ID D0LQB2_HALO1 Unreviewed; 641 AA.
AC D0LQB2;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ACY18921.1};
GN OrderedLocusNames=Hoch_6452 {ECO:0000313|EMBL:ACY18921.1};
OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium.
OX NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY18921.1, ECO:0000313|Proteomes:UP000001880};
RN [1] {ECO:0000313|EMBL:ACY18921.1, 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 -!- 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; ACY18921.1; -; Genomic_DNA.
DR AlphaFoldDB; D0LQB2; -.
DR STRING; 502025.Hoch_6452; -.
DR KEGG; hoh:Hoch_6452; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_000288_151_5_7; -.
DR Proteomes; UP000001880; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR013229; PEGA.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF08308; PEGA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000313|EMBL:ACY18921.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000001880};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ACY18921.1};
KW Transferase {ECO:0000313|EMBL:ACY18921.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 424..445
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..280
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 357..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..481
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 641 AA; 68428 MW; 742E10D9093CF5EA CRC64;
MGKYRYSQRI GRGGMADVFL GMQEGIGGFE KLVVIKRIFQ HYCEDERFLQ MFMDEARLAA
TIRHPNVVEI LDIERDATGF FIVMEYLSGE TLGFVVPELQ KRRVLPPPHL VCRIAASVAA
GLHEAHTATD ATGSPQPVVH RDVTPSNVLV GYNGVVKLLD FGVAKALSNN DNDTRVRGVK
GKLSYLAPEQ ISNDPVDART DIFQLGIVIH EMLTGRGLFH ADNAHRRVLA VMQRDIPPPS
TLHPDVPPIL DEVVMAALQR DPAKRLRSAE ELRARLEAVI SAIGLPASDR DVGMWLRETF
PASYEARVKL ERGTATQIRQ SRQMQTFGIE HTNGGGEWSG GGTGIGSAPR IQVVGLEQDG
SRPSSPSLGM YASGYSGPGS GPGSGPGSGA GSVSGVRPGE PSTMTMASEA LSTVDAPPQR
RRTWLVAGAL LLFVAVVAIA GVSLLDGDGA EPIQAAAPVL LSDDSADGDD AADDDGSDED
EARAQREDGS EDAPSMVVEA QPKNATLELD GVPVGRGSLE LVVDGSHHVL VVSADGYRPR
VVTFSDTPPP SRIELEPLAD DDDDDDSASS QRSGSRARNT RRARRASSRG LSAAEARERA
AAEAKSNANT DSANSADSAE PRPTSKPRRQ PTTDNLDPWA D
//
