ID A0A0V0UQF9_9BILA Unreviewed; 1543 AA.
AC A0A0V0UQF9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, 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=T09_2840 {ECO:0000313|EMBL:KRX53531.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX53531.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX53531.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX53531.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-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:KRX53531.1}.
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DR EMBL; JYDN01000199; KRX53531.1; -; Genomic_DNA.
DR Proteomes; UP000054681; 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; 2.
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:UP000054681};
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 87..147
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1144..1494
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 37..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1356..1375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1543 AA; 175788 MW; C70DEE777A33D7EE CRC64;
MISFQKRAVF VVLNCGVANN TIVMSIFNRL FGKKVPEREP SSESSTNAED KQNSSPRPPE
FNILGSAATD SLMDYDRSEF RQCWMPDSSG KECYECREKF TAFRRRHHCR ICGQIFCYRC
CRQELPGNLL GYTGELRVCD YCLSMVRRMH NLPSSLSECL QLHSDREKVV QKQQQQQQRQ
QQQQQQQCAV SDVESETIKD KDSTNSADSN LQLQEFRNFL DDPEPDWLRD IQNTEMNTEP
FVWQIPVQDA ICQQQIKSID DVVGFEKHHP LDFVVTQAVD EVPVVSETKS DETLDEVDYS
LDSNGPCTSS NNAELMGIFM EKIRHQLKYI LKLHALPENQ WYSLLLRLAE EVAMTVRPET
KANNDDMNIL RYVHVKTLRR SDIPKGELIY GTVCTKAVLR LTMLQRLQSP KILIVRGPIE
YERIGGKFCS MDPIIMQEAE HLRHVVNKIL ALQPDVLLVE HAVASVAADF LSQSGLTVLH
NVKRSALERI ARCTDADVLE SAEGQLFKFR MGTCGLFRTE HVTLLDNQRK TLCRFENCRP
KLGCTVLLSG PCELQLFLAK RVLRFLISVI YSARLEVDLL KLIGVNKMDI GQCIVQPDAH
LADEKCEQSE IALTTYSPFI ELSLDRSDCL MKNGTVVNSK SWTMFCGDCC QDSADNNSLN
PKLVHSFFTS STGFWGKETD VRGLLANYRA TGAKLLRQRC RSVEQDDPKN KQQLTKRLLD
NLIVEQCYKN VKHPFAQDHL TTLQSCHLSK PATPRRYCVG PRLLFAYYYQ STDLPLGAFL
EQYCFNQNYL CPKEGCGEGM QHHVRRFVRN HLCVDITVGS SAIANYPAKK NTVGCSLIFL
KEWCRECKTT GVEKQISKHL WQLSFATYLN YLFHGLALQS SLGSTSAELC CKHCVFHDHV
HFFTRDSVVV SFSVQAITLC SAKFASLTTP TEPQKVNTND GCVFADQFRK EVDDLLEKGS
NLFGQMSDQL ADLTNQIEST SGSVTVNLVQ GLLSELRELL DQSKSSFAET NGKMQSDVLP
LVNARGFLWR ESQWPIVHDS IILCMRVLAT LLLTWNCKIS DFLLNLSKKR LNELERESTV
SKMADDDKTA GCGMINDGEV NLKKPNSDDL KAMQKLINGA ILNWPFPVEQ HFSLPIGKVP
VAVDEHKPSS IIAYALASKE YLDFVRAEEK FTDQDVVEKL ANFSCSNNDS SSNFDTDSTL
PLEVQFSDSM AKFYCKIYFP RQFRLLRQMI FPLGESAFVR SLANCQPWQP SGGKSGAKFF
RSLDRRFVLK QMSRFETQSF VKFAPDYFRH VSSACFNGRA VSLVKIFGVF RIGYRNSHNN
AACKMDLVVM EYLFYTHEVQ QVYDLKGSLR NRMVPEMPKQ QQEQQQQHHH HHHQQQQQYI
QQGDLVLLDE NLLDRICDDT FYLDAAAKTA LDTAIRDDTA VLSANHIMDY SLLVGVDTDR
AVLVFGIVDY LRTYTWDKKI ESWVKSVSAS GQLPTVISPH LYRLRFIESM DMYFPTPPSD
SANLVGQCGK LPAFETNHYE PAISVYFTLN SLLKYTGYLL WFC
//
