ID   A0A015NGV8_RHIIW        Unreviewed;       642 AA.
AC   A0A015NGV8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Biotin--[acetyl-CoA-carboxylase] ligase BPL1 {ECO:0000313|EMBL:EXX78593.1};
GN   ORFNames=RirG_013500 {ECO:0000313|EMBL:EXX78593.1};
OS   Rhizophagus irregularis (strain DAOM 197198w) (Glomus intraradices).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=1432141 {ECO:0000313|EMBL:EXX78593.1, ECO:0000313|Proteomes:UP000022910};
RN   [1] {ECO:0000313|EMBL:EXX78593.1, ECO:0000313|Proteomes:UP000022910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM197198w {ECO:0000313|Proteomes:UP000022910};
RA   Lin K., Geurts R., Zhang Z., Limpens E., Saunders D.G., Mu D., Pang E.,
RA   Cao H., Cha H., Lin T., Zhou Q., Shang Y., Li Y., Ivanov S., Sharma T.,
RA   Velzen R.V., Ruijter N.D., Aanen D.K., Win J., Kamoun S., Bisseling T.,
RA   Huang S.;
RT   "Single nucleus genome sequencing reveals high similarity among nuclei of
RT   an endomycorrhizal fungus.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC       {ECO:0000256|ARBA:ARBA00009934}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXX78593.1}.
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DR   EMBL; JEMT01008925; EXX78593.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A015NGV8; -.
DR   STRING; 1432141.A0A015NGV8; -.
DR   HOGENOM; CLU_006150_1_1_1; -.
DR   Proteomes; UP000022910; 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; IPR019197; Biotin-prot_ligase_N.
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   Pfam; PF09825; BPL_N; 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, ECO:0000313|EMBL:EXX78593.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000022910}.
FT   DOMAIN          350..562
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   642 AA;  73344 MW;  3ECCAA3C587FB6A6 CRC64;
     MKSSKFFKNL QSRHIKNMRT KILVYSSNIT LNHHFSILNS MFNTFYDVIQ IDLNNLLNDP
     WFDTTSCLIF LSSNNNLNCL NNLNYNQKSV QFEKNFKDYL KFGGNYFGIG FDACQFLQKN
     LSTQFQNDIF NYKNLILNDQ NDKIELPLKL NRKFLLNYFP SVPNQIKIPC DNNAIGYFDN
     LINNNIINSV STYNNCSTII QYNIDKGKIL LCGFDPFLNN IHIEQNHFIR SLFSIFGLNL
     VKQNEILIPK LSYTLHLTSI RPALTSILLN NINNLMDSDN IIRASNDSFK IIENSNSFHN
     NQDLYTNVDY NNNIDIPKSI VIYHDQPPPS SITPFFNFKD FLNHLSEERN IKHGGGNNME
     FGSTVLYGEV VSSTQTLLDK NFKFTKNLPT GLVFVATQQI QGRGRGSNSW ISPPGCLQFS
     IILRHPSNSS SPVVFIQYLL SLAVVEAVRT KKGYEDIPLR LKWPNDIYVE SSSPNDESVK
     SPKIIKIGGV IVNSQYTQDE LDEFLLIAGC GVNVSNLAPT TAINHIISLY NHANNTQLEE
     FSQEQLLAAI LVKFESFYSD FCRNGYGFEP FLDIYYERWL HTDQVVNLET HDNQKAHIIG
     INEFGYLKAS TISDGVNLEE IITLEPGGNS FDMMKGMITR KL
//