ID A0A0W1SMB7_9EURY Unreviewed; 354 AA.
AC A0A0W1SMB7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Endoglucanase {ECO:0000313|EMBL:KTG27458.1};
GN ORFNames=AUR66_13990 {ECO:0000313|EMBL:KTG27458.1};
OS Haloferax profundi.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=1544718 {ECO:0000313|EMBL:KTG27458.1, ECO:0000313|Proteomes:UP000053157};
RN [1] {ECO:0000313|EMBL:KTG27458.1, ECO:0000313|Proteomes:UP000053157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB29 {ECO:0000313|EMBL:KTG27458.1,
RC ECO:0000313|Proteomes:UP000053157};
RA Zhang G., Stingl U., Rashid M.;
RT "Haloferax profundi sp. nov. isolated from the Discovery deep brine-
RT seawater interface in the Red Sea.";
RL Submitted (DEC-2015) 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}.
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:KTG27458.1}.
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DR EMBL; LOPV01000172; KTG27458.1; -; Genomic_DNA.
DR RefSeq; WP_058572120.1; NZ_LOPV01000172.1.
DR AlphaFoldDB; A0A0W1SMB7; -.
DR OrthoDB; 30642at2157; -.
DR Proteomes; UP000053157; 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 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 354 AA; 37151 MW; 7A54DF3FDE9BA600 CRC64;
MDDDQRSFLD ALLTTPSPSG YETDGQRVWV DYVSQFADDV TVDAYGNAVA VHEGSGDGPE
IAFTGHADQI GYIVRDIDDD GFVRIGPIGG ADRTVSKGQH VTVHNEDGDV PGVIGQTAIH
LRDVGKEEYD DLEEQFVDIG VTSKGDAKDY VEVGDPVTIE GRVRDLAGDR IAANGMDNRV
GTWSAAEGLR AAVDADVDAT VYAVSTVQEE VGVQGAKMVG YDLNPDAMVA VDVTHATDNP
DVPGKAKGPV ELGEGPSISR GSANHPNVVT LARDAAAEAD IDVQLEATGT YTGTDADAFY
TSRSGIPSLN IGIPNRYMHT PVEVISTEDL DDVAALLGAM AALAGDVESF GVEL
//
