UniProt: A0A1R3FZ54

Database: UniProt
Entry: A0A1R3FZ54_COCAP

LinkDB:  A0A1R3FZ54_COCAP 
Original site:  A0A1R3FZ54_COCAP

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (9)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (2)   
   SMART (1)   
All databases (14)   

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ID   A0A1R3FZ54_COCAP        Unreviewed;       268 AA.
AC   A0A1R3FZ54;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU367011};
DE            EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU367011};
GN   ORFNames=CCACVL1_30002 {ECO:0000313|EMBL:OMO51105.1};
OS   Corchorus capsularis (Jute).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX   NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO51105.1, ECO:0000313|Proteomes:UP000188268};
RN   [1] {ECO:0000313|EMBL:OMO51105.1, ECO:0000313|Proteomes:UP000188268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC   TISSUE=Whole seedling {ECO:0000313|EMBL:OMO51105.1};
RA   Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA   Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA   Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT   "Corchorus capsularis genome sequencing.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Reversible hydration of carbon dioxide.
CC       {ECO:0000256|ARBA:ARBA00002904, 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|ARBA:ARBA00000943,
CC         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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000256|ARBA:ARBA00004470}.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000256|RuleBase:RU367011}.
CC   -!- SIMILARITY: Belongs to the alpha-class carbonic anhydrase family.
CC       {ECO:0000256|ARBA:ARBA00006365}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OMO51105.1}.
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DR   EMBL; AWWV01015951; OMO51105.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R3FZ54; -.
DR   STRING; 210143.A0A1R3FZ54; -.
DR   EnsemblPlants; OMO51105; OMO51105; CCACVL1_30002.
DR   Gramene; OMO51105; OMO51105; CCACVL1_30002.
DR   OMA; HDLEIHI; -.
DR   OrthoDB; 751784at2759; -.
DR   Proteomes; UP000188268; Unassembled WGS sequence.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
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:SF285; ALPHA CARBONIC ANHYDRASE 4-RELATED; 1.
DR   PANTHER; PTHR18952; 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:UP000188268};
KW   Signal {ECO:0000256|RuleBase:RU367011};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|RuleBase:RU367011"
FT   CHAIN           23..268
FT                   /note="Carbonic anhydrase"
FT                   /evidence="ECO:0000256|RuleBase:RU367011"
FT                   /id="PRO_5025097148"
FT   DOMAIN          24..256
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000259|PROSITE:PS51144"
SQ   SEQUENCE   268 AA;  28893 MW;  A797F49B216C4A79 CRC64;
     MKCFAILLFA SLIFMIPSQT EGQEDFNYDE SSGKGPSQWG SLRPEWQTCG SGQSQSPIDI
     PVGNVVVASD LGDLQASYSS RSAVLKNRGH DIAVLWNGGD AGNINIDGID YKILQCHWHS
     PSEHTIGGTR HDLEIHIVHQ DAQKQIAVLS MLFQIGQPDS FLSGLLSAIE NVGGGEVNLG
     NKNPGDIGFV GRDYYRYEGS LSTPPCTEGV VWTVFREVKT ASTEQIQALK APLAEEVKDN
     SRPTQSLNGR EVLLYQPSGS TGRGGGCA
//

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