ID A0A091LAP3_CATAU Unreviewed; 495 AA.
AC A0A091LAP3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011};
DE EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011};
DE Flags: Fragment;
GN ORFNames=N323_09581 {ECO:0000313|EMBL:KFP53434.1};
OS Cathartes aura (Turkey vulture) (Vultur aura).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Accipitriformes; Cathartidae; Cathartes.
OX NCBI_TaxID=43455 {ECO:0000313|EMBL:KFP53434.1, ECO:0000313|Proteomes:UP000053745};
RN [1] {ECO:0000313|EMBL:KFP53434.1, ECO:0000313|Proteomes:UP000053745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N323 {ECO:0000313|EMBL:KFP53434.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Reversible hydration of carbon dioxide. Its role in saliva is
CC unknown. {ECO:0000256|ARBA:ARBA00025355}.
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:RU367011};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU367011};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00010718, ECO:0000256|RuleBase:RU367011}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01172}.
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; KL312938; KFP53434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091LAP3; -.
DR Proteomes; UP000053745; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR CDD; cd03125; alpha_CA_VI; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR InterPro; IPR018338; Carbonic_anhydrase_a-class_CS.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001759; Pentraxin-related.
DR PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR18952:SF110; CARBONIC ANHYDRASE 6; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR Pfam; PF00354; Pentaxin; 1.
DR PRINTS; PR00895; PENTAXIN.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SMART; SM00159; PTX; 1.
DR SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS00162; ALPHA_CA_1; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
DR PROSITE; PS51828; PTX_2; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|RuleBase:RU367011};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367011};
KW Reference proteome {ECO:0000313|Proteomes:UP000053745};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT DOMAIN 1..253
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP53434.1"
FT NON_TER 495
FT /evidence="ECO:0000313|EMBL:KFP53434.1"
SQ SEQUENCE 495 AA; 55549 MW; 30501B0F15426A4B CRC64;
EGELDEEHWG KHFADCAGKH QSPIDIQRKK VRYNPQLLQL ELSGYDGPLQ GDFTMTNNGH
SVQIDLPPTM HISRGLPGLY TAVQMHLHWG GLDLETSGSE HTIDGMRYFA ELHIVHYNSA
DYSSFEEAKD KPNGLAVLAF LYADGHFENT YYSEFISKLA KIRFAGQSTK LISLDVQAML
PENLSRFYRY QGSLTTPPCS ESVIWTIFHS PIVLSHTQIS LLENTLLDWQ NRTLRNDYRH
AQPLNGRVVE SSFRAKLTQE QCHPEEFSLR LEQIQMQLQD MKRELLNGVS HIGIKSSTFP
AFYFPVENIE SFVKVHPLHD MSLQAFTLCF WTKAQHAGSQ TIISYSTQER DNELVMTVGT
DVGLWIGGHF ISFPLYHKAQ DWLHYCMAWA SQSGMANLWL NGAAGKAKSI QKGYVSQAGG
TLVLGKDRDT LLGTFSNGFA GWMTHVNLWS QVLSPADVRA LALCKPGQLK GDVIAWGETS
MTLLGGVVLE SDTSC
//
