ID J9FJ49_9SPIT Unreviewed; 939 AA.
AC J9FJ49;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Phosphatidylinositol 4-kinase {ECO:0000313|EMBL:EJY78166.1};
GN ORFNames=OXYTRI_24682 {ECO:0000313|EMBL:EJY78166.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY78166.1};
RN [1] {ECO:0000313|EMBL:EJY78166.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY78166.1};
RX PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT with 16,000 Tiny Chromosomes.";
RL PLoS Biol. 11:E1001473-E1001473(2013).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJY78166.1}.
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DR EMBL; AMCR01009852; EJY78166.1; -; Genomic_DNA.
DR AlphaFoldDB; J9FJ49; -.
DR EnsemblProtists; EJY78166; EJY78166; OXYTRI_24682.
DR OrthoDB; 180480at2759; -.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05168; PI4Kc_III_beta; 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; 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; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF22; PHOSPHATIDYLINOSITOL 4-KINASE BETA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EJY78166.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 28..230
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 639..924
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 418..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 939 AA; 109130 MW; 56D3BDE46CCCAE0A CRC64;
MSSKLNNQEI QLNQSVQRDS NLNLFQDHLE KSPINIFQTE DLNLNSQQSP IRQRSFQYKQ
PQKKVKNKII FKNILNEVLD KKKWQEKWKK IKDFVKKKRS QGRNKNSERD DVFNAILALY
AGDEEDEVFS ELAILYEKYP EEIEFYVPQL CTYLFHFNSY QPKGSAIHPS THQGQHHQEL
LEKFLLNRAR RSLKFAHLIF WYIIAGLDDS ESIQLSQHQS PQIWEFLSRL INTAEEQIPR
QSFGSSEEQK NQDELLKNSI QLPKKEELAD TGSSSVIRYE YTQGMTQLDS MALISRHDQQ
IIRTLTNNMA EHQMFFSTPK FVSDLIHISE VLKTVNQPDR NDMLTQLLQQ LNKNLPANVY
IPISHDNIIS SKFQNKKSSS KSITSHKILQ VCTDFNFCLH SKERVPYHVI IEVEYEEPEF
NSRSSSHRRD TLSGDDSSHF STNDAGVNDK NNKQSNIQQK SKANSGGKII PDWQKNKSNT
QKGKKESSHI FSDEDFKSQN QSKYLNDDDY QVQRKAKSLE NERNVGKKYK LEKNKLTKEY
SQDFLEEYKS VSNPSNRPRG HKKNNFSKKF YESDANNESA GSKKNVNNLS DTMVDEKSDD
DDDFLYYKYQ QKSLVAKMCS CFTSSQEIVY DQQQCKPAGL FGSKTYEEAQ HELKLKSRFN
GLKNHGFISV IVKSGDDLRQ EQFASQLISK FKDIFDSHKL QLWLKPFNII ATCNDGGLIQ
TIPDTLSIDR LKKTYPQYPD LRSYFVNTYG GGSTQTGQSN AQRKKRFKEA RNNFIQSMAG
YSLLCYILQI KDRHNGNILL DSKGHVVHVD FGFLLSNSPG NFNFEAVTFK LTQEYVDVMG
GTSSPHYDKF TKLMTKGFLY LREHAEEIIS FVEMTMISGI DLPCFQGSDR VLESLRERFK
LEMSKNECKQ FIRQMVNKST NNLRTKLYDF YQKKTVGIW
//
