ID A0A0G3GYU4_9CORY Unreviewed; 791 AA.
AC A0A0G3GYU4;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:AKK04032.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:AKK04032.1};
GN ORFNames=CEPID_11015 {ECO:0000313|EMBL:AKK04032.1};
OS Corynebacterium epidermidicanis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1050174 {ECO:0000313|EMBL:AKK04032.1, ECO:0000313|Proteomes:UP000035368};
RN [1] {ECO:0000313|EMBL:AKK04032.1, ECO:0000313|Proteomes:UP000035368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45586 {ECO:0000313|EMBL:AKK04032.1,
RC ECO:0000313|Proteomes:UP000035368};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium epidermidicanis DSM 45586,
RT isolated from the skin of a dog suffering from pruritus.";
RL Submitted (MAY-2015) 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};
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DR EMBL; CP011541; AKK04032.1; -; Genomic_DNA.
DR RefSeq; WP_047240940.1; NZ_CP011541.1.
DR AlphaFoldDB; A0A0G3GYU4; -.
DR STRING; 1050174.CEPID_11015; -.
DR KEGG; cei:CEPID_11015; -.
DR PATRIC; fig|1050174.4.peg.2220; -.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000035368; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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:AKK04032.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035368};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:AKK04032.1}; Transferase {ECO:0000313|EMBL:AKK04032.1}.
FT DOMAIN 144..425
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 791 AA; 87165 MW; 562C45CC78D09929 CRC64;
MADNDHSLEP TNATEAVAFN PFDDDEDELT ALVNELDSLR EKTSAAARFD PFADDEDDET
GLDTAAVYAI AADQSEDVND RSRREALSTF RSRRGTTRAG RMVADGMVQL PFVPITDPQA
ALITPGPNVE PPTLKPGDMV AAQYEVLGVI AHGGMGWIYI ANDRNVSGRW VVLKGMIPGG
NPRDLGTAVA EREFLADITH PEIVKIYNFI DDARVPGGFI VMEFVGGPSL LDRRRAQPDN
VLPVDVAIAY ILEILPALEY LHSRGVVYND LKPDNIIVTE DQVKLIDLGA VSGIGAFGYI
YGTKGYQAPE VSTEGPSVAS DIYTIGRTLA ALVCRLPVVD GQLAPGLPSP FEEPLFRKHL
SLYRLLIRAT HSNPARRFRD VHELRTQLYG VLREILAVRD GKQFPAQHSL FSPQRTTFGT
KHQVFRTDQL IDGIERTVRI TPPEVVAALP VPLIDRTDSG FTMLTGSSYT EPSEALETMR
QALNSGEYTD SVELPLGIVR TLLDLGFVAE AHSWVGSLAE RLELDWRYQW LAGVTSLLLD
RFIDAQDHFN NVLSILPGEA APKLALAAVD ELLLQQAGVD GQAHLAPEVT QAVAELGGSL
TDLPPEFLAK LESNWSHITA DPMALRFHSM RLYRLVWVTN PTTVSAAFGL SRQLMAEGHS
ELAIAALDRV SQNSRHHRMA KLTSILQLIS GDLTESRIRR AARRLEEIPT NEPRLLQIRV
AVLNAGLQWL RSHDLSAAAS PNDLFDYPFT QRGLRTGLSE TLRLLARSAP FPRHRYALVD
MANAVRPTTW F
//
