ID A0A401UWR9_9CELL Unreviewed; 600 AA.
AC A0A401UWR9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=CTKZ_06600 {ECO:0000313|EMBL:GCD19098.1};
OS Cellulomonas algicola.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=2071633 {ECO:0000313|EMBL:GCD19098.1, ECO:0000313|Proteomes:UP000288246};
RN [1] {ECO:0000313|EMBL:GCD19098.1, ECO:0000313|Proteomes:UP000288246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TKZ-21 {ECO:0000313|EMBL:GCD19098.1,
RC ECO:0000313|Proteomes:UP000288246};
RA Yamamura H., Hayashi T., Hamada M., Serisawa Y., Matsuyama K., Nakagawa Y.,
RA Otoguro M., Yanagida F., Hayakawa M.;
RT "Draft genome sequence of Cellulomonas takizawaensis strain TKZ-21.";
RL Submitted (NOV-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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCD19098.1}.
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DR EMBL; BHYL01000050; GCD19098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401UWR9; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000288246; Unassembled WGS sequence.
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-EC.
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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
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 SMART; SM00220; S_TKc; 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; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 409..438
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 480..501
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 521..542
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 563..584
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..265
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 340..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..375
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 600 AA; 61650 MW; 8A7422FDADA88364 CRC64;
MERIGLTPGS DIGGYRIVAP LGSGGMGTVY RAVDGGGTAV ALKLLHPQLG SDAVARDRLR
REVRALQKLR HPGVAAILDA EADSTEAFLV TELVDGDTLE EHVRERGPLD AQDLLDLAEG
LRSALAAVHG AGVVHRDLKP ANVLVTDDGP VLIDFGIAQA ADDAPLTSDG LVIGTPGYLA
PELLDGDEPT AASDYWGWAA VLAFAATGRA PFGTRPLEAV LSRARSGTAD LDGLGTLTAT
ALRGALVADP DARTDPEDVV AALTVAATDG DVVTEDATAT TLVHAQDLTD TTHVGPGDAT
DTARLDPADA TGTALLAGAA ARPGGAAAAG TATLVANDGK TRTFEPGTDD VAGDDDGWDG
WSEDEDGWSD EEDPEGVEWI QDDLDASEEP GPEGSGYVRP PTERRWGTLL AAGLLVAAAG
TLFPVVTLVV VGVLVLVVRT FGTAVESMHA RRERSGVRRS DVPVTVAAGP WHLLRATAGL
VPSLVVGASV AVVVVGVLWW LLDSGRWTID GSPSGLPVQG LTASLVVGAL VLLAVLVVWW
GPLSSMTRVG ARRTLAVVAP GRLGGLVAVV VLLAAAAVLV ALLLDGRPIT WWPLPTPTMP
//
