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Database: UniProt
Entry: D7E5D4_NOSA0
LinkDB: D7E5D4_NOSA0
Original site: D7E5D4_NOSA0 
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
//
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