ID A0A087SEJ1_AUXPR Unreviewed; 2276 AA.
AC A0A087SEJ1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Phosphatidylinositol 4-kinase alpha 1 {ECO:0000313|EMBL:KFM24145.1};
GN ORFNames=F751_1410 {ECO:0000313|EMBL:KFM24145.1};
OS Auxenochlorella protothecoides (Green microalga) (Chlorella
OS protothecoides).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Auxenochlorella.
OX NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM24145.1, ECO:0000313|Proteomes:UP000028924};
RN [1] {ECO:0000313|EMBL:KFM24145.1, ECO:0000313|Proteomes:UP000028924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0710 {ECO:0000313|EMBL:KFM24145.1,
RC ECO:0000313|Proteomes:UP000028924};
RX PubMed=25012212; DOI=10.1186/1471-2164-15-582;
RA Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.;
RT "Oil accumulation mechanisms of the oleaginous microalga Chlorella
RT protothecoides revealed through its genome, transcriptomes, and
RT proteomes.";
RL BMC Genomics 15:582-582(2014).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. XPG subfamily.
CC {ECO:0000256|ARBA:ARBA00005283}.
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DR EMBL; KL662105; KFM24145.1; -; Genomic_DNA.
DR RefSeq; XP_011397031.1; XM_011398729.1.
DR STRING; 3075.A0A087SEJ1; -.
DR GeneID; 23612801; -.
DR KEGG; apro:F751_1410; -.
DR eggNOG; KOG0902; Eukaryota.
DR eggNOG; KOG2520; Eukaryota.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000028924; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd09904; H3TH_XPG; 1.
DR CDD; cd05167; PI4Kc_III_alpha; 1.
DR CDD; cd09868; PIN_XPG_RAD2; 2.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 2.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 2.
DR Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR008918; HhH2.
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; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR001044; XPG/Rad2_eukaryotes.
DR InterPro; IPR019974; XPG_CS.
DR InterPro; IPR006085; XPG_DNA_repair_N.
DR PANTHER; PTHR16171:SF7; DNA EXCISION REPAIR PROTEIN ERCC-5; 1.
DR PANTHER; PTHR16171; DNA REPAIR PROTEIN COMPLEMENTING XP-G CELLS-RELATED; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 2.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF00867; XPG_I; 1.
DR Pfam; PF00752; XPG_N; 1.
DR PRINTS; PR00853; XPGRADSUPER.
DR PRINTS; PR00066; XRODRMPGMNTG.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00484; XPGI; 1.
DR SMART; SM00485; XPGN; 1.
DR SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS00842; XPG_2; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFM24145.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000028924};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1639..1816
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1930..2260
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 313..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1931..1951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..379
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2276 AA; 241619 MW; 549097C42F1ABD9C CRC64;
MGVKKLWDLL EPCGRRISIE ALTGKRLAVD ASGWLFQFIK AMRDERGDLI RNAHLVGFFR
RICRLLFHRI KPVFVFDGAT PAIKRMTVIA RRRQREQQDA RLRRTAEKLL LNQLKQHALA
QVASQGGSDV LAQMAGTQKS RGTRPDPFQE VVVQDTDAAA GGRAAGAQPH AVPAQCVPEG
PALGASAPQP GEVEQELEAH LDLDLDQLGG VESGEIDAEV LSQLPPSVQL EVMLKLREAQ
VVANREKFAA AQGAPLAFSQ VQMAQYLKAT AFRRQVNEIK EAVNAAAGLL GASRRIAGEP
GREYVLLRDE EALDGPGVPG AQGASSPPEP SAAPASSAAP PSSGGPLPAQ DPLVLTFGAS
DLDPATDASE EEVGWEDVEE EPSLPGMLAS PGGSTEPVPD VGLREQRDLH WRERAARRQR
FWSLAQGFRQ GRALSDWGKA GDGAQGSPAL SPGRAEDGTR DEEEQALQAA IEASLQESRE
AWEVAGNSGP SGSGPARGGR ESGWVGTLPP ETALPPLAPD CQASFAGASE TNQASHAPAS
GSEEDWEDVA TEPAPPGLAP SRVAAGVNTA SETELNRLLS GARASAPDKP GQGLAVGLSV
ETVAPPHVGV SASAEKHSPA EELVSAIAST VSALAAGAQV EAILTEAGPT GGVEIQALDS
PSGPQVSPEK KAMETNTAGI VEGGKALNAV AADPLQPDAA EAADVTEFLG DMEPDAEEEE
PLTFVDDFGP GIGPGEAEAG LEALRHEALG LRQAQRAQRG QADAPTDEMY TEIQDMLQMF
GVPYIVAPGE AEAQCAWLDA AGLVDGVITD DDDAFLFGAQ TVYRHIFSTK QTVEEYRTRD
VESELGLSRP EFISLALLLG SDYTPGVRGI GIVNATEVVH AFQGMEGLQD FRAWVQAPDA
AVSELIAKAT DEATQSMRRA FQLRHRGVRR NWDLPSDFPS PAVLEAYLSP RLDTSRDRFL
FGRPDLALLR SLCTARLEWT PVQADELLLP VLKAWDEREH QQTLEPFLAF RKRFAKIQSK
RLQHAVRGIA GKTTADVRLL VNQVVTSTDT KSAGAASSQL IQLLSSPASQ HGSLDAVLLD
LQPLLGPGNG NPSSTLLDAH SGLGAACAAC LAEERVLALH GAAILGCLAA AAPLVFGGRA
STALLLTAAG VAASLRVTLA RRGSGEGDPA TEHPASDGAG HPSIVTEGPR PLIGVHDALA
FLAPLLTEAQ RVAAAELRAV VGPRLGKRAA LEALLDRGLD QALRTMCLRA RRETALGCGE
EADAAAEALE RAAANLVESL SEREAVVGAV PKNRPWTTGH GACALRLLRE LTEWMPCLLY
SRPVVRATLG LGGGGPDAPP AAQEWLQRMP RLAAARAPGA ASAAFETVLM EGLLGPGSGE
SAPTLASPAV LPAMLALEPG EEGGAGHRGF LMWTAKVRAL GAAQTQLRGL EGAAAHDALL
AAAMHGLQGA GDEDQPLANR RAGMVFPRAG AMCLEAAALL ILGLAEDKET TQDQAPSTPR
RPGRSLLRLE GATPARALLR ALCRAPLEAG DEGAAAAAAA TAWHWLAAAL GPVARSAVLE
ELAGAEATRA VSAVQEAVAR LPIWPASDRL SVEDAKQRLA LLRFLLSSEL ERLAVWESPL
DTKAHAAVAC DWPTVAQWET LAAAAWIASP RLALALKDRF PGFPALRLEL ERFVLVNAAA
KSLQLLPQAG ALLAEMAGEP AAADKLVHLQ SWAPLPLLQA LAVVNSAGGK KPEVLEYLSR
SLHECNPEEV AFFLPQLVQM LRTDHDGVVA RFLLDAAAVS VHFAVVLACQ LRSEGTPPDE
AFDPQVRRSG WSAPKDSGLW QVADKLRTRL MSGLPEDVAN LLKDELAYFD DITEVSGKLY
PVHKDKRKSA AVEFLKAVEL PRGDLFLPTN PDCTVLAHIP ESAAPMQSAA KCPILVAFKV
HVRQDVHPGF ADGEVEEAGS QGSGKEDEEP ETRACIFKVG DDCRQDILAL QVIGLLKKAF
LTAGLDLYLL PYGVIATGYE CGIIEVIPNS KSRAQLGELT DGGLAEVFAR EHGPPGTERH
EAARQNFIRS CAGYAVASYL LQSKDRHNGN IMLDGDGHLL HIDFGFILGI SPGGNLGFEN
AAFKLSYEMT EIIDPARSKT SPSYLHFKEL CIKGFLTFGH LLHIDFGFIL GISPGGNLGF
ENAAFKLSYE MTEIIDPARS KTSPSYLHFK ELCIKGFLTA RSSAESIVAT VAMMASSHLP
CFRGPKTAVE LRHRFRLDLG EKEAAAHMDG LVEAAYGRWT TGFYDWIQYL QNNIPK
//
