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Database: UniProt
Entry: A0A164CG47_9SYNE
LinkDB: A0A164CG47_9SYNE
Original site: A0A164CG47_9SYNE 
ID   A0A164CG47_9SYNE        Unreviewed;       626 AA.
AC   A0A164CG47;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   Name=ubiB_1 {ECO:0000313|EMBL:KZR90255.1};
GN   ORFNames=MITS9508_00804 {ECO:0000313|EMBL:KZR90255.1};
OS   Synechococcus sp. MIT S9508.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1801629 {ECO:0000313|EMBL:KZR90255.1, ECO:0000313|Proteomes:UP000076799};
RN   [1] {ECO:0000313|EMBL:KZR90255.1, ECO:0000313|Proteomes:UP000076799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT S9508 {ECO:0000313|EMBL:KZR90255.1,
RC   ECO:0000313|Proteomes:UP000076799};
RA   Cubillos-Ruiz A., Berta-Thompson J.W., Becker J.W., Chisholm S.W.;
RT   "Evolutionary Radiation of Lanthipeptides in Marine Picocyanobacteria.";
RL   Submitted (FEB-2016) 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:KZR90255.1}.
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DR   EMBL; LVHU01000003; KZR90255.1; -; Genomic_DNA.
DR   RefSeq; WP_067093450.1; NZ_LVHU01000003.1.
DR   AlphaFoldDB; A0A164CG47; -.
DR   STRING; 1801629.MITS9508_00804; -.
DR   PATRIC; fig|1801629.3.peg.866; -.
DR   Proteomes; UP000076799; 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   Transferase {ECO:0000313|EMBL:KZR90255.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          145..475
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   626 AA;  69912 MW;  56E5A8E2D03DAB4D CRC64;
     MALRPVAPQE LGDFIEAAGL LTYDPAAITR IYAGHPQRLL RRLWQTLVPI GMLLIGIGFD
     WIFQLLKDQK RARNRARECA ELLVELGPAF IKAGQALSTR PDIVPPVLLE ELAQLQDQLP
     GFDSALAMAC IEDDLGAPVD SIYAELEREP ISAASLGQVH RGTLHDGQRV AVKVQRPGLR
     EQITLDLYIV RNIAAWLNSN IGLIRSDLVA LIDELGSRVF EEMDYLNEAS NAEKFSELHQ
     QNPRIAVPKI YREATSRRVL TMEWIDGVKL TNLEAVREMG IDPDDMVSVG VNCSLQQLLE
     HGFFHADPHP GNLLALSDGR LCYLDFGMMS EVSRESRTGL IQAVVHLVNR NFGKLSKDFV
     NLGFLAEDVN LEPIVPAFET VFSQALEAGV SRMDFKAVTD DLSGVMYKFP FRVPPYYALI
     IRSLVTLEGI ALSVDSDFKI LGAAYPYFAR RLMEDPDPQL RQSLKEMLFD GDIFSWTRLE
     NLVASAASQD QLDLEALLDQ VLDFLVSTHG GMLRHQLVET AADRIDSLGW MTLQRLGRRL
     PRPLQPSRLM ASGAELDQDF YMDLEPVRQL IQVLQQLPGF SPDLLFSRLP RLMREPDARR
     MGVELAQGLA ERGVVRLVKA AAGVSP
//
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