ID A0A1I8M849_MUSDO Unreviewed; 959 AA.
AC A0A1I8M849;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 46.
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|ARBA:ARBA00012073, ECO:0000256|PIRNR:PIRNR000587};
GN Name=101893911 {ECO:0000313|EnsemblMetazoa:MDOA002225-PA};
GN Synonyms=LOC101893911 {ECO:0000313|RefSeq:XP_005179296.1};
OS Musca domestica (House fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Musca.
OX NCBI_TaxID=7370 {ECO:0000313|EnsemblMetazoa:MDOA002225-PA};
RN [1] {ECO:0000313|EnsemblMetazoa:MDOA002225-PA}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|EnsemblMetazoa:MDOA002225-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_005179296.1}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|RefSeq:XP_005179296.1};
RG RefSeq;
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 -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|PIRNR:PIRNR000587, ECO:0000256|PROSITE-ProRule:PRU00880}.
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DR RefSeq; XP_005179296.1; XM_005179239.3.
DR STRING; 7370.A0A1I8M849; -.
DR EnsemblMetazoa; MDOA002225-RA; MDOA002225-PA; MDOA002225.
DR GeneID; 101893911; -.
DR KEGG; mde:101893911; -.
DR VEuPathDB; VectorBase:MDOA002225; -.
DR eggNOG; KOG0906; Eukaryota.
DR OrthoDB; 10350at2759; -.
DR Proteomes; UP000095301; Unassembled WGS sequence.
DR Proteomes; UP000694905; Unplaced.
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:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd08397; C2_PI3K_class_III; 1.
DR CDD; cd00896; PI3Kc_III; 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:SF7; PHOSPHATIDYLINOSITOL 3-KINASE CATALYTIC SUBUNIT TYPE 3; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL 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; 2.
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:UP000694905};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000587}.
FT DOMAIN 37..191
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 284..589
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 676..943
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 959 AA; 109422 MW; 1E3D8B67CBE910B9 CRC64;
MDQPNDYFRY IYSSSLNELV QIKIGTLEGK KKRQPDYEKL LEDPILRFSG LYSEECPSFQ
VRLQIFNQGR PYCLPVTTSY KAFTKRWSWN EWVTLPLQFS DLPRTAMLVL TILDCAGAGQ
TSVIGGTSIS LFGKNGMFRQ GMYDLRVWLG VEGDGGNPSK TPGKGKDSSK SQMQRLGKLA
KKHRNGQVQK VDWLDRLTFR EIELINEREK RMSDYMYLMI EFPTVVVDDC FTYSIVYFEP
EGDKNYKFLN KPKLVTVPDS EILQENLVER KHHRLARSVR SRISDRDAKP TASIRDQLHT
IVYRYPPTCV LNSEEQDLLW KFRFYLSSHK KALTKFLKCI NWETPGEVEQ ALILLNKWAP
MDVEDALELL SPSFKHPHVR KYAISRLAQA PDEDLLLYLL QLVQALKYEN FSDIIESHKR
LFPDRDIVRS LDDNSTLFDQ SSLCSELSVG GGGGGVGGGS VGGTMGSTSS VLIATQRSGI
QRPGVQIERS TTMPMAISVN SSLADDNETS IGSLPSDVSN TLMSDNNTNV QYSTMTTNTA
TNLATFLIQR ASRNPTLANY LYWYLSIEVE DCESIRKQDE SVHEMYDMVL KMFLKVLENG
NFYLRGIFYN LRKQQRFIDE LVRLVKIVAK EPGNRNKKTE KFQKLLSEAD TFKINFTNFE
QIPFPLDPEI YITKIVPSKT SLFKSALMPA KLTFVTSIAQ HEYVAIFKHG DDLRQDQLIL
QMITLMDKLL RRENLDLKLT PYKVLATSSK HGFLQYIDSY TVADVLAREG SILNFFRKHN
PCDSAPYGIM PETMDTYIKS CAGYCVITYL LGVGDRHLDN LLLTTNGKLF HIDFGYILGR
DPKPMPPPMK LSKEMVEAMG GVTSEHHHEF RKQCYTAYLH LRRHANVVLN LFSLMVDASV
PDIALEPDKA VKKVEDNLQL GLTDEEAVQH LQGLLDISIT AVMPALVEQI HKLAQYWRK
//
