ID K1WID6_MARBU Unreviewed; 509 AA.
AC K1WID6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Serine/threonine-protein kinase psk1 {ECO:0000313|EMBL:EKD17415.1};
GN ORFNames=MBM_04276 {ECO:0000313|EMBL:EKD17415.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD17415.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD17415.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD17415.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
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DR EMBL; JH921436; EKD17415.1; -; Genomic_DNA.
DR RefSeq; XP_007292165.1; XM_007292103.1.
DR AlphaFoldDB; K1WID6; -.
DR STRING; 1072389.K1WID6; -.
DR GeneID; 18760211; -.
DR KEGG; mbe:MBM_04276; -.
DR eggNOG; KOG0598; Eukaryota.
DR HOGENOM; CLU_000288_63_37_1; -.
DR InParanoid; K1WID6; -.
DR OMA; DEDNPCR; -.
DR OrthoDB; 10768at2759; -.
DR Proteomes; UP000006753; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05123; STKc_AGC; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045270; STKc_AGC.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR24351:SF243; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EKD17415.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 158..419
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 420..499
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 509 AA; 56676 MW; 450E3963A7FEA49E CRC64;
MKSSTPAMNT VRGFNTPVMG SGDEDSDYGA RTPSKRRQVL EDVVSANSSP MLRSTSATAM
GGISQMKLKL ETLNLDIDSR NGSFVRSKSQ FRSQPQSSTG TSTSDGCSDD DNSDITSYEV
PLEHDFVSES VAEKPLYGAI EGGLVQDTVA RKMTATDFEP LRCLGKGTFG TVLLVKQQTT
GRLYAQKQFK KASLTVHKRL IEQTKTERSI LESVNRHPFV VKLFYAFQDH AKLYLILEYA
QGGELFKYLA EERMFPESTA SFYMAEMVLA LEHLHRNLGV VYRDLKPENC LLDSEGHLLL
TDFGLSKVSV DENDRCNSVL GTVEYMAPEV IQGHKYGMAV DWWSFGALGY DLLTGSPPFV
AQNTAKIQEK IVKQKVVMPY FLGPDSKDLL TRLLRKEPNK RLGGNMPKDM QAIKKHRFFR
KIDWKKLALR EIEPPIQPLV TDPELAENFS DEFTGLALSP VLTSTKAPWN STMVGSAVEK
DNPFGGFSYV ASQSMLDGDG FAGMFSYQE
//
