ID M2R939_CERS8 Unreviewed; 668 AA.
AC M2R939;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=CERSUDRAFT_96839 {ECO:0000313|EMBL:EMD34927.1};
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:EMD34927.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD34927.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD34927.1,
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; KB445801; EMD34927.1; -; Genomic_DNA.
DR AlphaFoldDB; M2R939; -.
DR STRING; 914234.M2R939; -.
DR HOGENOM; CLU_411028_0_0_1; -.
DR OrthoDB; 1534388at2759; -.
DR Proteomes; UP000016930; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd14016; STKc_CK1; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR InterPro; IPR000719; Prot_kinase_dom.
DR PANTHER; PTHR11909; CASEIN KINASE-RELATED; 1.
DR PANTHER; PTHR11909:SF406; KINASE, PUTATIVE-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000016930}.
FT DOMAIN 351..617
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 668 AA; 75923 MW; 23288F6820C5EC8E CRC64;
MFLFIPKSTL TIFESIISRR FDISIPKRAY GAMHPRYNTD LQADVCVATD ILEAEDVPYD
GQPLPEFQET IVRWDDPSPD FDEVEDPGRC PRIGAGVFRV IIFDLIGTLI DRDTAIIQAV
MSLTPQSGAT LPRHEALAMY IGCESSRTRD DPRARPVDTM RLALRDVATR LGCLIDDCTI
DRALAALRRP ILYEDARSGL DLLRSKAVEI FALPLPDTLF SSYLDLPLGV GVLKSAMAPP
NDLYLQISEK CDIILSRART IYPNIRASEI LLIAASTFRA IEPARAAGFQ SALIARAESL
TSSIRLDTAP PTYSADNLKN IFPLLESLLE DDQFYKLDLY RFPPFRIRGL WQCNEILGEG
SFVYNAFHLF TKDEVAIKVD MPDEELHLPC ALPYEAKIYR VLQGHLGILE PRWYGEEGGA
GVMIMDRLGP NLDQLRRFCR GTFSMKTICM LALQMISRIE FAHSRGIVIR DIKPTNFAMG
MNAHRNVLFI IDFGVAKLCM NPMTGRHIPF RSGRRHIGTA RYSSYNSHFG HEFGRRDDIE
AFGTTLLFLL HGKLPWQGIY APNEDAKLRR IGEMKAGDAM RKLLAQSPPE LTALFNHSRS
LSFEDKPDYD LIRGLFLRRM QQEKWTNDGL FDWIDPRFLR RGTLLPDEYL WDPELAFDSF
KHVVMPWT
//