ID A0A1H6VZB0_9BACT Unreviewed; 866 AA.
AC A0A1H6VZB0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=SAMN05192553_102378 {ECO:0000313|EMBL:SEJ09953.1};
OS Cyclobacterium xiamenense.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Cyclobacterium.
OX NCBI_TaxID=1297121 {ECO:0000313|EMBL:SEJ09953.1, ECO:0000313|Proteomes:UP000199403};
RN [1] {ECO:0000313|Proteomes:UP000199403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M 10761 {ECO:0000313|Proteomes:UP000199403};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FNZH01000002; SEJ09953.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6VZB0; -.
DR STRING; 1416801.SAMN05192553_102378; -.
DR Proteomes; UP000199403; 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-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; 3.
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; 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 Pfam; PF13374; TPR_10; 1.
DR Pfam; PF13424; TPR_12; 2.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 8.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:SEJ09953.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:SEJ09953.1};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000313|EMBL:SEJ09953.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 83..353
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 626..659
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT BINDING 114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 866 AA; 96981 MW; 621B19ED3CA327EC CRC64;
MGRADRRWET IASLFHELLE MPDAARAEKL AFLSRTDSLL YRQLFDLLNA DRQSHRLFNT
ESGTIFSILE NDYDLIGSRI GAFVLTEVIG QGAMGTVFKA GRDDGLFDQT VAVKLMKPVS
VNPSHRSLFE RERQILAKLN HPNIARLYDG GFTEDERPFF TMEWVSGQNL IAYCQFRKLS
ITARLHLFED ICQAVMHAHQ SLIVHLDLKP KNIVVTEEGQ VKLLDFGVAQ MLEEGTEQVS
SFTLAYASPE QIEQNNPNTA SDIYSLGVIL FEMLVEDHPF ETFFKDPLAL KNAILAGYSS
PFRLSGKFGY VHFAKDIGLI CQKAMERAPR DRYASVDELI RDVRDFRNDY PVLARPKSWT
YHTQKYLRRN RTVLYAVGVG FLLLGIMGIY YTFQLKEQRN IALSEARRAN QITGLITDVF
SAADPNIGGA DTITAVQLLD KGMQNLSKNL GDDPALYADM LSRMTGVYLS LGQYEQAKQM
AAESYAINLS LDAVSEERLA QNEVLISSSY FMFGELDSAF SFSQKAVNRL LAAGIHNGPD
LADALLELGS CLYDMTRYEA ADSTLSVGLE LAQKAYSGST IEIASFLHMK GATAMKRDNL
QEAERYLEEA LKMKKELYEE PHLEIAYSYN YFGSLYQNLG DYKKALSFVK HSLEQRRAIL
GTYHVETVAS MGNLARTYIG LGKPLEAIPI YQDAISVIDS LFGGSHYYYG ALNGSMGNAY
FAAELFTKAR DCYLISVESF DRLLSADDLR RATPRMRLGE IAQNEKRFAA ARVYYEEALA
IRERLLNEGD VKIAQSQLGL GACLLALGDH AAAISLFEKA RLIAQSDPEQ NTELLQKLNA
SLASAQEKQR ALESASVYEV KISKGK
//
