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Database: UniProt
Entry: A0A2C5ZKN8_9HYPO
LinkDB: A0A2C5ZKN8_9HYPO
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ID   A0A2C5ZKN8_9HYPO        Unreviewed;       284 AA.
AC   A0A2C5ZKN8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU367011};
DE            EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU367011};
GN   ORFNames=CDD83_3343 {ECO:0000313|EMBL:PHH90538.1};
OS   Cordyceps sp. RAO-2017.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX   NCBI_TaxID=2004951 {ECO:0000313|EMBL:PHH90538.1, ECO:0000313|Proteomes:UP000221130};
RN   [1] {ECO:0000313|Proteomes:UP000221130}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1346 {ECO:0000313|Proteomes:UP000221130};
RA   de Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PHH90538.1, ECO:0000313|Proteomes:UP000221130}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1346 {ECO:0000313|EMBL:PHH90538.1,
RC   ECO:0000313|Proteomes:UP000221130};
RA   De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT   "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT   behavioral manipulation genes and a possible major role for enterotoxins.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Reversible hydration of carbon dioxide.
CC       {ECO:0000256|RuleBase:RU367011}.
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|RuleBase:RU367011};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU367011};
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000256|RuleBase:RU367011}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PHH90538.1}.
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DR   EMBL; NJEV01000187; PHH90538.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C5ZKN8; -.
DR   STRING; 2004951.A0A2C5ZKN8; -.
DR   OrthoDB; 49814at2759; -.
DR   Proteomes; UP000221130; 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   CDD; cd03124; alpha_CA_prokaryotic_like; 1.
DR   Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
DR   InterPro; IPR041891; Alpha_CA_prokaryot-like.
DR   InterPro; IPR001148; CA_dom.
DR   InterPro; IPR036398; CA_dom_sf.
DR   InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR   InterPro; IPR018338; Carbonic_anhydrase_a-class_CS.
DR   PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1.
DR   PANTHER; PTHR18952:SF266; CARBONIC ANHYDRASE 2, ISOFORM A; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   SMART; SM01057; Carb_anhydrase; 1.
DR   SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR   PROSITE; PS00162; ALPHA_CA_1; 1.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU367011};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU367011};
KW   Reference proteome {ECO:0000313|Proteomes:UP000221130};
KW   Signal {ECO:0000256|RuleBase:RU367011};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|RuleBase:RU367011"
FT   CHAIN           20..284
FT                   /note="Carbonic anhydrase"
FT                   /evidence="ECO:0000256|RuleBase:RU367011"
FT                   /id="PRO_5025098834"
FT   DOMAIN          40..281
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000259|PROSITE:PS51144"
SQ   SEQUENCE   284 AA;  30805 MW;  F418C03CE7601479 CRC64;
     MKRFAKLLAT LLLCSTTAAV CNYGTAQNPR HQLLPRSAGP TYSYDGQDGP LVWHSLSAAN
     SVCATGKHQS PVNIVRGAYS TVDGSSLTFR PGSYPGGAEF ENLGHTVQVY LDGSVTLNQD
     VYRIVQFHLH TPSEHHVESE HYSMELHFVA QSQNQSLAVM AFIVELASDR DKTSDVLAAA
     LGRVQEIPQA GDRTLTDGLN FTTLQNHLSG SKVFQYSGSL TTPPCSEDVA FNVVSTPLYI
     GVDLYRALKS VVKFNARFTQ AAPGQLNVLQ CAHDSFVRDD GPDS
//
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