ID D4DD54_TRIVH Unreviewed; 407 AA.
AC D4DD54;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925};
DE EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925};
GN ORFNames=TRV_05061 {ECO:0000313|EMBL:EFE40217.1};
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE40217.1, ECO:0000313|Proteomes:UP000008383};
RN [1] {ECO:0000313|Proteomes:UP000008383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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 -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00006217}.
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:EFE40217.1}.
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DR EMBL; ACYE01000257; EFE40217.1; -; Genomic_DNA.
DR RefSeq; XP_003020835.1; XM_003020789.1.
DR AlphaFoldDB; D4DD54; -.
DR GeneID; 9577574; -.
DR KEGG; tve:TRV_05061; -.
DR HOGENOM; CLU_053879_1_2_1; -.
DR OrthoDB; 5392875at2759; -.
DR Proteomes; UP000008383; Unassembled WGS sequence.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR CDD; cd00883; beta_CA_cladeA; 1.
DR Gene3D; 3.40.1050.10; Carbonic anhydrase; 1.
DR InterPro; IPR001765; Carbonic_anhydrase.
DR InterPro; IPR015892; Carbonic_anhydrase_CS.
DR InterPro; IPR036874; Carbonic_anhydrase_sf.
DR PANTHER; PTHR11002; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR11002:SF83; CARBONIC ANHYDRASE; 1.
DR Pfam; PF00484; Pro_CA; 1.
DR SMART; SM00947; Pro_CA; 1.
DR SUPFAM; SSF53056; beta-carbonic anhydrase, cab; 1.
DR PROSITE; PS00705; PROK_CO2_ANHYDRASE_2; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..407
FT /note="carbonic anhydrase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003055774"
FT REGION 146..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 407 AA; 45455 MW; DD20B2A2C9A08D09 CRC64;
MRGSLWSFFL CPDICFSLWS WHWPQKLPWP YQKKTLLPVY THSFFSSSAA QEKKRAEGQG
RGVIIIQDNT HALPSALFLF FFFISALNYL HLGNFMGKTQ LTSASPFVSF SWAFANQPSV
IRTLPVSQRI IPCPTPSLAT RLADLPSAPR DSFSQRQQIK PFSSTRPGLK MSSSNNSNSH
PIPSMAAQNE QNTAPDSYQL AMAKNNIWAT KLDEEQPDLF PKLASGQSPE ILWIGCADSR
CPETTVLGLQ PGDVFVHRNI ANVVQYNDIS AATVIEFAVV YLKVKHIILC GHTSCGGINA
ALANKKLGLL DTWLMPLRRL REQHMDVLKD LELKEAAVKL AEINVENGLR VLRENSAVLD
AIEERGLKLH GVIYDVGSGK LRELEITESM DSISRRIASF KTVKNEE
//