ID A0A091K1D4_COLST Unreviewed; 826 AA.
AC A0A091K1D4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Phosphatidylinositol 3-kinase catalytic subunit type 3 {ECO:0000256|ARBA:ARBA00019787};
DE EC=2.7.1.137 {ECO:0000256|ARBA:ARBA00012073};
DE AltName: Full=Phosphoinositide-3-kinase class 3 {ECO:0000256|ARBA:ARBA00029930};
DE Flags: Fragment;
GN ORFNames=N325_03284 {ECO:0000313|EMBL:KFP30013.1};
OS Colius striatus (Speckled mousebird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coliiformes; Coliidae; Colius.
OX NCBI_TaxID=57412 {ECO:0000313|EMBL:KFP30013.1, ECO:0000313|Proteomes:UP000053615};
RN [1] {ECO:0000313|EMBL:KFP30013.1, ECO:0000313|Proteomes:UP000053615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N325 {ECO:0000313|EMBL:KFP30013.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KK538062; KFP30013.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091K1D4; -.
DR Proteomes; UP000053615; Unassembled WGS sequence.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd08397; C2_PI3K_class_III; 1.
DR CDD; cd00870; PI3Ka_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; 1.
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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFP30013.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053615};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 12..163
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 259..495
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 580..826
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 127..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP30013.1"
FT NON_TER 826
FT /evidence="ECO:0000313|EMBL:KFP30013.1"
SQ SEQUENCE 826 AA; 94338 MW; ACC0C56CAB0BE6D6 CRC64;
GSLEGKREQK SYKALLEDPM LKFSGLYQET CSDLYVTCQV FAEGKPLALP VRTSYKAFST
RWNWNEWLKL PVKYPDLPRN AQVALTIWDV YGPGKAVPVG GTTVSLFGKY GMFRQGMHDL
KVWPNVEADG SEPTKTPGRT SSTVSEDQMS RLAKLTKSHR QGHMVKVDWL DRLTFREIEM
INEREKRSSN FMYLMIEFRC VKCDDKEYGI VYYEKDDESS PILTSSEIVK IPDPQMSMEN
LVESKHHKLA RSLRSGPSDH DLKPNAATRD QLNIIVSYPP TKQLTYEEQD LVWKFRYYLT
NQEKALTKFL KCVNWDLPQE AKQALELLGK WKPMDVEDSL ELLSSHFTNP TVRRYAVARL
QQADDEDLLM YLLQLVQALK YENFDDIKNG LEPSKRDSQG SMSESMTTSG TNGAEIDSSQ
IMSPSPPVSS PPLTSKTKDL SDNENLDQDL CTFLISRACK NSTLANYLYW YVIVECEDQD
TQQRDPKTHE MYLNVMRRFS QALLKGDKSV RVMRSLLAAQ QTFVDRLVHV MKAVQRESGN
RKKKNERLQA LLADNEKMNL ADMELIPLPL EPQVKIKGII PEKATLFKSA LMPAQLFFKT
EDGGKYPVIF KHGDDLRQDQ LILQIISLMD KLLRKENLDL KLTPYKVLAT STKHGFMQFI
QSVPVAEVLA TEESIQNFFR KHAPSETGPH GISAEVMDTY VKSCAGYCVI TYILGVGDRH
LDNLLLTKTG KLFHIDFGYI LGRDPKPLPP PMKLNKEMVE GMGGTQSEQY QEFRKQCYTA
FLHLRRYSNL ILNLFSLMVD ANIPDIALEP DKTVKKVTGK LSLCFS
//
