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Database: UniProt
Entry: A0A094EFM6_9PEZI
LinkDB: A0A094EFM6_9PEZI
Original site: A0A094EFM6_9PEZI 
ID   A0A094EFM6_9PEZI        Unreviewed;       650 AA.
AC   A0A094EFM6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   13-SEP-2023, entry version 29.
DE   RecName: Full=Lipoyl-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=V499_04796 {ECO:0000313|EMBL:KFY75238.1};
OS   Pseudogymnoascus sp. VKM F-103.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY75238.1, ECO:0000313|Proteomes:UP000029295};
RN   [1] {ECO:0000313|EMBL:KFY75238.1, ECO:0000313|Proteomes:UP000029295}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY75238.1,
RC   ECO:0000313|Proteomes:UP000029295};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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:KFY75238.1}.
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DR   EMBL; JPKB01000728; KFY75238.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094EFM6; -.
DR   HOGENOM; CLU_000395_3_2_1; -.
DR   Proteomes; UP000029295; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR45007; CARBOXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G07570)-RELATED; 1.
DR   PANTHER; PTHR45007:SF1; CARBOXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G07570)-RELATED; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          7..453
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          122..318
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   650 AA;  69693 MW;  BEC76F802079C510 CRC64;
     MTQPYSTYYQ QLTRSRGEIA IRILSSAREL DLETYTLYTA DDTSHTLQST HAVSIPSPST
     YLDIPALIAI IKSHNIDSVH PGYGFLSESA EFAHRAWTEA GAVVIGPGWE TLARTGDKLA
     ARQLAEECKV PVLPALQTPT DNVEDIRRFA TQIGWPIIIK AVDGGGGRGI RIVREEGDLA
     GLMERALRES PQGLVFAEKA AVDGYRHVEV QIVGDGTGNV RHLWERECSI QRRFQKVVEF
     APSSIRDRAV VGRVIEAAMR MARKVSYLSL GTFEFLVHSS KPEFYFLEVN PRLQVEHTIT
     ESLCPGLDLV KVQLCLAAGQ ELDTLLPNIS RDPLVPPPLH SLQLRITAED ATANWALNTG
     TINSLALPSG NGIRVDHHLT AGLVVKTDFD SLLAKIVITT SSWTDLVAKA IRALNDTHII
     GVKTSLPALR GILAHPAFKA QACDTQWLES TLPALLAAGT SITATIPSPA TPSAAPAFAP
     SSSSAPLRKG DAWSLTLTPT TTASSSSTPP PAPAHLLLTK LLRNDFPSSL TADILFTAPS
     APPMSYTLAL TSTAASAGAL TSAHRRGEAG NARHIVFPFP GQLVELLVDV GDRVGKGDVV
     AVVKQMKMEL EIRASGEGVV GWVFEGEDGD EVGEGVLAVE LVDEGGRAKL
//
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