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Database: UniProt
Entry: C8VVC8_DESAS
LinkDB: C8VVC8_DESAS
Original site: C8VVC8_DESAS 
ID   C8VVC8_DESAS            Unreviewed;       278 AA.
AC   C8VVC8;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   SubName: Full=Pyrrolysine-tRNA ligase {ECO:0000313|EMBL:ACV60991.1};
GN   OrderedLocusNames=Dtox_0027 {ECO:0000313|EMBL:ACV60991.1};
OS   Desulfofarcimen acetoxidans (strain ATCC 49208 / DSM 771 / KCTC 5769 / VKM
OS   B-1644 / 5575) (Desulfotomaculum acetoxidans).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV60991.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV60991.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S., Chen F.,
RA   Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Chain P., Saunders E., Brettin T., Detter J.C.,
RA   Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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DR   EMBL; CP001720; ACV60991.1; -; Genomic_DNA.
DR   RefSeq; WP_012813443.1; NC_013216.1.
DR   AlphaFoldDB; C8VVC8; -.
DR   STRING; 485916.Dtox_0027; -.
DR   KEGG; dae:Dtox_0027; -.
DR   eggNOG; COG0441; Bacteria.
DR   HOGENOM; CLU_1010485_0_0_9; -.
DR   OMA; RPMLAPN; -.
DR   OrthoDB; 5417309at2; -.
DR   Proteomes; UP000002217; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProt.
DR   Gene3D; 1.10.287.540; Helix hairpin bin; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR041616; PheRS_beta_core.
DR   InterPro; IPR023877; Pyrrolysyl-tRNA_ligase_C.
DR   NCBIfam; TIGR02367; PylS_Cterm; 1.
DR   Pfam; PF17759; tRNA_synthFbeta; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Ligase {ECO:0000313|EMBL:ACV60991.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217}.
FT   DOMAIN          66..254
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   278 AA;  31779 MW;  C83097801563AB72 CRC64;
     MSFLWTVSQQ KRLSELNASE EEKNMSFSST SDREAAYKRV EMRLINESKQ RLNKLRHETK
     RPAICALENR LAAALRGAGF VQVATPVILS KKLLGKMTIT DEHALFSQVF WIEENKCLRP
     MLAPNLYYIL KDLLRLWEKP VRIFEIGSCF RKESQGSNHL NEFTMLNLVE WGLPEEQRQK
     RISELAKLVM DETGIDEYHL EHAESVVYGE TVDVMHRDIE LGSGALGPHF LDGRWGVVGP
     WVGIGFGLER LLMVEQGGQN VRSMGKSLTY LDGVRLNI
//
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