; Genomic_DNA.
DR STRING; 53326.A0A016UWA0; -.
DR Proteomes; UP000024635; 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; IPR002498; PInositol-4-P-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:UP000024635};
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 76..136
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1126..1453
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 143..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1469 AA; 166242 MW; E0CB9E703E5A73B1 CRC64;
MSAEXTVLTC IDAHAPCQFQ LVNVDGDRCM AHAANAVDNR DPVRRKEGVI TFFDRLEEEA
AEESLAGSSG QYWMPDSTGK ECYQCEERFS TFRRRHHCRL CGQIFCAKCC NIHVPGSALG
YIGDLRLCHY CAKMMAQYLP PEQDRLQSEE LNNGAITNEE PTAQSNDALG AGGRTVSTVS
SGSMMWSHPS DVGSSSLEKK DTSFTPPTTA TKPPSLLCAT ELYLQHEKRS SSQSDSIRSE
LREEEESGPD WFRNMDPDTN FPMKDTDHKL RNSVVHPAEN DFDPFPISIE GVAPEKVDEK
KPLSAKSSLQ LSPTKTNFDV DIDRAFDHRA EQLLTYVCTR ERLQDSRWKP IILNLAKEIA
HTVKVDVARR RDDMNILSYV HVKKLYVEQE EPSSELVWGV VCSKSVQHES MTEPLKDASV
MIVAGSIEYE RVPGRLSSLE PILCQEGEFL AKQVERILSR RPSILLVEGN VSKLASDLLR
EAGVRLVVNV SVPVLHRVAR STGADILPSS DAQLIQQNIG FCPYFTQRSV TFKDGRQKLL
LVMDECPPDR GCSVLIKGAD ARELKAVKRI LLFLTSLLYS SRLERAFLNM FNVRMAYQIS
NCEVCEARRE NIDHSNEKSD FELALADSVL CTSPFIDHEP PYLKSARGKN CSLLPYFNVP
VYQFFNEKDF DARVDDESNE VHRQLSQQCK TPVPNTPRHF YAFNGARDAN NKTDLAAFRA
ISGAIFKKRI QLRNLKTPAR ADSRERQHSR RHDILDPYVH QRIAVLFGSF SPKSPNAPYF
CVRPWVVNME FYGPHDMTLG EFLTKYCFNK SYECPSSNCE VPMLDHSRKL VYGRVCVEVT
TQVVVSGTDE SINSNAAPGQ IYAWTYCNSC KFSSAVIPVN MSVWHLSFGK YLDYIAYSTF
SKGGDTASPV KTKCSHCFFH EHSHFFSLGN YVASFKVTPV RPYNVQFSPV QCRIVPNQYT
KQALLDGVTR MASLADDIVR TAEDRLALFT KHDQYSQYAG TFHTVLRQVV DKCIAAIGEK
RKYAEELKCL DRNIITSNDI YAVKANEALM HIREAIYHLI TTWNDQSTVL AATVRAVKKT
VEDNGTASET TDIALERIDD PFPSYLHLGL KLQPRVGVVV RDIMDSRGNY KPDIGSIIAY
ALSSADYEEN RRKQREAAKG EQPPLNLNST SVAQDEQSLA AEHLEIEFQD NQASYYVKAY
YAARFRLLRK LLVTEGEEAF IRSLSQSTFW TPQGGKSGSF FYRTQDDRFV VKQMSRFEIQ
SFVEFAPHYF DYVKTAVVEN KLTTLCKVYG VFRVGYKSKT TQLKVDILVM EYLFYKHNVN
QVWDLKGSLR NRMAATAKTT SDLVLLDENL MKDLWNKQLY IYPHAKAALN QAISNDSHFL
SSQHVMDYSL LAGVDETNGE LILGIVDYMR TYTLDKKLES WVKIVAIPGA HLPTILSPEM
YCTRFSEAMD TYFPVVPDQW TGLASAVSY
//