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Database: UniProt
Entry: C9SCI8_VERA1
LinkDB: C9SCI8_VERA1
Original site: C9SCI8_VERA1 
ID   C9SCI8_VERA1            Unreviewed;       221 AA.
AC   C9SCI8;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   03-MAY-2023, entry version 53.
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=VDBG_02912 {ECO:0000313|EMBL:EEY16803.1};
OS   Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS   (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN   [1] {ECO:0000313|Proteomes:UP000008698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC   {ECO:0000313|Proteomes:UP000008698};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
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}.
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DR   EMBL; DS985216; EEY16803.1; -; Genomic_DNA.
DR   RefSeq; XP_003006773.1; XM_003006727.1.
DR   AlphaFoldDB; C9SCI8; -.
DR   STRING; 526221.C9SCI8; -.
DR   GeneID; 9532915; -.
DR   KEGG; val:VDBG_02912; -.
DR   eggNOG; KOG1578; Eukaryota.
DR   HOGENOM; CLU_053879_3_1_1; -.
DR   OMA; PANEIIG; -.
DR   OrthoDB; 5392875at2759; -.
DR   Proteomes; UP000008698; 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   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:SF51; 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; PS00704; PROK_CO2_ANHYDRASE_1; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003956};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008698};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003956}.
FT   COILED          130..157
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   221 AA;  25509 MW;  13C9774709809D09 CRC64;
     MAEQDITKYL TQTHDRLFEH NKIWAAEQAK KDPEFFTKLS AGQTPEYLWI GCADSRIPAE
     QITGLQPGEA FIHRNIANLV CNIDLNVMSV INYAVRHLHV KHIIVCGHYG CGGVKAAMTP
     KDLGILNPWL RNIRDVYRLH ENELDQIKDE SKRYDRLVEL NVVEQCRNVI KSAAVQQSYK
     ENQYPIVHGW VFGFQDGLLH DLKIDFESVL HDIQKIYNLN D
//
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