ID   A1T414_MYCVP            Unreviewed;       993 AA.
AC   A1T414;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   SubName: Full=Protein kinase {ECO:0000313|EMBL:ABM11914.1};
GN   OrderedLocusNames=Mvan_1076 {ECO:0000313|EMBL:ABM11914.1};
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM11914.1, ECO:0000313|Proteomes:UP000009159};
RN   [1] {ECO:0000313|EMBL:ABM11914.1, ECO:0000313|Proteomes:UP000009159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1 {ECO:0000313|Proteomes:UP000009159};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000511; ABM11914.1; -; Genomic_DNA.
DR   RefSeq; WP_011778349.1; NC_008726.1.
DR   AlphaFoldDB; A1T414; -.
DR   STRING; 350058.Mvan_1076; -.
DR   KEGG; mva:Mvan_1076; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG3055; Bacteria.
DR   HOGENOM; CLU_296626_0_0_11; -.
DR   Proteomes; UP000009159; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0031326; P:regulation of cellular biosynthetic process; IEA:UniProt.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 3.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   PANTHER; PTHR46260; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR46260:SF3; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01344; Kelch_1; 8.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00612; Kelch; 10.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF50965; Galactose oxidase, central domain; 2.
DR   SUPFAM; SSF117281; Kelch motif; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Kinase {ECO:0000313|EMBL:ABM11914.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009159};
KW   Transferase {ECO:0000313|EMBL:ABM11914.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        371..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          14..279
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          314..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   993 AA;  103950 MW;  8EBAE690DDCAE22A CRC64;
     MAGEIAYELA AAGFVDAVEV GRGGGGVVYR CHQQSLGRTV AIKVLASSLD EDDRERFLRE
     GYAMGGLSGH PNIVNILQVG MTEQDRPFIV MPYHARGSLA DQVRREGRIP WPDALRIGVK
     LCGALETAHR TGTLHRDIKP ANVLVNDYGD PQLSDFGTAR IVGGYKTVTG FFTGTLSYTA
     PEVLTGKPPT VEADVYSLGA TLYAMIAGKA AHERNTDEEL IAHYLRITSQ PVPDLRHLGI
     PSDVCSAIEK AMSLESAARF DSAAEFGRAL QEAQRHNGLT ADTMAIGEPT PAAAPPEGTQ
     ALPLSVPSDS VVLPPIPAAA PPASPPAPPP PPPPDMFARS PSNSPPITPW PVAPPPYPAS
     VAPAKNRKKT LIALAAAAAA VLLVIGTVVI VASRDNRSGE AGGVTTAARP TAEAQPGWRP
     IADSRIPLAA AAATEADGTI WIFGGMGADN RVSGAHEGYD PAIDSWKGGE ALPVPVQRAM
     SVTWQDTPVV LGGWRSEGAD TKVATDQVWR VVNSRWVQLP PLLQPRAAAA AAVVGDRIVV
     TGGVDAAGKV LDTTEVYDGS GWTQAAPMPT PRQLLAAASD GELVYAIGGT NGTADLATVE
     AYDPAADTWT AMPALPEPRS DFGVAVTDAR LVAVGGTAAG RPLKTVTALD LTTSTWSDLP
     DLGTARRGAA VAAVGKSVYV IGGSTGAGDG QATSSAEALK LAPRTPQPAA QWRSLPDAPT
     ARLMMAYTVL DDQIWIAGGI REGETLDTVE TYDTRTQQWQ SQPSLPIPLN HAVAATYRGE
     VVVIGGATDT ITQASDKVFA FRDGTWVELA SLQHARAAPA AAVVDDKLVV VGGQNDKQVV
     PQTEVFDGQS WTQAADMPTP REHLAAVSDG VYVYTVGGRL LSADENLAAF ERFDPESGNW
     EKLPDMPTPR GSYGAAYLDG RIVVVGGEEP TRVLPTVEIY DIANRKWSTQ APVNTPVHGQ
     AVAAVGSTVY CIGGADRPTH EGPVATVEAL DFT
//