(data stored in ACNUC7421 zone)

SWISSPROT: Q757L9_ASHGO

ID   Q757L9_ASHGO            Unreviewed;       469 AA.
AC   Q757L9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 111.
DE   SubName: Full=AEL019Wp {ECO:0000313|EMBL:AAS52666.1};
GN   ORFNames=AGOS_AEL019W {ECO:0000313|EMBL:AAS52666.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS52666.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52666.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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DR   EMBL; AE016818; AAS52666.1; -; Genomic_DNA.
DR   RefSeq; NP_984842.1; NM_210196.1.
DR   STRING; 33169.AAS52666; -.
DR   EnsemblFungi; AAS52666; AAS52666; AGOS_AEL019W.
DR   GeneID; 4621040; -.
DR   KEGG; ago:AGOS_AEL019W; -.
DR   HOGENOM; HOG000242744; -.
DR   InParanoid; Q757L9; -.
DR   KO; K01755; -.
DR   OMA; MPGRTHL; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IBA:GO_Central.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
DR   CDD; cd01359; Argininosuccinate_lyase; 1.
DR   Gene3D; 1.10.275.10; -; 1.
DR   HAMAP; MF_00006; Arg_succ_lyase; 1.
DR   InterPro; IPR029419; Arg_succ_lyase_C.
DR   InterPro; IPR009049; Argininosuccinate_lyase.
DR   InterPro; IPR024083; Fumarase/histidase_N.
DR   InterPro; IPR020557; Fumarate_lyase_CS.
DR   InterPro; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR022761; Fumarate_lyase_N.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   PANTHER; PTHR43814; PTHR43814; 1.
DR   Pfam; PF14698; ASL_C2; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   TIGRFAMs; TIGR00838; argH; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q757L9.
DR   SWISS-2DPAGE; Q757L9.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   DOMAIN          11..307
FT                   /note="Lyase_1"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          370..438
FT                   /note="ASL_C2"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
FT   COILED          448..469
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   469 AA;  53009 MW;  2D4B482E42548E47 CRC64;
     MSSGKQKLWG GRFAGDTDPL MHLYNASLPY DYKMYKADIL GTKVYTEGLQ KTGLLTKDEL
     ESIHEGLKQV EQEWEQGVFV KHVDDEDIHT ANERRLGEII GRHISGKVHT GRSRNDQVAT
     DMRLYCREML QDKVEPALFE LIKVLLHRAR EEIDVLMPGY THLQRAQPIR WSHWLSCYAT
     YFVEDFKRLK EVIARLNQSP LGAGALAGHP YGIDREYLAC ELGFDGVIGN SMTAVSDRDF
     VVEIMSWGSL FMNHISRLAE DLIIYSTAEF GFVKLADAYS TGSSLMPQKR NPDSLELLRG
     KSGRVFGQLA GFLMSLNSIP STYNKDMQED KEPLFDCLLT LEHTSLIATG VLSTLSVVKE
     KMFQALTVDM LATDLADYLV RKGVPFRETH HISGSCVALA EQLALSGIDQ LTLEHYKGID
     PRFEEDVFDV FDFELSVERR QSTGGTARAA VLKQVDNLEE QLKRMHNNT
//

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