ID A0A0N4ZSS2_PARTI Unreviewed; 288 AA.
AC A0A0N4ZSS2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011};
DE EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011};
OS Parastrongyloides trichosuri (Possum-specific nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Parastrongyloides.
OX NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0001155400.1};
RN [1] {ECO:0000313|WBParaSite:PTRK_0001155400.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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 AlphaFoldDB; A0A0N4ZSS2; -.
DR STRING; 131310.A0A0N4ZSS2; -.
DR WBParaSite; PTRK_0001155400.1; PTRK_0001155400.1; PTRK_0001155400.
DR Proteomes; UP000038045; Unplaced.
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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT DOMAIN 44..288
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
SQ SEQUENCE 288 AA; 32938 MW; 0CDE4C18A1C55373 CRC64;
MFKTLYRDSG VGNVREKVKA FEEHNNKDEI SDCESHKKAN MTPQIWNYDD NGPCGPCNWP
GDIHGKCQSP IDIDISKIVR VAADDQFQFK NYDKPLDGQF LNNGHSIQFL PKDNGEMPSI
IGGKLDQEYR FIQYHFHWGQ HNDEGSEHTL NSLQYPVELH LVHQGTKDPS KLAVVGVFIR
VSDDGKAFHT EEEGLDKLIE PNSKTLAKSQ KLVDKLPKNL SSFIRYDGSL TTPPCTENVT
WTIFTQPISI TTTQVQKLRK VKDIEGKVIL KNFRPTQDWH DRTVYHVC
//
