ID A0A1F9G5J5_9DELT Unreviewed; 566 AA.
AC A0A1F9G5J5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=A2138_03305 {ECO:0000313|EMBL:OGQ26800.1};
OS Deltaproteobacteria bacterium RBG_16_71_12.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=1797848 {ECO:0000313|EMBL:OGQ26800.1, ECO:0000313|Proteomes:UP000176731};
RN [1] {ECO:0000313|EMBL:OGQ26800.1, ECO:0000313|Proteomes:UP000176731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
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:OGQ26800.1}.
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DR EMBL; MGQY01000004; OGQ26800.1; -; Genomic_DNA.
DR Proteomes; UP000176731; Unassembled WGS sequence.
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; IPR013229; PEGA.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF08308; PEGA; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}.
FT DOMAIN 48..319
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 329..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 566 AA; 59581 MW; 436368071687784B CRC64;
MKSCPRCGKS YEDDQAYCGV DGASLSGSIT TPAPDSRTLR SGAQIGVYRI LSVIGKGGMG
IVYAAEHTRL GKRVAIKVLR SELVEDDVQV ARFFAEARTA NSVGHENIVE VHDFIEEGPH
RAFVMELIEG TTLSRELIAE QPLPLPRLAR IGRQVADALA AVHEKQIVHR DLKPDNIFLT
TRARQPDFVK LLDFGIAKLM QSSGDTLTQA GQVLGTPAYM APEQLRGEAI GPAADIYSLG
VILYQMASGK RPFKSKSVPE LMMKQVHDPP PPFSXXPGLP KVDVSLEKLI KQCLDKDPAK
RPSDMREVER RLAAIEELVT GGFFSGPHAP SSSASIPAAP GPPPAAFPAG ATTTIEAEPT
PGTTSGAARA LDRDLLPTDE GAAVDVDPIA SELEGRPLGR RRARLAAAAA ALAVAGVFAA
VALAGGDEAP ADRAGQPSAP AAKPLLVRVE TTPPGAQLRL GESLIGASPV TLTLDRSAGG
RELLIELSGY QPVTHALPTE DGAITEALVA VPTPAEVEDQ VGAPTKTHTP EPAAEATRPA
KPKPTAKPAK PKPAKRPKEA PLDPFK
//
