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Database: UniProt
Entry: A0A3L8SBD7_CHLGU
LinkDB: A0A3L8SBD7_CHLGU
Original site: A0A3L8SBD7_CHLGU 
ID   A0A3L8SBD7_CHLGU        Unreviewed;       287 AA.
AC   A0A3L8SBD7;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   RecName: Full=Carbonic anhydrase-related protein 10 {ECO:0000256|ARBA:ARBA00022137};
GN   ORFNames=DV515_00009884 {ECO:0000313|EMBL:RLV99291.1};
OS   Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC   Chloebia.
OX   NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV99291.1, ECO:0000313|Proteomes:UP000276834};
RN   [1] {ECO:0000313|EMBL:RLV99291.1, ECO:0000313|Proteomes:UP000276834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red01 {ECO:0000313|EMBL:RLV99291.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:RLV99291.1};
RX   PubMed=30282656;
RA   Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA   Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT   "A non-coding region near Follistatin controls head colour polymorphism in
RT   the Gouldian finch.";
RL   Proc. R. Soc. B 285:0-0(2018).
CC   -!- FUNCTION: Does not have a catalytic activity.
CC       {ECO:0000256|ARBA:ARBA00002258}.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000256|ARBA:ARBA00010718}.
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:RLV99291.1}.
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DR   EMBL; QUSF01000033; RLV99291.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L8SBD7; -.
DR   STRING; 44316.ENSEGOP00005009604; -.
DR   Proteomes; UP000276834; 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; cd03121; alpha_CARP_X_XI_like; 1.
DR   Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
DR   InterPro; IPR041878; Alpha_CARP_X/XI.
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:SF91; CARBONIC ANHYDRASE-RELATED PROTEIN 10; 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   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000276834}.
FT   DOMAIN          1..204
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000259|PROSITE:PS51144"
SQ   SEQUENCE   287 AA;  33137 MW;  91B26CFDF5D22875 CRC64;
     MYNTGRHVSL RLDKEHLVNI SGGPMTYSHR LEEIRLHFGS EDSQGSEHLL NGQAFSGEVQ
     LIHYNHELYT NVTEAAKSPN GLVVVSIFMK VSESSNPFLN RMLNRDTITR ITYKNDAYLL
     QGLNIEELYP ETSSFITYDG SMTIPPCYET ASWIIMNKPV YITRMQMHSL RLLSQNQPSQ
     IFLSMSDNFR PVQPLNNRCI RTNINFSLQG KDCPNNRAQK LQYRDFHGIS TVSSVYREIL
     GQAFLLEEVK EQRHDNLIIT IHRALWNPQQ EDPDLTSESH ESQRQNC
//
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