ID Q2HAM6_CHAGB Unreviewed; 1944 AA.
AC Q2HAM6;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=CHGG_02728 {ECO:0000313|EMBL:EAQ90793.1};
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ90793.1, ECO:0000313|Proteomes:UP000001056};
RN [1] {ECO:0000313|Proteomes:UP000001056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC {ECO:0000313|Proteomes:UP000001056};
RX PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR EMBL; CH408030; EAQ90793.1; -; Genomic_DNA.
DR RefSeq; XP_001229244.1; XM_001229243.1.
DR STRING; 306901.Q2HAM6; -.
DR GeneID; 4389419; -.
DR VEuPathDB; FungiDB:CHGG_02728; -.
DR eggNOG; KOG0902; Eukaryota.
DR HOGENOM; CLU_000893_1_0_1; -.
DR InParanoid; Q2HAM6; -.
DR OMA; TIEVWQS; -.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000001056; 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; cd00871; PI4Ka; 1.
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:UP000001056};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1374..1560
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1633..1928
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 37..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1944 AA; 216118 MW; FA5A94CE0DAA9909 CRC64;
MARDLRGQAL QRLAGLAAAS SDVSFDKSDL DRLCRATPPR QGSAPSLNGH HVSGPRPEIG
HVPMVVPDAL TIREYEILLA LCKTAPSLQT TQSAQKLSRH LVPYLMDSHI QAFAPSPFFR
KVEPSPTESL SFHVTAALLS LGAHHPDVRQ NISDSLTGFI NACARAAESI PRATDDDDDP
GAVEDATRTA TIVIALLGFL DAACAQADFW KSGGRLGLVT RVRDLLSQPF LVAVEAAFST
IRNAHPHDRH IKEWKRWTRH YDDVDRPLGA TLLQRSFMRL LVAATSLLVA EEGALRESHV
LDVIMSGHGL RRPLTARSAE ADFRSVELYA TVAIDQMNYL ESSADFDSLS PAKQRLASSV
KACALISYLN ACTLNDDAAD GEVLMSWLED TLGDAAAMTD DELAAVVLKS MALLCRVSPS
YAINVSRLLP RFIVQSGAKS QMVAVASKSL AFVLQKLSKD AVITTLYTLG NVLGPGNDRP
VTNGAGEGAS QGPSNVYGSR HSTGSSISLQ ISGEEESPIV QGNVVQAICE IAGASKDEKI
TGLAQSMLAQ KIVKLNSRLD ARIITGAATL ALSGGQSEFR YLLKRYAAVA HDAVMESKDG
VLQGILKART HISANIRRDS PLFAIYLEDL LDGIISQGDA HASQNHHAKE SDVELAAREI
GQLLPPLAIF MSAHPQAFDE SSDDDTRSML RDAWFNIVVH GFTPSTDRGK QSLKHLRIMA
IHSPPLVSEN RGEQDESDID LNPILRRGES SERESLQKKL LAELVPARSS EIKGLSYRKT
IFLQAACLVE SLRADAGDCT KALSYFLEPS MRRGEPSRTM DAIMNAVMDR YLYKTVNAAN
PTFSAQYAAA QLARIFCSCC HRIERVQQAA FGCADRLVES IPSALCQPSS LFTLLELLSL
MWSSCLEAET DRYEPRTTFR SSRGDVVVEL SDDYQFRQLT LANLHRKAKA WLARAINIAP
ADVKGLLQTY LSEFDEESGY GHMSLGRSFA VEIGSTIPST DQRLSSLDML GNCPINTASD
FMAQYTTRQE YRYSEALPDQ SREWSSFMRV GHRASFLTSP DNESADAITA LAHIEKRIIG
RKAASHTDVR DILRRAAALL CRSEKDECSI IHYLVSIPFA MFTKQSIKLG ISLWLGVMNE
NPRMEPRLLA EIVHRWESSV QKRQGLFSPS ITNPDPFFLR QEFAPSDNAA LARRKQLVHN
LLAPHSRLLQ FLGSHYNATR LGSPDTQHLF LRLLDITLEA IKNSTPHPMA REIRFQVILF
GLKVLNTSTT MGIVAKYRLK DQLLSAGLSW FDASPRWSFG SNILQLRTEI RLIEDVMAAL
RETVGIGAEP AGPVKSLAPK ERLLVLLLES EHSRLHVWVR PVDASRPQST FHHGGKESPL
EAAIQPLVRT AWTESPSLAV HLASRFPYPR VQREVRWLLL NFPSKAAKEP ESIPILIDGT
LPDDVSFQLK YLLFWAPVNP ITAVTLFLPA YRNHPYLIQY AMRALESHSV DVTFFYVPQI
VQTLRYDALG YVERYILETA QFSQLFAHQI IWNMKANAYK DDDQQIPDAI KPTLDKVMGH
MVESFSEVDR DFYEREFAFF DEVTSISGKL KPLIKRSKPE KKQKIEEELR KIKVEVGVYL
PSNPDGVVIG IDRKSGKPLQ SHAKAPYMAT FRIKRNKGGD EEVEELLEED AESTDKTGQE
NAIEVWQSAI FKVGDDCRQD VLALQMIAAF RGIFHSVGLD VYVFPYRVTA TAPGCGVIDV
LPNSISRDML GREAVNGLYD YFVSKYGNED SLRFQQARNN FVKSMAAYSV ISFLLQFKDR
HNGNIMIDDA GHILHIDFGF CFDIAPGGIK FERAPFKLTS EMVAVMGGSA EHQSFKWFEE
LCVKAFLASR QYTEKLSQIV LLMMDSGLPC FKPESVKHFK ERFVLEKSER EAAEFMRGLI
KRSYGSYSTG IYDQFQLLTN GIPY
//
