ID F8CJ72_MYXFH Unreviewed; 496 AA.
AC F8CJ72;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=S1E family peptidase {ECO:0000313|EMBL:AEI68854.1};
GN OrderedLocusNames=LILAB_34865 {ECO:0000313|EMBL:AEI68854.1};
OS Myxococcus fulvus (strain ATCC BAA-855 / HW-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=483219 {ECO:0000313|EMBL:AEI68854.1, ECO:0000313|Proteomes:UP000000488};
RN [1] {ECO:0000313|EMBL:AEI68854.1, ECO:0000313|Proteomes:UP000000488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-855 / HW-1 {ECO:0000313|Proteomes:UP000000488};
RX PubMed=21868801; DOI=10.1128/JB.05516-11;
RA Li Z.F., Li X., Liu H., Liu X., Han K., Wu Z.H., Hu W., Li F.F., Li Y.Z.;
RT "Genome sequence of the halotolerant marine bacterium Myxococcus fulvus HW-
RT 1.";
RL J. Bacteriol. 193:5015-5016(2011).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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DR EMBL; CP002830; AEI68854.1; -; Genomic_DNA.
DR AlphaFoldDB; F8CJ72; -.
DR STRING; 483219.LILAB_34865; -.
DR KEGG; mfu:LILAB_34865; -.
DR eggNOG; COG1318; Bacteria.
DR HOGENOM; CLU_030648_2_1_7; -.
DR Proteomes; UP000000488; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd21112; alphaLP-like; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 3.30.300.50; -; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR004236; Pept_S1_alpha_lytic.
DR InterPro; IPR001316; Pept_S1A_streptogrisin.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR InterPro; IPR035070; Streptogrisin_prodomain.
DR InterPro; IPR001254; Trypsin_dom.
DR Pfam; PF02983; Pro_Al_protease; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00861; ALYTICPTASE.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
FT DOMAIN 370..496
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 496 AA; 51973 MW; 9A9CB141788A7A80 CRC64;
MFAGLATLTG LPMTAEAADD VSPEIVSAMR RDLGLTEQQV HQRLTFEAKA PQLEQTMREQ
LGDAFGGAWL DADGTQLIVG VTDEARLPKA RVPGVKTVRV ARSLARLEQV KASLDQNVQA
LSPAIHSWYV DLPSNSVVVH ADDSSQSKPR ADAFLRGSAG LKDGSLRVVA SQHAPEPAYD
LRGGDPYYFS NYRCSVGFPV NGGFVTAGHC GGVGTPTTGH NGVALGTIRG SVWPGADYGW
VATNGSWTPQ PWVNNYGGGN VTVAGSQEAP VNASICRSGY TTGWRCGVLQ AKNVTVNYSV
GPVYNLHRTS ACAAGGDSGG SVLSGNQAQG VTSGVAGTCS NSNPATFYQP VNPILGAYGL
TLRTTGGGGS GRAFVSRLNN TKCIDVPNSN FSDGVPLQMW NCNGTNAQRW TFVNGTVRAG
GLCMDVAWGN TANGTTVQLA NCSGNPAQQF VLSGAGDLVS VLANKCVDIV NHNPNDGARL
IIYECTGNPN QKWDYR
//
