ID A0A5Q4H6A5_9CYAN Unreviewed; 742 AA. AC A0A5Q4H6A5; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 22-FEB-2023, entry version 13. DE SubName: Full=Polysaccharide biosynthesis tyrosine autokinase {ECO:0000313|EMBL:TVU51949.1}; DE EC=2.7.10.2 {ECO:0000313|EMBL:TVU51949.1}; GN ORFNames=EA414_20010 {ECO:0000313|EMBL:TVU51949.1}; OS Arthrospira sp. PLM2.Bin9. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Microcoleaceae; Arthrospira. OX NCBI_TaxID=2599626 {ECO:0000313|EMBL:TVU51949.1, ECO:0000313|Proteomes:UP000358204}; RN [1] {ECO:0000313|EMBL:TVU51949.1, ECO:0000313|Proteomes:UP000358204} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PLM2.Bin9 {ECO:0000313|EMBL:TVU51949.1}; RA Zorz J.K., Sharp C., Kleiner M., Dong X., Strous M.; RT "Metagenomes of soda lake microbial mats from the interior of British RT Columbia, Canada."; RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; CC Evidence={ECO:0000256|ARBA:ARBA00001074}; CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004429}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the etk/wzc family. CC {ECO:0000256|ARBA:ARBA00008883}. 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:TVU51949.1}. 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; REEX01000175; TVU51949.1; -; Genomic_DNA. DR AlphaFoldDB; A0A5Q4H6A5; -. DR Proteomes; UP000358204; Unassembled WGS sequence. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro. DR CDD; cd05387; BY-kinase; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR025669; AAA_dom. DR InterPro; IPR005702; EPS_synthesis. DR InterPro; IPR032807; GNVR. DR InterPro; IPR003856; LPS_length_determ_N_term. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR32309; TYROSINE-PROTEIN KINASE; 1. DR PANTHER; PTHR32309:SF13; TYROSINE-PROTEIN KINASE ETK-RELATED; 1. DR Pfam; PF13614; AAA_31; 1. DR Pfam; PF13807; GNVR; 1. DR Pfam; PF02706; Wzz; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR TIGRFAMs; TIGR01007; eps_fam; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:TVU51949.1}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:TVU51949.1}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}. FT TRANSMEM 29..50 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 15..109 FT /note="Polysaccharide chain length determinant N-terminal" FT /evidence="ECO:0000259|Pfam:PF02706" FT DOMAIN 378..455 FT /note="Tyrosine kinase G-rich" FT /evidence="ECO:0000259|Pfam:PF13807" FT DOMAIN 534..652 FT /note="AAA" FT /evidence="ECO:0000259|Pfam:PF13614" FT REGION 723..742 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 216..294 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 351..416 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 742 AA; 82635 MW; EF16A599BD8988AA CRC64; MVMDFSNIEH RESIDLDLGR YLQTLKRRWF WLLGVFVLTV SGAVYATQFL SPTYQNSGKI LFKVDRTSSL AGIGEGLGEL KALLADQTPL STQIELMHSN PLLETVIERL NLTNEDGDPI YPEDIRRNLD IRIIGGTDIV LLTYQSKNPQ EVADVINTIM EVYIDANVSG IRQEASGAKE FIQEQLPRVQ QELFLAEKSI QDFKERNYVV DLGTEFAISV QEMAQLNRNI TTLEAELNAV QSLVNSLGNQ VGLNLEEAIA INTLSQSPVV RSALQELENV EGELAQEQRR FRDENPRIIS LKGKRDNLES LLQREIQVYL GSGRAFSRGL LRVMDVKNNQ IEEFVNAEIR RMDLTKQLDS LYEARDGLER RASILPQLEQ QQQELERKAE VARLTYRTLL QNLEEAQVAA NKITNNARII ETANVPDEGR TAKIQLLALG VMGGLVASTT LLLLMEMGDK SLRTVAETRD LLGYTLLGII PSFAAPPFYR YFTGGDRSSV QVPVVDTPGS LISEIYRMIQ ANLKFLGSDR KVRVIVVTSS VPQEGKSTVS ANLAAAIAQL GHRVILIDGD MRQPIQHHIW GLTNAVGLSD VLVEQATLSE AVNRGIDQLD ILTAGVTPPN PLALLDSRRM TSLIRNFSEQ YDFVIIDTPP LVLAADALTL ASMASGVLMV ARPRILDRDS AKSAKEILAR SGQRILGTVI NGISKNESTK YFYHAQRYFP LQKSHRRDRS GSPQKISSKN SS //