ID U1HLZ0_ENDPU Unreviewed; 1946 AA.
AC U1HLZ0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=EPUS_03454 {ECO:0000313|EMBL:ERF71300.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF71300.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR EMBL; KE721224; ERF71300.1; -; Genomic_DNA.
DR RefSeq; XP_007803002.1; XM_007804811.1.
DR GeneID; 19238496; -.
DR eggNOG; KOG0902; Eukaryota.
DR HOGENOM; CLU_000893_1_0_1; -.
DR OMA; MKANFFV; -.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000019373; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000019373};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1355..1541
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1658..1930
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1645..1668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1650..1664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1946 AA; 218393 MW; 054E43DCD02D81EB CRC64;
MKLAALSLAP SDGEETEGIS RLTASLHRPK SLPSGLLDGI LRGVAPSSRL PMSLRELDVL
LALCKAAPGL QHVEHAQRLV VQLREYLPES HTQVFHSSPF LHDIKPSPWE ALTYDLTHAL
LAIGLRFPEL QLNISASIEA YISNCIKSLN AISPITQEDH TSNQHDDDQD AAEIVSITVS
LKGFMEAAAS HAHYWPSLDR VNIIRQLQGM LSERFLVAVE TASSTIRTSS HSEHQYRDWR
KYLRRYAAKG TPLGAMLLQQ GFMRFVVAST SRFVASETAV AAGDLLDHYM TGQRFGGLHD
ATVDEPMIEY LTEVITDEIR VLEEGSDYLQ LSSAWQQRLA FSVKAFALEA FLHCMMVDEG
IADAEVLFGW LEDSMSNEVQ MADENLAGVV LKSFAILAEV MAESAANFAR LLLRFIVQGT
SASPIVAIAA ESLAHVLRIL SQDAVITTLY SLGNVLSSGS GTEKIHNTAA SPNGHVVDQH
HSGSFTRVRT GSVISLSMSG DEETSIVCGN VAHAIAVVAN SCNDNRITAL VQSMILQKVG
RINLVVDARI LEESAVLATT GKENEFRALL RFYSRLNNEA LKNNNTIIIE AIHKARMHLA
AHLDNQTPLF RIFAIHLLER IVTKGDVVEG DTKRLPNIEQ AAEEIAPLLK PLAVVVSRKP
AENTEGSFEE DDELLAMARE AWFNIAVHGI TLQSRLGQQY YHELRILALN SEPLVDEDRA
ELLESDVELN TILRRSMTGQ HTAEQKKNLI SILPHRESEI RHLSYPKVVY LNAAFIVEGL
RARSGNCSEV LKYFLDPVMK DSDMGTCMSG IAQEIINIYL NRAVPGEFEE FGSVYVSRQL
AQILTGCCHR IAMVQQVART CADRIISQVP SALCQKSALF ALLEILTTMW SSCLDAEIDE
YEFKSTFTST RGKITLELSD DYAFRKRTLN TFYADAKKWV IGVLASAPLD VKGLLQTYLS
EYDDTGAYGH VSLGRSFALE IGSIIPPLDQ RLRAIERQAE HVNVNVASDF MAQYTTRQEY
RHADVPEHAR DMLPLVHTKE QVVNGYLKSN GTNQEVQTLL DDIEYRVSVG SHIADIELRD
VLRRVAALLC RSKGPQSIIV YHLVNIPFQA FTKASIKLGI SLWLGVIHEN PRMEPRILTE
IAQAWERTID RKVGIFSDQF NHKDPFYVKQ EFAPSDKGAI LKHQQLVQNM ISPHLRVHQV
FASHFNAIRL GSLNTQRAFI RMIRKTLDAF RKISTHPLAR EVYFHVILLA MQILRFNTCL
SENSAWQLKD QLLSTGLHWF SFPPVWSFGG NRLQMKAELS ILADVLSALS ATQHIGSTTI
NTRQTLQPKQ ELLRLLIESE RIRLAVWLFP LEHYPTHLAV KDTDLIPLLR TAWSTEPGIA
IQMATRFRSE ALRQAIRFLL LNFPEKATGE TDALEILLGP TLPSDVSFQL KYLLYWAPVN
PMQAVTYFLP AYGNHPFILQ YGMRALDYHS VDVTFFYVPQ IVQCLRYDAL GYVERYIIEA
GNFSQLFAHQ IIWNIKANAY KDEDSQVPDP VKPTLDKVMD SLISSFSLED RDFYEREFAF
FNEVTSISGK LKPYIKRPKP EKKVKIEEEL RMIKVEIGVY LPSNPDGVVV GIDRKSGKPL
QSHAKAPFMA TFRIRRSYEQ SAENVGDLVG DAPKDQERKR PKNISAGSAS DLSMMGGLTT
ANTFEVWQSA IFKVGDDCRQ DVLALQMIAA FRGIFNSCGL DVYVYPYRVT ATAPGCGVID
VLPNSISRDM LGREAVNGLY DYFITKYGGE DSIRFQEARA NFVKSMAAYS VISYLLQFKD
RHNGNIMIDD AGHILHIDFG FCFDIAPGGV KFERAPFKLT PEMMAVMGKE SSNPQPYRWF
EELTVKAFLA SRPYSEKLSH LVALMLDSGL PCFKPETMKN FKDRFVLDQT EREAAEFMKG
CIRKSEGNYS TKLYDEFQLL TNGIPY
//
