ID   Q0C233_HYPNA            Unreviewed;       828 AA.
AC   Q0C233;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   OrderedLocusNames=HNE_1496 {ECO:0000313|EMBL:ABI78332.1};
OS   Hyphomonas neptunium (strain ATCC 15444).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales;
OC   Hyphomonadaceae; Hyphomonas.
OX   NCBI_TaxID=228405 {ECO:0000313|EMBL:ABI78332.1, ECO:0000313|Proteomes:UP000001959};
RN   [1] {ECO:0000313|EMBL:ABI78332.1, ECO:0000313|Proteomes:UP000001959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15444 {ECO:0000313|EMBL:ABI78332.1,
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};
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DR   EMBL; CP000158; ABI78332.1; -; Genomic_DNA.
DR   RefSeq; WP_011646510.1; NC_008358.1.
DR   AlphaFoldDB; Q0C233; -.
DR   STRING; 228405.HNE_1496; -.
DR   KEGG; hne:HNE_1496; -.
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; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF13374; TPR_10; 1.
DR   Pfam; PF13424; TPR_12; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00028; TPR; 4.
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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000313|EMBL:ABI78332.1};
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:ABI78332.1};
KW   Transferase {ECO:0000313|EMBL:ABI78332.1}.
FT   DOMAIN          92..350
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   COILED          693..720
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   828 AA;  89972 MW;  D7FDFB3B71968471 CRC64;
     MKHIEAIWDR LDAAFAAALD LPPESRQPWL EETLSDDPET LQAIKALLEV ETESAEQFDR
     LEDIRDRLLA ELSGTSKEAS EGLQVGAVCG AWKVAGRLGD GGSSVVYEVE RADGRYEQRC
     ALKVIRSDHA GRSTDGFLRE RRILSALDHP GIVRILDAGE TETGAPWLVM DLVRGRNIAD
     HCRHAGLSLN ERLRLVMEVA EALQSAHSRL IIHRDIKPDN IVVSKDGRPR LLDFGVASLM
     NGEDNRSAPA AMTPNYASPE QRFFQEVTTA SDIYQLGRVL HEVCEPCHPL RPQVQAVIDE
     ATHQEPGARY QTAAGFAEDL RRVIAGDPPL ARPETPMEMV RRLIWRHKAL TGLAAVLVLS
     VGAWVVTLNV HARQLDEQRS LALAAADRAE RGRTVLLDLF RRMDPIQTDG SASLPGGIQD
     IVGPVLANVR EQLSDDSPLQ AELLAWAASL SERAADEDQA RIYLTEAIDL LDQAGSADTS
     IHADLIAYRG TLSIGVGDYA SGEADIFKAL AVARRAPVDD RFALSVIVRA ALSRNGQWAE
     QALLFEEALS RLGAGAANSE IEVRSGLGRA YLELGRMDEG KRQVDMALVR AEAVYGSDHP
     RLALPLSVKG QYLRRQGDME AAIEAGRRAY ELSRAAFGAG YKSTLSHQNN LALALADAGQ
     LDEAATLLLG LAETYARLDS DSSLRAGEAF QNLATIQMRA GRYEDALNSL ERAATSLNES
     LPGDAPRRYF PALTSSEALL ELGRFDQAKV QAEAAFNGLS ATLPAGHFAI EIARCRVGIA
     LIGQGLRDQG EPLVLRALDG LSNSAAVPQR HYTSCAEAEL EGRLRTTP
//