ID D7E5D4_NOSA0 Unreviewed; 414 AA.
AC D7E5D4;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Serine/threonine protein kinase with FHA domain {ECO:0000313|EMBL:ADI65494.1};
GN OrderedLocusNames=Aazo_4023 {ECO:0000313|EMBL:ADI65494.1};
OS Nostoc azollae (strain 0708) (Anabaena azollae (strain 0708)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC Trichormus.
OX NCBI_TaxID=551115 {ECO:0000313|EMBL:ADI65494.1, ECO:0000313|Proteomes:UP000001511};
RN [1] {ECO:0000313|EMBL:ADI65494.1, ECO:0000313|Proteomes:UP000001511}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0708 {ECO:0000313|EMBL:ADI65494.1,
RC ECO:0000313|Proteomes:UP000001511};
RX PubMed=20628610; DOI=10.1371/journal.pone.0011486;
RA Ran L., Larsson J., Vigil-Stenman T., Nylander J.A., Ininbergs K.,
RA Zheng W.W., Lapidus A., Lowry S., Haselkorn R., Bergman B.;
RT "Genome erosion in a nitrogen-fixing vertically transmitted endosymbiotic
RT multicellular cyanobacterium.";
RL PLoS ONE 5:E11486-E11486(2010).
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 Evidence={ECO:0000256|ARBA:ARBA00001433};
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; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR EMBL; CP002059; ADI65494.1; -; Genomic_DNA.
DR RefSeq; WP_013192506.1; NC_014248.1.
DR AlphaFoldDB; D7E5D4; -.
DR STRING; 551115.Aazo_4023; -.
DR KEGG; naz:Aazo_4023; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG1716; Bacteria.
DR HOGENOM; CLU_637370_0_0_3; -.
DR OrthoDB; 437733at2; -.
DR Proteomes; UP000001511; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00060; FHA; 1.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000253; FHA_dom.
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; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24363:SF0; SERINE_THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ADI65494.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001511};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ADI65494.1};
KW Transferase {ECO:0000313|EMBL:ADI65494.1}.
FT DOMAIN 26..79
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 157..410
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 414 AA; 46373 MW; F30E4E5EA37B50B3 CRC64;
MVTLTLLDMQ HKTPLNQWRF EGYTIIRIGR AVDNHVVLND SLVSRYHLEL KQFGTGKKGD
AWQVISQGTN GTFLNGVLVT KSTLPDNSLL QLAQGGPILK FQLQDIPEPT VAPWQPIHQE
TENLSISRCT HEGNSPNNIF CVHCGQPLTV LQRIRHYQIL RILGQGGMGT TYLAWDDTGL
STGVPQLLVL KQMNADMAKI AKAQELFERE ANALKCLNYP GIPKYYDFFV EGGKKYLGME
LIHGQDLEKR IYNTGPVTPN QAIAWMIQTC DILEYLHGQE PPLIHRDIKP ANLMVRSANN
RIVVLDFGAV KETGTAPGTR IGAEGYCAPE QERGQPLIQS DLYAIGPTLI FLLTGENPLK
FFRQRGRGFS FDLKTVPNIT HQLREVIECI TEPLPRDRYQ TAQDLAKALM SVTS
//