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Database: UniProt
Entry: U5E410_NOCAS
LinkDB: U5E410_NOCAS
Original site: U5E410_NOCAS 
ID   U5E410_NOCAS            Unreviewed;       833 AA.
AC   U5E410;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=pknG {ECO:0000313|EMBL:GAD83467.1};
GN   ORFNames=NCAST_20_00320 {ECO:0000313|EMBL:GAD83467.1};
OS   Nocardia asteroides NBRC 15531.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1110697 {ECO:0000313|EMBL:GAD83467.1, ECO:0000313|Proteomes:UP000017048};
RN   [1] {ECO:0000313|EMBL:GAD83467.1, ECO:0000313|Proteomes:UP000017048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 15531 {ECO:0000313|EMBL:GAD83467.1,
RC   ECO:0000313|Proteomes:UP000017048};
RX   PubMed=24884595; DOI=10.1186/1471-2164-15-323;
RA   Komaki H., Ichikawa N., Hosoyama A., Takahashi-Nakaguchi A., Matsuzawa T.,
RA   Suzuki K., Fujita N., Gonoi T.;
RT   "Genome based analysis of type-I polyketide synthase and nonribosomal
RT   peptide synthetase gene clusters in seven strains of five representative
RT   Nocardia species.";
RL   BMC Genomics 15:323-323(2014).
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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAD83467.1}.
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DR   EMBL; BAFO02000020; GAD83467.1; -; Genomic_DNA.
DR   RefSeq; WP_019049697.1; NZ_VBUS01000001.1.
DR   AlphaFoldDB; U5E410; -.
DR   STRING; 1824.SAMN05444423_101766; -.
DR   eggNOG; COG0515; Bacteria.
DR   Proteomes; UP000017048; Unassembled WGS sequence.
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   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; IPR031634; PknG_rubred.
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; PF16919; PknG_rubred; 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:GAD83467.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017048};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000313|EMBL:GAD83467.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          214..481
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..58
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   833 AA;  89356 MW;  AA8B7258CFC11A19 CRC64;
     MSTEPPPNGE PAQEDPARQE PTQLTQRPEG QLPGGWTLPP APAEDETMPL PVPPPKQAAH
     APTEIAAARP PATQATQRAA VAPATEAAFR VTEPPGTQAT PVESGGATWA SSPQTGPSTA
     RSGRSVRTAR SRPTRRLGAG LVPIPTVTPA DPRDAVLADP VVSEGRRFCW RCANPVGRST
     PAHAASSAGV CETCGAAYDF RPSLHEGDMV AGQYEIQGCI AHGGLGWIYL AIDRNVSDRW
     VVLKGLLHAG DAEAQAVAVA ERQFLAEVAH PSIVKIHNFV EHTAPDGSSI GYIVMEYVGG
     HSLRDILEAR PAGERMPLAE AIAYVLEILP ALDHLHSIGL TYNDLKPDNV MVTEDQVKLI
     DLGAVATIEA YGNLYGTKGF QAPEIARTGP TPASDVYTVG RTLAALTLHL PSEHGRYLDG
     IPDPAAEPLL ARYEFFHRFL LTATDTDPAL RFPSARAMSA QLAGVLREIL AYDTGSEHPQ
     LSTVFSPQRT SFGTEELISQ TDAYLDGVGR SPLLDSGDVV AALPIPLIDP ADPSAPLLAA
     TANLEPERVL EALHEARERA EADPDNAPET LAGELVFAEA RARLELGESA AVLHLLERVL
     GDTDWRADWF TGQAHLLELD FEAAFASFEA VLRVLPGEIA PKLALAATAE LILQHWDTDA
     PEQWRSFAER YYDTVWRTDR AVVSAAFGLA RQLAIAGRVG EAVHALDDVP AASRHFTTAQ
     TTAILLLLTS TPVADLDEQI LRLAASRAQA IPPGEHRATL MRTLVQGTAL AWLQAGNTPK
     RKDAKLFGRP FDERDLRDGT ESGLRALARN APGRAHRYAL VDLANAIRAK SWF
//
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