ID   Q0C0A2_HYPNA            Unreviewed;       803 AA.
AC   Q0C0A2;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 121.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ABI76756.1};
DE            EC=2.7.11.1 {ECO:0000313|EMBL:ABI76756.1};
GN   OrderedLocusNames=HNE_2144 {ECO:0000313|EMBL:ABI76756.1};
OS   Hyphomonas neptunium (strain ATCC 15444).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales;
OC   Hyphomonadaceae; Hyphomonas.
OX   NCBI_TaxID=228405 {ECO:0000313|EMBL:ABI76756.1, ECO:0000313|Proteomes:UP000001959};
RN   [1] {ECO:0000313|EMBL:ABI76756.1, ECO:0000313|Proteomes:UP000001959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15444 {ECO:0000313|EMBL:ABI76756.1,
RC   ECO:0000313|Proteomes:UP000001959};
RX   PubMed=16980487; DOI=10.1128/JB.00111-06;
RA   Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G.,
RA   Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D.,
RA   Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R.,
RA   Brinkac L.M., Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G.,
RA   Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N.,
RA   Ward N.L.;
RT   "Comparative genomic evidence for a close relationship between the
RT   dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
RT   crescentus.";
RL   J. Bacteriol. 188:6841-6850(2006).
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};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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DR   EMBL; CP000158; ABI76756.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0C0A2; -.
DR   STRING; 228405.HNE_2144; -.
DR   KEGG; hne:HNE_2144; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_007799_1_0_5; -.
DR   Proteomes; UP000001959; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
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; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR43671:SF13; LD04361P; 1.
DR   PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF13424; TPR_12; 2.
DR   Pfam; PF13432; TPR_16; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00028; TPR; 5.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ABI76756.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001959};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABI76756.1};
KW   Transferase {ECO:0000313|EMBL:ABI76756.1}.
FT   DOMAIN          80..340
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         111
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   803 AA;  86290 MW;  4D4470DCE8714E43 CRC64;
     MNSKMPDWQQ VEALLDAALE LPPEDQASFV RGQTSDPALI AEVLSLLNFA ESSEQFLEAG
     HALADDDGAP MDADARLGAW RIDGIIGRGG MGTVYRVRRA DGLYEQEAAL KLMRPLAPEH
     LALFESERQF LARLEHPGIA RLLDGGGGAD GRPWMVMEYA SGAPVDVWAR QTGAGPREIL
     GAMLQVCEAM VHAHGKLIVH RDIKPSNILI DETGRARVID FGVARIAGGD GIHVAPLSLD
     YAAPELFSGE AATTASDVYG LAATLYALLA GRPPLALSDA PVPTLARRAV EEVPPPLSAH
     IPKKDQTALI RDLDAILAKA LARNPADRYP AVEAFREDLT RALAGQAVSA RSQERGYVMG
     RFLSRNRWQA AAAAALVASM GIGLSASLWQ AREARIERDT ALREQARLEA VQQYLYFMLR
     DAADTAGGTE TSAREILETA AGQVTDMFAT DPARGGPVMH TLAELYLYLG DYEAAAPLLK
     RIVAAPETEP SVRAAAHYDL SQYHLRTADL DAAEELLTKA QAFWSEDAAL WRRRLVDSRL
     VEARILRDRG EIESAIALLQ EHLPERIRLS GEHHRHTGVF YNDLGVMLNA AGRREEAAAS
     LRQALEVWRV AALDNSPDAL NTLNNLAAIE TLSGRPEAAE PLFREAVQLR NTLYGASAAT
     SALLNNYGKT LLRLGRADEA LPFLRQASEM ALEHAGPGSL HYASAIAGVS EALSDAGEQE
     KSFQAATEGY TAVTAAVGEA HPAAGIIAIM LGRANAEAGD VTRAAELLAQ AERALAPLGA
     GAASQIDIIR SLRDRYDLPQ AVQ
//