(data stored in ACNUC7421 zone)

SWISSPROT: Q75CP0_ASHGO

ID   Q75CP0_ASHGO            Unreviewed;       939 AA.
AC   Q75CP0;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 100.
DE   SubName: Full=ACL121Cp {ECO:0000313|EMBL:AAS51107.2};
GN   ORFNames=AGOS_ACL121C {ECO:0000313|EMBL:AAS51107.2};
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:AAS51107.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51107.2, 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; AE016816; AAS51107.2; -; Genomic_DNA.
DR   RefSeq; NP_983283.2; NM_208636.2.
DR   STRING; 33169.AAS51107; -.
DR   EnsemblFungi; AAS51107; AAS51107; AGOS_ACL121C.
DR   GeneID; 4619403; -.
DR   KEGG; ago:AGOS_ACL121C; -.
DR   HOGENOM; HOG000040280; -.
DR   InParanoid; Q75CP0; -.
DR   KO; K00288; -.
DR   OMA; KVDTYTK; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004329; F:formate-tetrahydrofolate ligase activity; IBA:GO_Central.
DR   GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IBA:GO_Central.
DR   GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IBA:GO_Central.
DR   GO; GO:0009257; P:10-formyltetrahydrofolate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IBA:GO_Central.
DR   CDD; cd01080; NAD_bind_m-THF_DH_Cyclohyd; 1.
DR   HAMAP; MF_01543; FTHFS; 1.
DR   HAMAP; MF_01576; THF_DHG_CYH; 1.
DR   InterPro; IPR000559; Formate_THF_ligase.
DR   InterPro; IPR020628; Formate_THF_ligase_CS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000672; THF_DH/CycHdrlase.
DR   InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom.
DR   InterPro; IPR020867; THF_DH/CycHdrlase_CS.
DR   InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
DR   Pfam; PF01268; FTHFS; 1.
DR   Pfam; PF00763; THF_DHG_CYH; 1.
DR   Pfam; PF02882; THF_DHG_CYH_C; 1.
DR   PRINTS; PR00085; THFDHDRGNASE.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00721; FTHFS_1; 1.
DR   PROSITE; PS00722; FTHFS_2; 1.
DR   PROSITE; PS00767; THF_DHG_CYH_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75CP0.
DR   SWISS-2DPAGE; Q75CP0.
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   DOMAIN          3..119
FT                   /note="THF_DHG_CYH"
FT                   /evidence="ECO:0000259|Pfam:PF00763"
FT   DOMAIN          123..288
FT                   /note="THF_DHG_CYH_C"
FT                   /evidence="ECO:0000259|Pfam:PF02882"
SQ   SEQUENCE   939 AA;  101503 MW;  9B2581A042A4FAAB CRC64;
     MTLIDGKAIA AEIRGEIAEE IARLCADGLF QAKLTIFQVG ERHDSSTYVR MKRRAAAEAG
     IEVEFVQLGA DVDEEEVLAA IDARNADETV HGILVQLPLP PGMDEDRVTS RVAPEKDVDG
     FGSYNIGELN KRHGRPHFHP CTPKGIIELL RRMDVQIAGA NVVVLGRSDI VGAPVACLLR
     ALDATVTVLH SRSRDIPGYV GRADIVVVAI GQPEFVKGAW FTNPDAVVID VGTNFVEDST
     RKTGYRCVGD VEFGVASEKV RLITPVPGGV GPMTVAMLMQ NTLDAAKKCH SAPRKLSPLP
     LQLQKPVPSD YEISRSQVPK NIAVVAREAG LLPSEVELYG SVKAKVKLDT LDRLAHRENG
     KYVLVTGITP TPLGEGKSTT TVGLVQALAA HLDKVAFATV RQPSMGPTFG IKGGAAGGGY
     SQVIPMDEFN LHVTGDIHAI SMANNLLAAA IDTRMFHEAT QKDAALYKRL VPEKNGTRKF
     TSTMLRRLQK LGIHKTDPNS LTESEIARFA RLDIDADTIT WRRVVDCNDR FLRGITVGEA
     PTERGYKRQT GFDISVASEC MAILALADSL HDLRERLGRI VVAASRNGEP ITCEDIGCAG
     AMAALLKDAI KPNIMQTLEG TPVFVHAGPF ANISIGANSV LADKIALKLA GVDPNWSEAE
     KKKRQGYVVT EAGFDFTMGG ERFLNIKCRA SGISPDVVVI VATVRALKVH GGGPEVKAGA
     PLPSAYLNED VDLLRKGCAN LAKHIANART YNLPVVVGIN RMSSDTEREH EVIREEAIKA
     GAFDAIVSNH WEEGGQGAVK LAEGVIRATE ECRPEFHYLY DTEGPSIEDK ISTIAKTMYG
     AAEVEFLPEA RKKIELYTKQ GFNHLPICIA KTQYSLSHDA NLKGVPTGFK FPVRDIRASI
     GAGYLYALAA EIQTIPGLPT HCGFMNIEIN DKGEIDGMF
//

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