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Database: UniProt
Entry: Q1DC99_MYXXD
LinkDB: Q1DC99_MYXXD
Original site: Q1DC99_MYXXD 
ID   Q1DC99_MYXXD            Unreviewed;       693 AA.
AC   Q1DC99;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 127.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=pkn1 {ECO:0000313|EMBL:ABF86229.1};
GN   OrderedLocusNames=MXAN_1467 {ECO:0000313|EMBL:ABF86229.1};
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF86229.1, ECO:0000313|Proteomes:UP000002402};
RN   [1] {ECO:0000313|EMBL:ABF86229.1, ECO:0000313|Proteomes:UP000002402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA   Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA   Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA   Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA   Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
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=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR   EMBL; CP000113; ABF86229.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1DC99; -.
DR   STRING; 246197.MXAN_1467; -.
DR   EnsemblBacteria; ABF86229; ABF86229; MXAN_1467.
DR   KEGG; mxa:MXAN_1467; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_009977_0_0_7; -.
DR   Proteomes; UP000002402; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0035438; F:cyclic-di-GMP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 2.40.10.220; predicted glycosyltransferase like domains; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR009875; PilZ_domain.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1.
DR   Pfam; PF07238; PilZ; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50005; TPR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ABF86229.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABF86229.1};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transferase {ECO:0000313|EMBL:ABF86229.1}.
FT   DOMAIN          59..328
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REPEAT          630..663
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   BINDING         88
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   693 AA;  74287 MW;  FD532EABF38A7CE6 CRC64;
     MPEVSSGGGC GACGRRHGAD ASCPTLVRAD VRAGGTAHPR CAPVVEAQDP LVGVRCGSFR
     LVRRLGRGGM GAVYLGEHVS IGSRVAVKVL HAHLTMYPEL VQRFHAEARA VNLIGHENIV
     SIFDMDATPP RPYLIMEFLD GAPLSAWVGT PLAAGAVVSV LSQVCDALQA AHARGIVHRD
     LKPDNIFLVR RKRNAPFVKV LDFGIAKLAD AHMPQTHAGI IVGTPEYMAP EQSLGRGVDG
     RADLYALGVI AYQLLTGRLP FNDEGLAAQL VAHQLRPPPP PSSVYPAVSA ALEHVILRAL
     AKKPEDRYAS IAAFRNALQV ALAEHVRVSA RKTRPGGLAV LERAPVAPDM PTEGQSRGRL
     GVDARAGHVP SSLASTSQRR LAPAAPAVPR ASLVEVPVQV VLRPGESPVR LRGSGLSRGG
     LFLHGGRVLP PLCSRLPVVL ELASGPLSVM CEVVRVVPPA QARVWGMPTG FGVQFVEATA
     VLKAAVDALL QGEPVRAVPQ VPLTEDPAVA RLLEAWRQRS AGDAYAVLAL EPDSDMGTVR
     LRTREAWRSL ESLEQHSLTP PQRAQVDALR VRVREAAEAL GATVQRALYD AWRGNHRGVA
     KCLEAGLTAE QLESLRREFL ARRPQAMGTA RSHFQSGGAL ERDGQLSQAL DQYERGLKLA
     PLEVDMLQRY RRLRRVLGGR ATAPTGHDRA RSP
//
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