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Database: UniProt
Entry: A0A1M5CWS5_9FIRM
LinkDB: A0A1M5CWS5_9FIRM
Original site: A0A1M5CWS5_9FIRM 
ID   A0A1M5CWS5_9FIRM        Unreviewed;       514 AA.
AC   A0A1M5CWS5;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=2-octaprenylphenol hydroxylase {ECO:0000313|EMBL:SHF59154.1};
GN   ORFNames=SAMN02745133_03050 {ECO:0000313|EMBL:SHF59154.1};
OS   Desulforamulus putei DSM 12395.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=1121429 {ECO:0000313|EMBL:SHF59154.1, ECO:0000313|Proteomes:UP000184148};
RN   [1] {ECO:0000313|EMBL:SHF59154.1, ECO:0000313|Proteomes:UP000184148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12395 {ECO:0000313|EMBL:SHF59154.1,
RC   ECO:0000313|Proteomes:UP000184148};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC       kinase family. {ECO:0000256|ARBA:ARBA00009670}.
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DR   EMBL; FQUY01000038; SHF59154.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M5CWS5; -.
DR   STRING; 1121429.SAMN02745133_03050; -.
DR   Proteomes; UP000184148; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   CDD; cd05121; ABC1_ADCK3-like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR004147; ABC1_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   PANTHER; PTHR10566; CHAPERONE-ACTIVITY OF BC1 COMPLEX CABC1 -RELATED; 1.
DR   PANTHER; PTHR10566:SF129; PROTEIN KINASE UBIB-RELATED; 1.
DR   Pfam; PF03109; ABC1; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        456..478
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        484..506
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          82..415
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   514 AA;  58413 MW;  BFBE76235ED5973D CRC64;
     MPKLEIGELK SVGQRIRQVI EELGPTFIKM GQIASTRPDV VPSGIIDELE KLQDNVPSFP
     FSEVRQIIQE ELGIQIEKIF VDFEEVPLAA ASIGQVHRAV LISGETVAVK VQRPHISTII
     ETDLEILMDI AGLAEQRLDW AERYQITQII DEFAKSLRAE LDYTIEGRNA EKMARQFSDN
     SKIRIPKIYE DYSAKKVLTM EYIQGTKLSQ TERLIELGYD TSEIAKQIVE AIFHQILIEG
     FFHGDPHPGN ILVLPDQVIT FLDFGMVGRL TPQMKHHFAS LVIGMIRKNT DEMIRVILDM
     GIVPSDINIS RLRSDVDALK DKYLDIPLSQ VRLGQAVNEL FTVAFNHRIR IPPDLTLLGK
     SLLTLEGSVE KLDPKLSVMD IARPFGYKLL KERYRISSIT KTAFEKINEY VEVFLDVPKL
     LKEMTHNLKD GNIRVEVRIP ELGLILKKLD RISNQLSFSI VLLSFSILMM GIIIASALGE
     RLFIWHFSAV DLGFMLASLM FVWLLFSILR SGRF
//
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