ID A0A0K6FZ23_9AGAM Unreviewed; 708 AA.
AC A0A0K6FZ23;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925};
DE EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925};
GN ORFNames=RSOLAG22IIIB_04645 {ECO:0000313|EMBL:CUA71526.1};
OS Rhizoctonia solani.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX NCBI_TaxID=456999 {ECO:0000313|EMBL:CUA71526.1, ECO:0000313|Proteomes:UP000044841};
RN [1] {ECO:0000313|EMBL:CUA71526.1, ECO:0000313|Proteomes:UP000044841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBA 69670 {ECO:0000313|EMBL:CUA71526.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CYGV01001245; CUA71526.1; -; Genomic_DNA.
DR Proteomes; UP000044841; Unassembled WGS sequence.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.40.1050.10; Carbonic anhydrase; 1.
DR Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR InterPro; IPR001765; Carbonic_anhydrase.
DR InterPro; IPR036874; Carbonic_anhydrase_sf.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11002; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR11002:SF83; CARBONIC ANHYDRASE; 1.
DR Pfam; PF00484; Pro_CA; 1.
DR Pfam; PF00264; Tyrosinase; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SMART; SM00947; Pro_CA; 1.
DR SUPFAM; SSF53056; beta-carbonic anhydrase, cab; 1.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000044841};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..708
FT /note="carbonic anhydrase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005502837"
FT DOMAIN 91..300
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|Pfam:PF00264"
FT REGION 405..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 708 AA; 78327 MW; F42925476E3243FA CRC64;
MHTPSLLFAL SVIIGVIASP VEDTSTQAAE ASTASKCRNP EIRREWRKFS SSEKAAYIAA
VNCLARKPHT SALKPAYPRS NIPSVTEDSS YYDDMTYIHM DQTDQIHYTG LFLPWHRWFV
NEHVQQLKMQ CGYKGVMPYW VPIQLLGLVD SEIHFKTTEX XXXXXXXXTT GGFSNMTVAY
PVKHNIRRQF TLFPYLDWYW LQRPNEAANL TITKAYVDAA INGYVGDFVG FQNATEKAQA
FHPNIHMILG GDMAGTCPAT AGSSCVGGST WTPNDVCNRG FPIFFLHHAN MDRIWYLWQL
KNPANANAFK GGSEYYGSSA LGFGYGVTVI TEFARDLPRW GVGKLYLSGR SPAQVISLPL
PKCFHLNRIT PTLFNRVFSM FSSAIGPQSV TRASLRHKCK LNAIIPRSSQ SRQPHNFPFI
LPRSNSVSEQ KQNRPSEESR YKNQGLFSPT ATPRHPPAFR DSTLIPRSSL QSTSSSITFP
HTSPDPFGLP FYNPPEEMSE VALAPLIASN AKWAAEVREK YPTFFVDAAK GQSPKVLWIG
CADSRVPEST VLGCKPGEIF VHRNIANQFH PEDDSALAVL TYAVENLGVE HIVIAGHTQC
GGAAACHAAA QNLNAAAPPA TPLARWLNPL TQLAASLASE KTDTHDTSAE LSTLVEVNVR
KQVDNVVDTD VVQRAWASGK QVYVHGWVYM IETGTIKDLK VTVNPPAY
//
