ID A0A091GFG3_9AVES Unreviewed; 291 AA.
AC A0A091GFG3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Regucalcin {ECO:0000256|ARBA:ARBA00016808};
DE EC=3.1.1.17 {ECO:0000256|ARBA:ARBA00013227};
DE AltName: Full=Gluconolactonase {ECO:0000256|ARBA:ARBA00032464};
DE Flags: Fragment;
GN ORFNames=N303_15189 {ECO:0000313|EMBL:KFO79899.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO79899.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO79899.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO79899.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucono-1,5-lactone + H2O = D-gluconate + H(+);
CC Xref=Rhea:RHEA:10440, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16217, ChEBI:CHEBI:18391; EC=3.1.1.17;
CC Evidence={ECO:0000256|ARBA:ARBA00001589};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the SMP-30/CGR1 family.
CC {ECO:0000256|ARBA:ARBA00008853}.
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DR EMBL; KL448073; KFO79899.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091GFG3; -.
DR STRING; 55661.A0A091GFG3; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0004341; F:gluconolactonase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR008367; Regucalcin.
DR InterPro; IPR013658; SGL.
DR InterPro; IPR005511; SMP-30.
DR PANTHER; PTHR10907; REGUCALCIN; 1.
DR PANTHER; PTHR10907:SF64; REGUCALCIN; 1.
DR Pfam; PF08450; SGL; 1.
DR PRINTS; PR01791; REGUCALCIN.
DR PRINTS; PR01790; SMP30FAMILY.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000053760}.
FT DOMAIN 8..255
FT /note="SMP-30/Gluconolactonase/LRE-like region"
FT /evidence="ECO:0000259|Pfam:PF08450"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO79899.1"
FT NON_TER 291
FT /evidence="ECO:0000313|EMBL:KFO79899.1"
SQ SEQUENCE 291 AA; 32438 MW; B9BDFB7CC2314B95 CRC64;
VVKEKNRMGE CPVWEERESA LVYVDINSQK VCRWSPLTNK VQSVSVGARV GSVALRQCGG
YVIALGTRFA FLDWDTQAVT TILEVEQDKP DNRFNDGKVD PKGRFFAGTM AEERAPGVRA
RGQGALYTLF PDHSVVRQLD QVDISNGLDW SLDHRTFFYI DSLAYAVHAF SYDAHTGKIA
CPRLLYHLEK EEQMPDGMCI DAEGKLWVAC IDGGRVIRID PETGKRIQTL RLPTPRITSC
CFGGKDYSEM YVTSAYDGLD ENTLAKEPHA GEIFKITGLG VKGIPQNFYA A
//