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Database: UniProt
Entry: A0A151NX67_ALLMI
LinkDB: A0A151NX67_ALLMI
Original site: A0A151NX67_ALLMI 
ID   A0A151NX67_ALLMI        Unreviewed;       789 AA.
AC   A0A151NX67;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
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};
GN   ORFNames=Y1Q_0006286 {ECO:0000313|EMBL:KYO41492.1};
OS   Alligator mississippiensis (American alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO41492.1};
RN   [1] {ECO:0000313|EMBL:KYO41492.1, ECO:0000313|Proteomes:UP000050525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO41492.1};
RX   PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA   St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA   Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA   Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA   Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA   Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA   McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA   Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA   Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA   Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA   Ray D.A.;
RT   "Sequencing three crocodilian genomes to illuminate the evolution of
RT   archosaurs and amniotes.";
RL   Genome Biol. 13:415-415(2012).
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}.
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:KYO41492.1}.
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DR   EMBL; AKHW03001628; KYO41492.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151NX67; -.
DR   Proteomes; UP000050525; 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; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR008367; Regucalcin.
DR   InterPro; IPR013658; SGL.
DR   InterPro; IPR005511; SMP-30.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR10907; REGUCALCIN; 1.
DR   PANTHER; PTHR10907:SF54; REGUCALCIN; 1.
DR   Pfam; PF08450; SGL; 2.
DR   Pfam; PF13832; zf-HC5HC2H_2; 1.
DR   PRINTS; PR01791; REGUCALCIN.
DR   PRINTS; PR01790; SMP30FAMILY.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR   PROSITE; PS51805; EPHD; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          1..102
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   REGION          108..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          336..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          492..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..543
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   789 AA;  88895 MW;  78DD7DA3F0064EA0 CRC64;
     MKATRTGTKW AHVSCALWIP EVSIACPERM EPITKVSHIP PSRWALVCSL CKLKTGACIQ
     CSVKSCITAF HVTCAFEHSL EMKTILDDGD EVKFKSYCLK HSKNKQNSLP DIDENPKSMA
     DQKHTESEKT SLRAQKLREL EEEFYTLVKV EDVAAELALP KLAVDFIYNY WKLKRKSNFN
     KPLFPPKEDE ENGLVQPKED SIHTRMRMFM HLRQDLERVR NLCYMVSRRE KLKLSHSKVH
     EQVFNLQAQL TNQEIAAGHT LTSALENTLF YPPPRITLKL KMPKSALGDC KNNSLKPGNR
     PLSPDNNTTV YNKRSLQLSK ESFEIKMKSY SRYQHDNRSN GLLGGISKSR NETKDLGPAQ
     LPEFPHGQPS GKPLALQAAL HGQSSIGNGK MQQENARLVK SNGLMGRSGD VIQRDSSSQT
     PYEHDSVLTA HLASQSSFRK STIEHFSRSF KEATNSLVRT TEDLRCCEKP TRRLSTKERL
     WNKQVLEGAP YQDNDGYCPD LELSDSEAES DENKEQVRLR RSSSERGSPS KDFGRDCHSR
     NKKNMISHSS VQSAAGSRVF IAMSSIKVEC IVDENCKIGE SPVWEEKENS LLYVDINGKK
     ISRWNSITKR VQSIAVDAPV SSVGLRKSGN YVITLGTRFA ALKWNDQSVT TIMEVDKDKL
     NNRFNDGKVD PEGRYFAANR RSIYKLEKEE SIPDGMCIDT EGKLWVACYD GGRVIRLDPE
     TGKRLQTVKL PVDKTTSCCF GGNDYSEMYV TSACQGMDDK WLSRQPQAGG IFKVTGLGVK
     GIPPYSYAG
//
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