ID A0A345NQT8_9MICO Unreviewed; 872 AA.
AC A0A345NQT8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=DV701_15905 {ECO:0000313|EMBL:AXH97396.1};
OS Ornithinimicrobium avium.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Ornithinimicrobiaceae; Ornithinimicrobium.
OX NCBI_TaxID=2283195 {ECO:0000313|EMBL:AXH97396.1, ECO:0000313|Proteomes:UP000253790};
RN [1] {ECO:0000313|EMBL:AXH97396.1, ECO:0000313|Proteomes:UP000253790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMA3305 {ECO:0000313|EMBL:AXH97396.1,
RC ECO:0000313|Proteomes:UP000253790};
RA Bae J.-W.;
RT "Complete genome sequencing of Ornithinimicrobium sp. AMA3305.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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; CP031229; AXH97396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345NQT8; -.
DR KEGG; orn:DV701_15905; -.
DR OrthoDB; 1492512at2; -.
DR Proteomes; UP000253790; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0031179; P:peptide modification; IEA:InterPro.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.50.10.20; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR007822; LANC-like.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF05147; LANC_like; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01950; LANCSUPER.
DR SMART; SM01260; LANC_like; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF158745; LanC-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000253790}.
FT DOMAIN 183..437
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 337..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 872 AA; 93179 MW; A4FC788346B0CDCF CRC64;
MVTTFEMSVP LRSQGWKLHV AAHPGSSPAV LERVLPVLRA HRAPFKVAES PQTLMVLNAG
AGGPSQIGKF VTVYPQTDED ARQLALDLDA ATEGMAGPRI PSDRPLRPGS LVHYRFGSFT
GSALMQLPDG TVASALLTPS GTLEPDQRLS VYSPPSWAVD PFDSPEESLQ SLQPLEQGGN
ASYRVLGLLS NSGRGPVFIG LDVERRRRCV FKSSAKGMTD RPSDGELALR REAALLGSLP
AHGAWPAVYD LIETDEQLMI VTEDVEGVSL GERIADSTAG GSQLSPSEVV DLALEIGRAV
EALHREGVIH RDLKSSNVLV RPTGGVALID FEHAGRKQER VGSGGTRGYM SPQQRAGQPT
SESDDVYALG ALLMLLATSC EPSQAPDAAD LTTRPLELLR PDLPPSLARL IRSCLSTEPG
CRPRDATEFI SLLTDFRKDD LTASPSRVAG DTRASNCPAT AAIPDPLGTA QELCDALCNR
AAPGPDGTLT WISTSPGTLP VPYRQINNGV PGVLLGLASG WWILGRERHR DTLTRGARWL
MESEELPGAK ISGLYAGEAG VGASLLVAGL ACGDRSFLDG AYEVERRLRQ YPFDSVDLYH
GTAGRLRFLA MLWSLEQDRD VLEHALRCAE HLHATAVAPS DGLACWQGDE NTAGVALASY
AHGTAGVADA LLDLYEITRD ARHLDLVDRA VRWVSSAAVP SLHDGSGTDW GNGGAFGGLW
CYGASGVGLL YLHLMRVRTD PNDEDIARRA GNTTAFAGRY AGPGLCHGLG GSIEYLLDLH
QLTGDPAWLR HSSDLQRLLH AYRRSTPDGI GYPSTQDHPK DSSYMLGDAG LVGTMLRQGT
DGQLPRMLSI ASVHHLAKPP QMRQTQGASG PT
//