ID Q1DAX1_MYXXD Unreviewed; 542 AA.
AC Q1DAX1;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Peptidase, S8 (Subtilisin) family {ECO:0000313|EMBL:ABF86736.1};
GN OrderedLocusNames=MXAN_1967 {ECO:0000313|EMBL:ABF86736.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF86736.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF86736.1, ECO:0000313|Proteomes:UP000002402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; CP000113; ABF86736.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1DAX1; -.
DR STRING; 246197.MXAN_1967; -.
DR EnsemblBacteria; ABF86736; ABF86736; MXAN_1967.
DR KEGG; mxa:MXAN_1967; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_027871_0_0_7; -.
DR OrthoDB; 9790784at2; -.
DR Proteomes; UP000002402; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04843; Peptidases_S8_11; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034073; Subtilisin_DY-like_dom.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..542
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004188587"
FT DOMAIN 276..513
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
SQ SEQUENCE 542 AA; 57081 MW; F76BFFB8C22CA30E CRC64;
MWRLSMPMSS LLSMRPLRYA MLSLSVLAFA PSAVAAPPAK SLKPRALAAK PTGRELAGDA
YVERIVVKFH EGSRVRLRDQ QLVALSSDRD AAERSLLAGR GLGDARLEAD LGHVTSLLER
APRIGAMARL FDEAESTLEA RKASGERQSG EQLADLNLYF EVPLMPGTTS ERVADLVAAL
NGLDGVEVAY AEPPPEPAMV NFGMDAAVRS LLAAADLPPV TPLYESNQGY LNAAPGGIDA
KYAWTVLGGQ GQNVKVVDIE GGWRTTHEDM PDLFHMGGTQ YTDQSWRDHG TAVLGEIVGA
RNAYGVTGIA HQAKAGYESI GAQSTASAIT RAATAAGLGG IVLIELHARG PSDGTACSCN
TSQCDYIAME YWQANYDAIK TATANGVIVV EAAGNGSADL DAPAYGSAFN RNTRDSGAIF
VGGSTATTRL PMCWTNFGTR VDVHGWGERV YSMGYGNVFG ASYGEDQFYT SSFSGTSSAS
PIVVGAAASA QGVALANGRR LTSTQMRSLL RANGTPQPAN TRQIGPLPDL AKVLPKVIAG
DY
//
