ID E6TI57_MYCSR Unreviewed; 365 AA.
AC E6TI57;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Predicted aminoglycoside phosphotransferase {ECO:0000313|EMBL:ADT99060.1};
GN OrderedLocusNames=Mspyr1_24180 {ECO:0000313|EMBL:ADT99060.1};
OS Mycolicibacterium gilvum (strain DSM 45189 / LMG 24558 / Spyr1)
OS (Mycobacterium gilvum).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=278137 {ECO:0000313|EMBL:ADT99060.1, ECO:0000313|Proteomes:UP000008916};
RN [1] {ECO:0000313|Proteomes:UP000008916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45189 / LMG 24558 / Spyr1
RC {ECO:0000313|Proteomes:UP000008916};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., LaButti K., Ivanova N.M., Mikhailova N.M., Land M., Hauser L.,
RA Koukkou A.I., Drainas C., Kyrpides N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium sp. Spyr1.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADT99060.1, ECO:0000313|Proteomes:UP000008916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45189 / LMG 24558 / Spyr1
RC {ECO:0000313|Proteomes:UP000008916};
RX PubMed=22180818;
RA Kallimanis A., Karabika E., Mavromatis K., Lapidus A., Labutti K.M.,
RA Liolios K., Ivanova N., Goodwin L., Woyke T., Velentzas A.D.,
RA Perisynakis A., Ouzounis C.C., Kyrpides N.C., Koukkou A.I., Drainas C.;
RT "Complete genome sequence of Mycobacterium sp. strain (Spyr1) and
RT reclassification to Mycobacterium gilvum Spyr1.";
RL Stand. Genomic Sci. 5:144-153(2011).
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DR EMBL; CP002385; ADT99060.1; -; Genomic_DNA.
DR RefSeq; WP_011893979.1; NC_014814.1.
DR AlphaFoldDB; E6TI57; -.
DR KEGG; msp:Mspyr1_24180; -.
DR HOGENOM; CLU_061751_0_0_11; -.
DR Proteomes; UP000008916; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031326; P:regulation of cellular biosynthetic process; IEA:UniProt.
DR Gene3D; 3.90.1200.10; -; 1.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR015897; CHK_kinase-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR23020:SF41; AMINOGLYCOSIDE PHOSPHOTRANSFERASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR23020; UNCHARACTERIZED NUCLEAR HORMONE RECEPTOR-RELATED; 1.
DR Pfam; PF01636; APH; 1.
DR SMART; SM00587; CHK; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Transferase {ECO:0000313|EMBL:ADT99060.1}.
FT DOMAIN 112..291
FT /note="CHK kinase-like"
FT /evidence="ECO:0000259|SMART:SM00587"
FT BINDING 61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 365 AA; 39131 MW; 08E0E1531244AF21 CRC64;
MTIPRTPADL TPTWLESVLD AGVDDVTVTA IGTGQTGATY RVSATYDNPT AADLPATFAV
KLPAQDDAVR ERVALGYLSE VDFYSTITAD VAVPVPGCYH SEISSDGTDF VLVLADMAPA
EQGDQIAGCT AAEAALAVEA IAGLHGPSWG DRRYFDLPSI VMPKPGDEAA ASGMGEVAVM
AANMTLEKLG GSVDDEDRDT LLTSMSLVTP WLMAVPDRFS LMHGDYRLDN LLYDPERTRV
TVVDWQTVGI GLPTRDLAYF TATSLLPDDR AAVERDLVQR YHAALLAHGV SGYDVETCWQ
DYRLGVFQAP LITALGFAFA ASTERGDEMI LTMLHRGCRA IRELGAIDLV RSYQASTQPS
SPTTA
//
