ID E0DDH9_9CORY Unreviewed; 761 AA.
AC E0DDH9;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Kinase domain protein {ECO:0000313|EMBL:EFM49431.1};
GN ORFNames=HMPREF0299_7496 {ECO:0000313|EMBL:EFM49431.1};
OS Corynebacterium matruchotii ATCC 14266.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=553207 {ECO:0000313|EMBL:EFM49431.1, ECO:0000313|Proteomes:UP000004218};
RN [1] {ECO:0000313|EMBL:EFM49431.1, ECO:0000313|Proteomes:UP000004218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14266 {ECO:0000313|EMBL:EFM49431.1,
RC ECO:0000313|Proteomes:UP000004218};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (AUG-2010) 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:EFM49431.1}.
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DR EMBL; ACSH02000004; EFM49431.1; -; Genomic_DNA.
DR RefSeq; WP_005525093.1; NZ_ACSH02000004.1.
DR AlphaFoldDB; E0DDH9; -.
DR STRING; 553207.HMPREF0299_7496; -.
DR eggNOG; COG0515; Bacteria.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000004218; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR031636; PknG_TPR.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24363:SF0; SERINE/THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF16918; PknG_TPR; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EFM49431.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004218};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000313|EMBL:EFM49431.1}.
FT DOMAIN 121..402
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 84329 MW; 04017C26DF1535D1 CRC64;
MTDTDHTQPH STADHTQPQT AAVPFNPFDD DDDTFNTAAA PFNPFDDDDD DPLPDPSARS
RTEALNTFRS RRSTTREGRS VANGMVRLPF VPIKETRLMD PATTNLEPPL LKEGDIVANQ
YKILGVVAHG GMGWIYLAQD QNVSGRVVVL KGLIGSGNPH DIGAAIAERE FLADITHPVI
VKAYNFIDDP RVAAGFIVME YVPGPSLRKR RQEQPGGVFA IDIAIGYILE TLPALEYLHA
RGVVYNDFKP DNIIVTEDQV KLIDLGAVTG IGAFGYIFGT KGFQAPEVAT EGPSVASDIY
TVGRTLAAMT INMPKKDGAY APGLPGPDEE PLFAQYLSYY RLLRRATDPD PKQRFSTVQE
LTTQLYGVLR EYLAVHDGRQ FPAQHSLFSP QRSTFGTKHI VFKTDQLIDG IERSVRITPP
EVVAALHVPL LDRSDPGAAM IAGSSYTEPS EALETMREAM AREKFAQSKE IPLGIIRSLL
DLGFTTESKD WLKKLESSLG DDWRYQWYSG ITSLLLDDFL PAQDAFNKVF NILPGEAAPK
LARAAVCELI LQSKGMDNKP LLQPATAIEV ASLKGEIVNE LAGLWTHLTQ DPAVLRYKAI
YLYSLVWATN PATVSSGFGL ARQLMAERQV DVAVQALDKV PASSMHRRMA ELTSVLYLVS
DVPNEQRIRR AARRLEEIPT NEPRFLQVQI AVLNAALHWL RLEGLEASAS RNDLFDYPFT
QLGLRRGLER ALRLQARSAP TAAHRYQLVD TSNKIRPRTW F
//