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Database: UniProt
Entry: A0A0F6QXI1_9CORY
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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
//
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