ID A0A0F6QXI1_9CORY Unreviewed; 798 AA.
AC A0A0F6QXI1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Protein kinase family protein {ECO:0000313|EMBL:AKE39992.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:AKE39992.1};
GN ORFNames=UL81_10290 {ECO:0000313|EMBL:AKE39992.1};
OS Corynebacterium camporealensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=161896 {ECO:0000313|EMBL:AKE39992.1, ECO:0000313|Proteomes:UP000033566};
RN [1] {ECO:0000313|EMBL:AKE39992.1, ECO:0000313|Proteomes:UP000033566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44610 {ECO:0000313|EMBL:AKE39992.1,
RC ECO:0000313|Proteomes:UP000033566};
RX PubMed=26021938;
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete Genome Sequence of Corynebacterium camporealensis DSM 44610,
RT Isolated from the Milk of a Manchega Sheep with Subclinical Mastitis.";
RL Genome Announc. 3:e00572-15(2015).
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; CP011311; AKE39992.1; -; Genomic_DNA.
DR RefSeq; WP_046453553.1; NZ_CP011311.1.
DR AlphaFoldDB; A0A0F6QXI1; -.
DR KEGG; ccj:UL81_10290; -.
DR PATRIC; fig|161896.4.peg.2005; -.
DR HOGENOM; CLU_011707_0_0_11; -.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000033566; 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-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 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:AKE39992.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033566};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000313|EMBL:AKE39992.1}.
FT DOMAIN 150..396
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 798 AA; 88756 MW; A852D920A400321F CRC64;
MDPKPTERTE DTARTEHEDV GTQAVQYDPF ADDESEPGTS AVAFDPFADE DEDDEGLGTD
ADDIAALLAD LDNLRDRPHK EDPSQRSRRQ ALDTFRERRS TRRTDRHVAD GMVTLPFVVP
VNPQDALIDP EEKKAPAPQL QPGDMVAGQY EILGVIAHGG MGWIYLANDH FVSGRVVVLK
GMQAHKSEDE TAAAAAEREF LADITHPGIV KIFNFIDDAR VPGGFIVMEY VGGPSLRQHR
NTQPNKLLPI DIAIAYILEI LPALDYLHAR GVVYNDLKPD NIIISEDQVK LIDLGAVSGI
GAFGYIYGTR GFQAPEVARE GPSIASDIYT IGRTLAALTL PLPVSEEGTY HPGIPSPSAI
PELRHYLSFY RLLLRATDRD PKRRFSNIEE LRTQLYGVLR EVIALRDGIQ HPAQHSMFSP
QRTTFGTKHL VFRTDQLIDG IDRTVRITAP EVVSALPTPL LDRSDIGAAL LQGASYTEPQ
EALETLHQAM QTEEYEHSAE IPLGVVRSMI DLGYTRQARQ WLASIADKLG DDWRFQWYSG
VAELLHDDFV DAQKHFARVL EQLPGEPAPK LAIAAINELL LQQLGYNEAS LLDGPIARAS
ANITTSLGAM DNEHFEDQPE LWDHITQDPA MLRFNSMRLY GIVWATNPTT VSSAFGLARQ
LRAEGQIELA VSTLDKVPNA SRHHRMARLT TILQLITQDL TESRIRRAAR RLEEIPTNEP
RFLQVKVAVV SAGLNFLRGN NLAKAASPND LFEFAFTQRG LRYGLADTLR ALARQAPYAR
HRYALVDLAN QVRPVTTF
//