ID   A0AAN1HQD5_9ACTN        Unreviewed;       620 AA.
AC   A0AAN1HQD5;
DT   02-OCT-2024, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2024, sequence version 1.
DT   27-NOV-2024, entry version 2.
DE   SubName: Full=Serine/threonine-protein kinase PrkC {ECO:0000313|EMBL:AUA13102.1};
DE            EC=2.7.11.1 {ECO:0000313|EMBL:AUA13102.1};
GN   Name=prkC_4 {ECO:0000313|EMBL:AUA13102.1};
GN   ORFNames=CFP59_05257 {ECO:0000313|EMBL:AUA13102.1};
OS   Streptomyces sp. M56.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1495638 {ECO:0000313|EMBL:AUA13102.1, ECO:0000313|Proteomes:UP000232019};
RN   [1] {ECO:0000313|EMBL:AUA13102.1, ECO:0000313|Proteomes:UP000232019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M56 {ECO:0000313|EMBL:AUA13102.1,
RC   ECO:0000313|Proteomes:UP000232019};
RA   Kim K.K.Hyun., Klassen J.L., Ruzzini A.A.C., Beemelmanns C.C., Clardy J.J.;
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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DR   EMBL; CP025018; AUA13102.1; -; Genomic_DNA.
DR   Proteomes; UP000232019; Chromosome.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR050660; NEK_Ser/Thr_kinase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43671:SF13; LD04361P; 1.
DR   PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:AUA13102.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Transferase {ECO:0000313|EMBL:AUA13102.1}.
FT   DOMAIN          127..394
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..40
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..91
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         156
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   620 AA;  65986 MW;  4F98DEBA5E015340 CRC64;
     MTNDGGRANE PTSYSLRPPH APAAPVPAPQ PPPEASDAPP QGSRPPGRAA EAAVPARSAY
     EPTQFADPRG GPQPPTGEPP TGEPPTGEPP AGELPTGDRS AEEPSAGRQP AAGAQDPNSG
     RLIGGRYQLV SRLGHGGMGT VWRAHDQIVD RDVAVKEPRV PDHLPERERQ TVYQRMQREA
     RAAARIDHPS VVTVHDVVVE GGRPWIVMEL VRGQSLGDRL MEGTLDPREA ARIGLSVLGA
     LAAAHEAGVL HRDVKPDNVL LGRSGRVVLT DFGIAQIEGE QRLTETGGFV GSPEFIAPER
     VLGQRPGPES DLWSLGVVLY AAVEGMSPFR RSHAPATLQA VLGSEPQVPA RATGPLATLI
     MQLLRKDPAM RPAAPEVRQA LEAAAKEPQP VPTMLATAGY APGGAQRSAG GRFVPPILHK
     NRKAQLGLGG LVLVVAAALV LTIMKPFSGE GLPPGWTVRE ERDVVGASLA VPGEYRRVQD
     DSDSDNPVVT YYDPSGVFTV SLKRSTPDGE NDPASLDAAA DQIVAFYKDG GGATVEEAKS
     EQTEAGQQGK AARDVTTSYL PYGTSSNKNP IRYVKRDHLY LNKAKVAWDL TVTMPAHGDA
     QERGEELYER IVRNLRIDQL
//