ID A0A1D3L3V0_9EURY Unreviewed; 338 AA.
AC A0A1D3L3V0;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Putative zinc metalloprotease EGY1,chloroplastic {ECO:0000313|EMBL:SCG86334.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:SCG86334.1};
GN Name=EGY1 {ECO:0000313|EMBL:SCG86334.1};
GN ORFNames=MCBB_1783 {ECO:0000313|EMBL:SCG86334.1};
OS Methanobacterium congolense.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX NCBI_TaxID=118062 {ECO:0000313|EMBL:SCG86334.1, ECO:0000313|Proteomes:UP000094707};
RN [1] {ECO:0000313|EMBL:SCG86334.1, ECO:0000313|Proteomes:UP000094707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Buetzberg {ECO:0000313|EMBL:SCG86334.1};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; LT607756; SCG86334.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D3L3V0; -.
DR STRING; 118062.MCBB_1783; -.
DR KEGG; mcub:MCBB_1783; -.
DR PATRIC; fig|129848.4.peg.1821; -.
DR OrthoDB; 19110at2157; -.
DR Proteomes; UP000094707; Chromosome I.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06160; S2P-M50_like_2; 1.
DR InterPro; IPR044838; EGY1-like.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR31412; ZINC METALLOPROTEASE EGY1; 1.
DR PANTHER; PTHR31412:SF5; ZINC METALLOPROTEASE EGY2, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:SCG86334.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000313|EMBL:SCG86334.1};
KW Protease {ECO:0000313|EMBL:SCG86334.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094707};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 77..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 103..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 317..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 108..278
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 338 AA; 36731 MW; DB57F9B459730050 CRC64;
MENFDIIEDY ISKHFQIHGF HSTEEGSFFT VLSYDKKIFT QLVHEMDEIG YIPFIEPYNG
FYRIGIAQKP ERGESRVWIN LLLFLATIAT TLYAGYTFGG GKIWDAVAFS IAIIAVLGTH
ETAHFAAARK HGVDATLPYF VPAPTLIGTF GAVINVKSPI PTKNALFDLG FSGPLAGIIV
AIPVLIIGIL LSSVEPVSAG VLTFNPPLLM SILTYFLLPP VPSGYALNLH PVAFAGWVGI
IVTMLNLMPV AFLDGGHISR SLFSEGVHKV VSMIGITVTV VLGWIPMAVL MFIILFATKR
HPGALDNVSG ITKWRKAMAV VMLLVFILCL SPVPGSPF
//
