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Database: UniProt
Entry: A0A0C3CDV0_HEBCY
LinkDB: A0A0C3CDV0_HEBCY
Original site: A0A0C3CDV0_HEBCY 
ID   A0A0C3CDV0_HEBCY        Unreviewed;       343 AA.
AC   A0A0C3CDV0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU003956};
DE            EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU003956};
DE   AltName: Full=Carbonate dehydratase {ECO:0000256|RuleBase:RU003956};
GN   ORFNames=M413DRAFT_440519 {ECO:0000313|EMBL:KIM46960.1};
OS   Hebeloma cylindrosporum h7.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Hebeloma.
OX   NCBI_TaxID=686832 {ECO:0000313|EMBL:KIM46960.1, ECO:0000313|Proteomes:UP000053424};
RN   [1] {ECO:0000313|EMBL:KIM46960.1, ECO:0000313|Proteomes:UP000053424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG   DOE Joint Genome Institute;
RA   Kuo A., Gay G., Dore J., Kohler A., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000053424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Reversible hydration of carbon dioxide.
CC       {ECO:0000256|RuleBase:RU003956}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17544; EC=4.2.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000943,
CC         ECO:0000256|RuleBase:RU003956};
CC   -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC       {ECO:0000256|ARBA:ARBA00006217, ECO:0000256|RuleBase:RU003956}.
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DR   EMBL; KN831770; KIM46960.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C3CDV0; -.
DR   STRING; 686832.A0A0C3CDV0; -.
DR   HOGENOM; CLU_053879_3_2_1; -.
DR   OrthoDB; 5392875at2759; -.
DR   Proteomes; UP000053424; 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; Carbonic anhydrase; 1.
DR   InterPro; IPR001765; Carbonic_anhydrase.
DR   InterPro; IPR036874; Carbonic_anhydrase_sf.
DR   PANTHER; PTHR11002; CARBONIC ANHYDRASE; 1.
DR   PANTHER; PTHR11002:SF83; CARBONIC ANHYDRASE; 1.
DR   Pfam; PF00484; Pro_CA; 1.
DR   SMART; SM00947; Pro_CA; 1.
DR   SUPFAM; SSF53056; beta-carbonic anhydrase, cab; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|RuleBase:RU003956};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053424};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|RuleBase:RU003956}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..343
FT                   /note="Carbonic anhydrase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002162491"
SQ   SEQUENCE   343 AA;  36572 MW;  DEBE2CDC30599AE9 CRC64;
     MHAFGLAFVL AAISSVLTHP IHQEQRQEIH VVGREQSTMV PVAPETSAEL ELLSKGNKAF
     RDNIAVTDPG LLKKLADEGQ SPPFMFLGCS DSRVSEGTVF NAKPGTLFAE RNIANQFQSS
     DTNAHSVLSY AVTVLGVKHV IVMGHYGCGG VAASIASPPK GQIDAANGAV QNWIEPIREI
     FRASNRSEIV ELRNKNAGRT DIKEPKINEP GFRALVEENV KASVRRIATN PVITNHYGLL
     KSGAGNSTSG TRKSARDVFI HGWVYDLATG KVHDLGISVG PPGKPVPTLP LAAVSKSTTQ
     SLGSAVEASV WPNAACLASL VKRSAKGIIL LRGYSLPLGT WWS
//
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