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Database: UniProt
Entry: A0A0F7DBW7_9EURY
LinkDB: A0A0F7DBW7_9EURY
Original site: A0A0F7DBW7_9EURY 
ID   A0A0F7DBW7_9EURY        Unreviewed;       339 AA.
AC   A0A0F7DBW7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Peptidase family M50 {ECO:0000313|EMBL:AKG91811.1};
GN   ORFNames=GAH_00859 {ECO:0000313|EMBL:AKG91811.1};
OS   Geoglobus ahangari.
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Geoglobus.
OX   NCBI_TaxID=113653 {ECO:0000313|EMBL:AKG91811.1, ECO:0000313|Proteomes:UP000034723};
RN   [1] {ECO:0000313|EMBL:AKG91811.1, ECO:0000313|Proteomes:UP000034723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=234 {ECO:0000313|EMBL:AKG91811.1,
RC   ECO:0000313|Proteomes:UP000034723};
RA   Manzella M.P., Holmes D.E., Rocheleau J.M., Chung A., Reguera G.,
RA   Kashefi K.;
RT   "The complete genome sequence of the hyperthermophilic, obligate iron-
RT   reducing archaeon Geoglobus ahangari strain 234T.";
RL   Submitted (APR-2015) 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; CP011267; AKG91811.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F7DBW7; -.
DR   STRING; 113653.GAH_00859; -.
DR   KEGG; gah:GAH_00859; -.
DR   PATRIC; fig|113653.22.peg.858; -.
DR   HOGENOM; CLU_028221_0_1_2; -.
DR   InParanoid; A0A0F7DBW7; -.
DR   Proteomes; UP000034723; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034723};
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..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        132..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        163..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        263..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        311..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          106..262
FT                   /note="Peptidase M50"
FT                   /evidence="ECO:0000259|Pfam:PF02163"
SQ   SEQUENCE   339 AA;  37689 MW;  4EB8877D90DA84ED CRC64;
     MRSVDESTLS RFFHVYYKEA QGDVVRYYVM PLVSLNDPNL QLFLQELSAD YDVRVYSRYG
     EIVLEVKPRR ESHRLNVILF ILTFLSVTFT GSMFYGSFDL FLGLQFAVAV MFVLGSHEMG
     HFLASKRWGM KASLPYFIPF PTIIGTLGAI IKQRGVIKNR KALMEIGASG PLAGIVASIF
     VTYLGLRMSV PVAPERVEGA ILLGEPLLFR FVASLAGFDG QFIHPVAFAG WVGMFITALN
     LIPVGQLDGG HVMRAMIGER AEVVSRIFPF VLLGIGFVFR ESGVWFFWGL LTLFFSMQRH
     PKPADDSPLP ASHVLLGVLT FAIGVLCFTP VPFTIAESL
//
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