ID A8PER9_COPC7 Unreviewed; 342 AA.
AC A8PER9;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 2.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU003956};
DE EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU003956};
DE AltName: Full=Carbonate dehydratase {ECO:0000256|RuleBase:RU003956};
GN ORFNames=CC1G_03059 {ECO:0000313|EMBL:EAU80883.2};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU80883.2, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU80883.2, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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|ARBA:ARBA00000943,
CC ECO:0000256|RuleBase:RU003956};
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00006217, ECO:0000256|RuleBase:RU003956}.
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:EAU80883.2}.
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; AACS02000008; EAU80883.2; -; Genomic_DNA.
DR RefSeq; XP_001840830.2; XM_001840778.2.
DR AlphaFoldDB; A8PER9; -.
DR STRING; 240176.A8PER9; -.
DR GeneID; 6017485; -.
DR KEGG; cci:CC1G_03059; -.
DR VEuPathDB; FungiDB:CC1G_03059; -.
DR eggNOG; KOG1578; Eukaryota.
DR HOGENOM; CLU_811371_0_0_1; -.
DR InParanoid; A8PER9; -.
DR OrthoDB; 5392875at2759; -.
DR Proteomes; UP000001861; 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:SF83; 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:UP000001861};
KW Zinc {ECO:0000256|RuleBase:RU003956}.
FT REGION 245..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 342 AA; 37810 MW; C366D792D9725204 CRC64;
MCRAARQQPD FAVHKHRRVR ARVSEGTIFD AQPGTLFAHR NVANQFLSTD PNVESALAYA
TSALNVHHII VMGHYGCGGV ASAIMSRPKG PNIDAAQSAI HNWIEPLREL YASSDRERLK
NHTRIPEPPL HEPGFRALVE ENVKSTVRRI ADSTIVRNKT GSPDTSNPYI HAIKPRPKPR
PHVLFIHGWV YDIETGKIVD LDVSIGPPGK KIPRVPSLDS VLKSTSTSAS STTTTTTTTM
TMTMISPEDD DEDEQVAANR DDAMIPESDR TATTHDDDEK NPHQRPLASP RQAIIPHRPP
SISSVSRFLQ QLPAIPSLSQ SPLPALTQVL RLIQFDLKRL SM
//
