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Database: UniProt
Entry: A0A0V8T8W0_9CELL
LinkDB: A0A0V8T8W0_9CELL
Original site: A0A0V8T8W0_9CELL 
ID   A0A0V8T8W0_9CELL        Unreviewed;       446 AA.
AC   A0A0V8T8W0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=ATM99_09860 {ECO:0000313|EMBL:KSW29075.1};
OS   Cellulomonas sp. B6.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1295626 {ECO:0000313|EMBL:KSW29075.1, ECO:0000313|Proteomes:UP000054319};
RN   [1] {ECO:0000313|EMBL:KSW29075.1, ECO:0000313|Proteomes:UP000054319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B6 {ECO:0000313|EMBL:KSW29075.1,
RC   ECO:0000313|Proteomes:UP000054319};
RA   Piccinni F.E., Campos E.;
RT   "Draft Genome Sequence of Cellulolytic and Xylanolytic Cellulomonas strain
RT   Isolated from Decaying Forest Soil.";
RL   Submitted (NOV-2015) 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:KSW29075.1}.
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DR   EMBL; LNTD01000073; KSW29075.1; -; Genomic_DNA.
DR   RefSeq; WP_062102125.1; NZ_LNTD01000073.1.
DR   AlphaFoldDB; A0A0V8T8W0; -.
DR   STRING; 1295626.ATM99_09860; -.
DR   OrthoDB; 9762169at2; -.
DR   Proteomes; UP000054319; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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: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; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF37; SERINE_THREONINE-PROTEIN KINASE A; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 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   Kinase {ECO:0000313|EMBL:KSW29075.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054319};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:KSW29075.1};
KW   Transferase {ECO:0000313|EMBL:KSW29075.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        367..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          14..271
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          276..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..347
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   446 AA;  46663 MW;  C7A8E7B25BE379A1 CRC64;
     MRTAPGVALG GGRYRLLRRI AVGGMGEVWE ANDDALARAV AVKVLRAEFA GDAGFLERFR
     TEARNSASLH HPHIAALFDY GEQDGSAYLV MELVVGEPLS DLLEREPVLS PQRLLPVLAQ
     TARGLHAAHL AGVVHRDVKP GNILLARSGK VKITDFGVSL ASNQKTMTAT GMVMGTAQYL
     SPEQAVGRPA TPLSDLYSLG VVAYEALAGK RPFTGPTAVD IAVAHVNDPV PPLPAAVDRK
     LAALVLRLLS KEPAERPASG EELAALLDQL VPRTPPSGVA VLVSKPTRAR EDRAPARPRT
     APAGPGGATA GGTSSAPPSY APVRRDRGGR STAPDDRRRR SRHEAPSTRP ADGVAARALA
     WARRLRLPLV VLVLVLVAML GAALADRLLG AEAAHGTGQI VTDQYPRGGA PDGMIAAVQH
     RDGAAAPADG TRAAAHDPRS TEVKDA
//
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