ID A0A328VKG9_9CHLR Unreviewed; 1332 AA.
AC A0A328VKG9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RAQ94725.1};
GN ORFNames=A4R35_04200 {ECO:0000313|EMBL:RAQ94725.1};
OS Thermogemmatispora tikiterensis.
OC Bacteria; Chloroflexota; Ktedonobacteria; Thermogemmatisporales;
OC Thermogemmatisporaceae; Thermogemmatispora.
OX NCBI_TaxID=1825093 {ECO:0000313|EMBL:RAQ94725.1, ECO:0000313|Proteomes:UP000248706};
RN [1] {ECO:0000313|EMBL:RAQ94725.1, ECO:0000313|Proteomes:UP000248706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T81 {ECO:0000313|EMBL:RAQ94725.1,
RC ECO:0000313|Proteomes:UP000248706};
RA Tomazini A., Lal S., Stott M., Henrissat B., Polikarpov I., Sparling R.,
RA Levin D.B.;
RT "Analysis of Carbohydrate Active Enzymes in Thermogemmatispora T81 Reveals
RT Carbohydrate Degradation Ability.";
RL Submitted (AUG-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 -!- 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:RAQ94725.1}.
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DR EMBL; MCIF01000002; RAQ94725.1; -; Genomic_DNA.
DR OrthoDB; 3404503at2; -.
DR Proteomes; UP000248706; 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR045269; Atg1-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011528; NERD.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24348:SF22; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1.
DR Pfam; PF08378; NERD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR PROSITE; PS50965; NERD; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000248706}.
FT DOMAIN 11..123
FT /note="NERD"
FT /evidence="ECO:0000259|PROSITE:PS50965"
FT DOMAIN 153..461
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 482..731
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 513
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1332 AA; 150869 MW; 965BF0E61B6A2F45 CRC64;
MAELISTTIA FASDGEQQAA MVLRQGLPDS WLLICNKVFP AKNGRSFEID FLAIGNRCIF
VIDEKSWQGS LRGNEEFWTR ADGSSERSPL AKVDYVAKIV ASSVKERFAA LKGGEHFVHG
IVLLSSPTVQ PMIHDARASR GLFRLDEVCE RLQERDEQEG NPLVGQLHAA LKSWLTGLPT
RPPIPRHIGD TLQIEEAEQV RPKLYRCHAV GKISGANRPR IVMLYELDHD PLEQQEAKEF
YTRTYKALEK LQSTGLVSQA ETPFPWADRF MVVPIVPPEG RTLSALPLPE TREEFLQELQ
IAAKAFRGLA QIHAQGVLHR ALTPAALIVQ FTKGQSPRVL FSDFYAARVG GMSIAAKLDK
TAVDDPYAAE DVLIGYEFAT SQTDTFSLAL VMLERLSGTP IASLRPTVNE KPHLPDSPRW
TVFLAPEQSA ALTELFRSVL VPSQEEQSPS AAEVARCLEE IARQVQQKQV SDLPQTLLNG
TFVVQRLLGQ GSMARTYLAS YQEFPGLGPL VLKQFLQPAA VYDHAIQEYK ALENIKSKYF
PTIRQIYRPE EDAHIAMEYI PGPTLQQLEE EFPWSLERWW PFAQDLLRAL EVLEDRGILH
RDIKPANIIL HEVDHHPVLI DFGFAIRQGE ERSLAGTPLY LPPEALTAAS PPPDSDRYAA
AVVLFKALIG QLPFAYDESG RRILRAVEDL PISDEQVRRL AAVLLRALDP DPARRPVSAR
QFLEELEQAR LAAMVAAGET TPALESGQER EKRVNPWVEQ VRGLYRHSAS GNADNRGLDS
DFTRRTYVPT ALDRELLPLV LEQRPFALFL SGNPGDGKTA FLEQVRQKLI EQGASSIEER
SDQSGWELIY NGHVFRSCYD ASEAHRGLSA DEQLTQKLAG LEGSERPQAA LTVLVAINDG
RLADYFERYG ERFAWLKTQL QQARRSQSLR EQDVWLVDLK RRAFVSLPGE QERSLFRRVL
NSLLAKEHWA VCRNCCAEAI CPIYQNAQML RRNRTQQRLE YLLLLTHLRH QRHITMRDLR
SALAYLITGN LSCHEVHAAR QSEDGGASLI ERSCWQSAFA PAEIDDELLR DLRVLDPARF
PQPHLDRFLH FHQGPQDALL RAELMADAKD LPRQRFREER DWLAAWKRRL YFYGPRLDED
GQSYLPTVRW LDLLPYRYAL LYLQLLQGEQ EQLEETRSKL ALGILRSDGI NADLPDGHLS
VVVRASEEQQ LIMLKQLPLA DFILEPVGTS DNEVVETLPE FLVLRHRSGT PRLEISLDLF
ELLLRLADGL QPEAAELQPL LEDLRHFKHA LLLMETRDLI LIENGQRFHR LTQRDGKVIR
QPLLDPLEGG QL
//
