ID C6W594_DYAFD Unreviewed; 606 AA.
AC C6W594;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Peptidase M61 domain protein {ECO:0000313|EMBL:ACT92454.1};
GN OrderedLocusNames=Dfer_1205 {ECO:0000313|EMBL:ACT92454.1};
OS Dyadobacter fermentans (strain ATCC 700827 / DSM 18053 / CIP 107007 / KCTC
OS 52180 / NS114).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=471854 {ECO:0000313|EMBL:ACT92454.1, ECO:0000313|Proteomes:UP000002011};
RN [1] {ECO:0000313|EMBL:ACT92454.1, ECO:0000313|Proteomes:UP000002011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700827 / DSM 18053 / CIP 107007 / KCTC 52180 / NS114
RC {ECO:0000313|Proteomes:UP000002011};
RX PubMed=21304649; DOI=10.4056/sigs.19262;
RA Lang E., Lapidus A., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H.,
RA Cheng J.F., Land M., Hauser L., Chang Y.J., Jeffries C.D., Kopitz M.,
RA Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA Mavrommatis K., Chen A., Palaniappan K., Chain P., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Goker M., Rohde M., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Dyadobacter fermentans type strain (NS114).";
RL Stand. Genomic Sci. 1:133-140(2009).
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DR EMBL; CP001619; ACT92454.1; -; Genomic_DNA.
DR RefSeq; WP_015810708.1; NC_013037.1.
DR AlphaFoldDB; C6W594; -.
DR STRING; 471854.Dfer_1205; -.
DR KEGG; dfe:Dfer_1205; -.
DR eggNOG; COG3975; Bacteria.
DR HOGENOM; CLU_022755_0_1_10; -.
DR OrthoDB; 9778516at2; -.
DR Proteomes; UP000002011; Chromosome.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.60.40.3650; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR024191; Peptidase_M61.
DR InterPro; IPR007963; Peptidase_M61_catalytic.
DR InterPro; IPR040756; Peptidase_M61_N.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF05299; Peptidase_M61; 1.
DR Pfam; PF17899; Peptidase_M61_N; 1.
DR PIRSF; PIRSF016493; Glycyl_aminpptds; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002011};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..606
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002972489"
FT DOMAIN 23..189
FT /note="Peptidase M61 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17899"
FT DOMAIN 284..402
FT /note="Peptidase M61 catalytic"
FT /evidence="ECO:0000259|Pfam:PF05299"
FT DOMAIN 510..570
FT /note="PDZ"
FT /evidence="ECO:0000259|Pfam:PF13180"
SQ SEQUENCE 606 AA; 68101 MW; 8D37D5CB736F3969 CRC64;
MKKLAALLAT PLICSYAFAQ KIQYDVSFPN IVHHEARIAL SVSDAPQKEL LFRMSRSSPG
RYATHEYGKN VYDVKAFDKS GKPVAIARVD GDVYKVSGID GYVRVEYILY ANHADGTYAG
IDQNSVHLNM PAAFMWVKGL EKSPMEIRFD LPQNSQWTIA TQLKTTADAH TFTAPDLQYF
MDSPTKIGKL TVKDWNVPNA DSKPARFRLA LEAKSSDSLA TVFANKIKRI TEEARMVFGE
FPAFDNGHYT FLASINPYVK GDGMEHRNST MISVPVVFNA SDNLLGVFSH EFFHAWNVER
IRPKTLEPFN FEKSNMSFEL WFAEGFTQYY GELLLERAGF HSVDEYCNIL GMLVNAKENT
VGARRISPVE ASCNAVFVDA GVAVDKANYP NMHTSYYTYG AALALALDLQ LREKGLNLDD
FMKAVWAKHG KPEAAYNVAD LQAVLESYTR DKAFAQRFFS KYISGHESID YAPLLAKAGL
LLRKQFEGQA WIGDFVRYKE GTGLTITTNT TIGSPLYTAG LDIDDEILKV DGKVISTNDE
LLAILKAHKP GDQITVEYRH RDDYKTAVVE MVQHPRWQVA TFEQAGKTVT PEMQTFRNAW
LGSKWK
//
