ID A0L916_MAGMM Unreviewed; 705 AA.
AC A0L916;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 24-JAN-2024, entry version 79.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ABK44459.1};
GN OrderedLocusNames=Mmc1_1951 {ECO:0000313|EMBL:ABK44459.1};
OS Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetococcus.
OX NCBI_TaxID=156889 {ECO:0000313|EMBL:ABK44459.1, ECO:0000313|Proteomes:UP000002586};
RN [1] {ECO:0000313|Proteomes:UP000002586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1
RC {ECO:0000313|Proteomes:UP000002586};
RX PubMed=19465526; DOI=10.1128/AEM.02874-08;
RA Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT coccus strain MC-1.";
RL Appl. Environ. Microbiol. 75:4835-4852(2009).
RN [2] {ECO:0000313|EMBL:ABK44459.1, ECO:0000313|Proteomes:UP000002586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1
RC {ECO:0000313|Proteomes:UP000002586};
RX PubMed=22581902;
RA Bazylinski D.A., Williams T.J., Lefevre C.T., Berg R.J., Zhang C.L.,
RA Bowser S.S., Dean A.J., Beveridge T.J.;
RT "Magnetococcus marinus gen. nov., sp. nov., a marine, magnetotactic
RT bacterium that represents a novel lineage (Magnetococcaceae fam. nov.;
RT Magnetococcales ord. nov.) at the base of the Alphaproteobacteria.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2012).
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DR EMBL; CP000471; ABK44459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0L916; -.
DR STRING; 156889.Mmc1_1951; -.
DR KEGG; mgm:Mmc1_1951; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG0790; Bacteria.
DR HOGENOM; CLU_413220_0_0_5; -.
DR Proteomes; UP000002586; Chromosome.
DR GO; GO:0005524; F:ATP 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 Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR006597; Sel1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR11102:SF160; ERAD-ASSOCIATED E3 UBIQUITIN-PROTEIN LIGASE COMPONENT HRD3; 1.
DR PANTHER; PTHR11102; SEL-1-LIKE PROTEIN; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08238; Sel1; 8.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00671; SEL1; 9.
DR SUPFAM; SSF81901; HCP-like; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ABK44459.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002586};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ABK44459.1};
KW Transferase {ECO:0000313|EMBL:ABK44459.1}.
FT DOMAIN 21..301
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 705 AA; 78284 MW; 8EBFECE1DEDEC425 CRC64;
MIRDTMPISD VLPNYTRVSD YTIQACLGRG RLGVTYLAQH ANGDRVALRE FMPRHYARRG
EEGHLQPILG SETILERYRQ AFLAQNNYLQ NIRHPSLATP RGTFMVDGGL FMLLPYVEGE
SLQQRFKRRG LTPRELLNLT CDLGSALRKM HTQGVVHLDL QPDHILLDIE DGVPVCIGFT
GVEKIKVGEP SRTLNTPAVG YSAPEVALNR TQHIGPCSDI YSLAAMLYES VAGFVPCDAR
VRQRYQREFG WDDPLIPAKI VGAGSYPEPF LAAIDAALTL EPAARPQSIQ AWLEGVQHLF
KQRNLQQSHH TPLLTVLRRG DHAWLHGDSE ESQRAYSEAA SHGSAIALKA LGWMKLSGEQ
ADPLTAAVWY QRAATLGDVA AMYQLGLLFL QVAQELGDGG EEGKRWFYQA AKRHHAPSWY
QLGRIYRYGD GGQQDHKKAL HCFQLAAGQG NADAQLHLGL MVREGRAKKL TLQKAAPWFE
LAMIQNHPQA HYQMAQLYEL GRGVKKDLHR AFTLYQKAAD GQVSLAKVAL GRFFAQGLGV
ASNIRAAIDL LEREAEQGSG EAAYELGLLY KEGPEGHSDG MMAEAWFLRG AELGFAAAWD
PLGLLYEQGL SMDGKDMARA LSYYQRGAEA GDGPACFHLA RLYERGNGVE LDLATAISYY
EKALAAGESR ARQPLKQLQD RAAELTNYRA YSHRPRARLK RDSEA
//