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Database: UniProt
Entry: U7KV98_9CORY
LinkDB: U7KV98_9CORY
Original site: U7KV98_9CORY 
ID   U7KV98_9CORY            Unreviewed;       979 AA.
AC   U7KV98;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=HMPREF1281_01886 {ECO:0000313|EMBL:ERS50718.1};
OS   Corynebacterium sp. KPL1855.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1203562 {ECO:0000313|EMBL:ERS50718.1, ECO:0000313|Proteomes:UP000017096};
RN   [1] {ECO:0000313|EMBL:ERS50718.1, ECO:0000313|Proteomes:UP000017096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KPL1855 {ECO:0000313|EMBL:ERS50718.1,
RC   ECO:0000313|Proteomes:UP000017096};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Jacobson B., Goguen K.,
RA   Pagano E., Lemon K.P., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA   Goldberg J., Gnerre S., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Corynebacterium sp. KPL1855.";
RL   Submitted (OCT-2013) 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:ERS50718.1}.
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DR   EMBL; AXLX01000029; ERS50718.1; -; Genomic_DNA.
DR   RefSeq; WP_023024037.1; NZ_KI515744.1.
DR   AlphaFoldDB; U7KV98; -.
DR   PATRIC; fig|1203562.3.peg.1816; -.
DR   HOGENOM; CLU_011707_0_0_11; -.
DR   Proteomes; UP000017096; 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   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   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT   DOMAIN          332..613
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          245..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..283
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   979 AA;  106975 MW;  EA81CF689C0CB0BF CRC64;
     MKHNPNFSED ELEYLEPENL DTQRQFRKPT KASYRDADRD QDPDQDRSQD RDLGATDSPD
     AASTASTADA ADPAGPDTAA ARPNSANRNI DVDTAATPHN AGNSNKGASE ADVDTAAAQV
     SGTAPAAAFP DTEATGRRTA GGSTAGPNAA GQRTTGPGAE GQGTAAQGVR NGNDADESDD
     AGDTGGVGTA AVAYDPFASE PIEHREDPGT SAVAFDPFAD DDEDDDGSID PDHLSSLLAD
     LENIRAQRES ERDEKTAQEK SSERSRRQAI DTFRERRGTQ RTERPVADGM VRLPFITPAN
     PTAALIDPTE KIKGKKVPPP QLEPGDMVAE QYEILGVIAH GGMGWIYLAN DHYVSGRVVV
     LKGMQAQKSA DETAAAEAER EFLADITHPG IVKIFNFIDD DRVPGGFIVM EYVGGPSLRS
     RRNKQPNELL PVDIAIGYIL EILPALEYLH SRGVVYNDLK PDNIIVTEDQ VKLIDLGAVS
     GIGAFGFIYG TQGFQAPEVA SKGPSIASDI YTIGRTLAAL CLKLPSEDGV FLPGIPNPSK
     EPELRRFLSL YRLLLRATHR DPQRRFSSIK ELRTQLYGVL REVLAIRDGR QYPSQHSLFS
     PQRTTFGTKH LVFRTDQLID GIDRTIQITA PEVVSALPTP LVDRDDVGAS LLQGTSYAEP
     QEALETLRQA MRTPEYEHSA EIPLGVVRSM IDLGYTDEAR QWLGSIEDRL GRDWRYQWYA
     GITELLHDDY VDAQEYFATV LDLLPGEAAP KLAIAAINEL ILQQIDYSET SLIDATVARA
     CSNLYTTLAD LPSSAFEGQP EVWSHVTQDP GALRFNSMRL YGIVWATNPT TVSSAFGLAR
     QLRAEGQVEL SVATLDKVPN ASRHFRMALL TTVLQLIVHD LSESRIRRAA RRLEEVPTNE
     PRFLQIKIAV ISAGLNFLRN ADLARASSPN DLFEYAFTQR GLRTGLAETL RALARQAPFS
     RHRYALVDLA NQVRPITTF
//
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