ID A0A176WFK7_MARPO Unreviewed; 2045 AA.
AC A0A176WFK7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=AXG93_4586s1020 {ECO:0000313|EMBL:OAE30916.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE30916.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE30916.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE30916.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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:OAE30916.1}.
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DR EMBL; LVLJ01001225; OAE30916.1; -; Genomic_DNA.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
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; cd05167; PI4Kc_III_alpha; 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; IPR045495; PI4K_N.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF15; PHOSPHATIDYLINOSITOL 4-KINASE ALPHA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF19274; PI4K_N; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1498..1670
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1751..2029
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 193..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2045 AA; 225162 MW; 1C66ACEC7BB475DF CRC64;
MAGGGGASLR ELSSLLAGNA ELAAEKLGVI LCQCPPSGSL HDGSTRLHPR QLSAILAVAQ
FLSQSSSSAE EIQMDLWHVI LEFLRTIPYY GQDDIWSSAF SSLWATAFFK DFMLAVVKFT
KSRAVLAAEL STIIADIIQK ITALSNREVS APIAPGVKFF LVALSENCPH LSADDVERVI
KALLEQWAVN FQPGNTQPSS SDTSYHSSPS MSKKSHQHTP QSNGTSSPYK DSQSTPPQYN
SINVHGLVSR YEHQLDPSPT TSTSTILTNA STPSKLVEDH VTSRSGQLNG SGRGGLDYFY
NAQPEVQGER GSSMRLQGNA LEGESLYVLE RQEIAFRLVS HILEKADGDR VVSDLVQLRN
SAGRRQDWPA DGEDLKIKLE LKIRASHGAT VLKTRCILLS ESDEKTKGSL RESFPLLLDA
ADVCLASPWR KLRSCEELFD ALLSGVAQVA IVLGNQIQRS VLLRLKSVIL GTCAQAETWG
TGQSFVYESM LKSSCLLLET AWNSDKSSVE SFLLSLAAHI RERVEHGEKE RHVIYIQTNL
ISFLADLATR FSKREMGEII LPQFVESLEQ ADTSVPGLLR LKLIEALARI GSSGCEKSYR
EVVILLTRSY LDKVTSVDAT YTRAQPTEGT TEHLDTLAGA LLQLARGLQQ PPKLRADLRE
RLLNLCSNVG LAAEAKNGRI GADFLGPLLP AVAEICTDFD PTQDVEPAML KMYRNLWFYI
ALFGLAPPVQ KQQQLSLRQI SNQAGNISST HSSLMALQAV GGTYMWNSQW SAAATLITHG
TPPLVVSSVK WLEDEHELKA LHKPDSRRGA GSEKAATTQR AALSAAIGGL VDASAMSTIS
GVKATYLLAV AFLEILRLSH CGGVLGSSSL KGGCTTALTC AFKYLESPDL PLAVQQCLAA
IVHQAFNAAL SWLGERTLLT EEQAAEREAI VAAHTCFLIK AVAHREENVR DMADSLLNQI
KTRFPQVLWN PQCLDEVLRL AAEFGADAGA PASSRGLWNQ RVREWIAYAI VLAPCTVQGL
LQEQFRKLNT WQKAAQTSDL LSLLSDVRLD SSKTDGWSGN INLPAVLAAA AAAAGASPQS
SKVGSTEVLS TGIISANIKS NYAGEIAGMK KLYAGMGAMN LGTVSTNAKP QVQGEDTTLH
EMLTTRFVQL LQQFVVTAER GSIVDSVAFR EACLRGAALL LSDTDHIENA VSEGFDQLLR
LLCWCPAHIF TPETMETGVF VWTWLLTASP KLGSRVLSEL VDAWLWTVDT KKGLFASGIE
NSGPAAKLRP QLTTGVPGPC DDKELVQGIT AHQVWLGFLL DRFEVVRNVS SDQLYLMSRL
LQGSVKSPTQ FSSHPAATGS FFTLILLSLK FCAFQAQVSS GVSNTGICLL EKRSYRAALG
WFAVEPGWYD GNVEGVLQAE AKAMGIFVQY LMSNRPQGSA NIEGSFRHTQ ENPFSDSVQG
DSQHSWGRDE DYFDRERQRQ LLLMLCQCEA DRLETWANPL MKESSAPRIK VTADQWIEYV
RTAWSVDPRI ALSLVSRFPT VSPVKVEVTS MVQKHLLDLV HIPEALPYFV TPKAVDEDSV
VLRNLLHWAP CSITRALQFL TPDYKGHHRV MAYVLRVMET YPPERVTFFM PQLVQSLRYD
QKGLVEGYLM VAAQRSNLFA HILIWQLQGE ERPSSEEAAF GETENTEGNL YDIVPKVRQR
IIDSFTPEAN DVFLREFDFF AKVTSISGVL YPLPKDERRA GIKRELEKIT IPGQDLYLPT
APNKYVRGIQ LDSGIPLQSA AKVPIMITFD VVDKDGDPNN LKPQACIFKV GDDCRQDVLA
LQVIALLRDI FTAVGINLYL FPYGVLPTGF GRGIIEVVPN TRSRNQMGEI SDGGLYEIFQ
DDFGPVGSPK FEEARENFIV SSAGYAVASL LLQPKDRHNG NLLFDKDGRL VHIDFGFILE
TSPGNNMRFE SAHFKLSHEM TQLLDPSGAM KSDYWYRFVS LCVKGYLTAR QHMDGIINTV
LLMKDSGLPC FSRGDPIGNL RKRFHPEMTE REAANYMIKT CGDAYNKWTT AGYDLIQFLQ
QGIEK
//
