ID D0LS30_HALO1 Unreviewed; 1007 AA.
AC D0LS30;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Serine/threonine protein kinase with TPR repeats {ECO:0000313|EMBL:ACY13727.1};
GN OrderedLocusNames=Hoch_1157 {ECO:0000313|EMBL:ACY13727.1};
OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium.
OX NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY13727.1, ECO:0000313|Proteomes:UP000001880};
RN [1] {ECO:0000313|EMBL:ACY13727.1, ECO:0000313|Proteomes:UP000001880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2
RC {ECO:0000313|Proteomes:UP000001880};
RX PubMed=21304682; DOI=10.4056/sigs.69.1277;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A.,
RA Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F.,
RA Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A.,
RA Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Haliangium ochraceum type strain (SMP-2).";
RL Stand. Genomic Sci. 2:96-106(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};
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; CP001804; ACY13727.1; -; Genomic_DNA.
DR AlphaFoldDB; D0LS30; -.
DR STRING; 502025.Hoch_1157; -.
DR KEGG; hoh:Hoch_1157; -.
DR eggNOG; COG0457; Bacteria.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_009368_0_0_7; -.
DR Proteomes; UP000001880; 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; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
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 SMART; SM00028; TPR; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ACY13727.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001880};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ACY13727.1};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000313|EMBL:ACY13727.1}.
FT DOMAIN 60..366
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 664..697
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1007 AA; 111116 MW; 7EA109CFF0AC49AB CRC64;
MKSNDSGGLI PTLLRTEEPC GTPSAVGPPH RFGLASKLDK QHAFAGLFDE EPQLVGVGHF
KLLRFLGGGG MGEVYEAYDE ELDRLVALKL VRSDRAMSGL AEERLLREAQ TLAQLSHPNV
VQVYQAGRCS GRVYIAMELV RGRTLRSWMH ERTRGDAPVK LWEIIEVMIA AGRGLQAAHE
MGLVHRDFKP ENVLVGDDGR PRVVDFGLAR GMGTLALLEG GLSAHRRDAL AQEDTAPLDE
RTSAMIEAAT APLRRVDRVF TSHGRLLGTP RYMAPEQMRG EMVDHRCDQF SFCVSVYEAV
CGVKPFAAEK LEGLREAVIR GELQEPARGR RLPRGMRKVL LRGLSAEPDD RFSDMAALLA
ELSAWSTRRR RVQGGAFALA LGTLVLHCAV GAREPDVCDD ADERVRATWT DERRASIRDA
FVRTGLPYAE TTWSSLETYL DHYASELAGE LVTVCEAAHE LGVQSVALAE KRVMCLSSRE
NRLRALLELF ASADQHTVEQ AHRAAGALPE LAPCQHTETL RYGMPAPGSG LADEVERLRV
ELADAHTLDL LGHRTEALDI ARASLRRAEA LEYVPVEAEA LYQLGRMLVH DGQTRAEAER
GSSMLQRAQR LAERSRHDEL AAELWNQLVL GAARNDAGTE RARDWFEHAE AAIARIGNPM
RLRADALRNI GRVYYHESRF AQAAEYQERA LSLLEQVSDA PRLLRGVYLH DLASTRRRLG
AFDAAKRDYA QALAVYRSVL GEGHPYIADL RYGVAMVDFD RGSSDAAREQ LAALVDTVDE
TLSPLHPVRT NIHVALADLE RQRGALDSAH THATAARQLV ERVYGRDHVE YARASLRQGA
IALYRGAYVA ARDAYEGALE IFVRHLGETH LDVGLTLANL VEVELALGDY SAARASRERA
EPILAPHLAS IPALKPYLDS MRGQTLLGEE RFVDAVRVLE SALQGAAALE DVVRADTYWA
LARALAASGA SPERTRSMAR SALAIYEQQS AEMRTPSRAV RDWLEAL
//
