ID A0YKL5_LYNSP Unreviewed; 694 AA.
AC A0YKL5;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=ABC-1 {ECO:0000313|EMBL:EAW38554.1};
GN ORFNames=L8106_07124 {ECO:0000313|EMBL:EAW38554.1};
OS Lyngbya sp. (strain PCC 8106) (Lyngbya aestuarii (strain CCY9616)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Lyngbya.
OX NCBI_TaxID=313612 {ECO:0000313|EMBL:EAW38554.1, ECO:0000313|Proteomes:UP000000737};
RN [1] {ECO:0000313|EMBL:EAW38554.1, ECO:0000313|Proteomes:UP000000737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC8106 {ECO:0000313|Proteomes:UP000000737};
RA Stal L., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC kinase family. {ECO:0000256|ARBA:ARBA00009670}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAW38554.1}.
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DR EMBL; AAVU01000004; EAW38554.1; -; Genomic_DNA.
DR AlphaFoldDB; A0YKL5; -.
DR eggNOG; COG0661; Bacteria.
DR Proteomes; UP000000737; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000000737}.
FT DOMAIN 181..510
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..694
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 694 AA; 77899 MW; E48491294B21B381 CRC64;
MPLVDSQAPT PMRATQLDPV DPVTSNTVDV RSQLVSVEEI PTPGESEADQ SFSNPHVSLR
YDPVAIANYY RSRFLKVWGR LLTVIWKFSS LALGIWLDQK RGCAEKNEGK RATQLRVTLT
QLGPAFIKVG QALSTRPDLV SPTFLEELTK LQDQLPPFSN EIAYGFIEEE LGGKPEQIYA
ELSRDPLAAA SLGQVYKGKL KTGETVAVKV QRPGLSELIA LDIYLLRTLA IWAQKNITRI
RSDLVAIMDE FGYRIFEEMD YTHEGHNAER FNELYGHLPD IYVPKIYWEY TGKRVLTMEW
VNGTKLTNLD EVQAKGIDAR YLIEVGVQCS LRQLLEHGFF HADPHPGNLL ASPDGKLVYL
DFGMMSEVKP YQRYGLLEAV VHLVNRDFEG LANDYVKLEF LTPDTDLTPI IPALSSVFND
ALGASVAELN FKSITDKLSA LMYEYPFQVP AYYALIIRSL VTLEGIAINV DPNFKVLSKA
YPYVAKRLLT DPSPQLRTSL KDLLFKDGSL RWNRLENLLK NARNSDDYDI NQVLDQTLDF
LFSERGEFIR EKLANEIVKN VDLASRNALT NAQLKVAEWM GIKPPLSNGK KPVATSNQNQ
SNLEHIQRIV GILQETKGFD PMILVQKVPD LLAKPEVRQL GQQVAGELAQ KTAARLIREL
LISEDHSETP KNGHRSSSQP PAKPLPPVSL PAGY
//