ID A0A1I1E559_9FIRM Unreviewed; 738 AA.
AC A0A1I1E559;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Tetratricopeptide repeat-containing protein {ECO:0000313|EMBL:SFB82207.1};
GN ORFNames=SAMN02910398_00747 {ECO:0000313|EMBL:SFB82207.1};
OS Butyrivibrio sp. YAB3001.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1520812 {ECO:0000313|EMBL:SFB82207.1, ECO:0000313|Proteomes:UP000198944};
RN [1] {ECO:0000313|EMBL:SFB82207.1, ECO:0000313|Proteomes:UP000198944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YAB3001 {ECO:0000313|EMBL:SFB82207.1,
RC ECO:0000313|Proteomes:UP000198944};
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; FOKR01000003; SFB82207.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1E559; -.
DR STRING; 1520812.SAMN02910398_00747; -.
DR Proteomes; UP000198944; 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-EC.
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; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
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; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13174; TPR_6; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 3.
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.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000198944};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..323
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 637..670
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 738 AA; 85079 MW; 3EEAB9BB60C13293 CRC64;
MNSNDKKKSF LETYEIKEQL GEGSGGTVYK AYHKNLRKDV VLKKMNEKAA EVLNKRTETD
ALKNLRHSYI PQVLDFVELD DGIYTVMDYI PGTTFKKLMD TGRRFSQKEA LKYARQLFET
LEYIHSRKPK IIHGDIKPDN IMLTPEDNIC LIDFNISGIA DGEGAVIDGF SYDYSAPEQV
EGFKRKREQK TKQSDENFEY EKTEIISAEA ENNDDYEKTS LVEEAFLDKD ELRYENVNTD
HKQDFYIDER ADIYSAAASI YHILTGVRPK VKEGRIPPAN SIDPKISEGF SYILEHAMEQ
KPDKRFQSSS DVLKALNEIH KLDNRYKKLI RQQNLLFCVA IFMMSVGVAL IFNGINSRKM
DNLSTYDRNI ELMTEMIRKA QNGDEISSQE FDELYDECVK INNKQLDVYL NKAIFLYTQK
NYDAAIEYLE ENVLDDPVLS VQTDLETAYY IYGSSLKNCE EPDYESAIES MEKAISKGYT
NASCYRELAE TYLVIGKLAK AKEILSEAEE KSVSGADMDL MAGEVNLAQN NYSDAKKNYE
SCIEKALLTG DYDVLLRAYL GLNELIITEN KNETSLNEAV SVLNKAMNNL PGDYQLQVVQ
SQIQNYVDLY QLTQDSVFAE KGIELLEKSI SRGWKDYTNY VNLAFLYEQK ADYNKAKEIL
EKLMNEYPDN YVAYKRMAYL EVDVQKNKEV NEREYSFFAY CYETAKTKYK NSKKIGGDLE
MDYLDAMYSE AVENGWIE
//
