ID A0A202E9V1_9EURY Unreviewed; 353 AA.
AC A0A202E9V1;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Endoglucanase {ECO:0000313|EMBL:OVE85031.1};
GN ORFNames=B2G88_11810 {ECO:0000313|EMBL:OVE85031.1};
OS Natronolimnobius baerhuensis.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronolimnobius.
OX NCBI_TaxID=253108 {ECO:0000313|EMBL:OVE85031.1, ECO:0000313|Proteomes:UP000196084};
RN [1] {ECO:0000313|EMBL:OVE85031.1, ECO:0000313|Proteomes:UP000196084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3597 {ECO:0000313|EMBL:OVE85031.1,
RC ECO:0000313|Proteomes:UP000196084};
RA Zhao B.;
RT "Natronthermophilus aegyptiacus gen. nov.,sp. nov., an aerobic, extremely
RT halophilic alkalithermophilic archaeon isolated from the athalassohaline
RT Wadi An Natrun, Egypt.";
RL Submitted (FEB-2017) 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:OVE85031.1}.
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DR EMBL; MWPH01000002; OVE85031.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A202E9V1; -.
DR OrthoDB; 30642at2157; -.
DR Proteomes; UP000196084; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000196084}.
FT ACT_SITE 208
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 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 318
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; 37470 MW; B951C03B35DBE3EC CRC64;
MNASSRDFLV ELLETPSPSG YETRGQRVWL DYVDQFADDV RTDAYGNAIA VHEGDPDAPE
VVLTGHADEI GFIVRSIDDD GFVRPGRIGG SDPSVSQGQH VTIHAADGPV EGVVGQTAIH
LRDESDDDPE ISDLWIDIGA ESETEASERL EIGDPITFSS TVSWLSETRL AARGLDNRVG
TWAAAEGFRN AVENDTEATV YAVSTVQEEV GREGAKMVGF DLEPDAVVVV DVGHAVDYPS
APSEKTSQME LGGGPALGRG SSNHPVLFEA LRSVAADREI DVQLEALGLG TGTDADGFFT
AAGGIPSQVV SVPNRYMHTP VEVIDTDDLE DVATLLGGFA NRASEFAPFA VDI
//