ID A0A2G4SXA5_RHIZD Unreviewed; 2374 AA.
AC A0A2G4SXA5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=RHIMIDRAFT_127459 {ECO:0000313|EMBL:PHZ13006.1};
OS Rhizopus microsporus ATCC 52813.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=1340429 {ECO:0000313|EMBL:PHZ13006.1, ECO:0000313|Proteomes:UP000242254};
RN [1] {ECO:0000313|EMBL:PHZ13006.1, ECO:0000313|Proteomes:UP000242254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 52813 {ECO:0000313|EMBL:PHZ13006.1,
RC ECO:0000313|Proteomes:UP000242254};
RX PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT "Lipid metabolic changes in an early divergent fungus govern the
RT establishment of a mutualistic symbiosis with endobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
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DR EMBL; KZ303848; PHZ13006.1; -; Genomic_DNA.
DR STRING; 1340429.A0A2G4SXA5; -.
DR OrthoDB; 5481504at2759; -.
DR Proteomes; UP000242254; 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; 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; 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; IPR027410; TCP-1-like_intermed_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; 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; SSF54849; GroEL-intermediate 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:UP000242254};
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 223..283
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 2016..2336
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1600..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1673..1708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1784..1807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1793..1807
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2374 AA; 268301 MW; 7AF477815530B04A CRC64;
MDKENNNSLT SFQFEPKDNR TSEEGVLSKI LDKVKSAVSG QPTSWAHDNA SMHSTHSERR
ISNSTEPSVI SIPHTVSNVI AVTEYPNSSS NSSTTSQRLP KDSVLANFPV SSDSLSKSST
IATTATTVIV GKHGKLPEDM IVEPAHSSST VQFIMPSTSN NNNNRKSLEE NSVDLLPLYT
RKSIDSDTQS VATNFSISNS NSLGKILARL RGQKNDKEFW MPDEQCKECY KCRKPFTLLR
RKHHCRTCGQ IFCGKCASHI VSGKLYKQKG QVRVCNFCYK KQQQQLQEKS ISSTTEPIMH
FKTVSSPLSR QIITDNNSEE TSQLTLLDQA EQYSSEIIPS QKPPLAVPNM QIPTAALKQA
RGAYGNENTT TFALEIPIYG SESYSSSQLE RPHSPFVAMA EQPTSPTLYN TSTIANTSSF
SVTNMPDNHI YTGVKRLLDA GTSFIKPRPR SNTSSSAPLL EDFRSTQLPF RSVPYLDHGG
GTVLAESELS SFPSAVVDPD EQYEDEAAAL YDRPLTPLKT PLYNDKPNSS NSDPLSPAIN
GGISDDESYD HRLRAKRTEE LRGKNVQLIS SKSSYHSYRR PSITGSTTPK LRNSGLHKIN
TVGLPKYDYP PSSAGPLQLE QTWSPNPLLS PYNDDANKFF PQSDSNNRFR FVPRQRRTSG
PPPTVELSLS ARQHARLLLR QFMQDIQFTE SSKEEWEDVI MNILMKVANN VQPDTRAGDD
MDVRHYVKIK KIPGGLPSDS FYVKGVVCTK NVAHKRMVRN MSSPRILILL FSLDYSRVEM
ENQLLSITPV ISQEREHISK LVGRIVALKP SLLLVKSTVS RFALEFLLEA NIPVIHNVKH
SVIEAVARCT EAAIVTSVDK LQHGVSFGRC GSFEIRTFMH EWIPNRRKTY LIFDDCSPEL
GGTIVLRGEK VETLKVIKRL IDFMVFVVNN LKYETSLLRD SFAKNRGASE SEERKRSPLM
RQSSLGIEKL HDLEDEGHNC TELLLQAYQN TILSVSQFVV FKPPYLLLKL KETEERLAMV
IQQKRKKSIS CLSILKDAAS TVSTPAVLSL SASPTRTTFD KQVRSPMEKQ QSISHPASTS
SYDTQEGDEF TSEFEQELIT KSHQIARAWE AYHGETPESI SPLYHQNIVV LYSSVCTVTT
VPCQGPEIRI FGYYRMPSDK TLGQYIMDLC ADAHQPCTSF MCDHPMLQHY RSYAHGNARV
NVMIEQFPCP LPGMSDKLLM WSYCRECNKP TPVLPMSENT WNYSFGKFLE IFLYQEGVHC
RADICPHDMA KNHVRYFGYM DMTVRFQCDP IELLEVSVPP MKLHIKSKIQ RDLKEAELKS
LRTKINRFYQ SIVDRNKAFP FDLVDPRKLE ACKAELQELS LEAQGEKKDT LQLLQNVYAT
SDPVDTLTIN GVRRSLFQIV AHWEAVYADF VRFYLEPERE LKKITTIHLR KMFPTDFSDM
NTDERTKRAT EVTDLPLLGI GLDDNDGDAL IGRILKKKST ATIKPDESTT RQNNDMIMPA
LSSTPSSMPI TDMMEEDRDE DNMALGAQSD NKTSFLRPEV RRRLSLELMR EFNEKLKYEE
VTSAGAANTT NDISSFSQTR PNRYLQLRVS GSLSAAYTPS RIPLYSGKNN SPLSVYQQSS
KQATASTNES KTAYKTTVGP SNFSHVCSIE RFPRFPPHQR HHSIAHDYHI HQRYGKSKAS
SSVDDNDEFE PSPSFLRRSA TSKDKRFRSR LPRKKTYIQV YDQANDLVRE DIDDEFYPGG
QADDTLSISS RQAAHRLKTD LSLPRRKPTS YRQARHQRHL QLGYHAHESG TDADNDDDSD
DEGEEAFDMG KGVDYFTPLA PFTFEVLDEP ETDNKLEVEN TQGKSDDGST ANYVVVKPYF
GLSDGQVDLM SGISGDDETD LDFLPLASDL LMAQQSANDA LAISDLHNIH PELTTTTTNT
STSIRYITAA ANDDNRNSPE KMSFMKTITN FLTDSGIGNL LPLESPLQPT EYLFPDSYVV
VREDEPSTII AYTLSSEDYL DKMHDIQNCH SESGMNDTHL KTYDSINIDR KAPSENYTFE
NGLHNNIPQA AEAIQETLLR ESGSHMRYNF STGSTKFFCK IFFSEQFDAL RRNCGCDESY
IMSLASCIKW DSSGGKSGSA FLKTKDDRLL MKQMSRYELD AFLGFAPAYF QYMSEAFFSE
LPTALAKIFG FYSIGYKNSS TGKSMRMDVL VMENLFYQRN IKKIFDLKGS MRNRHVQSTG
KQDEVLLDEN LVELIYQSPL FIRAHSKEIL RSSLHNDTLF LSNRNVMDYS LLVGIDADRQ
ELVVGIVDFI RTFTWDKKLE SWVKESGILG GGGKEPTIVS PRQYRIRFRE AMERYFLMVP
DFWALTRQNR ALYTVLHHHT TSQQAATSIN DENA
//
