ID M2PPJ3_CERS8 Unreviewed; 1088 AA.
AC M2PPJ3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=PI3K/PI4K catalytic domain-containing protein {ECO:0000259|PROSITE:PS50290};
GN ORFNames=CERSUDRAFT_82660 {ECO:0000313|EMBL:EMD38409.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD38409.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD38409.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD38409.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
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DR EMBL; KB445795; EMD38409.1; -; Genomic_DNA.
DR AlphaFoldDB; M2PPJ3; -.
DR STRING; 914234.M2PPJ3; -.
DR HOGENOM; CLU_002446_2_0_1; -.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000016930; 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; cd05168; PI4Kc_III_beta; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
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; 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; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000016930};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1088
FT /note="PI3K/PI4K catalytic domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004022645"
FT DOMAIN 785..1073
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 217..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1088 AA; 120372 MW; A002EE94CC557507 CRC64;
MSHALLLRLF LSPSFFSVHV ALQYLRVYAD NIGITYYLTR RLRELDVQEL REVWGFICHL
LVTRPSKSRA LECFVVETAQ KSTHVAMMTL WYMQAYLKDL APPRNKPECF LICQRILHQC
HEIIFGDLPG QSHAPYSSLQ LPNSLAFMKR KVKPHVEPAL IGIGMVLAGA PAMPVITNIM
GEVAAEQGRI DELGQDIKSL EQLEDDDDSA PVITTENLTL QADQSRESED SIEEASGLAD
HTGQPHMPTQ DDFSGTIAAR RLGVTSRRQT IAAQTSPALP LHLKDARKPR LSVDPFDQLG
ASSTAPTPTP FQSTPTFSAT KPLSRTNSLN KADSLLQKYD SRAQMHLLRS HYCRSEIRFL
LALENISNRL LVVPKPARVS ALRAELTGLN HILPAEVCMP MWCSSADTPQ PPHGIPQPHH
RIVRIPPGES VVLNSAERAP YVLILEILHD DLDFDPVRRG NRDTLRRILA KENERKEPSH
EIINFTGPTS QKLPTLLIDH VNGSELALGT DSMDLTGESS AVAAPVSPGS PVDEEIDLVE
QLYGENNSVR GVDLSESVVL PPALKNRDLD MAAWSRSSSM PQTPVTDDDA STESPIPRTS
VVSASVSRQS TIRGSPSLVD PSSGSGLRHA LSLDEYSERM RTAAVMLAQL NANMVRDSNA
APGTPNPDSS SLPFRWLPGS SWIMGSPVST ENSAGPSVVT GGTSESSSSA HPASSSAYMR
MRLQPAEAAA IRDRIMAEML ALEEERMARM RETGIDDDVL GITKISGGLK TAEDEGIIRR
ELAKADPSAV VFSESWASKR SRIRQASPYG HLADWDCISM IVKTGGDLRQ EQLAVQLIQA
FENIWREENC ACWVRYFRIL VMGNNSGLVE TITDAVSIHS IKKAEYARRM AEGQLGHVSL
LDHFRTTYGD PSSAKFARAQ RNFVKSLAGY SLVTYLLQVK DRHNGNILLD RDGHLIHIDF
GFMLSNSPGN IGFEAAPFKL PLEYIEVMGG VESPSYREFK KLFREGFDAA RKHCDRIVTL
VELMQKDSTL PCFTALGEQT ATQLRERFQQ GLTQAAVEEH VQRLIDTSLG SNWTRLYDSY
QYYSQSIL
//
