ID A0A093I919_STRCA Unreviewed; 2116 AA.
AC A0A093I919;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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 ORFNames=N308_00984 {ECO:0000313|EMBL:KFV88360.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV88360.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV88360.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV88360.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KL206994; KFV88360.1; -; Genomic_DNA.
DR STRING; 441894.ENSSCUP00000017810; -.
DR Proteomes; UP000053584; 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; 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; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR043548; PIKfyve.
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; 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; 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 SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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:UP000053584};
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 169..229
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1776..2102
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 60..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1541..1639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1714..1783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1799..1820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1574..1639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1714..1731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV88360.1"
FT NON_TER 2116
FT /evidence="ECO:0000313|EMBL:KFV88360.1"
SQ SEQUENCE 2116 AA; 239014 MW; EB9D6B475E9516AE CRC64;
EMAADDKQPP TLEATNDLPH SPGSPSHLTH FKPLTPDQDE PPFKSAYSSF VNLFRFSKDD
GRLSSPVERG ETGQGDPQAL SSGWSSPQHP ARAQSLRSPV PYKKQLTGEL QRRSSATLDN
RRKVEPPLGG HDPRTAVQLR SLSTVLKRLK EIMEGKSQDS DLKQYWMPDS QCKECYDCSE
KFTTFRRRHH CRLCGQIFCS RCCNQEIPGK FMGYTGDLRA CTYCRKIALS YAHSTDSNSI
GEDLNALSDS ACSVSVLDPG EPRTPVGSRK ASRNIFLEED LTWQSLIHPD SSTTTLSTRL
GSVQEDAGKS PARNRSASIT NLSLDRSGSP MVPAYETSVS PQASRTHMKA ETSEDERKIL
LVPFRLLFVL LLKDVGGVQT VSVNHLLDTS VEFRMLATCK NISYISRVQA IAIGQALVDG
RWLDCVSHHD QLFRDEYALY RPLQSTEFSE TPSPDSDSVN SVEGHSEPSW FKDIKFDDSD
TEQIADEGED NLANSASPSK RTSVSSFQST MDSDSAASIS LNVELDNVNF HIKKHSKYPH
VPPHPADQKE YLNPDNGGQQ MFSISDAFIK ESLFNRRVEE KSKELFFTPL GWHHSNLDLL
REENGEKQAM ERLLSANHNH MMALLQQLLY NESLSLSWRD IIVPVVCQVV QTVRPDVKNR
DDDMDIRQFV HIKKIPGGKK FDSMVVNGFV CTKNVAHKKM NSYIKNPKIL LLKCSIEYLY
REETKFTCID PIVLQEREFL KNYVQRIVDV RPNLVLVEKT VSRIAQDMLL EHGITLVINV
KPQVLDRVSR MTQGDLVMSM DQLLTKPRLG TCHKFYMQVF QLPNDQTKTL MFFEGCPQHL
GCTIKLCGAA EYELARVKEI LIFMVCVAYH SQLEISFLMD EFAMPPTLTK NASFHSLIEE
SGDENEHQNL FNGEDFSTAV RDIELSSDKL PVISESVSSD EVSLVEQRNL FERGDQESSQ
QETVCSKQQE HHKMESTFPV FNSVPSAIPE TSLLPLHGMD QHLVALDSQP LEPPQQADDL
QESKSQMRVF RDPLQDDTGL YITEEVASSE DRLKAYSAAF KQELKDVILC ISPVMMFREP
FLLTEKGMRC PAREYFPEQV YWSPLLNKEY KELESRRKKQ LLRDLSGLQG MNGSIQAKAV
QILPSHELVN TRIAEHLGDS QSLARMLADY RARGGRILQK NADPFAQSKD VSGVPTGKTG
CRTEEDEKGL AQSESSWSNK VDCLSPVNHQ RLCVLFSSSS AQSSNAPSAC VSPWIVTMEF
YGKNDLTLGV FLERYCFRPS YQCPSMFCET PMVHHIRRFV HGQGCVQIVL KELDSPVPGY
QHTILTYSWC RLCKQVTPVV PLSNDSWSMS FAKYLELRFY GHQYTRRANA EPCGHSIHHD
YHQYFSYNQM VASFSYSPIR LLEVCVPLPK IYIKRQAPLK VTILQDLKDF SQKVSQVYLA
VDDRLASLKT DTFSKSREEK MEDLFAQKEM EEGEFRNWTE KIQARLLSSS LDTPQQLQSV
FESLIAKKQG LCEMLQAWNN RVRENGTVTV TYQVYRRSAL KRKRPKTHQE IRVVSMDASP
RNVSPALQNG EKEDRFLTTL SSQSSTGSTH LQLPTPPEVV SEQLTSGSSF ANALSEQDAT
SSSEEVFDGH SLGSTDSQVK EKSTMKAILA NLLPGNSYNP IPFPFDPDKH YLMYEHERVP
IAVCEKEPSS IIAFALSCKE YRNALDELSK ASLKNSSEEG FQPNSMPDKP KSSSPVRLPE
ANMGPSNRTA EPEQPKKPSG VLSFFRGTGG KSPDLSSQKK ETLRGADSAY YQVGQMGKEG
AENQGAEPQD ETDGGDGQKK QLVNPHVELQ FSDANAKFYC RIYYAGEFHK MREVILGSSE
EDFIRSLSHS MPWQARGGKS GAAFYVTEDD RFILKQMPRL EVQSFLDFAP HYFTYIINAV
QQKKPTALAK ILGVYRIGYK NSQNNTEKKL DLLVMENLFY GRKMAQVFDL KGSLRNRNVK
TDTGKESCDV VLLDENLLKM VRDNPLYIRS HCKAVLRASI HSDSQFLSSH LIIDYSLLVG
RDDTNNELVV GIIDYIRTFT WDKKLEMVVK STGILGGQGK MPTVVSPELY RTRFCEAMDK
YFLMVPDHWT GLGLNC
//
