ID W6LE39_9TRYP Unreviewed; 250 AA.
AC W6LE39;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=BPL/LPL catalytic domain-containing protein {ECO:0000259|PROSITE:PS51733};
DE Flags: Fragment;
GN ORFNames=GSHART1_T00002149001 {ECO:0000313|EMBL:CCW71592.1};
OS Phytomonas sp. Hart1.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Phytomonas.
OX NCBI_TaxID=223615 {ECO:0000313|EMBL:CCW71592.1, ECO:0000313|Proteomes:UP000053358};
RN [1] {ECO:0000313|EMBL:CCW71592.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Hart1 {ECO:0000313|EMBL:CCW71592.1};
RA Genoscope - CEA;
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCW71592.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hart1 {ECO:0000313|EMBL:CCW71592.1};
RX PubMed=24516393; DOI=10.1371/journal.pgen.1004007;
RA Porcel B.M., Denoeud F., Opperdoes F., Noel B., Madoui M.A.,
RA Hammarton T.C., Field M.C., Da Silva C., Couloux A., Poulain J.,
RA Katinka M., Jabbari K., Aury J.M., Campbell D.A., Cintron R., Dickens N.J.,
RA Docampo R., Sturm N.R., Koumandou V.L., Fabre S., Flegontov P., Lukes J.,
RA Michaeli S., Mottram J.C., Szoor B., Zilberstein D., Bringaud F.,
RA Wincker P., Dollet M.;
RT "The Streamlined Genome of Phytomonas spp. Relative to Human Pathogenic
RT Kinetoplastids Reveals a Parasite Tailored for Plants.";
RL PLoS Genet. 10:e1004007-e1004007(2014).
CC -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC {ECO:0000256|ARBA:ARBA00009934}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HF955212; CCW71592.1; -; Genomic_DNA.
DR AlphaFoldDB; W6LE39; -.
DR EnsemblProtists; CCW71592; CCW71592; GSHART1_T00002149001.
DR OrthoDB; 5471761at2759; -.
DR Proteomes; UP000053358; Unassembled WGS sequence.
DR GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:InterPro.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR CDD; cd16442; BPL; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR NCBIfam; TIGR00121; birA_ligase; 1.
DR PANTHER; PTHR12835; BIOTIN PROTEIN LIGASE; 1.
DR PANTHER; PTHR12835:SF5; BIOTIN--PROTEIN LIGASE; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Reference proteome {ECO:0000313|Proteomes:UP000053358}.
FT DOMAIN 1..185
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CCW71592.1"
SQ SEQUENCE 250 AA; 28086 MW; 8243539042B2E5AB CRC64;
MSVIEPCIEF LGEVTTTMEV VKEKFERYAG KPFGIVAESQ CAGRGTTGRK WLSPKGNLYF
SFCIPQNDPK YISRDLVPVL PMLCGMAARK AILELLPGLP VDRLGVKWPN DIIYDHKKIG
GALIESAGNY HVIGIGINVE ITPTVFDSGR EATSLKRLAE DFNLQLPTLP ELAQKIWVHL
FKLSVDSSMT RQKVTLEFDK VMDRTLKLHK RLPGGRDEEE LTAVSLNEWG HLKVRHIDGT
EEELCADYLF
//
