ID A0A1G7T715_9EURY Unreviewed; 353 AA.
AC A0A1G7T715;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Endoglucanase {ECO:0000313|EMBL:SDG30862.1};
GN ORFNames=SAMN05216218_12320 {ECO:0000313|EMBL:SDG30862.1};
OS Halorientalis regularis.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halorientalis.
OX NCBI_TaxID=660518 {ECO:0000313|EMBL:SDG30862.1, ECO:0000313|Proteomes:UP000199076};
RN [1] {ECO:0000313|EMBL:SDG30862.1, ECO:0000313|Proteomes:UP000199076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M 10760 {ECO:0000313|EMBL:SDG30862.1,
RC ECO:0000313|Proteomes:UP000199076};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|PIRSR:PIRSR001123-2};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000256|PIRSR:PIRSR001123-2};
CC -!- SIMILARITY: Belongs to the peptidase M42 family.
CC {ECO:0000256|ARBA:ARBA00006272, ECO:0000256|PIRNR:PIRNR001123}.
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DR EMBL; FNBK01000023; SDG30862.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7T715; -.
DR OrthoDB; 30642at2157; -.
DR Proteomes; UP000199076; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05656; M42_Frv; 1.
DR Gene3D; 2.40.30.40; Peptidase M42, domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008007; Peptidase_M42.
DR InterPro; IPR023367; Peptidase_M42_dom2.
DR PANTHER; PTHR32481; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR32481:SF0; AMINOPEPTIDASE YPDE-RELATED; 1.
DR Pfam; PF05343; Peptidase_M42; 1.
DR PIRSF; PIRSF001123; PepA_GA; 1.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670}.
FT ACT_SITE 209
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 353 AA; 36731 MW; 024BDFDA7626E95B CRC64;
MDEQRRAFLD DLLDTATPSG FETAGQQRWT EYVSTFADEV RTDDYGNAVA VLEGDADGPA
VALAGHGDEI GFMIRDITDS GMLSLTRIGG SDRTVSKGQH VQIHTDDGPV PGVIGQTAIH
LRDSGEESVD DISEQSIDVG ASDAEEAEEL VERGDPVTFQ QTVTELSNGR VAARGMDNRI
GIFAAAEGLR RAAERDPDAT VYAVSTVQEE LGLQGAKMVG FDLAPDAVIA TDVTHATDSP
TAPASSASGV ALGEGPVVAR GSANHPAVVT AVREAAADAD IDVQLAASGS RTGTDADAFY
TSRGGIPSLN LGVPNRYMHT PVEVVELEDL DATADLLAAF ATEAGGRSFS TDL
//
