ID A0A1F1L0H9_9CORY Unreviewed; 812 AA.
AC A0A1F1L0H9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:OFS22434.1};
GN ORFNames=HMPREF3067_03655 {ECO:0000313|EMBL:OFS22434.1};
OS Corynebacterium sp. HMSC04H06.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1581050 {ECO:0000313|EMBL:OFS22434.1, ECO:0000313|Proteomes:UP000177657};
RN [1] {ECO:0000313|EMBL:OFS22434.1, ECO:0000313|Proteomes:UP000177657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC04H06 {ECO:0000313|EMBL:OFS22434.1,
RC ECO:0000313|Proteomes:UP000177657};
RA Ploux O.;
RL Submitted (MAR-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:OFS22434.1}.
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DR EMBL; LWPR01000028; OFS22434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F1L0H9; -.
DR STRING; 1581050.HMPREF3067_03655; -.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000177657; 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 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:0000313|EMBL:OFS22434.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000177657};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:OFS22434.1}; Transferase {ECO:0000313|EMBL:OFS22434.1}.
FT DOMAIN 165..446
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 812 AA; 89989 MW; E3CA2BC1DB330967 CRC64;
MTIPRRHAMT DRSDHMARGP ESDMDAATAA VPFDPFADGD EGETGTAAVA FDPFADDDED
DEFAADSDNI AALIKDLGNL RDKKARDAQQ VADTSQRSRQ KALDTFRSRR ATRRRDREVA
DGMVHLPFVS PSHPRQALLD VDEVVKRKKI PRPQLNPGDM VASQYEILGV IAHGGMGWIY
LANDHFVSGR VVVLKGMQAH KSADETAAAA AEREFLADIT HPGIVKIFNF IDDARVPGGF
IVMEYVGGPS LRSRRNAQPG KVLPIDIAIA YILELLPALD YLHSRGVVYN DLKPDNIIVT
EDQVKLIDLG AVSGIGAYGF IYGTQGFQAP EVSTQGPSVA SDIYTIGRTL AALTIDLPSE
DGIYLPGLPS PVKEPQFRRH LSFYRLLLRA TERDPDKRFR NLGELRTQLY GVLREVIAVR
DGVQHPSQHS LFSPQRTTFG TKHLVFRTDQ LIDGIDRTVR TTAPEVVSAL PTPLLDRSDV
GAALLQGASY TEPQEALETL RQAMQTDEYE QSAEIPLGVV RSMIDLGYTG QARSWLSSLE
QRLGGDWRFE WYSGVTALLL DDYAEAQKHF STVLSLLPGE AAPKLALAAI NELLLQQLGY
DDSCLLMPKV ARACAVQDLS LGDLPDEDFA GQPELWEHVT QDPGVLRFNS MRLYGLVWAT
NPTTVSSAFG LARQLRAEHQ VEMAVNTLDR VPNASRHQRM ARLTTVLQLI SHSLTEPRVR
RAARRLEEIP TNEPRFLQIK VAVLSAGLTF LRDHQLTHAA SPNDLFEYAF TQRGLRYGLA
DTLRALARQA PFSRHRYALV DLANQVRPVT TF
//