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Entry: A0A1F1V0F1_9CORY
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ID   A0A1F1V0F1_9CORY        Unreviewed;       802 AA.
AC   A0A1F1V0F1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:OFT31838.1};
GN   ORFNames=HMPREF3171_01140 {ECO:0000313|EMBL:OFT31838.1};
OS   Corynebacterium sp. HMSC08F01.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1581139 {ECO:0000313|EMBL:OFT31838.1, ECO:0000313|Proteomes:UP000176366};
RN   [1] {ECO:0000313|EMBL:OFT31838.1, ECO:0000313|Proteomes:UP000176366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMSC08F01 {ECO:0000313|EMBL:OFT31838.1,
RC   ECO:0000313|Proteomes:UP000176366};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-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:OFT31838.1}.
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DR   EMBL; LWNT01000023; OFT31838.1; -; Genomic_DNA.
DR   RefSeq; WP_070482303.1; NZ_KV789281.1.
DR   AlphaFoldDB; A0A1F1V0F1; -.
DR   OrthoDB; 137117at2; -.
DR   Proteomes; UP000176366; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
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:OFT31838.1};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000313|EMBL:OFT31838.1}; Transferase {ECO:0000313|EMBL:OFT31838.1}.
FT   DOMAIN          146..391
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          68..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   802 AA;  88014 MW;  C133FBA28480E781 CRC64;
     MAKPHDHDDV QPTEAVAFDP FADDEPGTEA VAFDPFADDD DLDDDSDAAY AGLGEMAGLL
     KDLDKLRKGS GREDTSQRSR QAALDTFRER RGTRRASRII ADGMVELPWV EPTEPREALI
     DPEPAVVKKG IAPPVLHPGD IVAGQYEITG VIAHGGMGWI YLAQDHYVAG RVVVLKGLHS
     TDNPDEAAAA EAEREFLADI THPGIVKIFN FIDDPRVPGG FTVMEYVGGP SLRARRNSSP
     SGVLEPDIAI AYILEVLPAL DYLHSRGVVY NDLKPDNIIV TEDQVKLIDM GAVSGIGAYG
     FIYGTKGFQA PEVATEGPSI ASDIYTVGRT LASLVADLPQ TDGIYDPGLP TPTDEPLFRQ
     YTSLYRLLAR CCNEDPARRF DSVSELESQL LGVLREVVAV HDGRTYPAQH SLFSPQRRTF
     GTKHLVFRTD QLIDGISRTV DITPQEVVAA LPSPLINRDD VGAAMLQGSS YAEPRETLET
     LRQAMTTPQY EHSVEIPFGV VRTMIDLGLT SQARSWLLTL QDRFGDTWRF SWYSGVVEML
     LGDFPTATRS FSEVLNQLPG EAAPKLALAA VSELLLQERG LQEQSLIDDS LARTATNLEH
     PLSNVPTTVL RAMVENGQMD PTWTVTALEP GALRFHAIRL YSLVWLTNPT TVSSAFGLAR
     MLMREGETDL ALRALDKVPN ASRHSRMAQL TAILYLVLPV AGTGADPTEA QIREAAARLD
     QIPTTEPRFL QIKTAVLDAA LHYLVTEGSA NTPTLFEYSF TEREIRHGLA QTLRAQARVA
     PYAQHRYALV DMANKVRPAT WF
//
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