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Database: UniProt
Entry: A0A0N4Y9V3_NIPBR
LinkDB: A0A0N4Y9V3_NIPBR
Original site: A0A0N4Y9V3_NIPBR 
ID   A0A0N4Y9V3_NIPBR        Unreviewed;       200 AA.
AC   A0A0N4Y9V3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU003956};
DE            EC=4.2.1.1 {ECO:0000256|RuleBase:RU003956};
DE   AltName: Full=Carbonate dehydratase {ECO:0000256|RuleBase:RU003956};
GN   ORFNames=NBR_LOCUS13125 {ECO:0000313|EMBL:VDL76714.1};
OS   Nippostrongylus brasiliensis (Rat hookworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Heligmosomidae; Nippostrongylus.
OX   NCBI_TaxID=27835 {ECO:0000313|Proteomes:UP000038043, ECO:0000313|WBParaSite:NBR_0001312401-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:NBR_0001312401-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDL76714.1, ECO:0000313|Proteomes:UP000271162}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Reversible hydration of carbon dioxide.
CC       {ECO:0000256|RuleBase:RU003956}.
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:RU003956};
CC   -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC       {ECO:0000256|ARBA:ARBA00006217, ECO:0000256|RuleBase:RU003956}.
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DR   EMBL; UYSL01020950; VDL76714.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N4Y9V3; -.
DR   STRING; 27835.A0A0N4Y9V3; -.
DR   WBParaSite; NBR_0001312401-mRNA-1; NBR_0001312401-mRNA-1; NBR_0001312401.
DR   OMA; MEWACSQ; -.
DR   Proteomes; UP000038043; Unplaced.
DR   Proteomes; UP000271162; 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   Gene3D; 3.40.1050.10; Carbonic anhydrase; 1.
DR   InterPro; IPR001765; Carbonic_anhydrase.
DR   InterPro; IPR036874; Carbonic_anhydrase_sf.
DR   PANTHER; PTHR11002; CARBONIC ANHYDRASE; 1.
DR   PANTHER; PTHR11002:SF69; CARBONIC ANHYDRASE; 1.
DR   Pfam; PF00484; Pro_CA; 1.
DR   SMART; SM00947; Pro_CA; 1.
DR   SUPFAM; SSF53056; beta-carbonic anhydrase, cab; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|RuleBase:RU003956};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271162};
KW   Zinc {ECO:0000256|RuleBase:RU003956}.
SQ   SEQUENCE   200 AA;  22797 MW;  4A39B095AC501E2A CRC64;
     MFVVRNSGNM IPHAAHYGPS GYEVSVTTEP AALELAVTRG HIHHVIVCGH SDCKAINTLY
     NLHKHPKSFD PQSPMDHWLR RHGFTSLKRL EERLADPSAK PLKFVSDNPN FNFEAIIDPD
     NKWGVEDKLS QINTLQQLEN IASHGFMAEF LEKKTVDIHA MWFDIFAGEM YMFSKPHSQF
     VLVDEETVGQ LEKEIEQQVS
//
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