ID A0LE03_MAGMM Unreviewed; 1143 AA. AC A0LE03; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 02-SEP-2026, entry version 96. DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ABK46196.1}; GN OrderedLocusNames=Mmc1_3711 {ECO:0000313|EMBL:ABK46196.1}; OS Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1). OC Bacteria; Pseudomonadati; Pseudomonadota; Magnetococcia; Magnetococcales; OC Magnetococcaceae; Magnetococcus. OX NCBI_TaxID=156889 {ECO:0000313|EMBL:ABK46196.1, 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:ABK46196.1, 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). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000471; ABK46196.1; -; Genomic_DNA. DR RefSeq; WP_011715249.1; NC_008576.1. DR AlphaFoldDB; A0LE03; -. DR STRING; 156889.Mmc1_3711; -. DR KEGG; mgm:Mmc1_3711; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG3087; Bacteria. DR eggNOG; COG3206; Bacteria. DR HOGENOM; CLU_277401_0_0_5; -. DR OrthoDB; 9801841at2; -. DR Proteomes; UP000002586; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0016020; C:membrane; IEA:TreeGrafter. DR GO; GO:0000407; C:phagophore assembly site; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro. DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1. DR Gene3D; 3.30.70.1070; Sporulation related repeat; 3. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR045269; Atg1-like. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR007730; SPOR-like_dom. DR InterPro; IPR036680; SPOR-like_sf. DR PANTHER; PTHR24348:SF22; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1. DR PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF05036; SPOR; 3. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF110997; Sporulation related repeat; 3. DR SUPFAM; SSF57997; Tropomyosin; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS51724; SPOR; 3. PE 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABK46196.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Reference proteome {ECO:0000313|Proteomes:UP000002586}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ABK46196.1}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 12..294 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 814..898 FT /note="SPOR" FT /evidence="ECO:0000259|PROSITE:PS51724" FT DOMAIN 924..1008 FT /note="SPOR" FT /evidence="ECO:0000259|PROSITE:PS51724" FT DOMAIN 1055..1139 FT /note="SPOR" FT /evidence="ECO:0000259|PROSITE:PS51724" FT REGION 388..419 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 639..757 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 388..413 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1143 AA; 126986 MW; 3F36D153A6E11485 CRC64; MNIGTHIVDD LYTIRDMLAQ GPLGPTFLAT DRLTDAPMVI KPIPAELTRD QGALIWFQQR YQRLKGLKHP VLHTKYNHAY DQASGRHYMT APFVPGEHLG LWLKRQKDGR VDLGKALTLT KRIAEALDMA HQAGLPHLSL KLENVIVTPD ESIILVDHAL SYARHLPAWR RLDKDLQPAH LISCFTAPEI IQTLWLDQLP SHNALRQANE DLKGDMPGVA ADIYALGAIL FTMLTGQPPF TANAYLEALA HGELPSLHMD QHLPLTLHAH LAHAMERTPS ERYASTTALM DALLASWKQW ERQASRTEHP TPEKAVEAAP VVLSLAAAAA SNDTVLELEI DPRDAGSLSM GDAHDFMISS PEDDLIEDLD DVDELPILDL AAIETQRMEK DTAAEQAPDR VATRHNPESM ADPREEEDEG TLPMEMHEEA LLELQHEDLL DDPDGHSHKI ERQKQQEATQ PAEAILVDMH VDDDEEDGYA DPHADLAVEQ PEAWTDAETN VTVEPALHPG NHDQPNGRPY ETIGRPLDHL VDEDEVTNLP TKKRKSSPLL RAAAVAGILV GAGMGWFLLT QEPQSPFQIV ELQPTLPFMT EQPAPEQQVP QIKAPEDLTL VPAAPESLRK DPALRTRAVL EQLDNHAAIG LLRQQLTEVE QKHDEATAAL DTRQNKLQKL EQDLEQTQNE LDNTRQALRN ANRELADYAN ARMKIGSLEE RVKSLLQQRD GAVESAAMQK TQDEKRVNRL EQRLQANKER YRTTQLRGDE MLLKPEAGEI IPNSAPPRER DEPFMASQNL ITPAAPPAPR SASFLEEDEK NFTATKGGLI YVQVASHGQA AIANAQRNTL ANRTIHGRKW PVVTQQARVN GQLYHRVRFG PLASAEEATT LSLALSRELK MDGIMVRKRS QEESATTAML AKQVAPIQES IATGRQARGY SVQVAAFSTA EAAQEMEMKM QTMDWPTQDL PIFREAKMVD GRLFHRVRIG PFAYKNQAAR MNALVHERTH IASIVVNHRI TEENRAQVEP KPMVDAAKVT GAKVAKAVTR PVPKVAKVTK KEIYKRVDSG YMVQLGAYTS NQAANSVKRK LDAIRQVEGA LPVVQETTTL AGQDLIHLKL GPFSSKVEAE QMQAMVKAKT GMNGGTIVDN GEW //