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Database: UniProt
Entry: A0A109IPC2_9ACTN
LinkDB: A0A109IPC2_9ACTN
Original site: A0A109IPC2_9ACTN 
ID   A0A109IPC2_9ACTN        Unreviewed;       661 AA.
AC   A0A109IPC2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=GA0070623_5405 {ECO:0000313|EMBL:SCG81032.1};
OS   Micromonospora rifamycinica.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=291594 {ECO:0000313|EMBL:SCG81032.1, ECO:0000313|Proteomes:UP000198226};
RN   [1] {ECO:0000313|EMBL:SCG81032.1, ECO:0000313|Proteomes:UP000198226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44983 {ECO:0000313|EMBL:SCG81032.1,
RC   ECO:0000313|Proteomes:UP000198226};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-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};
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DR   EMBL; LT607752; SCG81032.1; -; Genomic_DNA.
DR   RefSeq; WP_067301903.1; NZ_LT607752.1.
DR   AlphaFoldDB; A0A109IPC2; -.
DR   OrthoDB; 308915at2; -.
DR   Proteomes; UP000198226; Chromosome i.
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   GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR   CDD; cd06577; PASTA_pknB; 4.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.30.10.20; -; 4.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR045269; Atg1-like.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR005543; PASTA_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR   PANTHER; PTHR24348:SF22; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR   PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1.
DR   Pfam; PF03793; PASTA; 4.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 4.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51178; PASTA; 4.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:SCG81032.1};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:SCG81032.1};
KW   Transferase {ECO:0000313|EMBL:SCG81032.1}.
SQ   SEQUENCE   661 AA;  70224 MW;  24A25E3EE3BF5DA4 CRC64;
     MDIQVADTLL GSLLDGRYRI RGRVARGGMA TVYTATDERL ERTVAVKIIH PSQATEARSR
     LAGFPGRFTD EAKAIARLTH PNVVAVYDQG THQGLPYLVM EYVRGRTLRE VLAERRRLNP
     DEALAIMEQM LAAIAAAHRA GLVHRDVKPE NVLVAEAPTG GVANLVDSVV KVADFGLARA
     VEASAEEGDG NQLMATVAYV APELVTDGQA DPRTDVYSAG IVLFEMLTGR VPYDGDRPVE
     VAWQHVDRDV PAPSILVPGL PRVLDELVGR ATRRDPGARP ADAGALLAEV QVARDELGNP
     NAHTAVLGRV GEELPAVAQP TMVVAAVSPV NRPTWARLPE PVAPQRPHRR RAVEDAALGS
     RFAQLRTRVM GTPRGRLSVA AAVVVIGLLA AMGGWWVGVG RYTVAPQLVN LSRADAQAQA
     DRAGFRLSFA EPRYDEKIPR DGVVAQDPGS AAKILKGGTI TLTLSLGPER FPVPDVVGKE
     FDLAEADLTG AKLVVAKGSP RYDDNLPAGV VVDTNPKVGT EVKPGTKVTV ILSRGRAPVT
     VPDLVGKSLG DARTALSQLG LVAVETYKES DKPRDEVLGQ SPADGAGVEK GTKVKLDVSK
     GPPQVTVPRV VDLPCQQAKQ QLEGAGFTVN VQFNPNGIVR FQNPGENSQV PPGTPVTLGC
     L
//
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