ID K7FJ02_PELSI Unreviewed; 787 AA.
AC K7FJ02;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Phosphatidylinositol 3-kinase catalytic subunit type 3 {ECO:0000256|ARBA:ARBA00019787, ECO:0000256|PIRNR:PIRNR000587};
DE EC=2.7.1.137 {ECO:0000256|PIRNR:PIRNR000587};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000008012.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000008012.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216;
CC EC=2.7.1.137; Evidence={ECO:0000256|PIRNR:PIRNR000587};
CC -!- SUBCELLULAR LOCATION: Midbody {ECO:0000256|ARBA:ARBA00004214}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR EMBL; AGCU01029977; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K7FJ02; -.
DR STRING; 13735.ENSPSIP00000008012; -.
DR Ensembl; ENSPSIT00000008054.1; ENSPSIP00000008012.1; ENSPSIG00000007352.1.
DR eggNOG; KOG0904; Eukaryota.
DR GeneTree; ENSGT00940000164913; -.
DR HOGENOM; CLU_002191_1_2_1; -.
DR OMA; HFIRTCA; -.
DR TreeFam; TF102031; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd08398; C2_PI3K_class_I_alpha; 1.
DR CDD; cd00872; PI3Ka_I; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR002420; PI3K-type_C2_dom.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR008290; PI3K_Vps34.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR PANTHER; PTHR10048:SF95; PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE 3-KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR PIRSF; PIRSF000587; PI3K_Vps34; 3.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51547; C2_PI3K; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000587};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000587};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000007267};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000587}.
FT DOMAIN 44..195
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 231..408
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 479..765
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 787 AA; 90860 MW; 39F2D4478247C763 CRC64;
MLMSKESLYS QLPANVFVLP SYARRPGPST HATGDLPAKS LWSVPSLLRI CIVCATYVNV
NIRDIDKIYV RTGIYHGGEP LCDNVNTQRV LCSNPRWNEW LSYDIYLADL PRAARLCLSI
CCVKGRKGTK EEHCPLAWGN INLFDYKDTL VAGKMALNLW PVPHGLEDLL NPIGVGGSNP
NKETPCLELE FTCFSHAVKF ADAVQIEEHA NRSMLRELGL NCCLVGLSNR LARDSSLLDS
ELEQLHSICH RDPLSEITEQ EKDFLWRHRH YCVNIPDTLP KLLLSVKWNS RDEVAQMYCL
LQEWPLIKPE LSMELLDCNF PDPRVREFAL KCLVKGLTDD KLSQYLIQLV QVLKYEQYLD
NPLARFLLRK ALTNQRIGHF YFWHLKSEMH SRTVSQRFGL MLEAFCRGCG MYLKHLNRQV
EAMEKLVNLT DTLRQEKKDE TQKMQMKFLV EQMRRPDYMD ALQGFVCPLN PVHQLGNIRL
DECRIMSSAK RPLWLNWENP DIMSELLFTN HEIIFKNGDD LRQDMLTLQI IRIMENMWQN
QGLDLRMLPY GCLSIGDCVG LIEVVRSSHT IMQIQCKGGL KGALQFNSHA LHHWLREKNK
GDSYDAAIDL FTRSCAGYCV ATFVLGIGDR HNSNIMVKDD GQLFHIDFGH FLDHKKKKFG
YKRERVPFVL TQDFLLVISK GVQECTKTKE FERFQEMCYA AYLAIRQHAN LLITLFSLML
SSGLPELQSF DDIAYLRKTL ALDTSEQQAL EYFTKQMNEA HHGGWTTKMD WIFHTIRHMP
LTEAGHD
//
