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Database: UniProt
Entry: G0SH88_CHATD
LinkDB: G0SH88_CHATD
Original site: G0SH88_CHATD 
ID   G0SH88_CHATD            Unreviewed;       166 AA.
AC   G0SH88;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   25-OCT-2017, entry version 23.
DE   RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU003956};
DE            EC=4.2.1.1 {ECO:0000256|RuleBase:RU003956};
DE   AltName: Full=Carbonate dehydratase {ECO:0000256|RuleBase:RU003956};
GN   ORFNames=CTHT_0069120 {ECO:0000313|EMBL:EGS17577.1};
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Chaetomiaceae;
OC   Chaetomium.
OX   NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN   [1] {ECO:0000313|EMBL:EGS17577.1, ECO:0000313|Proteomes:UP000008066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC   {ECO:0000313|Proteomes:UP000008066};
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R.,
RA   Devos D.P., Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
CC   -!- FUNCTION: Reversible hydration of carbon dioxide.
CC       {ECO:0000256|RuleBase:RU003956}.
CC   -!- CATALYTIC ACTIVITY: H(2)CO(3) = CO(2) + H(2)O.
CC       {ECO:0000256|RuleBase:RU003956}.
CC   -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC       {ECO:0000256|RuleBase:RU003956}.
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DR   EMBL; GL988047; EGS17577.1; -; Genomic_DNA.
DR   RefSeq; XP_006697195.1; XM_006697132.1.
DR   EnsemblFungi; EGS17577; EGS17577; CTHT_0069120.
DR   GeneID; 18260950; -.
DR   KEGG; cthr:CTHT_0069120; -.
DR   KO; K01673; -.
DR   OrthoDB; EOG092C5PE7; -.
DR   Proteomes; UP000008066; Unassembled WGS sequence.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1050.10; -; 1.
DR   InterPro; IPR001765; Carbonic_anhydrase.
DR   InterPro; IPR036874; Carbonic_anhydrase_sf.
DR   Pfam; PF00484; Pro_CA; 1.
DR   SMART; SM00947; Pro_CA; 1.
DR   SUPFAM; SSF53056; SSF53056; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008066};
KW   Lyase {ECO:0000256|RuleBase:RU003956};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW   Zinc {ECO:0000256|RuleBase:RU003956}.
SQ   SEQUENCE   166 AA;  18153 MW;  5ED96A7F16D99340 CRC64;
     MSAVQQNLEA ASAKYSSTFT QGHLALPPSK QYLVLTCMDA RIDPAAAFGI ELGDAHAGAS
     ARDALRSIII SEQLLGTTEI ILVKHTGCGM LTFTNKDAYE IVEKNLGAEA ALELKERNLD
     FLPFPDLEKA VREDIDFIKS TKLVPDNVIL SGWIYEVETG KTRRVV
//
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