ID A0A1F8THR2_9CHLR Unreviewed; 1170 AA.
AC A0A1F8THR2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=A2Z37_00215 {ECO:0000313|EMBL:OGO71753.1};
OS Chloroflexi bacterium RBG_19FT_COMBO_62_14.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797671 {ECO:0000313|EMBL:OGO71753.1, ECO:0000313|Proteomes:UP000176680};
RN [1] {ECO:0000313|EMBL:OGO71753.1, ECO:0000313|Proteomes:UP000176680}
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 -!- 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:OGO71753.1}.
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DR EMBL; MGOM01000022; OGO71753.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8THR2; -.
DR Proteomes; UP000176680; 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; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
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 PANTHER; PTHR16305:SF28; ADENYLATE CYCLASE 10; 1.
DR PANTHER; PTHR16305; TESTICULAR SOLUBLE ADENYLYL CYCLASE; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 2.
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}.
FT DOMAIN 8..264
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1170 AA; 129021 MW; FA7C8C97FA3C8040 CRC64;
MALVGRRYQL LNELGAGGMG KLYRAVDRLT GRTLAVKRVA TPDGHPGGVS SGQNGDSARL
ALAQEFRLLA SLHHPHVINV LDFWFDESGQ PFFTMELQED AQTIVEAGKG QPQAVQVNLL
AQMLQALAYV HRRGIIHRDL KPGNVLVKGG QVKVVDFGVS ITRERPVETV AGTLAYMAPE
VLRGEGATEA SDLYAVGIIA YELLSGHKPY VAKDVHQLIT EILNTQPDLS GFGLSPEQEA
VLAQLLDKKP AARHSTAELA MEAICRAWGQ PQPQETPLIR ESYLQAAKLV GRGPELSQLA
SALDGMLEGR GSSWLVGGES GVGKSRLLDE LRAQALVRGA LVLRGQAIRE GGTPFQVWRD
AVRWVALISD LNDFECEVLK GLIPDIGGLL GREVNDAPQL EPEAALARLL TVVQDIFMRM
RQPAVLILED VHWAGSNSLT LLSRLNRVIE KLPVLILASY RDDERPEVSG LLPRMHEIHL
RRLTSASIAE LCEAMLGPGG RQPQVIALLS KETEGNPFFL VEVIRALAQE AGQLSMVGKK
HLPLQVFTGG MQRIIASRLS KISAKSRALL YYAAAVGRQL DLEVLRAIAP DVGLDTWLTV
CANAAVLELQ DGLWRFAHDK IRDALLNEVA ADKRPVLHAR IAAAIESVHP DSADQAAVLA
YHWRMAGDVA KEGKYAAVAG AQSLKNGAYK EAITFLTRAL EIEGPDGAVG QSRAHLELLL
GEAHNGQGQL KEARIHFGRA LEILGWSMPG SQAGLILGLL GQVLLQVLHR VSPPRESRRA
EARREQRLEA TRAYERLLEI AHFANETLLT LYAGLRALNL AEDAGPSSPE LARAYASMCY
AAGLAPLRSV AEDYRRRALQ IAADLKELPA MGWALFISGY YFTGLGLWDR SAKEISQALE
IYKRLGDLRR QGETTAVRSY THYFKGEFES GATSYVQLYE AARQRDDWQQ QAWALDGQAM
HLLRMGKTDQ ALALLRVAEP LFETINDRVE EIQHHGLLAL GHLRRGELEF ARVHADKAED
MIAQSRPSAP YAIDGYSTVV EVYLAIWESA SKPDERKEAI RMTRKALTSL EGFARVFPVG
RPRYWLWKGL SEWLDGKRSR AQRSWQQSLN LASHLQMPYE EALGHYEIGR HLTDSDRVRD
EHLDRACDLF SQLSAAYDWA HAKLALEGTA
//
