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Database: UniProt
Entry: A1CNQ7_ASPCL
LinkDB: A1CNQ7_ASPCL
Original site: A1CNQ7_ASPCL 
ID   A1CNQ7_ASPCL            Unreviewed;      1250 AA.
AC   A1CNQ7;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 105.
DE   SubName: Full=Urea amidolyase, putative {ECO:0000313|EMBL:EAW07278.1};
GN   ORFNames=ACLA_019830 {ECO:0000313|EMBL:EAW07278.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW07278.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW07278.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; DS027059; EAW07278.1; -; Genomic_DNA.
DR   RefSeq; XP_001268704.1; XM_001268703.1.
DR   AlphaFoldDB; A1CNQ7; -.
DR   STRING; 344612.A1CNQ7; -.
DR   EnsemblFungi; EAW07278; EAW07278; ACLA_019830.
DR   GeneID; 4701460; -.
DR   KEGG; act:ACLA_019830; -.
DR   VEuPathDB; FungiDB:ACLA_019830; -.
DR   eggNOG; KOG0238; Eukaryota.
DR   HOGENOM; CLU_002162_0_1_1; -.
DR   OMA; TLQMWNR; -.
DR   OrthoDB; 313213at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 3.30.1360.40; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 2.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR001882; Biotin_BS.
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; IPR003778; CT_A_B.
DR   InterPro; IPR003833; CT_C_D.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
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   Pfam; PF02626; CT_A_B; 1.
DR   Pfam; PF02682; CT_C_D; 1.
DR   SMART; SM00796; AHS1; 1.
DR   SMART; SM00797; AHS2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF50891; Cyclophilin-like; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF160467; PH0987 N-terminal 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; PS00188; BIOTIN; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000006701}.
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          1155..1235
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   COILED          1101..1135
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1250 AA;  136986 MW;  C12B558F3B176DAB CRC64;
     MDSLKTLLVA NRGEIAVRIV KTAKKLNIRT IAIYTEPDAS SIHVHQADEA VLLHGSPSQA
     YIDGEQIIQV ATQHKVDAII PGYGFLSENA DFARAVATAG MVFVGPSPES IEAFGLKHTA
     RDLATKAGAP IVPGSPGLVK SEEEAVTLAK ALGFPVMLKA TAGGGGMGLL TCSSEAEVRK
     AFATVKSRGE ALFKNAGLFI ERYYPSSHHI EVQVFGNGNG KAIYIGEREC SIQRRHQKVI
     EECPSPLVSR NPGLRKALGE AAVRLAESIN YGSAGTIEYL VDDETGAFFF LEMNTRLQVE
     HGITELCYGL DLVELMLKQA DAQLSGSKGI EASFLASLPI ENPSGAAIEA RVYAENPIRD
     FAPSPGTLQS VEWKEIPGSR IDTWVYRGIK VSANYDPLLA KVMYHSPDRQ QTIAGLRDML
     KESRICGPPT NLEFLAKILD SEEFAAGNTL TRFLDTFQFA PCAIDVISGG SYTLIEDWPG
     RPALGKGFCH SGPMDPLAFR VANALVGNPI GREGLEITLS GPDLRFLGPA IVSLCGAPIE
     AKLDGKPIRM WSRVKVDAGQ RLTIGRTTGN GCRTYLAVFG GFLNVAEWFG SKSTSPMVGV
     GGYQGRQLSS GDLLTITSDV PDLIGDILIP EHLIPKYPSD WELLAIPGPY DEGFLTPESI
     DVLFDTQWKI SHNAARGGIR LIGPKPTWAR SDGGEGGAHP SNLIEYGYAI GSLNWTGDDP
     VIFPQDAPDF GGFVSSHTIV KADLWKLGQV KAGDTLKYRA VALADALDAR RDMERFVDEL
     VNACKQGQGF GYVVPLQHMP PEQTAKTRGK GIVHQIQEDG NQPFVSYRQA GDDYLLVDYG
     HGSFDLNHRC RITALKKALN EEKRDRDSLS NGLIGMVGCG NSLMLYYDGL KVPQGKLIDY
     LCDLENRLGD LSQAKMPSRL FKLPLTFESQ RQKDAMQRYM ETQRPYASYL PDNMDFVAKN
     NALKMEELKN IYLTAKLMVV SVGFFMALPL ALPVDPRHRM NCPKMNPSRV YTPAGSVSWG
     GSCMALYNVD SPGGYQMTGM TIPGVDILGS KKGYSADRPW LFEEFDQITF YQVSEAEYEK
     QLALFNSGKY EHQWEEVIFD MAEHNRLLND TRDEVAAIRA RQRQAQAEMD KFEAQLLERW
     ATEKAEKWVS QDAIEDLLQD PEIIAIEAPL NANVWKVEVK QAEKLEEGRV VVILEAMKLE
     IAVRVESSAA GTTVEKVLVQ PGGPIEAGKP LMLVRKAACA DGYCLEKRPQ
//
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