ID A0A067RDT3_ZOONE Unreviewed; 330 AA.
AC A0A067RDT3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011};
DE EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011};
GN ORFNames=L798_04082 {ECO:0000313|EMBL:KDR21153.1};
OS Zootermopsis nevadensis (Dampwood termite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Termopsidae; Zootermopsis.
OX NCBI_TaxID=136037 {ECO:0000313|EMBL:KDR21153.1, ECO:0000313|Proteomes:UP000027135};
RN [1] {ECO:0000313|EMBL:KDR21153.1, ECO:0000313|Proteomes:UP000027135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole organism {ECO:0000313|EMBL:KDR21153.1};
RX PubMed=24845553; DOI=10.1038/ncomms4636;
RA Terrapon N., Li C., Robertson H.M., Ji L., Meng X., Booth W., Chen Z.,
RA Childers C.P., Glastad K.M., Gokhale K., Gowin J., Gronenberg W.,
RA Hermansen R.A., Hu H., Hunt B.G., Huylmans A.K., Khalil S.M.,
RA Mitchell R.D., Munoz-Torres M.C., Mustard J.A., Pan H., Reese J.T.,
RA Scharf M.E., Sun F., Vogel H., Xiao J., Yang W., Yang Z., Yang Z., Zhou J.,
RA Zhu J., Brent C.S., Elsik C.G., Goodisman M.A., Liberles D.A., Roe R.M.,
RA Vargo E.L., Vilcinskas A., Wang J., Bornberg-Bauer E., Korb J., Zhang G.,
RA Liebig J.;
RT "Molecular traces of alternative social organization in a termite genome.";
RL Nat. Commun. 5:3636-3636(2014).
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|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; KK852570; KDR21153.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067RDT3; -.
DR STRING; 136037.A0A067RDT3; -.
DR EnsemblMetazoa; KDR21153; KDR21153; L798_04082.
DR eggNOG; KOG0382; Eukaryota.
DR InParanoid; A0A067RDT3; -.
DR OMA; WIVATKP; -.
DR OrthoDB; 3674322at2759; -.
DR Proteomes; UP000027135; 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; cd00326; alpha_CA; 1.
DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
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|RuleBase:RU367011};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367011};
KW Reference proteome {ECO:0000313|Proteomes:UP000027135};
KW Signal {ECO:0000256|RuleBase:RU367011};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU367011"
FT CHAIN 25..330
FT /note="Carbonic anhydrase"
FT /evidence="ECO:0000256|RuleBase:RU367011"
FT /id="PRO_5025094261"
FT DOMAIN 75..330
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
SQ SEQUENCE 330 AA; 37592 MW; 32957A9640EF9474 CRC64;
MVPPASRVAI AILWLSHVFL TARGLVHHYS DFLPPPTSWY NLWLPRPTDD LLLLHIQQPP
AQGRYQHSRA LSRRRHFGYS RHNGPDAWPL EYPKCNGERQ SPINLESDEM YRLVVADRLQ
WHGYWDRPRN LTLTNNGHTI QVSGNWETAP TISGGPLESE YSFSQLHFHW GSNDKIGSEH
TVGNVSFPME MHLVHYKKAY GSQDEAVKYE DGLAVVSFLF QLSEWPNPGL NAIIPFLDAM
VGAELEVTLV RPFPLEILDV SFPSEYVTYL GSLTTPPCSE VVTWIVSSRP LTLSHEQLAK
FRYLSSADGE LENNFRPVQP TNGRPVFYVT
//
