SPKD_SYNY3
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 03-AUG-2022, entry version 137.
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; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified 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}.
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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; 1148.1006577; -.
DR PaxDb; P54735; -.
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 OMA; AYHCIAG; -.
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:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
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 Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08239; SH3_3; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00287; SH3b; 1.
DR SUPFAM; SSF56112; SSF56112; 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
