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Database: UniProt
Entry: E9D7I3_COCPS
LinkDB: E9D7I3_COCPS
Original site: E9D7I3_COCPS 
ID   E9D7I3_COCPS            Unreviewed;       464 AA.
AC   E9D7I3;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Carbonic anhydrase {ECO:0000256|ARBA:ARBA00014628, ECO:0000256|RuleBase:RU367011};
DE            EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU367011};
GN   ORFNames=CPSG_05785 {ECO:0000313|EMBL:EFW17342.1};
OS   Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=443226 {ECO:0000313|Proteomes:UP000002497};
RN   [1] {ECO:0000313|Proteomes:UP000002497}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 757 / Silveira {ECO:0000313|Proteomes:UP000002497};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
RN   [2] {ECO:0000313|Proteomes:UP000002497}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 757 / Silveira {ECO:0000313|Proteomes:UP000002497};
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Neafsey D., Orbach M., Henn M.R., Cole G.T., Galgiani J., Gardner M.J.,
RA   Kirkland T.N., Taylor J.W., Young S.K., Zeng Q., Koehrsen M., Alvarado L.,
RA   Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA   Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Pearson M.,
RA   Richards J., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S., Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Coccidioides posadasii strain Silveira.";
RL   Submitted (MAR-2010) 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|ARBA:ARBA00010718, ECO:0000256|RuleBase:RU367011}.
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DR   EMBL; GL636494; EFW17342.1; -; Genomic_DNA.
DR   STRING; 443226.E9D7I3; -.
DR   VEuPathDB; FungiDB:CPSG_05785; -.
DR   VEuPathDB; FungiDB:D8B26_000077; -.
DR   eggNOG; KOG0382; Eukaryota.
DR   HOGENOM; CLU_710173_0_0_1; -.
DR   OMA; WHSISRE; -.
DR   Proteomes; UP000002497; 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:SF265; CARBONIC ANHYDRASE; 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:UP000002497};
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..464
FT                   /note="Carbonic anhydrase"
FT                   /evidence="ECO:0000256|RuleBase:RU367011"
FT                   /id="PRO_5040558444"
SQ   SEQUENCE   464 AA;  52109 MW;  6F814F86DE725A42 CRC64;
     MVLLFSLLFL VFYAGSVLSS CAHGTFLHPR AAGGIGELPN FDYGPVRGPT NWHSISRENI
     LCAVGLQQSP INLNGRIPIE PVGFVRSSIP RQDILFENLG TTAEVVLNGT TLVRGVGEFR
     LKQFHFHTPS EHRILGQHFP VELHLVHTSV ANPSQIAVIA LFFQLTSRGG FSDLERIITH
     VPRISSPGQT VGLRGFDFGI LSRTISSMPM FRYVGSLTTP PCTEGVTFLV GTQPLFMNVE
     IFNLLKGVTR FNSRFIQADI PGRQNVLLSG LHNIGLTNQQ CRRLVSGREL IGKPGRRNGN
     NRGGRKGKNR QKEVVSTIVS GNSTQVVTST VQQTVTSSNL VTETTRNGQV TTTISSVVAS
     QTAMEDYQRD RDDDRRDDRR DDDDRRDDDD RRDDDDRRDD DDRRDDDDRR DDDDRRDDDD
     RRDDDRQRQE QDQGRQTVQT TANTATASAA FIQRRNYMHF GRQA
//
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