ID Q2W2D2_PARM1 Unreviewed; 696 AA. AC Q2W2D2; DT 10-JAN-2006, integrated into UniProtKB/TrEMBL. DT 10-JAN-2006, sequence version 1. DT 04-NOV-2026, entry version 97. DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011}; GN OrderedLocusNames=amb3189 {ECO:0000313|EMBL:BAE51993.1}; OS Paramagnetospirillum magneticum (strain ATCC 700264 / AMB-1) OS (Magnetospirillum magneticum). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Rhodospirillales; Magnetospirillaceae; Paramagnetospirillum. OX NCBI_TaxID=342108 {ECO:0000313|EMBL:BAE51993.1, ECO:0000313|Proteomes:UP000007058}; RN [1] {ECO:0000313|EMBL:BAE51993.1, ECO:0000313|Proteomes:UP000007058} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700264 / AMB-1 {ECO:0000313|Proteomes:UP000007058}; RX PubMed=16303747; DOI=10.1093/dnares/dsi002; RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.; RT "Complete genome sequence of the facultative anaerobic magnetotactic RT bacterium Magnetospirillum sp. strain AMB-1."; RL DNA Res. 12:157-166(2005). 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; AP007255; BAE51993.1; -; Genomic_DNA. DR RefSeq; WP_011385554.1; NC_007626.1. DR AlphaFoldDB; Q2W2D2; -. DR STRING; 342108.amb3189; -. DR KEGG; mag:amb3189; -. DR HOGENOM; CLU_404840_0_0_5; -. DR OMA; AEPMMGF; -. DR OrthoDB; 7166208at2; -. DR Proteomes; UP000007058; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. 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 PANTHER; PTHR24348:SF22; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1. DR PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Reference proteome {ECO:0000313|Proteomes:UP000007058}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 675..695 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..300 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 1..23 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..22 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 696 AA; 77252 MW; 5DCFE49B6E90E725 CRC64; MSEIDEAEIE TEIDPAEDDD GDDVKVEVVK QTGPPGVLRD RYTIRSNQPL PELSTPSADA FVAEDKRDPS RALFGLICKP ELPPRVNAMR ALKGVSTPGL MQLVEWGPMN WPPAGRQCMT VVYERPGGNR VMANMRSDVP RIDEYQITKR VIEPLTAALK EMDGRGVPHR SIRPTNLFFS DGNGERLAFG DCVCAPPAFD QPVLFETVES GMCTPIARGS GDHTEDYYSL GVTIAFLILG RNPVAGLSDD AILGMKIQQG SYNMLIGDER LPLPMIELLR GLLCDDGSQR WDAEDLDLWL SGRRMSPLQP RGEKRAARGF PFMGKEYFNG RELSQAMSKN WDQAIPPVVE GKLELWLRRA VEDKDKANVV AEVVRMALNS TTDKKSSTDL MLCKVLILLD QAAPIRYKGF NAMPDGFGSA LAAVMASRGD TRLLTEIILR EVPRLWFEMR GEYQPDNSLM ESNFKELRSY LSQTGMGYGL ERCLYELNDA LPCQSSLLGE EYVVEVKELL PALNVASSKR ADGKQIPVDR HIAAFLGARM RSDIDRNLTA LGDPNQSIAM MAALNLFAVL QYRLGPESLP GLAAWVGAMI APIVQGFHGR EKRRELEKEI PRLVRKGSVV EIYNLLENAE ERVRDEQEFT FAQAQYSAAE EEIKHILLET EERSAEADKI GRQTAAVTGI LVAMVTASIV VISAVF //