ID A0A091NTC8_APAVI Unreviewed; 2092 AA.
AC A0A091NTC8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=N311_12152 {ECO:0000313|EMBL:KFP92392.1};
OS Apaloderma vittatum (Bar-tailed trogon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Trogoniformes; Trogonidae; Apaloderma.
OX NCBI_TaxID=57397 {ECO:0000313|EMBL:KFP92392.1, ECO:0000313|Proteomes:UP000054244};
RN [1] {ECO:0000313|EMBL:KFP92392.1, ECO:0000313|Proteomes:UP000054244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N311 {ECO:0000313|EMBL:KFP92392.1};
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; KL393317; KFP92392.1; -; Genomic_DNA.
DR Proteomes; UP000054244; 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:UP000054244};
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 160..220
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1752..2078
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1516..1611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1688..1759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1775..1796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1525..1545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1553..1611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1688..1711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP92392.1"
FT NON_TER 2092
FT /evidence="ECO:0000313|EMBL:KFP92392.1"
SQ SEQUENCE 2092 AA; 236805 MW; 90F41B1AE0EF1553 CRC64;
EMAADDKRSP TLDSTSDLPH SPSSPSHLTH FKPLTPDQDE PPFKSAYSSF VNLFRFSKER
AEAGQSDPQA LSGGWSSPQH PTRAQSLRSP VSYKKQLTGE LQRRSSATLD NRRKVEPPLG
GHDPRTAVQL RSLSTVLKRL KEIMEGKSQD SDLKQYWMPD SQCKECYDCS EKFTTFRRRH
HCRLCGQIFC SRCCNQEIPG KFMGYTGDLR ACTYCRKIAL SYAHSTDSNS IGEDLNALSD
SAYSVSVLDP GEPRTPVGSR KASRNIFLEE DLTWQSLIHP DSSATTLSAR LGSVQEDAGK
SPARNRSASI TNLSLDRSGS PMVPAYETSV SPQASRTHMK AEASEDERKI LLVPFRFLYF
LFCEACLCHK LCVFRTRLGY LYSYTSRVQA IAIGQALVDG RWLECVSHHD QLFRDEYALY
RPLQSTEFSE TPSPDSDSVN SVEGHSEPSW FKDIKFDDSD TEQIAEEGED NLANSASPSK
RTSVSSFQST MDSDSAASIN LNVELDNVNF HIKKHSKYPH VPPHPADQKE YLNPENGGQQ
MFSISDAFIK ESLFNRRVEE KSKELFFTPL GWHHSNLDLL REENGEKQAM ERLLSANHNH
MMALLQQLLY NESLSLSWRD IIVPVVCQVV QTVRPDVKNR DDDMDIRQFV HIKKIPGGKK
FDSMVVNGFV CTKNVAHKKM NSCLKNPKIL LLKCSIEYLY REETKFTCID PIVLQEREFL
KNYVQRIVDV RPNLVLVEKT VSRIAQDMLL EHGITLVINV KPQVLDRVSR MTQGDLVMSM
DQLLTKPRLG TCHKFYMQVF QLPNDQTKTL MFFEGCPQHL GCTIKLCGAA EYELTRVKEI
LIFMVCVAYH SQLEISFLMD EFAMPPTLTK NTSFHSLIEE PGDENEQQNF FNGEDFSTAV
RDIELSSEKL PAISESVSSD EVTLLEQRGL FERSDQENSQ LETASSKQQE QHKVESLFPV
FNSVPPAVPE TSLLPIHGMN QHLPTLDSQA LEPLQQADDL QESKSQMRVF RDPLQDDTGL
YVTEEVTSSE DRLKTYSAAF KQELKDVILC ISPVMMFREP FLLTEKGMRC PAREYFPEQV
YWSPLLNKEY KELESRRKRQ LLRDLSGLQG MNGSIQAKTI QILPSHELIN TRIAEHVGDS
QSLARMLADY RARGGRILQK STDPFAQSKD VSSVSAGKTG CRLEEDEKGL AQSESSWSHK
VDCLSPVNHQ KLCVLFSSSS AQSSNAPSAC VSPWIVTMEF YGKNDLTLGI FLERYCFRPS
YQCPSMFCET PMVHHIRRFV HGQGCVQIVL KELDSPVPGY QHTILTYSWC RLCKQVTPVV
PLSNDSWSMS FAKYLELRFY GHQYTRRANV EPCGHSIHHD YHQYFSYNQM VASFSYSPIR
LLEVCVPLPK IYIKRQAPSK VTVLQDLKDF SQKVSQVYLA VDDRLASLKT DTFSKTREEK
MEDLFAQKEM EEGEFRNWTD KIQARLLSSS LDTPQQLQSV FESLIAKKQG LCEMLQAWNS
RFILCEKEKA KVIRKGRAMN TRRTDNERVG SSYSLDASPR NASPGLQNGE KEDRFLTTLS
SQSSTGSTHL QLPTPPEVVS EHTTGASTLS EQDTTSSSED VFDGHSLGST DSQVKEKSTM
KAILANFLPG NNYNPIPFPF DPDKHYLMYE HERVPIAVCE KEPSSIIAFA LSCKEYRNAL
DELSKASMKN TSEEGLQLSS MSDSKPKNSS PVRLPEATMG PSSRSAEAEQ PKKPSSVLSF
FRGTGGKSPD LSSQKRETLR GADSAYYQVG QMGKEGAENQ GAESQDDIDG GDGQKKQLVN
PHVELQFSDA NAKFYCRIYY AGEFHKMREV ILGSSEEDFI RSLSHSMPWQ ARGGKSGAAF
YVTEDDRFIL KQMPRLEVQS FLDFAPHYFT YIINAVQHKK PTALAKILGV YRIGYKNSQN
NTEKKLDLLV MENLFYGRKM AQVFDLKGSL RNRNVKTDTG KESCDVVLLD ENLLKMVRDN
PLYIRSHCKA VLRASIHSDS QFLSSHLIID YSLLVGRDDT NNELVVGIID YIRTFTWDKK
LEMVVKSTGI LGGQGKMPTV VSPELYRTRF CEAMDKYFLM VPDHWTGLGL NC
//
