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Database: UniProt
Entry: U5VNH1_9ACTN
LinkDB: U5VNH1_9ACTN
Original site: U5VNH1_9ACTN 
ID   U5VNH1_9ACTN            Unreviewed;       279 AA.
AC   U5VNH1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
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=AFR_00225 {ECO:0000313|EMBL:AGZ38334.1};
OS   Actinoplanes friuliensis DSM 7358.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ38334.1, ECO:0000313|Proteomes:UP000017746};
RN   [1] {ECO:0000313|EMBL:AGZ38334.1, ECO:0000313|Proteomes:UP000017746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ38334.1,
RC   ECO:0000313|Proteomes:UP000017746};
RX   PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA   Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA   Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT   "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT   HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL   J. Biotechnol. 178:41-42(2014).
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DR   EMBL; CP006272; AGZ38334.1; -; Genomic_DNA.
DR   RefSeq; WP_023357278.1; NC_022657.1.
DR   AlphaFoldDB; U5VNH1; -.
DR   STRING; 1246995.AFR_00225; -.
DR   KEGG; afs:AFR_00225; -.
DR   PATRIC; fig|1246995.3.peg.46; -.
DR   eggNOG; COG2815; Bacteria.
DR   HOGENOM; CLU_092033_0_0_11; -.
DR   OrthoDB; 3293034at2; -.
DR   Proteomes; UP000017746; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd06577; PASTA_pknB; 1.
DR   Gene3D; 3.30.10.20; -; 1.
DR   InterPro; IPR005543; PASTA_dom.
DR   Pfam; PF03793; PASTA; 1.
DR   SMART; SM00740; PASTA; 1.
DR   PROSITE; PS51178; PASTA; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017746};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        118..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          190..255
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   REGION          1..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          148..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          255..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..171
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   279 AA;  29639 MW;  A9772D42D32EEF40 CRC64;
     MSDDREPRRQ DETNEYFPFG EEGENRPNDG PRKEDTFGDR TEQMPRAPFP DDDSTSVLPP
     ATDDGTRTLS DYRSTDNWAD DGDPVWSGRA GVRPQRPGYG DEETDWATVP ADEPRGKWWM
     PIVVGIVGLI LLGLLGWGIY LIAQSSGDTT DTTPAVTAPA APPPAATEPT TTPPSTAPTT
     TEPTSSPAPS PTDVTVPALR GLSLDEARGA LDRKGLSYRL RYVTSESPAG TVIDSDPAEG
     QQVPADTVVA LIIAAAPTTP ATPTETPATT DPGEQPEGE
//
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