ID A0A161XIG3_DAUCS Unreviewed; 264 AA.
AC A0A161XIG3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Alpha-carbonic anhydrase domain-containing protein {ECO:0000259|PROSITE:PS51144};
GN ORFNames=DCAR_007756 {ECO:0000313|EMBL:KZN06919.1};
OS Daucus carota subsp. sativus (Carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=79200 {ECO:0000313|EMBL:KZN06919.1, ECO:0000313|Proteomes:UP000077755};
RN [1] {ECO:0000313|EMBL:KZN06919.1, ECO:0000313|Proteomes:UP000077755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DH1 {ECO:0000313|Proteomes:UP000077755};
RC TISSUE=Leaf {ECO:0000313|EMBL:KZN06919.1};
RX PubMed=27158781; DOI=10.1038/ng.3565;
RA Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT "A high-quality carrot genome assembly provides new insights into
RT carotenoid accumulation and asterid genome evolution.";
RL Nat. Genet. 48:657-666(2016).
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:KZN06919.1}.
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DR EMBL; LNRQ01000002; KZN06919.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A161XIG3; -.
DR STRING; 79200.A0A161XIG3; -.
DR EnsemblPlants; KZN06919; KZN06919; DCAR_007756.
DR Gramene; KZN06919; KZN06919; DCAR_007756.
DR OMA; RMRMENN; -.
DR Proteomes; UP000077755; Chromosome 2.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 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; PS51144; ALPHA_CA_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000077755};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..264
FT /note="Alpha-carbonic anhydrase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007829654"
FT DOMAIN 30..264
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
FT REGION 243..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 264 AA; 29119 MW; 7C130E802D6DF6F7 CRC64;
MASFRFSVLV ITISLVIVTA YSTLDADETI EFGYVGPKGP DKWGSLDPKF AVCADGKAQS
PIDISRTKAT PNNQLRALSR DYYSAGAKLV NNGFNIAVHF DSSAGTMNID GKNYSLLQLH
WHTPSEHTMD GKQLDAELQL VHKADDGSMS ITGILYQVGN GDSFLGRVQK HLKELAKDKC
GPNEHSEIPL GNLSTRQLKR STRNYFRYTG SFTTPPCTEN PSSMSQQQID ALKAPMEEAY
KMNARPVQPD NGRPVNLHDE PKKV
//