ID K1X1V8_MARBU Unreviewed; 1292 AA.
AC K1X1V8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Serine/threonine-protein kinase-like protein {ECO:0000313|EMBL:EKD18997.1};
GN ORFNames=MBM_02234 {ECO:0000313|EMBL:EKD18997.1};
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:EKD18997.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD18997.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD18997.1,
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CHEK2 subfamily.
CC {ECO:0000256|ARBA:ARBA00005575}.
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DR EMBL; JH921431; EKD18997.1; -; Genomic_DNA.
DR RefSeq; XP_007290123.1; XM_007290061.1.
DR STRING; 1072389.K1X1V8; -.
DR GeneID; 18758169; -.
DR KEGG; mbe:MBM_02234; -.
DR eggNOG; KOG0615; Eukaryota.
DR HOGENOM; CLU_003637_1_0_1; -.
DR InParanoid; K1X1V8; -.
DR OMA; PRRDNEY; -.
DR OrthoDB; 2045964at2759; -.
DR Proteomes; UP000006753; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR44167; OVARIAN-SPECIFIC SERINE/THREONINE-PROTEIN KINASE LOK-RELATED; 1.
DR PANTHER; PTHR44167:SF18; SERINE_THREONINE-PROTEIN KINASE RAD53; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 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}; Kinase {ECO:0000313|EMBL:EKD18997.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW Transferase {ECO:0000313|EMBL:EKD18997.1}.
FT DOMAIN 155..209
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 321..605
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..804
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1023
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1278..1292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 350
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1292 AA; 144383 MW; 104D3ED3688B2927 CRC64;
MEDSPLRPSQ VTQPGTANSS SIALPSSPLF PDPSSPANPQ DNFADDPYWV ATQIVTDPRR
LGQAGSGLSS EDLGDIICIL HPTTQAASRA AALIHEDPNA HPGCTLVSAN NVEMRVKGSK
DTAKDTSYQL AAEGLVLCDL VLRLSAPLKD PLGGFQFGRS PSRCDFVLGK DQASKRISNI
HFRIYLNEHG YLMLEDQSTN GTAVDGALLR GKEKENNKQH RRTLEHGSVI TLAMTPPEQD
YQFMVRIPPR DQASEQELWS QNLRAFILHT ANLRMHKEAR IAAGGLEKKG PPNLFPTAPA
TPDPNLPSGK VIRVWKGGPK YNRLEMIGKG AFAVVYKLTD KYDGVPYAAK ELEKRRFMKN
GILDQKVDNE MKIMRKIKHP HVVQFIEHVD WDEYLYIIME FIPGGDLGSL ISREGYLPEP
DVQIMAKQLL SALKYLHDGG ITHRDVKPDN ILISTRNPLH VKLTDFGLSK MIDGEDTFLR
TFCGTLLYCA PEVYSEYREY DETGKRSLRG MDKRFLPPQR YGHAVDIWST AGVLFYALCG
SPPFPVKKNT SYQELLNQIM TCHLDIRPLQ LANVSENGIR FVKSMLIVRP EQRATIEQLE
QRSWFLGGNS FQDSMENDEV DQIGGDDSNF ETQLEQGTSQ LSINPELEEF DDSQLMIDDD
LSHLLDDSQE MMDGDDMSLP LELQPREIPS SFANSDSNSS AETQTYRMVH GGGNSEDTVG
RLFGEVNASA IGSSGALPLD HLHLPFQTTA NNHGTAPDDS QQSRYLQESP GDNHRGQSQG
IPAAATVPTI MPPPPPPPPT PSTRNPITAA RHPEIEDRAV RESSLMGAEA MVGNLNMHSP
ASATSPGAEA MVGNLNSPAS ATFPGTESLA PTTEDTREAF GSVRRPREEE EEDWDDESWR
PADLPIKRRK SSRQIDMRIP PTVFWDPSDR STHHYDYPSM TSMQFKSYQE YAEKKGEVFA
HGQNIFEVTM QSFRNSRSPS LEPERAASEP IKDEGRRMLM KRDERKLEEP RGGRGKSESR
TGEHPVAQEN FIPLTAHPFD TASKAKSTTT HYAFDFPSVG NDFQAPKRIL AKAVSTVDSC
LAISLNITDS AFSWGRGEST TTRYANGKED RVPKYAFKTM LFKPGYYKDK PAPLDTTHVW
NQRDTDMSFY ISTKATLGIW VNGAHIPGHD LQHPNAESLF WGELRNGDII TVWRNDSKVP
GAKKHTRLRF ECFWGKSMEV RKEPFHIIEE GAFLDELEEA CLIQEGAIIN ENKHRRAEDM
KVLQREKEEK SARQNEKAIK FESSFSGAPS TE
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