(data stored in ACNUC7421 zone)

SWISSPROT: Q750X1_ASHGO

ID   Q750X1_ASHGO            Unreviewed;       803 AA.
AC   Q750X1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 90.
DE   RecName: Full=Cleavage and polyadenylation specificity factor subunit 2 {ECO:0000256|RuleBase:RU365006};
DE   AltName: Full=Cleavage and polyadenylation specificity factor 100 kDa subunit {ECO:0000256|RuleBase:RU365006};
GN   ORFNames=AGOS_AGL182C {ECO:0000313|EMBL:AAS54309.2};
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:AAS54309.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54309.2, 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).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365006}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC       metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.
CC       {ECO:0000256|RuleBase:RU365006}.
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DR   EMBL; AE016820; AAS54309.2; -; Genomic_DNA.
DR   RefSeq; NP_986485.2; NM_211547.2.
DR   STRING; 33169.AAS54309; -.
DR   EnsemblFungi; AAS54309; AAS54309; AGOS_AGL182C.
DR   GeneID; 4622778; -.
DR   KEGG; ago:AGOS_AGL182C; -.
DR   HOGENOM; HOG000001120; -.
DR   InParanoid; Q750X1; -.
DR   KO; K14402; -.
DR   OMA; WKNKESG; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IEA:EnsemblFungi.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006378; P:mRNA polyadenylation; IEA:EnsemblFungi.
DR   GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IEA:EnsemblFungi.
DR   CDD; cd16293; CPSF2-like_MBL-fold; 1.
DR   Gene3D; 3.60.15.10; -; 2.
DR   InterPro; IPR022712; Beta_Casp.
DR   InterPro; IPR027075; CPSF2.
DR   InterPro; IPR025069; Cpsf2_C.
DR   InterPro; IPR035639; CPSF2_MBL.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   PANTHER; PTHR45922; PTHR45922; 1.
DR   Pfam; PF13299; CPSF100_C; 1.
DR   Pfam; PF16661; Lactamase_B_6; 1.
DR   SMART; SM01027; Beta-Casp; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q750X1.
DR   SWISS-2DPAGE; Q750X1.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   mRNA processing {ECO:0000256|RuleBase:RU365006};
KW   Nucleus {ECO:0000256|RuleBase:RU365006};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT   DOMAIN          253..376
FT                   /note="Beta-Casp"
FT                   /evidence="ECO:0000259|SMART:SM01027"
FT   REGION          525..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          424..444
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        548..571
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..588
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   803 AA;  89592 MW;  9E9728125D2EC157 CRC64;
     MTYTFTYCKD ESGSTTGTIL SFDNCTLLID PGWSGGCSYD ECMAYWKEWI PQVDIILLSQ
     PIQECIGAYA ALFFDYISHF NSRIQVYSTL PVANLGRVAT VDLYASLGII GPFDTNRIDI
     EDIDTAFDHL NTVKYSQLVD LKSRFDGLSL VAYSSGFAPG GTIWCANTYS EKVLYAPRWN
     HTRDTILNSA DLLDKGGKPS TALMRPSAVI MSAAHVGPST PYRKRSQKFK EVIKKALSAN
     TSVILPSAIG GKFLELFVLV HDILHENKKS GLQADAPVLL LSYSRGRTLT YARSMLEWLS
     SQLVKTWESR DNKSPFDLGN RLKIVNVNDL ANYPGTKICF ISQVETLIND ALSKVCTKEK
     AMLVLTEKPT YYSHTIAILA KAYAKWERAL NSNNLNAVEG NPIAYSESLS LQFSKTKPLT
     GSDLEEFKER IEARRKERAE LLSSFQSNDN PAGASAFTAI EDDDDEEEDV LRPHGAGALS
     TKVEIPTDLI IQPNALPKHK MFPFQPGKVA HDDYGELVDF ERFLPQSAPS SAKRGATNEE
     DEESYDPHDF EDIRRNGSGG KRRRREQDAL QRQMNQDNLS YLDTLTKPQH RTSNTQKVVI
     RCTMAFVDLA GLVDERSMSI IWPALKPRKM VLLPSDAASV SPVAQQLQKK GLDVIEPELN
     KSLVINTSLR SLDIFIDAEM DQMLNWQRIS EVYTVAHVVG RLTKEKDTKV SHRDKWVLKP
     LPNASARMQT TDSLRIGDVR LAELKRKLTA ASHVAEFRGE GTLVVDGRVI VRKISESETV
     VDGTPSDLFY KVKSAVADML AKV
//

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