ID K1X4F0_MARBU Unreviewed; 1057 AA.
AC K1X4F0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361162};
DE EC=2.7.11.21 {ECO:0000256|RuleBase:RU361162};
GN ORFNames=MBM_06181 {ECO:0000313|EMBL:EKD15553.1};
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:EKD15553.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD15553.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD15553.1,
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.21; Evidence={ECO:0000256|RuleBase:RU361162};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC5/Polo subfamily. {ECO:0000256|RuleBase:RU361162}.
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DR EMBL; JH921441; EKD15553.1; -; Genomic_DNA.
DR RefSeq; XP_007294070.1; XM_007294008.1.
DR AlphaFoldDB; K1X4F0; -.
DR STRING; 1072389.K1X4F0; -.
DR GeneID; 18762116; -.
DR KEGG; mbe:MBM_06181; -.
DR eggNOG; KOG0575; Eukaryota.
DR HOGENOM; CLU_000288_46_0_1; -.
DR InParanoid; K1X4F0; -.
DR OMA; SPWIDFY; -.
DR OrthoDB; 5471704at2759; -.
DR Proteomes; UP000006753; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd13118; POLO_box_1; 1.
DR CDD; cd14099; STKc_PLK; 1.
DR Gene3D; 3.30.1120.30; POLO box domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033701; POLO_box_1.
DR InterPro; IPR000959; POLO_box_dom.
DR InterPro; IPR036947; POLO_box_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR PANTHER; PTHR24345:SF0; SERINE_THREONINE-PROTEIN KINASE PLK1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF82615; Polo-box domain; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50078; POLO_BOX; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|RuleBase:RU361162, ECO:0000313|EMBL:EKD15553.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361162};
KW Transferase {ECO:0000256|RuleBase:RU361162}.
FT DOMAIN 131..393
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 711..730
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT REGION 86..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1057 AA; 119134 MW; FA58C300F81E8AFD CRC64;
MFHNRLLRHR FNVTKFPVKF LAAFFLKPGS ALGLPTSPVY CCHNINLTWR NLPLGQQAER
YLAWECIYPD SIDMEALSPR DANAQIRAKQ PAPKAKQPPP KLTNKEKDHP PPPPSEVQEP
PSTDRPNGAI YKTGKCLGKG GFAICYEGQL AGTRQLYALK IVKSNMSLKK MEQKFQTELQ
IHSKMKQANI VQFHRAFSYE KCTYIVLELC PNGSLMDMVR KRKYITQPEV RYWTVQMAGA
IKYMHAKGII HRDLKMGNIF LDKDMNVKVG DFGLAALLMS GKDWQACRRT TLCGTPNYIA
PEILAKDKGG HDHAVDIWSL GIIIFAMLTG KPPFQSATSD EIYRRARERE YDWPKLDTSE
NVISDEAKNL VSELLQAAEK RPDPDTIVQH PFFTCGLVPQ PEEMTPSLRE RHPDPSQFLS
ASIRGGRSNI YTRNLKKLCI KCEVGPWNSE PKKHTSTYRE VADEEKAGLT PAVPLPEDVV
YRPFHQFLQE QAKQFLSNDE GSLKAASVFE KILSPARATL NEQPVPSIKH PAQSFAAQQR
ARPQGLAGNP ASRLVKAHQP TKEVRFRPLL TMNPRAKSKT VEAKVELKEP VVNLRTRSKT
VEAKAEPKEP EAVADVEDRL AADLVKQLAK AEAERKSAEL PDPTISIPIN ASIFNPREKL
EVLPNTNPDS VLEGLRQFQA ELERALSSRT IAIQVKKEYQ NPTIVVKWVD YTNKYGLGYI
LSNGSVGCIF RAMSAGSQYP NRGNIPPTCV VVRDAERHLS NRDNEAYVDR RQIVPISGPN
IEFYENRAAK GIFCGKVNPQ NFKIPMNPDG KPGGQLAPGV DEWDHRKREI IVLWKKFANY
MTVNYPYQEA LARESLDRIS EVNAAGNVVT FYQRFGDVGC WYFCDGHLQF NFPDHTKIVI
STDGKWCDFY PLPLEAVHEL ATKGTIAAAS LNDRQHLSYP LQTLLSFMSK PSRPTKPTSR
KHPEIDPMLQ GILQANDFRR KVEFIRDVVS EWTTNGGIGI SDLSFTGRLR WKGSRETVNV
KVPTKHVWVA VGGRGTDDRK VAVYNPLKPN DAMPDIE
//
