ID SPKD_SYNY3 Reviewed; 505 AA. AC P54735; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 143. DE RecName: Full=Serine/threonine-protein kinase D; DE EC=2.7.11.1; GN Name=spkD; OrderedLocusNames=sll0776; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae; OC Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION. RX PubMed=12168951; DOI=10.1093/dnares/9.3.71; RA Kamei A., Yuasa T., Geng X., Ikeuchi M.; RT "Biochemical examination of the potential eukaryotic-type protein kinase RT genes in the complete genome of the unicellular Cyanobacterium RT synechocystis sp. PCC 6803."; RL DNA Res. 9:71-78(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27184 / PCC 6803 / N-1; RX PubMed=8590279; DOI=10.1093/dnares/2.4.153; RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., RA Sugiura M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region RT from map positions 64% to 92% of the genome."; RL DNA Res. 2:153-166(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}. 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; AB046600; BAB17036.1; -; Genomic_DNA. DR EMBL; BA000022; BAA10726.1; -; Genomic_DNA. DR PIR; S77034; S77034. DR AlphaFoldDB; P54735; -. DR SMR; P54735; -. DR IntAct; P54735; 14. DR STRING; 1148.gene:10500230; -. DR PaxDb; 1148-1006577; -. DR EnsemblBacteria; BAA10726; BAA10726; BAA10726. DR KEGG; syn:sll0776; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG3064; Bacteria. DR eggNOG; COG4991; Bacteria. DR InParanoid; P54735; -. DR PhylomeDB; P54735; -. DR BRENDA; 2.7.11.1; 382. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR003646; SH3-like_bac-type. DR PANTHER; PTHR44167; OVARIAN-SPECIFIC SERINE/THREONINE-PROTEIN KINASE LOK-RELATED; 1. DR PANTHER; PTHR44167:SF8; OVARIAN-SPECIFIC SERINE_THREONINE-PROTEIN KINASE LOK; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF08239; SH3_3; 1. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00287; SH3b; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS51781; SH3B; 1. PE 1: Evidence at protein level; KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..505 FT /note="Serine/threonine-protein kinase D" FT /id="PRO_0000171242" FT DOMAIN 9..271 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 436..505 FT /note="SH3b" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01117" FT ACT_SITE 136 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 15..23 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 40 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" SQ SEQUENCE 505 AA; 55213 MW; C4F12A1886C4D51C CRC64; MNVQVLDRYE IVKSLGSGGF GDTFLAKDTQ IPSQKLVVIK RLKPANANSN TSTELIQKLF EKEASVLEDL GEHNSQIPKL YSYFSNDNEF YLVQEYIQGV SLNEIAPISS EQAKTILSSL LTTLKYIHSK GIIHRDIKPE NIILRDSDHL PVLIDFGAVK ETMGAVTLGS GSTVSSVVIG TRGFMAPEQS SGRSVFSTDL YALGLTIIYT LTKKLPVEFS SDQQTGQLDW QSHVSKIDSV LAKVINKAIE MEPSRRYSSA EAMYQALHSL ISSGAEPALP METVRVAPSN EFLVTRSSTK TAETVVKPVG NSHNNYSNNN GKSKIATLLT VLIGIIVVTA GLGGGFIITQ QIKEAEARAA QAEKEKQEAE QKRIEAEQKI AENEKRQREL EQKRVEEERQ RLAAEAERAK QERQRLAAER QRVQVLANQA KAMASGASAT IGGIPGSKNI RSGPGTDYGV ITQGYTGEGL DILDSSTDSS GHVWYKVYHY GSGSTGWIAS QLVNF //