ID H1Z2J8_9EURY Unreviewed; 697 AA.
AC H1Z2J8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Peptidase M3A and M3B thimet/oligopeptidase F {ECO:0000313|EMBL:EHQ35524.1};
GN ORFNames=Metlim_1420 {ECO:0000313|EMBL:EHQ35524.1};
OS Methanoplanus limicola DSM 2279.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoplanus.
OX NCBI_TaxID=937775 {ECO:0000313|EMBL:EHQ35524.1, ECO:0000313|Proteomes:UP000005741};
RN [1] {ECO:0000313|EMBL:EHQ35524.1, ECO:0000313|Proteomes:UP000005741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2279 {ECO:0000313|EMBL:EHQ35524.1,
RC ECO:0000313|Proteomes:UP000005741};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Wirth R., Brambilla E.-M., Klenk H.-P.,
RA Eisen J.A.;
RT "The Improved High-Quality Draft genome of Methanoplanus limicola DSM
RT 2279.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|ARBA:ARBA00006040}.
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DR EMBL; CM001436; EHQ35524.1; -; Genomic_DNA.
DR RefSeq; WP_004077277.1; NZ_CM001436.1.
DR AlphaFoldDB; H1Z2J8; -.
DR STRING; 937775.Metlim_1420; -.
DR PATRIC; fig|937775.9.peg.1609; -.
DR HOGENOM; CLU_001805_2_0_2; -.
DR InParanoid; H1Z2J8; -.
DR OrthoDB; 110158at2157; -.
DR Proteomes; UP000005741; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06455; M3A_TOP; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR024080; Neurolysin/TOP_N.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11804:SF84; SACCHAROLYSIN; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000005741};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 9..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 247..691
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 697 AA; 78958 MW; BCA2EE0F65582A26 CRC64;
MHKDSNKFLR YSFSFIIILT VILLMAAGCL QNTRDEETAG TELPEENSPI KAHYSPGEIT
QLTEEAEEAA DVSLNAIAEI PPEERNFDNT VLAFDRITTD YSDAIGPLTL MGYVYPDAEI
AAEGTSCEES AYTFETGVYT RRDLYDALKE HKPRNPEEAR LYSVIIREFE KNGLKLPEEK
LSEVREMKNR LGQLETRYSA NLNSDNTTLE FTAEELAGVP LSSVKTFAKT PQGTYLVTTK
SPDYLAVMTY AEDERTRMRM YGAYNNRQAD TNTALLEEAI LLRQKIAKAL GYSTWADYKT
DGRMAENTGN VMEFLASMKE PIKEKYTGEM RELLTVKRST DPEAATVSPW DITYLQNIKK
KEQYAYNEEK VREYFPAETV LQGLFNTYGT LFDIRFSGVE NAPVWSPDVQ LYEVKNATGN
ETIGYMYLDL YPREGKYGHF CASPLITGRL KDDGYSVPVV TIIGNFHRPE EERPSLLTVN
EIETLFHEAG HAMHFLLTDA PYGSLSGFHV EWDFIETPSQ TLEEWAWDPE VLRSISGHYN
NSSEKIPAEL CERVIDARNV GSGSKYSRLI INSLEDMRFH TAAGPVNATE IWYQTYEEMT
GTRPPAGIHQ PASFGHMMGG YDAGYYGYLW SKVYAMEIVD EFKENGMTNQ TTGMKFRNEI
LSKGNMQDGM TLLKNFLGRE PGPEALYKHL GIEKTQA
//
