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Database: UniProt
Entry: E0DDH9_9CORY
LinkDB: E0DDH9_9CORY
Original site: E0DDH9_9CORY 
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
//
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