ID A0A2Y9RAC7_TRIMA Unreviewed; 2003 AA.
AC A0A2Y9RAC7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=LOC101359894 {ECO:0000313|RefSeq:XP_023588824.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023588824.1};
RN [1] {ECO:0000313|RefSeq:XP_023588824.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_023588824.1; XM_023733056.1.
DR Proteomes; UP000248480; Unplaced.
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; cd03334; Fab1_TCP; 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; IPR043548; PIKfyve.
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; IPR027410; TCP-1-like_intermed_sf.
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; PTHR46715; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE; 1.
DR PANTHER; PTHR46715:SF1; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE; 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; SSF54849; GroEL-intermediate 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 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480};
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 171..231
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 380..455
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT DOMAIN 1663..1989
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1417..1499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1604..1707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1442..1456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1464..1484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1623..1639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1681..1698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2003 AA; 225392 MW; 014CF6EBC60DEC24 CRC64;
MATDDKTSPT LDSANDLPQS PTSPSHLTHF KPLTPDQDEP PFKSAYSSFV NLFRFNKERA
EGGQGEQQSL SGSWTSPQLP TRTQSVRSPT PYKKPLNEEL HRRSSTVLAE NSLQHPQEST
DARRKAEPNF GGHDPRTAVQ LRSLSTVLKR LKEIMEGKSQ DSDLKQYWMP DSQCKECYDC
SEKFTTFRRR HHCRLCGQIF CSRCCNQEIP GKFMGYTGDL RACTYCRKIA LSYAHSTDSN
SIGEDLNALS DSACSVSVLD PSEPRTPVGS RKASRNIFLE DDLAWQSLIH PDSSNTALSA
GLVSVQEDAG KSPARNRSAS ITNLSLDRSG SPMVPSYETS VSPQANRTYI RTETTEDERK
ILLVPDSVQL KDLWKKICHH SSGMEFQDHR YWLRTHPNCI VGKELVNWLI RNGHIATRAQ
AIAIGQAMVD GRWLDCVSHH DQLFRDEYAL YRPLQSTEFS ETPSPDSDSV NSVEGHSEPS
WFKDIKFDDS DTEQIAEEGD DNLANSASPS KRTSVSSFQS TVDSDSAASI SLNVELDNVN
FHIKKPSKYP HVPPHPADQK EYLISDNGGQ QLSISDAFIK ESLFNRRVEE KSKELPFTPL
GWHHNNLELL REENGEKQAM ERLLSANHNH LMALLQQLLH NESLSPSWRD IIVPLVCQVV
QTVRPDVKNR DDDMDIRQFV HVKKIPGGKK FDSVVVSGFV CTKNIAHKKM NSCIKNPKIL
LLKCSIEYLY REETKFTCID PIVLQEREFL KNYVQRIVDV RPTLVLVEKT VSRIAQDMLL
EHGITLVINV KSQVLDRISR MTQGDLVMSM DQLLTKPRLG TCHKFYMQMF QLSNEQTKTL
MFFEGCPQHL GCTVKLRGGS DYELARVKEI LIFMICVAYH SQLEISFLMD EFAMPPTLTQ
NSSFHSLIEG CGEEGAAQEQ FSGSTLPRDP DFPPDRPIMI SEALPSDDGS SLESRIVFEK
GDQENKSVLQ DVVSLKHQEC AATACVSGIP CALFPSLPES LLPLHMDDQQ DVIGSEQPET
LQQTDELHDP KSQMRAFRDP LQDDTGLYVA MEVTSSEDKR KTYSLAFKQE LKDVILCMSP
VITFREPFLL TEKGMKCSTR DYFAEQVYWS PLLNKEFKEM ESRRKKQLLR DLTGLQGMNG
SIQAKSIQVL PSHELVSTRI AEHLGDSQSL GRMLADFRAR GGRIQQKNLD PFAHSKDASG
TSGSKSGSRA ESDEEKGLVP SDALWSTKVD CLNPGNHQRL CVLFSSSSAQ SSNAPSACVS
PWIVTMEFYG KNDLTLGIFL ERYCFSYSPI RLLEVCVPLP KIVIKRQAPL KVSLLQDLKD
FFQKVSQVYL AVDERLASLK TDTFSKTREE KMEDIFAQKE MEEGEFKNWI EKMQARLMSS
SVDTPQQLQS IFESLIAKKQ SLCEVLQAWN NRLQDLFQQE KGRKRPSVPP SPGRLRQGEE
SKISTMDATP RNVSPGLQNG EKEDRFLTTL SSQSSTSSAH LQLPTPPEVM SEQMVGGPPE
LDTVSSSEDV FDGHLLGSTD SQVKEKSTMK AIFANLLPGN SYNPIPFPFD PDKHYLMYEH
ERVPIAVCEK EPSSIIAFAL SCKEYRNALE ELSKATLWNS AEEGLQTNST LDSRPKSSSP
VRLPDISGGQ TNRTAEAEPQ PTKKASGVLS FFRGTAGKSP DLSSQKRETL RGADSAYYQV
GQTGKEGTEN QGNEPQDEAD GGDTQKKQLT NPHVELQFSD ANAKFYCRLY YAGEFHKMRE
VILGSGEEDF IRSLSHSSPW QARGGKSGAA FYATEDDRFI LKQMPRLEVQ SFLDFAPHYF
NYITNAVQQK RPTALAKILG VYRIGYKNSQ NNTEKKLDLL VMENLFYGRK MAQVFDLKGS
LRNRNVKTDT GKESCDVVLL DENLLKMVRD NPLYIRSHSK AVLRASIHSD SHFLSSHLII
DYSLLVGRDD TNNELVVGII DYIRTFTWDK KLEMVVKSTG ILGGQGKMPT VVSPELYRTR
FCEAMDKYFL MVPDHWTGLG LNC
//
