ID M5G1C6_DACPD Unreviewed; 764 AA.
AC M5G1C6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Pkinase-domain-containing protein {ECO:0000313|EMBL:EJU04036.1};
GN ORFNames=DACRYDRAFT_114461 {ECO:0000313|EMBL:EJU04036.1};
OS Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJU04036.1, ECO:0000313|Proteomes:UP000030653};
RN [1] {ECO:0000313|EMBL:EJU04036.1, ECO:0000313|Proteomes:UP000030653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJU04036.1,
RC ECO:0000313|Proteomes:UP000030653};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily.
CC {ECO:0000256|ARBA:ARBA00006485}.
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DR EMBL; JH795858; EJU04036.1; -; Genomic_DNA.
DR AlphaFoldDB; M5G1C6; -.
DR STRING; 1858805.M5G1C6; -.
DR HOGENOM; CLU_365236_0_0_1; -.
DR OrthoDB; 244018at2759; -.
DR Proteomes; UP000030653; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd07843; STKc_CDC2L1; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR045267; CDK11/PITSLRE_STKc.
DR InterPro; IPR002925; Dienelactn_hydro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR PANTHER; PTHR24056:SF107; CYCLIN-DEPENDENT KINASE 11A-RELATED; 1.
DR Pfam; PF01738; DLH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EJU04036.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030653};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 99..382
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 764 AA; 85515 MW; 9E36237090061085 CRC64;
MSAPQQAESS SAGRKRSKWE SLDEADEPTP RRVKIKRPKR EAVESSPLPN SVSSLRAGTS
TPPSRSPRLV TAADSSRSRY VPRRSLYPPI APCRSVYTYE RLNHIEEGSY GVVFRARDRD
TGDIVALKKL KLDQEKGGFP ITSLREVMAL MTCRHKHVVP IREIVVGDTL TQIFIVMDFI
EHDLKTLLTV MPTPFLQSEI KTLLLQLLSA VAHCHANWVL HRDLKTSNLL MNNRGQIKVA
DFGLARTFGD PLGKMTELVV TLWYRAPELL LGAKTYSTAI DVWSVGCIFG ELLLNEPLFQ
AKGEIEMLSM ISKLLGPPTE QTWPGVEDLP LASTINWPAR TSSLRSRFPY ITEAGLDLLD
RFLTYDPEKR ISAEEAMGHP YFSESPLPKH PDLFGSFPSI AAGENSVPFC TPTDRQLPNG
IRFRLIVADP SIGRRRYTSL TRRADCSTSI RLTSPGVIGV QYQRRRAKFM GDVAGHVIGN
GLMGCRRTSS FYIPTRAPVC RSTTSASVNQ QEFPMAQYLA QHTTEACCQA VKHTGTPRGE
LIDVGGVQTY ITYPPDKSTD RVIIFYCDVY GPHFLNNQLV MDFFAEHGYT VISPDYFNGE
QLEKLREQPG FDTMAWAAPY RVSVPKFVVD KFLPAVKEKF TSVKAYASVG YCFGAPMVLN
DLVAGRSEAG AVAHPSTLTE QVFRDIKKPI FLSCAEVDRA FPPESRHKAE AILAEGKKIY
HFQLFSGVSH GFAIKGDMNN ENERWAKEQS AWGIISWFDR FLKK
//
