GenomeNet

Database: UniProt
Entry: G7JS40_MEDTR
LinkDB: G7JS40_MEDTR
Original site: G7JS40_MEDTR 
ID   G7JS40_MEDTR            Unreviewed;      1801 AA.
AC   G7JS40; A0A0C3X7B6;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 2.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=1-phosphatidylinositol-3-phosphate 5-kinase {ECO:0000256|ARBA:ARBA00012009};
DE            EC=2.7.1.150 {ECO:0000256|ARBA:ARBA00012009};
GN   OrderedLocusNames=MTR_4g124590 {ECO:0000313|EMBL:AES92138.2};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880 {ECO:0000313|EMBL:AES92138.2, ECO:0000313|Proteomes:UP000002051};
RN   [1] {ECO:0000313|EMBL:AES92138.2, ECO:0000313|Proteomes:UP000002051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A17 {ECO:0000313|EMBL:AES92138.2}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:AES92138,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=22089132; DOI=10.1038/nature10625;
RA   Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA   Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA   Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA   Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA   Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA   Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA   Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA   Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA   Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA   Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA   Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA   Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA   Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA   Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA   Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA   Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA   Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA   Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA   Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA   Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA   Town C.D., Roe B.A.;
RT   "The Medicago genome provides insight into the evolution of rhizobial
RT   symbioses.";
RL   Nature 480:520-524(2011).
RN   [2] {ECO:0000313|EMBL:AES92138.2, ECO:0000313|Proteomes:UP000002051}
RP   GENOME REANNOTATION.
RC   STRAIN=A17 {ECO:0000313|EMBL:AES92138.2}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:AES92138,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA   Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA   Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA   Schwartz D.C., Town C.D.;
RT   "An improved genome release (version Mt4.0) for the model legume Medicago
RT   truncatula.";
RL   BMC Genomics 15:312-312(2014).
RN   [3] {ECO:0000313|EnsemblPlants:AES92138}
RP   IDENTIFICATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES92138};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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DR   EMBL; CM001220; AES92138.2; -; Genomic_DNA.
DR   RefSeq; XP_003609941.2; XM_003609893.2.
DR   STRING; 3880.G7JS40; -.
DR   PaxDb; 3880-AES92138; -.
DR   EnsemblPlants; AES92138; AES92138; MTR_4g124590.
DR   Gramene; AES92138; AES92138; MTR_4g124590.
DR   eggNOG; KOG0230; Eukaryota.
DR   HOGENOM; CLU_000480_4_0_1; -.
DR   Proteomes; UP000002051; Chromosome 4.
DR   GO; GO:0010008; C:endosome membrane; IBA:GO_Central.
DR   GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0010256; P:endomembrane system organization; IEA:EnsemblPlants.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009555; P:pollen development; IEA:EnsemblPlants.
DR   GO; GO:0007033; P:vacuole organization; IEA:EnsemblPlants.
DR   CDD; cd03334; Fab1_TCP; 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:SF21; 1-PHOSPHATIDYLINOSITOL-3-PHOSPHATE 5-KINASE; 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:UP000002051};
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..102
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          1451..1775
FT                   /note="PIPK"
FT                   /evidence="ECO:0000259|PROSITE:PS51455"
FT   REGION          677..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1192..1226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1245..1271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..691
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1192..1217
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1801 AA;  200909 MW;  B08D85DDFDFB96D8 CRC64;
     MGTPDKKISD LVDVVRSWIP RRVEPPNVSR DFWMPDQSCP LCYECDSQFT VFNRRHHCRI
     CGRVFCAKCT ANFVPSSPRE PNIGREDWER IRVCNYCFKQ WEKGVAAVDN VTPSATPCLS
     PSPSSTSLVS SKSSCTCHSS SSTAGSVPYS TGSYQCVPSS PHQSSQMNLI TDEQENLNSG
     MSTNPSEAVE NLNSNQYGYC FNRSDDEDDD YGVYHSDTES RHYSRINDYD DLVNIQGIDR
     VYGPHIMHSD GDNIQERSSS CLAPPQNLEL DGTDGVQALG KEADEHDHTD ECETSPYQEE
     ANNMEPVDFE NNGLLWLPPE PEDEEDDREA ALFDDDEDEG STGEWGYLRS SASFGSGEFR
     SRDKSGENNR KAMKNVVEGH FRALVAQLLQ VESLTVDDDG KESWLDIITT LSWEAATLLK
     PDTSRGGGMD PGGYVKVKCI ACGHRNESMV VKGIVCKKNV AHRRMTSKID KPRFIILGGA
     LEYQRVSNQL SSVDTLLQQE MDHLKMAVTK IAAHHPNVLL VEKSVSRYAQ EYLLAKDISL
     VLNIKRPLLE RIARCTGAQI VPSVDHLSSQ KLGYCEAFHV DKFFEEHGSA GQGGKKLTKT
     LMFFEDCPKP LGCTILLKGS NGDELKKPII WRWKHLFLAD EGASPLEFPL KSPITVALPD
     KPSSIVKSIS TIPGFSSVTG RGHQGAQTNK EGPKCNDGYK THRTLPSCSG SIERSLAGES
     IHMHEISGDV SQLAQDMSSS HCNSFLTNTA FEKDGKERPK ESLHCRQDEG TKTMIHADII
     SDFFGTLEPS GRDGNNHIKA VSLASNQGPD PESPIVKHDD NNNNFDNDMI HSKEDFPPST
     SDHQSILVFL STRCVWKGTV CERSHLVRIK YYGSSDKPLG RFLKDQLFDE KYTCRSCEMP
     PEAHVHCYTH RQGSLTISVK KLSEFPLPGE GEGKIWMWHR CLKCPRVNGF PPATRRVVMS
     DAAWGLSFGK FLELSFSNHA AASRVANCGH SLHRDCLRFY GFGKMVACFR YASIDLNSVY
     LPPSKLEFNY DSQDWLQKEA HEVHNKAEIL FSEVCSALNQ ISEKFSGSVL QEGGKAVADF
     RHLIVELKEI LQKEKEESEV GGLRCCDSSF CIKRAIAGGL MVDVLELCKL RRHILILSFV
     WDQRLIYASN QGKITFSEDS KNSYQKVKSI GSKEKAVETD VVTRSARSHS SSDSFLLETK
     PDGNLDLENS SHLSQSGEMI KGEDKSKDIG QSKFDLSLSH DANINDKSNS SEFGGAIRRR
     RTSSEGGSRN VANLSDTLDA AWTGENHPEN ILYEENGCPA PDVAAVTVHS PTVIATAKSN
     LDNYTAGIGG TETGNTHDSK LHSKGLDTRW SGMPFANSYS FDKTSAFNTQ KLVDYNFVHI
     LSFRELDRQT GARLLLPVGI NDTIVPVYDD EPTSVIAHVL VSKDYHIQMS DSDRPKDSLE
     SSVSLPLFDS TSLLSLNSLD ETITNSYRSF GSSEESMTLS TSGSRMVGDS LLYSKDFHAR
     VSFNDDSSLG KVKYNVTCYY AKRFEALRRT CCPSELDFVR SLSRCKKWGA QGGKSNVFFA
     KTLDDRFIVK QVTKTELESF IKFAPAYFKY LSESISTGSP TCLAKILGIY QVTSKHLKGG
     KETKMDVLVM ENLLYRRNIR RLYDLKGSSR SRYNPDTSGS NKVLLDQNLI EAMPTSPIFV
     GNKAKRLLER AVWNDTAFLA SIYVMDYSLL VGVDEEKHEL VLGIIDFMRQ YTWDKHLETW
     VKTSGILGGP KNTSPTVISP QQYKKRFRKA MSLYFLMVPD QWSPPSLQTS ESQNDLCDEN
     S
//
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