ID A0A1G5RSI7_9FIRM Unreviewed; 655 AA.
AC A0A1G5RSI7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:SCZ76956.1};
GN ORFNames=SAMN03080599_00492 {ECO:0000313|EMBL:SCZ76956.1};
OS Acidaminobacter hydrogenoformans DSM 2784.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XII. Incertae Sedis; Acidaminobacter.
OX NCBI_TaxID=1120920 {ECO:0000313|EMBL:SCZ76956.1, ECO:0000313|Proteomes:UP000199208};
RN [1] {ECO:0000313|EMBL:SCZ76956.1, ECO:0000313|Proteomes:UP000199208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2784 {ECO:0000313|EMBL:SCZ76956.1,
RC ECO:0000313|Proteomes:UP000199208};
RA de Groot N.N.;
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};
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; FMWL01000002; SCZ76956.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5RSI7; -.
DR STRING; 1120920.SAMN03080599_00492; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000199208; 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; cd06577; PASTA_pknB; 3.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR005543; PASTA_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF03793; PASTA; 3.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:SCZ76956.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000199208};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:SCZ76956.1};
KW Transferase {ECO:0000313|EMBL:SCZ76956.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 342..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..274
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 369..436
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 437..503
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 506..573
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 655 AA; 72270 MW; 1CBFCF9B6F3E7151 CRC64;
MDRIIGRVLK NRYEILDKIG DGGMALVYRA KDMLLDRSVA IKILRPEFVS DEEFIRKFDK
ESKAAASLSH PSIVSVYDVG HEEDLRYIVM EFINGPTLKK YIKDHDGFFE NREIIRVAKQ
VARALENAHA NHIVHRDIKP HNILMGADGA VKVADFGIAR AITSATIINT TDMMGSVHYA
SPEQSRGGFV DEKSDIYSLG ILMYEMAAKR LPFEGESAVA VALKHLKEEA HAPSDFNPAL
SVGLEGVILK AIQKNPEFRY GSVTEMLNDL DEVLLRPDHI VMIEGGDEDA KTMMIPKIDE
ELLFNDTRSI ENTNPTRFVQ RKLAEEVEPE PEVPQKTDKK RLIITVLLAL IAAFVFIGAG
FMMKNLLEET QPVPVPNVTG LDVDVALQLL EDHSFKGEIG DRIYSRSYAP DEVISQSHEE
GALLKPGYTI TLTLSLGTEL FQVPNLVQKP LAEAEIMIVN AGFKVGSVDE IENDAPEGTV
ISQSPFAGLS EEKGTAIDLY VSKGKTPGKS IMPKIVGSAL ESARMTLEQY GISVGEVKYD
FSDTFAANLV IAQSIEGGQE VQPEDRVDLV VSKGKDPNST PEPVEKTLTI PLEFDQEEFE
VKVVMVKDGA SEIVYQKLHS KAEERVSVTI SGTGTVGINI YFNDVLVSSS EEVFN
//
