ID Q1RL54_CIOIN Unreviewed; 1879 AA.
AC Q1RL54;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=1-phosphatidylinositol-3-phosphate 5-kinase {ECO:0000256|ARBA:ARBA00012009};
DE EC=2.7.1.150 {ECO:0000256|ARBA:ARBA00012009};
DE Flags: Fragment;
GN Name=Ci-ZF(FYVE)-8 {ECO:0000313|EMBL:FAA00211.1};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719 {ECO:0000313|EMBL:FAA00211.1};
RN [1] {ECO:0000313|EMBL:FAA00211.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16519883; DOI=10.1016/j.ydbio.2006.01.024;
RA Miwata K., Chiba T., Horii R., Yamada L., Kubo A., Miyamura D., Satoh N.,
RA Satou Y.;
RT "Systematic analysis of embryonic expression profiles of zinc finger genes
RT in Ciona intestinalis.";
RL Dev. Biol. 292:546-554(2006).
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; BR000180; FAA00211.1; -; mRNA.
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:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04448; DEP_PIKfyve; 1.
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; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR037378; PIKfyve_DEP.
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; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
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; PF00610; DEP; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF01504; PIP5K; 1.
DR SMART; SM00049; DEP; 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 SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS51455; PIPK; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 2: Evidence at transcript level;
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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 36..97
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 215..289
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT DOMAIN 1507..1869
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 700..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1291..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1458..1483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1723..1746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1469..1483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1725..1746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:FAA00211.1"
FT NON_TER 1879
FT /evidence="ECO:0000313|EMBL:FAA00211.1"
SQ SEQUENCE 1879 AA; 211804 MW; 5D0CEDE45170A47B CRC64;
RTLATVKDYS TSFLPQEYRG QSDNSSEDLK QYWMPDKHCH ECYECGDRFT TFRRRHHCRI
CGHIFCSRCC YQFIPREVIA QAVGMLRSCT YCYSLLTSYT KPTVTNTTAK NLQILNEYDG
LIDVRINISH INILYIISFS RHPKGRSRSL VSGRGSPIED GVMSPMQTEA TRVSWKLCEY
KGAAHFTPIF TLHKQFTFAK GSVQLHELWA KISDDKDGLE FRDHRYRLRK FTQSVTGTEL
VDWLITRGIT ETRPQGCAIA QALLDAEWIK SVVDDRVFHD EYCLYQHGSN ATRADSYYKS
TGLVLQSTPI KQSRRPSRQS RVLSHEYGTT LDNEPNWVKE ISNEEEKDSD DGLHFWRLSD
SSPPPLESGL KQPKFVDENV TSISADYIRS KFGPFTALPL SHGVGNHYPT TNSSRLKKLY
FRHSMKFLHQ LFVREKLHTS WSDVVVPLAK QICDTVTPNA EVNMEICHYV HVKKLLDNEP
QDSRLLWGVV FSHNVVHNKM MNRIDNPTIM LLATPLEYQR VQYKLSSLDP IVQQEPEFLK
HLISRIVSRK PDIVMSQCSV SHEGRRLLLD AGITLIINVK QPVMERLSRC TNADVAYSID
QLKTVRLGSC ERWFVVMGES STNAYKTLIY VDGCDPTKGC SVILRDLPHY LRRQDTDHVI
QDRLSRVKRV LLFLIRIMYH GKLEISYLLD QQDVASSFPS SRKKKRCRRS KPTVAPPPIK
GFSSETSESE VHSAEESVVA SGGFVSSVSD DNTITPDFLS ANDRTPDSCP DSPLFNAAHK
GATFTLPNVD KPNIEVSTEL EQSKHGKVLE EKSKVFQDFL KTSLLRLICG TSPLIQPVVP
FLLTNKGPSS PLRKYLPERL FWSDSFSTSG PSTSGPSTFG HATSEHATSG RATSGRATSK
HATSGHATSG HATSGHATSE HATSGHATSE HATSGHATSG HKEEMTWKRN KHIFLTSSLS
KPASSTQMKD LLAKDLTEPT LPPLDCLEPH NHQHIFVLFS SYSLQSPNAP YPCVIPWAVD
IDYYHGNDIT IGGFLERYCF RPSYHCPSPT CKRPMVEHVR SFVHGNTAMN IVLKELSKPI
PVPHILSWCW DPTTKTSTDI RPLSEDGWSM SFAKFLELRL QTHPTVKQDG EVPAFGAFQY
FLFKDIVAAF KCYHVQVHDV ALPSSKMAFN ESTTWLVSAM DSIQDMILDA KSSNPYDLLD
VGDVGFDVGT LQQTRGNHFD ELLSMYQDER CHLRDTADNI HLTLLSIKKS VIVMRPCEKE
NLSSSLLKLA CLVDKLVLTW NNRISKVFQQ DKNSRRGSKS VPSYPNPPLP LDAVLTSENL
KPKRSPKSPL TSSQSVPRGV ESVPRGVESV PRGVESAPKS VERQSSVKRF SKTASSSKCV
LSMRSILTHL RTTTPINMVE PPFPPDEHYL LPDTLNLGHV VRDTEPSSII AYSLATSLYQ
KSSDARFSDA RFSDARFSDA RSSDARSSDA RSSDAVSSVA RCSVARSSDA RSSDARFSDA
KSSDARSSDA RSCYAKSSVA SSSDAKSKQS KRSFDVWQSR SRAVFTQPIH SNISPTQAPT
QPPHNPPEHL EIQFSDSTTK FYCKIYFASK FKDLREKFLD IPESTYITSL SRCVRWDARG
GKSGLSFHKT LDDRLVLKQM SKFELQSFLD VAPSYLDHVS DAIRENTPTA LSKILGVYRV
SFRNMTTNRS FKQDLLIMEN LFYKRNIQQV FDLKGSVRNR HVKTGNDPGV STSGGTTATN
NPMGGDNSFT NQNDLVLLDE NLLSIMKDHP LYVHQHTKVI IKKALHHDSS FLARHLIIDY
SLLVGIDDEK KEIVVGIIDY MRTFTWDKKL EMVVKSYGMI GRQGTRSMPT VVSPELYKTR
FCDAMERYFQ VVPDRWYGL
//
