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Database: UniProt
Entry: K1XKD9_MARBU
LinkDB: K1XKD9_MARBU
Original site: K1XKD9_MARBU 
ID   K1XKD9_MARBU            Unreviewed;       272 AA.
AC   K1XKD9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   03-MAY-2023, entry version 36.
DE   SubName: Full=Carbonic anhydrase {ECO:0000313|EMBL:EKD12934.1};
GN   ORFNames=MBM_08888 {ECO:0000313|EMBL:EKD12934.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD12934.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD12934.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD12934.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
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DR   EMBL; JH921453; EKD12934.1; -; Genomic_DNA.
DR   RefSeq; XP_007296777.1; XM_007296715.1.
DR   AlphaFoldDB; K1XKD9; -.
DR   STRING; 1072389.K1XKD9; -.
DR   GeneID; 18764823; -.
DR   KEGG; mbe:MBM_08888; -.
DR   eggNOG; KOG0382; Eukaryota.
DR   HOGENOM; CLU_039326_4_0_1; -.
DR   InParanoid; K1XKD9; -.
DR   OMA; WHTHTPS; -.
DR   OrthoDB; 49814at2759; -.
DR   Proteomes; UP000006753; Unassembled WGS sequence.
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 1; 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:UP000006753};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..272
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003853138"
FT   DOMAIN          41..272
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000259|PROSITE:PS51144"
SQ   SEQUENCE   272 AA;  29173 MW;  712D54B893AB44C7 CRC64;
     MIRALFAIAA LASNVLACPD HSPSKAALRK RLLAGDGTNA DDWTWDNTGA WPAISAICGN
     GTMQSPIDLD PGNFSQVMVP TFNYAMDTVC GSLTNSGYGP AFTLTAMEQD DIDEHPSFTA
     DGVSYYLLGW HTHTPSEHTF GGQAVEAELH LVHGDKDGNA IGVVGFPLTV GDESSFLAQF
     MGSTTMPSKE TETPVAVSDI NMGLILKDAG DFQTYWSYAG SLTTPPCSEG KRWWVSGQTV
     TISPAQWEDL QAVSAPSARE VQKIGRHRLN QD
//
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