ID A7HEA0_ANADF Unreviewed; 623 AA.
AC A7HEA0;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Peptidase M28 {ECO:0000313|EMBL:ABS27046.1};
DE Flags: Precursor;
GN OrderedLocusNames=Anae109_2846 {ECO:0000313|EMBL:ABS27046.1};
OS Anaeromyxobacter sp. (strain Fw109-5).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=404589 {ECO:0000313|EMBL:ABS27046.1, ECO:0000313|Proteomes:UP000006382};
RN [1] {ECO:0000313|EMBL:ABS27046.1, ECO:0000313|Proteomes:UP000006382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fw109-5 {ECO:0000313|EMBL:ABS27046.1,
RC ECO:0000313|Proteomes:UP000006382};
RX PubMed=25614562; DOI=10.1128/genomeA.01449-14;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA Loeffler F.E., Fields M.W.;
RT "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT metal-reducing bacterium isolated from a contaminated subsurface
RT environment.";
RL Genome Announc. 3:0-0(2015).
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DR EMBL; CP000769; ABS27046.1; -; Genomic_DNA.
DR AlphaFoldDB; A7HEA0; -.
DR STRING; 404589.Anae109_2846; -.
DR KEGG; afw:Anae109_2846; -.
DR eggNOG; COG0750; Bacteria.
DR eggNOG; COG2234; Bacteria.
DR HOGENOM; CLU_019932_1_0_7; -.
DR Proteomes; UP000006382; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04822; PA_M28_1_3; 1.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147:SF26; ENDOPLASMIC RETICULUM METALLOPEPTIDASE 1; 1.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022438};
KW Protease {ECO:0000256|ARBA:ARBA00022438};
KW Reference proteome {ECO:0000313|Proteomes:UP000006382};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 38..623
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002710166"
FT DOMAIN 516..586
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 623 AA; 66132 MW; 71984D625A4376AF CRC64;
MEAALPRRAC RPIYRRMRLP GTLALLALAL ASCGRRAATR AAPEPAFDAG RARAEVGWLA
DPARTGRGVG TPGAAQAADW IAARFREAGL APAWDEGYLQ RFEAPFRATL GERNAFAVGS
SHGELERDFL PFDFSDDGAV EAEVVFAGHG ITAPALGHDD YGGLDVKGKI VLVAQDFPRE
SDAASPFRDP RHYRFAEWRY KATNAREHGA AALIGVRDVW AEGHGGADDL PPWRGQVSSR
AGIVAARVTA AALARAGVDV RALAAPGEAD GKPHSRPLGV RARLEVRVLH ERATTANVVA
ILPGRDPAVA GECVVVGAHH DHLGLGGDSS LAPERLGTVH PGADDNASGV AALLAVARAF
AAEGPPRRTL LFAAFGAEEL GILGSSELAQ HPPPRCPTER MQLMVNLDMV GRPAAGKVYV
DGADTARGLR DLVKALAERP PRLPLKLAFG EGDGYGPSDH TSFYARDVPV LFLFTGPHPD
YHRPSDTPDK IDGAGLAAVA RLAYRAAREA AERDGRLEVV RTASPPPRER GERGYGTYLG
AIPDFAERSA PGVLLTGVRA GSPAERAGIA AGDVLLRVGP TKLLGLQDLA FALRSHRPGD
EVEVEWERAG ARRTAKVRLE ERR
//
