ID B6QDD6_TALMQ Unreviewed; 686 AA.
AC B6QDD6;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=Biotin apo-protein ligase, putative {ECO:0000313|EMBL:EEA24764.1};
GN ORFNames=PMAA_087420 {ECO:0000313|EMBL:EEA24764.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA24764.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC {ECO:0000256|ARBA:ARBA00009934}.
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DR EMBL; DS995901; EEA24764.1; -; Genomic_DNA.
DR RefSeq; XP_002148275.1; XM_002148239.1.
DR AlphaFoldDB; B6QDD6; -.
DR STRING; 441960.B6QDD6; -.
DR VEuPathDB; FungiDB:PMAA_087420; -.
DR HOGENOM; CLU_006150_1_1_1; -.
DR OrthoDB; 317678at2759; -.
DR PhylomeDB; B6QDD6; -.
DR Proteomes; UP000001294; 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 CDD; cd03144; GATase1_ScBLP_like; 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 InterPro; IPR029062; Class_I_gatase-like.
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; SSF52317; Class I glutamine amidotransferase-like; 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:EEA24764.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001294}.
FT DOMAIN 403..605
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 686 AA; 75771 MW; 6027B2CDAA7C699C CRC64;
MSAGRTISSG RLNVLVYSDH GSTVESVRHC LYTLRRLLAP NYAVIPITAD MLIKEPWLST
CAMLVMPGGA DLGYCASLNG AGNRRITQFV QNGGAYLGFC AGGYYGSRRC EFEVGDKKMQ
VIGERELAFF PGICRGSAFE GFVYSSEAGA RAVEVKVSKS ALSSDGTLPE TFHSYYNGGG
VFVDAETYAD EGVEILASYT EELAVDSGKG AAAVIYRKIG DGAAVLTGPH PEFAAVNLNK
SAGSPEYAEL IDQLATDDTA RTDFVKACLT KLGLQVSQET TTVPSLSCLH LSSVEPEYTQ
AIVSSLEEIM TKDGRKEILK DNVDTFQVER AHDKTYKMDD LKNALEEEVA EEKATSNDGI
IDYNAIVKRL LIHDELPSSK QTPYFNHHAF YSNLRHYQSL SKEAVVDFGR SIIYGEVVTS
TSSMLEKNTR LLRRLPAGFT MTATVQVAGR GRGSNVWVSP AGALIFSTVV RHPMEKMQSA
PIVFIQYLAA MAVVKGIKTY DKGYEQLPIK MKWPNDVYAM DPAEPDKQKY TKICGILVNS
HYSSEEYVSV VGIGINATNA APTTSLNAIV EKFASPATIK SSPIILEKLL ARILTVFEEL
YIRFLRTGFD KQFEDMYYED WLHMHQIVTL EEQGGVRARI KGITRDFGLL LAEELGWEDR
PTGRVWQLQS DNNSFDFFRG LLKRKV
//
