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Database: UniProt
Entry: Q2UQP5_ASPOR
LinkDB: Q2UQP5_ASPOR
Original site: Q2UQP5_ASPOR 
ID   Q2UQP5_ASPOR            Unreviewed;       684 AA.
AC   Q2UQP5;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   03-MAY-2023, entry version 110.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:BAE56120.1};
GN   ORFNames=AO090005001159 {ECO:0000313|EMBL:BAE56120.1};
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE56120.1, ECO:0000313|Proteomes:UP000006564};
RN   [1] {ECO:0000313|EMBL:BAE56120.1, ECO:0000313|Proteomes:UP000006564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; AP007151; BAE56120.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2UQP5; -.
DR   STRING; 510516.Q2UQP5; -.
DR   EnsemblFungi; BAE56120; BAE56120; AO090005001159.
DR   HOGENOM; CLU_000395_3_3_1; -.
DR   OMA; MYYDSMI; -.
DR   OrthoDB; 313213at2759; -.
DR   Proteomes; UP000006564; Chromosome 1.
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; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-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; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00866; CPSASE_1; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000006564}.
FT   DOMAIN          3..459
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          121..321
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          602..682
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   COILED          548..582
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   684 AA;  75281 MW;  6660ECEF410B1CA5 CRC64;
     MESLKTLLVA NRGEIAVRIL KTAKKLNLRT IALYTEPDAA SAHVQLADEA FLLDGPPSKA
     YIDGDQIIKL AKRNHVDAII PGYGFLSENA DFARAIAKAG MVFAGPSPEC IEAFGLKHTA
     RDLATKAGVP IVPGSTGLVT SEEDAVKVAK DLGFPVMLKA TAGGGGMGLL TCSSEDEVRE
     SFATVRSRGE ALFKNAGLFI ERYYPSSHHI EVQVFGNGDG KAIAIGEREC SIQRRHQKII
     EECPSPFVTR NPGLRESLGD AAVRLAESIK YGSAGTIEYL VDDETGAFFF LEMNTRLQVE
     HGITELCYGV DLVELMLKQA DAQLSGKKGL EVAFLTGITV DAPSGAAIEA RVYAENPTKD
     FAPCPGTLQS VEWKELPGSR IDTWVYRGIK VSANYDPLLA KVMLHSPSRT QAIEGMRTIL
     TQSRICGPPT NLEFLAEILT DERFVTGNTL TRFLDDFQWK LVTALKKVLN EGNGDITFSN
     KLISMIGCGN CVDILGSKKG YTPDRPWLFE EFDQITFYRV SEEEYEKELA LFNSGRYEYQ
     WEEVIFDMAE HNKLLHDTKE EVAAIRARQR KAQDEMDKLE AELLEHWAKE KAEKGVPVDA
     IENLLKDPQI LPIEAPLNAN IWKVEVKQGD KLDEGQIVVI LEAMKLEIAV RTELHAAGAT
     VEKVLVQPGD SIEAGKPLIL VRNA
//
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