GenomeNet

Database: UniProt
Entry: E9FX52_DAPPU
LinkDB: E9FX52_DAPPU
Original site: E9FX52_DAPPU 
ID   E9FX52_DAPPU            Unreviewed;       454 AA.
AC   E9FX52;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011};
DE            EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011};
GN   Name=CAA6F {ECO:0000313|EMBL:EFX88012.1};
GN   ORFNames=DAPPUDRAFT_442468 {ECO:0000313|EMBL:EFX88012.1};
OS   Daphnia pulex (Water flea).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX   NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX88012.1, ECO:0000313|Proteomes:UP000000305};
RN   [1] {ECO:0000313|EMBL:EFX88012.1, ECO:0000313|Proteomes:UP000000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21292972; DOI=10.1126/science.1197761;
RA   Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A.,
RA   Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J.,
RA   Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q.,
RA   Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D.,
RA   Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D.,
RA   Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J.,
RA   Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M.,
RA   Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y.,
RA   Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H.,
RA   Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R.,
RA   Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P.,
RA   Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.;
RT   "The ecoresponsive genome of Daphnia pulex.";
RL   Science 331:555-561(2011).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GL732526; EFX88012.1; -; Genomic_DNA.
DR   AlphaFoldDB; E9FX52; -.
DR   STRING; 6669.E9FX52; -.
DR   EnsemblMetazoa; EFX88012; EFX88012; DAPPUDRAFT_442468.
DR   KEGG; dpx:DAPPUDRAFT_442468; -.
DR   eggNOG; KOG0382; Eukaryota.
DR   HOGENOM; CLU_039326_2_0_1; -.
DR   InParanoid; E9FX52; -.
DR   Proteomes; UP000000305; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
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:SF259; CARBONIC ANHYDRASE 4; 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, ECO:0000313|EMBL:EFX88012.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU367011};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000305};
KW   Signal {ECO:0000256|RuleBase:RU367011};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|RuleBase:RU367011"
FT   CHAIN           26..454
FT                   /note="Carbonic anhydrase"
FT                   /evidence="ECO:0000256|RuleBase:RU367011"
FT                   /id="PRO_5025097066"
FT   DOMAIN          159..414
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000259|PROSITE:PS51144"
SQ   SEQUENCE   454 AA;  49456 MW;  1419EB09C95DE31B CRC64;
     MQVSRPNGIL AIVVVFMGLL APTKCFPIIG EPFVAPEFLP TTARANPAIP EAIPYTRIPY
     TPSTAAPKEN AAYPSPSTYS YTLKPEVTTT ALSSTSDKIQ SIVATTTSTI DAPGLAATSA
     ITTSSIIPSD ATTSPPVNAG RVDDSAFEHF SLKPHQAKPS WTHKDSVGWH SKFPTCGGSQ
     QSPIDIQPKS TVLTAYPKFT FHNYGNLISM ELINNGHSAV YNLPPDYPTE EMPHITGGGL
     DDTFAFVQFH LHWGSESSKG SEHLIKSKGY PGELHLVHFN TKYGSFAEAS QHSDGVAVLG
     IFLKVGPSDS QSFQPLVEQL GEISKDGDET VLRKPVALND ILPGRTSSFY RYSGSLTTPN
     CQQIVIWTIF DNPIEISEKQ LDKFRSLQGD DGFNMVNNFR PTLPVNGRTV FYRSFTGCEI
     PRSWPITSSP FSEAYKWSKC LMGFAYKSVA PSSL
//
DBGET integrated database retrieval system