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Conserved domains on  [gi|1668545465|ref|WP_138219662|]
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M10 family metallopeptidase [Pseudomonas mosselii]

Protein Classification

M10 family metallopeptidase( domain architecture ID 11560623)

M10 family metallopeptidase similar to serralysin and Pseudomonas aeruginosa alkaline protease, which include an N-terminal peptidase domain and a C-terminal calcium-binding domain

Gene Ontology:  GO:0005509|GO:0004222|GO:0008270|GO:0006508
PubMed:  10361285|32860773|7674922

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 38-223 8.30e-53

Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.


:

Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 181.84  E-value: 8.30e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465  38 TTSLSYSFVVvGKSMFANRYSDSSEYLKAYNLSAAQQTAVKGALGAWSAVANIKFTQVTETStsVGDLRFGGFSGMGNTA 117
Cdd:cd04277     1 DTTLTYSFSN-TGGPYSYGYGREEDTTNTAALSAAQQAAARDALEAWEDVADIDFVEVSDNS--GADIRFGNSSDPDGNT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 118 AAWAYYPANS---PSGGDVWIGPATNQAKPVAGTYDYMTFMHEIGHALGLKHPFESASNNSAVLPAALDDVRYTLMSYSN 194
Cdd:cd04277    78 AGYAYYPGSGsgtAYGGDIWFNSSYDTNSDSPGSYGYQTIIHEIGHALGLEHPGDYNGGDPVPPTYALDSREYTVMSYNS 157

                         170       180
                  ....*....|....*....|....*....
gi 1668545465 195 DYYNAQMTAYVEPTTPMLYDIAAIQYLYG 223
Cdd:cd04277   158 GYGNGASAGGGYPQTPMLLDIAALQYLYG 186
Peptidase_M10_C super family cl23859
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ...
 224-340 1.96e-18

Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix metallopeptidases (MMPs). The peptidase unit is found at the N terminal while this domain at the C terminal forms a corkscrew and is thought to be important for secretion of the protein through the bacterial cell wall. This domain contains the calcium ion binding domain pfam00353.


The actual alignment was detected with superfamily member pfam08548:

Pssm-ID: 451582 [Multi-domain]  Cd Length: 222  Bit Score: 85.12  E-value: 1.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 224 ANMTWQTGNNTYSFKPG-------------QVVFqTIWDAGGTDTLDASNQTAGVLLNLNEGEFSNIGALfydyarnemi 290
Cdd:pfam08548   1 ANLTTRTGDTVYGFNSNtgrdfytatdassKLIF-SVWDAGGNDTFDFSGYSQNQRINLNEGSFSDVGGL---------- 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1668545465 291 NNGLAIAYGAKIENATGSAFADTLIGNALDNVLDGRAGADIMRGGLGNDT 340
Cdd:pfam08548  70 KGNVSIAHGVTIENAIGGSGNDVLIGNDADNILKGGAGNDILYGGGGADQ 119
Peptidase_M10_C super family cl23859
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ...
 672-813 1.87e-15

Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix metallopeptidases (MMPs). The peptidase unit is found at the N terminal while this domain at the C terminal forms a corkscrew and is thought to be important for secretion of the protein through the bacterial cell wall. This domain contains the calcium ion binding domain pfam00353.


The actual alignment was detected with superfamily member pfam08548:

Pssm-ID: 451582 [Multi-domain]  Cd Length: 222  Bit Score: 76.26  E-value: 1.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 672 IGNAGNNTLNGGAGNDVLNGGAGNDVLIGGLGTDTMTGGQGADIFVFSLLKEmGLGDKRDVITDFNGAEgDRIDLTKIDA 751
Cdd:pfam08548  85 IGGSGNDVLIGNDADNILKGGAGNDILYGGGGADQLWGGAGNDIFVYASAKD-SLTAAPDTIRDFVSGI-DKIDLSALNN 162

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1668545465 752 NV-LLKGVNAFTfiGSGdftGAGQLRFADEILSGNIDAKLGSDGKfTADFEIKLVGVTSFSQD 813
Cdd:pfam08548 163 NSdGLQFVDRFS--GKA---GEALLRYNEVSNITNLAIDFSGQLS-NNDFLVKIVGQALQTAD 219
COG2931 COG2931
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ...
 291-527 5.19e-13

Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 442175 [Multi-domain]  Cd Length: 252  Bit Score: 69.93  E-value: 5.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 291 NNGLAIAYGAKIENATGSAFADTLIGNALDNVLDGRAGADIMRGGLGNDTYIVDNVSDVVIEESTLASEIDTVRASVSYT 370
Cdd:COG2931    18 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGGGGGGDDTDGGGDGGDGG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 371 LSANVENLVLTGKANLNGGGNALDNVITGNAGINTLVGGAGNDSLYGGAGNDRLEGGEGNDLLDGGVGIDTLIGGRGNDI 450
Cdd:COG2931    98 GGGTGDDTGDGGGGNDTLTGGDGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTLYGGAGNDTLDGGAGNDT 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1668545465 451 YYVDNLRDVVIelAGAAEGRDLVRASVSYVLAANVEDGELLGKASLSLTGNALDNVLTGNDGANVLRGGGGADTLIG 527
Cdd:COG2931   178 LTGGAGNDTLT--GGAGNDTLDGGGGDDTLGGGGGDDGLDGGDGDDGLGGGGGDDTLGGGGGGDGGGGGGGDDGLGG 252
COG2931 COG2931
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ...
 530-773 7.63e-12

Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 442175 [Multi-domain]  Cd Length: 252  Bit Score: 66.47  E-value: 7.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 530 GNDTYYVDSVDDLIIESGTSAKEIDSVFSSVSWTLSSNLENLTLTGTDNINGTGNTQNNRITGNAGDNWLDGGEGIDTLV 609
Cdd:COG2931     1 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 610 GGQGNDTYVVDNLRDVVTEGANAGIDTVRASVNWTLGANFENLTLTGLDNLNGTGNTLNNVIIGNAGNNTLNGGAGNDVL 689
Cdd:COG2931    81 GGGGDDTDGGGDGGDGGGGGTGDDTGDGGGGNDTLTGGDGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 690 NGGAGNDVLIGGLGTDTMTGGQGADIFVFSLLKEMGLGDKRDVITDFNGAEGDRIDLTKIDANVLLKGVNAFTFIGSGDF 769
Cdd:COG2931   161 YGGAGNDTLDGGAGNDTLTGGAGNDTLTGGAGNDTLDGGGGDDTLGGGGGDDGLDGGDGDDGLGGGGGDDTLGGGGGGDG 240


                  ....
gi 1668545465 770 TGAG 773
Cdd:COG2931   241 GGGG 244
 
Name Accession Description Interval E-value
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 38-223 8.30e-53

Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 181.84  E-value: 8.30e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465  38 TTSLSYSFVVvGKSMFANRYSDSSEYLKAYNLSAAQQTAVKGALGAWSAVANIKFTQVTETStsVGDLRFGGFSGMGNTA 117
Cdd:cd04277     1 DTTLTYSFSN-TGGPYSYGYGREEDTTNTAALSAAQQAAARDALEAWEDVADIDFVEVSDNS--GADIRFGNSSDPDGNT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 118 AAWAYYPANS---PSGGDVWIGPATNQAKPVAGTYDYMTFMHEIGHALGLKHPFESASNNSAVLPAALDDVRYTLMSYSN 194
Cdd:cd04277    78 AGYAYYPGSGsgtAYGGDIWFNSSYDTNSDSPGSYGYQTIIHEIGHALGLEHPGDYNGGDPVPPTYALDSREYTVMSYNS 157

                         170       180
                  ....*....|....*....|....*....
gi 1668545465 195 DYYNAQMTAYVEPTTPMLYDIAAIQYLYG 223
Cdd:cd04277   158 GYGNGASAGGGYPQTPMLLDIAALQYLYG 186
Peptidase_M10_C pfam08548
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ...
 224-340 1.96e-18

Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix metallopeptidases (MMPs). The peptidase unit is found at the N terminal while this domain at the C terminal forms a corkscrew and is thought to be important for secretion of the protein through the bacterial cell wall. This domain contains the calcium ion binding domain pfam00353.


Pssm-ID: 430067 [Multi-domain]  Cd Length: 222  Bit Score: 85.12  E-value: 1.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 224 ANMTWQTGNNTYSFKPG-------------QVVFqTIWDAGGTDTLDASNQTAGVLLNLNEGEFSNIGALfydyarnemi 290
Cdd:pfam08548   1 ANLTTRTGDTVYGFNSNtgrdfytatdassKLIF-SVWDAGGNDTFDFSGYSQNQRINLNEGSFSDVGGL---------- 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1668545465 291 NNGLAIAYGAKIENATGSAFADTLIGNALDNVLDGRAGADIMRGGLGNDT 340
Cdd:pfam08548  70 KGNVSIAHGVTIENAIGGSGNDVLIGNDADNILKGGAGNDILYGGGGADQ 119
Peptidase_M10_C pfam08548
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ...
 672-813 1.87e-15

Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix metallopeptidases (MMPs). The peptidase unit is found at the N terminal while this domain at the C terminal forms a corkscrew and is thought to be important for secretion of the protein through the bacterial cell wall. This domain contains the calcium ion binding domain pfam00353.


Pssm-ID: 430067 [Multi-domain]  Cd Length: 222  Bit Score: 76.26  E-value: 1.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 672 IGNAGNNTLNGGAGNDVLNGGAGNDVLIGGLGTDTMTGGQGADIFVFSLLKEmGLGDKRDVITDFNGAEgDRIDLTKIDA 751
Cdd:pfam08548  85 IGGSGNDVLIGNDADNILKGGAGNDILYGGGGADQLWGGAGNDIFVYASAKD-SLTAAPDTIRDFVSGI-DKIDLSALNN 162

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1668545465 752 NV-LLKGVNAFTfiGSGdftGAGQLRFADEILSGNIDAKLGSDGKfTADFEIKLVGVTSFSQD 813
Cdd:pfam08548 163 NSdGLQFVDRFS--GKA---GEALLRYNEVSNITNLAIDFSGQLS-NNDFLVKIVGQALQTAD 219
COG2931 COG2931
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ...
 291-527 5.19e-13

Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442175 [Multi-domain]  Cd Length: 252  Bit Score: 69.93  E-value: 5.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 291 NNGLAIAYGAKIENATGSAFADTLIGNALDNVLDGRAGADIMRGGLGNDTYIVDNVSDVVIEESTLASEIDTVRASVSYT 370
Cdd:COG2931    18 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGGGGGGDDTDGGGDGGDGG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 371 LSANVENLVLTGKANLNGGGNALDNVITGNAGINTLVGGAGNDSLYGGAGNDRLEGGEGNDLLDGGVGIDTLIGGRGNDI 450
Cdd:COG2931    98 GGGTGDDTGDGGGGNDTLTGGDGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTLYGGAGNDTLDGGAGNDT 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1668545465 451 YYVDNLRDVVIelAGAAEGRDLVRASVSYVLAANVEDGELLGKASLSLTGNALDNVLTGNDGANVLRGGGGADTLIG 527
Cdd:COG2931   178 LTGGAGNDTLT--GGAGNDTLDGGGGDDTLGGGGGDDGLDGGDGDDGLGGGGGDDTLGGGGGGDGGGGGGGDDGLGG 252
COG2931 COG2931
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ...
 530-773 7.63e-12

Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442175 [Multi-domain]  Cd Length: 252  Bit Score: 66.47  E-value: 7.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 530 GNDTYYVDSVDDLIIESGTSAKEIDSVFSSVSWTLSSNLENLTLTGTDNINGTGNTQNNRITGNAGDNWLDGGEGIDTLV 609
Cdd:COG2931     1 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 610 GGQGNDTYVVDNLRDVVTEGANAGIDTVRASVNWTLGANFENLTLTGLDNLNGTGNTLNNVIIGNAGNNTLNGGAGNDVL 689
Cdd:COG2931    81 GGGGDDTDGGGDGGDGGGGGTGDDTGDGGGGNDTLTGGDGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 690 NGGAGNDVLIGGLGTDTMTGGQGADIFVFSLLKEMGLGDKRDVITDFNGAEGDRIDLTKIDANVLLKGVNAFTFIGSGDF 769
Cdd:COG2931   161 YGGAGNDTLDGGAGNDTLTGGAGNDTLTGGAGNDTLDGGGGDDTLGGGGGDDGLDGGDGDDGLGGGGGDDTLGGGGGGDG 240


                  ....
gi 1668545465 770 TGAG 773
Cdd:COG2931   241 GGGG 244
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 63-224 8.85e-12

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 63.52  E-value: 8.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465   63 YLKAYNLSAAQQTAVKGALGAWSAVANIKFTQVTETSTSvgDLRFG-GFSGmgnTAAAWAYYPanspsGGDVWIGPATnq 141
Cdd:smart00235  13 VIDSSSLSPEEREAIAKALAEWSDVTCIRFVERTGTADI--YISFGsGDSG---CTLSHAGRP-----GGDQHLSLGN-- 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465  142 akpvaGTYDYMTFMHEIGHALGLKHPFESASNNSAVLPaalddvrytlmsysnDYYNAQMTAYVEpttpMLYDIAAIQYL 221
Cdd:smart00235  81 -----GCINTGVAAHELGHALGLYHEQSRSDRDNYMYI---------------NYTNIDTRNFDL----SEDDSLGIPYD 136


                   ...
gi 1668545465  222 YGA 224
Cdd:smart00235 137 YGS 139
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 71-223 1.12e-11

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 63.79  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465  71 AAQQTAVKGALGAWSAVANIKFTqvtETSTSVGDLRFG----------GFSGMGNTAAAwAYYPANSPsGGDV------- 133
Cdd:pfam00413  21 AEVRRAIRRAFKVWSEVTPLTFT---EVSTGEADIMIGfgrgdhgdgyPFDGPGGVLAH-AFFPGPGL-GGDIhfdddet 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 134 WigpaTNQAKPVAGTYDYMTFMHEIGHALGLKHPfesasnnsavlpaaldDVRYTLMsYSndYYNAQMTAYVEPTTPmly 213
Cdd:pfam00413  96 W----TVGSDPPHGINLFLVAAHEIGHALGLGHS----------------SDPGAIM-YP--TYSPLDSKKFRLSQD--- 149

                         170
                  ....*....|
gi 1668545465 214 DIAAIQYLYG 223
Cdd:pfam00413 150 DIKGIQQLYG 159
HemolysinCabind pfam00353
RTX calcium-binding nonapeptide repeat (4 copies);
398-433 6.35e-07

RTX calcium-binding nonapeptide repeat (4 copies);


Pssm-ID: 459777 [Multi-domain]  Cd Length: 36  Bit Score: 46.28  E-value: 6.35e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1668545465 398 TGNAGINTLVGGAGNDSLYGGAGNDRLEGGEGNDLL 433
Cdd:pfam00353   1 YGGDGNDTLVGGAGNDTIYGGAGNDTLDGGAGNDTL 36
COG2931 COG2931
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ...
 230-488 1.34e-05

Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442175 [Multi-domain]  Cd Length: 252  Bit Score: 47.59  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 230 TGNNTYSFKPGQVVFQTIWDAGGTDTLDASNQTAGVLLNLNEGEFSNIGALFYDYARNEMINNGLAIAYGAKIENATGSA 309
Cdd:COG2931    40 GGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGGGGGGDDTDGGGDGGDGGGGGTGDDTGDGGGGNDTLTGGD 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 310 FADTLIGNALDNVLDGRAGADIMRGGLGNDTYIvdnvsdvvieestlaseidtvrasvsytlsanvenlvltgkanlngg 389
Cdd:COG2931   120 GNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLY----------------------------------------------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 390 GNALDNVITGNAGINTLVGGAGNDSLYGGAGNDRLEGGEGNDLLDGGVGIDTLIGGRGNDIYYVDNLRDVVIELAGAAEG 469
Cdd:COG2931   153 GGAGNDTLYGGAGNDTLDGGAGNDTLTGGAGNDTLTGGAGNDTLDGGGGDDTLGGGGGDDGLDGGDGDDGLGGGGGDDTL 232

                         250
                  ....*....|....*....
gi 1668545465 470 RDLVRASVSYVLAANVEDG 488
Cdd:COG2931   233 GGGGGGDGGGGGGGDDGLG 251
Peptidase_M10_C pfam08548
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ...
 583-624 9.02e-05

Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix metallopeptidases (MMPs). The peptidase unit is found at the N terminal while this domain at the C terminal forms a corkscrew and is thought to be important for secretion of the protein through the bacterial cell wall. This domain contains the calcium ion binding domain pfam00353.


Pssm-ID: 430067 [Multi-domain]  Cd Length: 222  Bit Score: 44.67  E-value: 9.02e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1668545465 583 GNTQNNRITGNAGDNWLDGGEGIDTLVGGQGNDTYVVDNLRD 624
Cdd:pfam08548  95 GNDADNILKGGAGNDILYGGGGADQLWGGAGNDIFVYASAKD 136
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 230-715 1.02e-04

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 45.92  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 230 TGNNTYSFKPGQVVFQTIWDAGGTDTLDASNQTAGVLLNLNEGEFSNIGALFYDYARNEMINNGLAIAYGAKIENATGSA 309
Cdd:COG4625    39 GGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGS 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 310 FADTLIGNALDNVLDGRAGADIMRGGLGNDTYIVDNVSDVVIEESTLASEIDTVRASVSYTLSANVENLVLTGKANLNGG 389
Cdd:COG4625   119 AGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGG 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 390 GNALDNVITGNAGINTLVGGAGNDSLYGGAGNDRLEGGEGNDLLDGGVGIDTLIGGRGNDIYYVDNLRDVVIELAGAAEG 469
Cdd:COG4625   199 GGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGG 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 470 RDLVRASVSYVLAANVEDGELLGKASLSLTGNALDNVLTGNDGANVLRGGGGADTLIGGLGNDTYYVDSVDDLIIESGTS 549
Cdd:COG4625   279 GGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGG 358

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 550 AKEIDSVFSSVSWTLSSNLENLTLTGTDNINGTGNTQNNRITGNAGDNWL-DGGEGIDTLVGGQGNDTYVVDNLRDVVTE 628
Cdd:COG4625   359 GGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGGGAGGTgGGGAGGGGGAAGGGGGGTGAGGGGGGGGT 438

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 629 GANAGIDTVRASVNWTLGANFENLTLTGLDNLNGTGNTLNNVIIGNAGNNTLNGGaGNDVLNGGAGNDVLIGGLGTDTMT 708
Cdd:COG4625   439 GAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGNNTYTGTTTVNGG-GNYTQSAGSTLAVEVDAANSDRLV 517


                  ....*..
gi 1668545465 709 GGQGADI 715
Cdd:COG4625   518 VTGTATL 524
 
Name Accession Description Interval E-value
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 38-223 8.30e-53

Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 181.84  E-value: 8.30e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465  38 TTSLSYSFVVvGKSMFANRYSDSSEYLKAYNLSAAQQTAVKGALGAWSAVANIKFTQVTETStsVGDLRFGGFSGMGNTA 117
Cdd:cd04277     1 DTTLTYSFSN-TGGPYSYGYGREEDTTNTAALSAAQQAAARDALEAWEDVADIDFVEVSDNS--GADIRFGNSSDPDGNT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 118 AAWAYYPANS---PSGGDVWIGPATNQAKPVAGTYDYMTFMHEIGHALGLKHPFESASNNSAVLPAALDDVRYTLMSYSN 194
Cdd:cd04277    78 AGYAYYPGSGsgtAYGGDIWFNSSYDTNSDSPGSYGYQTIIHEIGHALGLEHPGDYNGGDPVPPTYALDSREYTVMSYNS 157

                         170       180
                  ....*....|....*....|....*....
gi 1668545465 195 DYYNAQMTAYVEPTTPMLYDIAAIQYLYG 223
Cdd:cd04277   158 GYGNGASAGGGYPQTPMLLDIAALQYLYG 186
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 68-222 3.57e-20

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 88.32  E-value: 3.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465  68 NLSAAQQTAVKGALGAWSAVANIKFTQVTETSTsvGDLRFGGFSGMGNTAAAWAYYPANS-PSGGDVWIGPATNQAKPVA 146
Cdd:cd04268    11 SVPDKLRAAILDAIEAWNKAFAIGFKNANDVDP--ADIRYSVIRWIPYNDGTWSYGPSQVdPLTGEILLARVYLYSSFVE 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1668545465 147 GTYDYM--TFMHEIGHALGLKHPFESASNNSAVLPAALDDVRYTLMSYSNDYYNAQMTAYvEPTTPMLYDIAAIQYLY 222
Cdd:cd04268    89 YSGARLrnTAEHELGHALGLRHNFAASDRDDNVDLLAEKGDTSSVMDYAPSNFSIQLGDG-QKYTIGPYDIAAIKKLY 165
Peptidase_M10_C pfam08548
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ...
 224-340 1.96e-18

Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix metallopeptidases (MMPs). The peptidase unit is found at the N terminal while this domain at the C terminal forms a corkscrew and is thought to be important for secretion of the protein through the bacterial cell wall. This domain contains the calcium ion binding domain pfam00353.


Pssm-ID: 430067 [Multi-domain]  Cd Length: 222  Bit Score: 85.12  E-value: 1.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 224 ANMTWQTGNNTYSFKPG-------------QVVFqTIWDAGGTDTLDASNQTAGVLLNLNEGEFSNIGALfydyarnemi 290
Cdd:pfam08548   1 ANLTTRTGDTVYGFNSNtgrdfytatdassKLIF-SVWDAGGNDTFDFSGYSQNQRINLNEGSFSDVGGL---------- 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1668545465 291 NNGLAIAYGAKIENATGSAFADTLIGNALDNVLDGRAGADIMRGGLGNDT 340
Cdd:pfam08548  70 KGNVSIAHGVTIENAIGGSGNDVLIGNDADNILKGGAGNDILYGGGGADQ 119
Peptidase_M10_C pfam08548
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ...
 672-813 1.87e-15

Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix metallopeptidases (MMPs). The peptidase unit is found at the N terminal while this domain at the C terminal forms a corkscrew and is thought to be important for secretion of the protein through the bacterial cell wall. This domain contains the calcium ion binding domain pfam00353.


Pssm-ID: 430067 [Multi-domain]  Cd Length: 222  Bit Score: 76.26  E-value: 1.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 672 IGNAGNNTLNGGAGNDVLNGGAGNDVLIGGLGTDTMTGGQGADIFVFSLLKEmGLGDKRDVITDFNGAEgDRIDLTKIDA 751
Cdd:pfam08548  85 IGGSGNDVLIGNDADNILKGGAGNDILYGGGGADQLWGGAGNDIFVYASAKD-SLTAAPDTIRDFVSGI-DKIDLSALNN 162

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1668545465 752 NV-LLKGVNAFTfiGSGdftGAGQLRFADEILSGNIDAKLGSDGKfTADFEIKLVGVTSFSQD 813
Cdd:pfam08548 163 NSdGLQFVDRFS--GKA---GEALLRYNEVSNITNLAIDFSGQLS-NNDFLVKIVGQALQTAD 219
COG2931 COG2931
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ...
 291-527 5.19e-13

Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442175 [Multi-domain]  Cd Length: 252  Bit Score: 69.93  E-value: 5.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 291 NNGLAIAYGAKIENATGSAFADTLIGNALDNVLDGRAGADIMRGGLGNDTYIVDNVSDVVIEESTLASEIDTVRASVSYT 370
Cdd:COG2931    18 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGGGGGGDDTDGGGDGGDGG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 371 LSANVENLVLTGKANLNGGGNALDNVITGNAGINTLVGGAGNDSLYGGAGNDRLEGGEGNDLLDGGVGIDTLIGGRGNDI 450
Cdd:COG2931    98 GGGTGDDTGDGGGGNDTLTGGDGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTLYGGAGNDTLDGGAGNDT 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1668545465 451 YYVDNLRDVVIelAGAAEGRDLVRASVSYVLAANVEDGELLGKASLSLTGNALDNVLTGNDGANVLRGGGGADTLIG 527
Cdd:COG2931   178 LTGGAGNDTLT--GGAGNDTLDGGGGDDTLGGGGGDDGLDGGDGDDGLGGGGGDDTLGGGGGGDGGGGGGGDDGLGG 252
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 59-222 8.35e-13

Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 67.16  E-value: 8.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465  59 DSSEYLKAYNLSAAQQTAVKGALGAWSAVANIKFTQVTETSTSVgDLRFGGFSGMGNTA-AAWAYYPANSPS-GGDVWIg 136
Cdd:cd00203     9 ADDRDVEEENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIDKA-DIAILVTRQDFDGGtGGWAYLGRVCDSlRGVGVL- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 137 patnQAKPVAGTYDYMTFMHEIGHALGLKHPF----ESASNNSAVLPAALDDVRYTLMSY-SNDYYNAQMTAyvepttPM 211
Cdd:cd00203    87 ----QDNQSGTKEGAQTIAHELGHALGFYHDHdrkdRDDYPTIDDTLNAEDDDYYSVMSYtKGSFSDGQRKD------FS 156

                         170
                  ....*....|.
gi 1668545465 212 LYDIAAIQYLY 222
Cdd:cd00203   157 QCDIDQINKLY 167
COG2931 COG2931
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ...
 530-773 7.63e-12

Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442175 [Multi-domain]  Cd Length: 252  Bit Score: 66.47  E-value: 7.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 530 GNDTYYVDSVDDLIIESGTSAKEIDSVFSSVSWTLSSNLENLTLTGTDNINGTGNTQNNRITGNAGDNWLDGGEGIDTLV 609
Cdd:COG2931     1 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 610 GGQGNDTYVVDNLRDVVTEGANAGIDTVRASVNWTLGANFENLTLTGLDNLNGTGNTLNNVIIGNAGNNTLNGGAGNDVL 689
Cdd:COG2931    81 GGGGDDTDGGGDGGDGGGGGTGDDTGDGGGGNDTLTGGDGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 690 NGGAGNDVLIGGLGTDTMTGGQGADIFVFSLLKEMGLGDKRDVITDFNGAEGDRIDLTKIDANVLLKGVNAFTFIGSGDF 769
Cdd:COG2931   161 YGGAGNDTLDGGAGNDTLTGGAGNDTLTGGAGNDTLDGGGGDDTLGGGGGDDGLDGGDGDDGLGGGGGDDTLGGGGGGDG 240


                  ....
gi 1668545465 770 TGAG 773
Cdd:COG2931   241 GGGG 244
COG2931 COG2931
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ...
 540-788 7.70e-12

Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442175 [Multi-domain]  Cd Length: 252  Bit Score: 66.47  E-value: 7.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 540 DDLIIESGTSAKEIDSVFSSVSWTLSSNLENLTLTGTDNINGTGNTQNNRITGNAGDNWLDGGEGIDTLVGGQGNDTYVV 619
Cdd:COG2931     2 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 620 DNLRDVVTEGANAGIDTVRASVNWTLGANFENLTLTGLDNLNGTGNTLNNVIIGNAGNNTLNGGAGNDVLNGGAGNDVLI 699
Cdd:COG2931    82 GGGDDTDGGGDGGDGGGGGTGDDTGDGGGGNDTLTGGDGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTLY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 700 GGLGTDTMTGGQGADIFVFSLLKEMGLGDKRDVITDFNGAEGDRIDLTKIDANVLLKGVNAFTFIGSGDFTGAGQLRFAD 779
Cdd:COG2931   162 GGAGNDTLDGGAGNDTLTGGAGNDTLTGGAGNDTLDGGGGDDTLGGGGGDDGLDGGDGDDGLGGGGGDDTLGGGGGGDGG 241


                  ....*....
gi 1668545465 780 EILSGNIDA 788
Cdd:COG2931   242 GGGGGDDGL 250
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 63-224 8.85e-12

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 63.52  E-value: 8.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465   63 YLKAYNLSAAQQTAVKGALGAWSAVANIKFTQVTETSTSvgDLRFG-GFSGmgnTAAAWAYYPanspsGGDVWIGPATnq 141
Cdd:smart00235  13 VIDSSSLSPEEREAIAKALAEWSDVTCIRFVERTGTADI--YISFGsGDSG---CTLSHAGRP-----GGDQHLSLGN-- 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465  142 akpvaGTYDYMTFMHEIGHALGLKHPFESASNNSAVLPaalddvrytlmsysnDYYNAQMTAYVEpttpMLYDIAAIQYL 221
Cdd:smart00235  81 -----GCINTGVAAHELGHALGLYHEQSRSDRDNYMYI---------------NYTNIDTRNFDL----SEDDSLGIPYD 136


                   ...
gi 1668545465  222 YGA 224
Cdd:smart00235 137 YGS 139
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 71-223 1.12e-11

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 63.79  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465  71 AAQQTAVKGALGAWSAVANIKFTqvtETSTSVGDLRFG----------GFSGMGNTAAAwAYYPANSPsGGDV------- 133
Cdd:pfam00413  21 AEVRRAIRRAFKVWSEVTPLTFT---EVSTGEADIMIGfgrgdhgdgyPFDGPGGVLAH-AFFPGPGL-GGDIhfdddet 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 134 WigpaTNQAKPVAGTYDYMTFMHEIGHALGLKHPfesasnnsavlpaaldDVRYTLMsYSndYYNAQMTAYVEPTTPmly 213
Cdd:pfam00413  96 W----TVGSDPPHGINLFLVAAHEIGHALGLGHS----------------SDPGAIM-YP--TYSPLDSKKFRLSQD--- 149

                         170
                  ....*....|
gi 1668545465 214 DIAAIQYLYG 223
Cdd:pfam00413 150 DIKGIQQLYG 159
COG2931 COG2931
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ...
 521-772 1.52e-11

Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442175 [Multi-domain]  Cd Length: 252  Bit Score: 65.31  E-value: 1.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 521 GADTLIGGLGNDTYYVDSVDDLIIESGTSAKEIDSVFSSVSWTLSSNLENLTLTGTDNINGTGNTQNNRITGNAGDNWLD 600
Cdd:COG2931     1 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 601 GGEGIDTLVGGQGNDTYVVDNLRDVVTEGANAGIDTVRASVNWTLGANFENLTLTGLDNLNGTGNTLNNVIIGNAGNNTL 680
Cdd:COG2931    81 GGGGDDTDGGGDGGDGGGGGTGDDTGDGGGGNDTLTGGDGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 681 NGGAGNDVLNGGAGNDVLIGGLGTDTMTGGQGADIFVFSLLKEMGLGDKRDVITDFNGAEGDRIDLTKIDANVLLKGVNA 760
Cdd:COG2931   161 YGGAGNDTLDGGAGNDTLTGGAGNDTLTGGAGNDTLDGGGGDDTLGGGGGDDGLDGGDGDDGLGGGGGDDTLGGGGGGDG 240

                         250
                  ....*....|..
gi 1668545465 761 FTFIGSGDFTGA 772
Cdd:COG2931   241 GGGGGGDDGLGG 252
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 74-223 4.32e-10

Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239803  Cd Length: 197  Bit Score: 60.03  E-value: 4.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465  74 QTAVKGALgAWSAV------ANIKFTQVTETSTSVGDLRFGGFSGMGNTAAAWAYYPA--NSPSG----GDVWIGPA--- 138
Cdd:cd04276    24 DAIREGVL-YWNKAfekagfKNAIIVKVLPDDADPGDIRYNVIRWIHSPNGGWAYGPSvvDPRTGeilkADVILYSGflr 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 139 TNQAKPVAGTYDYM--TFMHEIGHALGLKHPFE---SASNNSAVLPAALDDV--RYTLMSYSNDYYNAQMTAYVE--PTT 209
Cdd:cd04276   103 QDQLWYEDLLAASLryLLAHEVGHTLGLRHNFKassDGSNEELEDPLGTKEKgaTSSVMDYPPPNVAAQGEDQGDyyPPT 182

                         170
                  ....*....|....
gi 1668545465 210 PMLYDIAAIQYLYG 223
Cdd:cd04276   183 IGPYDKWAIEYGYT 196
COG2931 COG2931
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ...
 257-506 9.88e-10

Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442175 [Multi-domain]  Cd Length: 252  Bit Score: 59.92  E-value: 9.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 257 DASNQTAGVLLNLNEGEFSNIGALFYDYARNEMINNGLAIAYGAKIENATGSAFADTLIGNALDNVLDGRAGADIMRGGL 336
Cdd:COG2931     1 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 337 GNDTYIVDNVSDVVIEESTLASEIDTVRASVSYTLSANVENLVLTGKA-NLNGGGNALDNVITGNAGINTLVGGAGNDSL 415
Cdd:COG2931    81 GGGGDDTDGGGDGGDGGGGGTGDDTGDGGGGNDTLTGGDGNDTLTGGAgDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 416 YGGAGNDRLEGGEGNDLLDGGVGIDTLIGGRGNDIYYVDNLRDVVIELAGAAEGRDLVRASVSYVLAANVEDGELLGKAS 495
Cdd:COG2931   161 YGGAGNDTLDGGAGNDTLTGGAGNDTLTGGAGNDTLDGGGGDDTLGGGGGDDGLDGGDGDDGLGGGGGDDTLGGGGGGDG 240

                         250
                  ....*....|.
gi 1668545465 496 LSLTGNALDNV 506
Cdd:COG2931   241 GGGGGGDDGLG 251
COG2931 COG2931
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ...
 458-709 2.01e-09

Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442175 [Multi-domain]  Cd Length: 252  Bit Score: 59.15  E-value: 2.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 458 DVVIELAGAAEGRDLVRASVSYVLAANVEDGELLGKASLSLTGNALDNVLTGNDGANVLRGGGGADTLIGGLGNDTYYVD 537
Cdd:COG2931     1 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 538 SVDDLIIESGTSAKEIDSVFSSVSWTLSSNLENLTLTGTDNINGTGNTQNNRITGNAGDNWLDGGEGIDTLVGGQGNDTY 617
Cdd:COG2931    81 GGGGDDTDGGGDGGDGGGGGTGDDTGDGGGGNDTLTGGDGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 618 VVDNLRDVVTEGANAGIDTVRASVNWTLGANFENLTLTGLDNLNGTGNTLNNVIIGNAGNNTLNGGAGNDVLNGGAGNDV 697
Cdd:COG2931   161 YGGAGNDTLDGGAGNDTLTGGAGNDTLTGGAGNDTLDGGGGDDTLGGGGGDDGLDGGDGDDGLGGGGGDDTLGGGGGGDG 240

                         250
                  ....*....|..
gi 1668545465 698 LIGGLGTDTMTG 709
Cdd:COG2931   241 GGGGGGDDGLGG 252
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 71-223 2.22e-09

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 56.83  E-value: 2.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465  71 AAQQTAVKGALGAWSAVANIKFTQVTETSTSVGDLRFGG--------FSGMGNTAAAwAYYPanSPSGGDV-------WI 135
Cdd:cd04278    21 DDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARgnhgdgypFDGPGGTLAH-AFFP--GGIGGDIhfdddeqWT 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 136 gpatnqAKPVAGTYD-YMTFMHEIGHALGLKHpfesasnnsavlpaalddvrytlmsySNDyYNAQMTAYVEPTTPML-- 212
Cdd:cd04278    98 ------LGSDSGGTDlFSVAAHEIGHALGLGH--------------------------SSD-PDSIMYPYYQGPVPKFkl 144

                         170
                  ....*....|...
gi 1668545465 213 --YDIAAIQYLYG 223
Cdd:cd04278   145 sqDDIRGIQALYG 157
COG2931 COG2931
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ...
 449-700 5.06e-09

Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442175 [Multi-domain]  Cd Length: 252  Bit Score: 57.99  E-value: 5.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 449 DIYYVDNLRDVVIELAGAAEGRDLVRASVSYVLAANVEDGELLGKASLSLTGNALDNVLTGNDGANVLRGGGGADTLIGG 528
Cdd:COG2931     1 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 529 LGNDTYYVDSVDDLIIESGTSAKEIDSVFSSVSWTLSSNLENLTLTGTDNINGTGNTQNNRITGNAGDNWLDGGEGIDTL 608
Cdd:COG2931    81 GGGGDDTDGGGDGGDGGGGGTGDDTGDGGGGNDTLTGGDGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 609 VGGQGNDTYVVDNLRDVVTEGANAGIDTVRASVNWTLGANFENLTLTGLDNLNGTGNTLNNVIIGNAGNNTLNGGAGNDV 688
Cdd:COG2931   161 YGGAGNDTLDGGAGNDTLTGGAGNDTLTGGAGNDTLDGGGGDDTLGGGGGDDGLDGGDGDDGLGGGGGDDTLGGGGGGDG 240

                         250
                  ....*....|..
gi 1668545465 689 LNGGAGNDVLIG 700
Cdd:COG2931   241 GGGGGGDDGLGG 252
AidA COG3468
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ...
 239-679 3.62e-08

Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442691 [Multi-domain]  Cd Length: 846  Bit Score: 57.26  E-value: 3.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 239 PGQVVFQTIWDAGGTDTLDASNQTAGVLLNLNEGEFSNIGALFYDYARNEMINNGLAIAYGAKIENATGSAFADTLIGNA 318
Cdd:COG3468     3 SGGGGGATGLGGGGTGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAGSG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 319 LDNVLDGRAGADImRGGLGNDTYIVDNVSDVVIEESTLASEIDTVRASVSYTLSANVENLVLTGKANLNGGGNALDNVIT 398
Cdd:COG3468    83 GTGGNSTGGGGGN-SGTGGTGGGGGGGGSGNGGGGGGGGGGGGTGGGGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGGGT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 399 GNAGINTLVGGAGNDSLYGGAGNDRLEGGEGNDLLDGGVGIDTLIGGRGNDIYYVDNLRDVVIELAGAAEGRDLVRASVS 478
Cdd:COG3468   162 GSGGGGSGGGGGAGGGGGGGAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGGG 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 479 YVLAANVEDGELLGKASLSLTGN------ALDNVLTGNDGANVLRGGGGADTLIGGLGNDTYYVDSVDDLIIESGTSAKE 552
Cdd:COG3468   242 GGSAGGTGGGGLTGGGAAGTGGGgggtgtGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGGSN 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 553 IDSVFSSVSWTLSSNLENLTLTGTDNINGTGNTQNNRITGNAGDNWLDGGEGIDTLVGGQGNDTYVVDNLRDVVTEGANA 632
Cdd:COG3468   322 AGGGSGGGGGGGGGGGGGGTTLNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGLTTGGTG 401

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1668545465 633 GIDTVRASVNWTLGANFENLTLTGLDNLNGTGNTLN-NVIIGNAGNNT 679
Cdd:COG3468   402 NNGGGGVGGGGGGGLTLTGGTLTVNGNYTGNNGTLVlNTVLGDDNSPT 449
HemolysinCabind pfam00353
RTX calcium-binding nonapeptide repeat (4 copies);
398-433 6.35e-07

RTX calcium-binding nonapeptide repeat (4 copies);


Pssm-ID: 459777 [Multi-domain]  Cd Length: 36  Bit Score: 46.28  E-value: 6.35e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1668545465 398 TGNAGINTLVGGAGNDSLYGGAGNDRLEGGEGNDLL 433
Cdd:pfam00353   1 YGGDGNDTLVGGAGNDTIYGGAGNDTLDGGAGNDTL 36
HemolysinCabind pfam00353
RTX calcium-binding nonapeptide repeat (4 copies);
672-707 1.18e-06

RTX calcium-binding nonapeptide repeat (4 copies);


Pssm-ID: 459777 [Multi-domain]  Cd Length: 36  Bit Score: 45.51  E-value: 1.18e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1668545465 672 IGNAGNNTLNGGAGNDVLNGGAGNDVLIGGLGTDTM 707
Cdd:pfam00353   1 YGGDGNDTLVGGAGNDTIYGGAGNDTLDGGAGNDTL 36
HemolysinCabind pfam00353
RTX calcium-binding nonapeptide repeat (4 copies);
407-442 2.04e-06

RTX calcium-binding nonapeptide repeat (4 copies);


Pssm-ID: 459777 [Multi-domain]  Cd Length: 36  Bit Score: 44.74  E-value: 2.04e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1668545465 407 VGGAGNDSLYGGAGNDRLEGGEGNDLLDGGVGIDTL 442
Cdd:pfam00353   1 YGGDGNDTLVGGAGNDTIYGGAGNDTLDGGAGNDTL 36
Peptidase_M10_C pfam08548
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ...
 498-541 7.90e-06

Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix metallopeptidases (MMPs). The peptidase unit is found at the N terminal while this domain at the C terminal forms a corkscrew and is thought to be important for secretion of the protein through the bacterial cell wall. This domain contains the calcium ion binding domain pfam00353.


Pssm-ID: 430067 [Multi-domain]  Cd Length: 222  Bit Score: 47.75  E-value: 7.90e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1668545465 498 LTGNALDNVLTGNDGANVLRGGGGADTLIGGLGNDTYYVDSVDD 541
Cdd:pfam08548  93 LIGNDADNILKGGAGNDILYGGGGADQLWGGAGNDIFVYASAKD 136
HemolysinCabind pfam00353
RTX calcium-binding nonapeptide repeat (4 copies);
663-698 9.32e-06

RTX calcium-binding nonapeptide repeat (4 copies);


Pssm-ID: 459777 [Multi-domain]  Cd Length: 36  Bit Score: 42.81  E-value: 9.32e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1668545465 663 TGNTLNNVIIGNAGNNTLNGGAGNDVLNGGAGNDVL 698
Cdd:pfam00353   1 YGGDGNDTLVGGAGNDTIYGGAGNDTLDGGAGNDTL 36
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 70-166 1.15e-05

Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239819 [Multi-domain]  Cd Length: 198  Bit Score: 46.99  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465  70 SAAQQTAVKGALGAWSAVANIKFTQVTETStsvGDLRFGGFSGMGNtaaaWAY-------YPANSPSGGDVWIGPATNQA 142
Cdd:cd04327    18 DAFLKDKVRAAAREWLPYANLKFKFVTDAD---ADIRISFTPGDGY----WSYvgtdallIGADAPTMNLGWFTDDTPDP 90

                          90       100
                  ....*....|....*....|....
gi 1668545465 143 KPVAgtydymTFMHEIGHALGLKH 166
Cdd:cd04327    91 EFSR------VVLHEFGHALGFIH 108
COG2931 COG2931
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ...
 230-488 1.34e-05

Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442175 [Multi-domain]  Cd Length: 252  Bit Score: 47.59  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 230 TGNNTYSFKPGQVVFQTIWDAGGTDTLDASNQTAGVLLNLNEGEFSNIGALFYDYARNEMINNGLAIAYGAKIENATGSA 309
Cdd:COG2931    40 GGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGGGGGGDDTDGGGDGGDGGGGGTGDDTGDGGGGNDTLTGGD 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 310 FADTLIGNALDNVLDGRAGADIMRGGLGNDTYIvdnvsdvvieestlaseidtvrasvsytlsanvenlvltgkanlngg 389
Cdd:COG2931   120 GNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLY----------------------------------------------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 390 GNALDNVITGNAGINTLVGGAGNDSLYGGAGNDRLEGGEGNDLLDGGVGIDTLIGGRGNDIYYVDNLRDVVIELAGAAEG 469
Cdd:COG2931   153 GGAGNDTLYGGAGNDTLDGGAGNDTLTGGAGNDTLTGGAGNDTLDGGGGDDTLGGGGGDDGLDGGDGDDGLGGGGGDDTL 232

                         250
                  ....*....|....*....
gi 1668545465 470 RDLVRASVSYVLAANVEDG 488
Cdd:COG2931   233 GGGGGGDGGGGGGGDDGLG 251
HemolysinCabind pfam00353
RTX calcium-binding nonapeptide repeat (4 copies);
682-716 1.58e-05

RTX calcium-binding nonapeptide repeat (4 copies);


Pssm-ID: 459777 [Multi-domain]  Cd Length: 36  Bit Score: 42.42  E-value: 1.58e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1668545465 682 GGAGNDVLNGGAGNDVLIGGLGTDTMTGGQGADIF 716
Cdd:pfam00353   2 GGDGNDTLVGGAGNDTIYGGAGNDTLDGGAGNDTL 36
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 223-691 1.97e-05

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 48.24  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 223 GANMTWQTGNNTYSFKPGQVVFQTIWDAGGTDTLDASNQTAGVLLNLNEGEFSNIGALFYDYARNEMINNGLAIAYGAKI 302
Cdd:COG4625    12 GGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGTG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 303 ENATGSAFADTLIGNALDNVLDGRAGADIMRGGLGNDTYIVDNVSDVVIEESTLASEIDTVRASVSYTLSANVENLVLTG 382
Cdd:COG4625    92 GVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGGGGGGGGGG 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 383 KANLNGGGNALDNVITGNAGINTLVGGAGNDSLYGGAGNDRLEGGEGNDLLDGGVGIDTLIGGRGNDIYYVDNLRDVVIE 462
Cdd:COG4625   172 GGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGG 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 463 LAGAAEGRDLVRASVSYVLAANVEDGELLGKASLSLTGNALDNVLTGNDGANVLRGGGGADTLIGGLGNDTYYVDSVDDL 542
Cdd:COG4625   252 GGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 543 IIESGTSAKEIDSVFSSVSWTLSSNLENLTLTGTDNINGTGNTQNNRITGNAGDNWLDGGEGIDTLVGGQGNDTYVVDNL 622
Cdd:COG4625   332 GGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGGGAGGTGGG 411

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1668545465 623 RDVVTEGANAGIDTVRASVNWTLGANFENLTLTGLDNLNGTGNTLNNVIIGNAGNNTLNGGAGNDVLNG 691
Cdd:COG4625   412 GAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTG 480
DUF4953 pfam16313
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
 155-223 2.06e-05

Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic met-zincin mmotif HExxHxxGxxH, the extended zinc-binding domain of metallopeptidases.


Pssm-ID: 435269  Cd Length: 319  Bit Score: 47.25  E-value: 2.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 155 MHEIGHALGLKHPFeSASnnSAVLPAALDDVRYT--------LMSYSNDYYNAQ---MTAYVEPTTPML--YDIAAIQYL 221
Cdd:pfam16313  18 AHEVGHTLGLRHNF-AAS--SAYPVDSLRDKSFTrkygttpsIMDYARFNYVAQpedQIDLSGLYPPGIgpYDKWAIEWG 94


                  ..
gi 1668545465 222 YG 223
Cdd:pfam16313  95 YR 96
HemolysinCabind pfam00353
RTX calcium-binding nonapeptide repeat (4 copies);
416-450 2.06e-05

RTX calcium-binding nonapeptide repeat (4 copies);


Pssm-ID: 459777 [Multi-domain]  Cd Length: 36  Bit Score: 42.04  E-value: 2.06e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1668545465 416 YGGAGNDRLEGGEGNDLLDGGVGIDTLIGGRGNDI 450
Cdd:pfam00353   1 YGGDGNDTLVGGAGNDTIYGGAGNDTLDGGAGNDT 35
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 230-699 2.20e-05

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 48.24  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 230 TGNNTYSFKPGQVVFQTIWDAGGTDTLDASNQTAGVLLNLNEGEFSNIGALFYDYARNEMINNGLAIAYGAKIENATGSA 309
Cdd:COG4625    48 GGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAG 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 310 FADTLIGNALDNVLDGRAGADIMRGGLGNDTYIVDNVSDVVIEESTLASEIDTVRASVSYTLSANVENLVLTGKANLNGG 389
Cdd:COG4625   128 GAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGG 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 390 GNALDNVITGNAGINTLVGGAGNDSLYGGAGNDRLEGGEGNDLLDGGVGIDTLIGGRGNDIYYVDNLRDVVIELAGAAEG 469
Cdd:COG4625   208 GGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGS 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 470 RDLVRASVSYVLAANVEDGELLGKASLSLTGNALDNVLTGNDGANVLRGGGGADTLIGGLGNDTYYVDSVDDLIIESGTS 549
Cdd:COG4625   288 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGG 367

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 550 AKEIDSVFSSVSWTLSSNLENLTLTGTDNINGTGNTQNNRITGNAGDNWLDGGEGIDTLVGGQGNDTYVVDNLRDVVTEG 629
Cdd:COG4625   368 GGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATG 447

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 630 ANAGIDTVRASVNWTLGANFENLTLTGLDNLNGTGNTLNNVIIGNAGNNTLNGGAGNDVLNGGAGNDVLI 699
Cdd:COG4625   448 GGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGNNTYTGTTTVNGGGNYTQSAGSTLAVEVDAANSDRLV 517
FhaB COG3210
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ...
 230-695 2.43e-05

Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442443 [Multi-domain]  Cd Length: 1698  Bit Score: 48.22  E-value: 2.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465  230 TGNNTYSFKPGQVVFQTIWDAGGTDTLDASNQTAGVLLNLNEGEFSNIGALFYDYARNEMINNGLAIAYGAKIENATGSA 309
Cdd:COG3210    293 GDTTTNGTSSVTGAGGTGVLGGGTAAGITTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGL 372

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465  310 FADTLIGNALDNVLDGRAGADIMRGGLGNDTYIVDNVSDVVIEESTLASEIDTVRASVSYTLSANVENLVLTGKANLNGG 389
Cdd:COG3210    373 TTAGAGTVASTVGTATASTGNASSTTVLGSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGS 452

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465  390 GNALDNVITGNAGINTLVGGAGNDSLYGGAGNDRLEGGEGNDLLDGGVGIDTLIGGRGNDIYYVDNLRDVVIELAGAAEG 469
Cdd:COG3210    453 GTTNGAGLSGNTDVSGTGTVTNSAGNTTSATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGT 532

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465  470 RDLVRASVSYVLAANVEDGELLGKASLSLTGNALDNVLTGNDGANVLRGGGGADTLIGGLGNDTYYVDSVDDLIIESGTS 549
Cdd:COG3210    533 GGDGTTLSGSGLTTTVSGGASGTTAASGSNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATG 612

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465  550 AKEIDSVFSSVSWTLSSNLENLTLTGTDNINGTGNTQNNRITGNAGDNWLDGGEGIDTLVGGQGNDTYVVDNLRDVVTEG 629
Cdd:COG3210    613 TITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLN 692

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1668545465  630 ANAGIDTVRASVNWTLGANFENLTLTGLDNLNGTGNTLNNVIIGNAGNNTLN-------GGAGNDVLNGGAGN 695
Cdd:COG3210    693 AATGGTLNNAGNTLTISTGSITVTGQIGALANANGDTVTFGNLGTGATLTLNagvtitsGNAGTLSIGLTANT 765
FhaB COG3210
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ...
 387-809 2.53e-05

Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442443 [Multi-domain]  Cd Length: 1698  Bit Score: 48.22  E-value: 2.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465  387 NGGGNALDNVITGNAGINTLVGGAGNDSLYGGAGNDRLEGGEGNDLLDGGVGIDTLIGGRGNDIYYVDNLRDVVIELAGA 466
Cdd:COG3210    817 SGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANAGTL 896

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465  467 AE-GRDLVRASVSYVLAANVEDGELLGKASLSLTGNALDNVLTGNDGANVLRGGGGADTLIGGLGNDTYYVDSVDDLIIE 545
Cdd:COG3210    897 TNlGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSSA 976

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465  546 SGTSAKEIDSVFSSVSWTLSSNLENLTLTGTDNINGTGNTQNNRITGNAGDNWLDGGEGIDTLVGGQGNDTYVVDNLRDV 625
Cdd:COG3210    977 VGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGGQNGVGVNASGISGG 1056

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465  626 VTEGANAGIDTVRASVNWTLGANFENLTLTGLDNLNGTGNTLNNVIIGNAGNNTLNGGAGNDVLNGGAGNDVLIGGLGTD 705
Cdd:COG3210   1057 NAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTVGATGTSTAS 1136

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465  706 TMTGGQGADIFVFSLLKEMGLGDKRDVITDFNGAEGDRIDLTKIDANVLLKGVNAFTFIGSGDFTGAGQLRFADEILSGN 785
Cdd:COG3210   1137 TEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKGGDSTGGSTTTIGTTNV 1216

                          410       420
                   ....*....|....*....|....
gi 1668545465  786 IDAKLGSDGKFTADFEIKLVGVTS 809
Cdd:COG3210   1217 TTTTTLTASDTGNTTATGGSSAGQ 1240
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
111-198 5.75e-05

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 44.72  E-value: 5.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 111 SGMGNTAAAWAYYPANSPSGGDVWIGPATNQAKPVAGTyDYMTFMHEIGHALGLKHPFESASNNSAVLPAAL--DDVRYT 188
Cdd:pfam13688  99 TNCSGGGLAWLGQLCNSGSAGSVSTRVSGNNVVVSTAT-EWQVFAHEIGHNFGAVHDCDSSTSSQCCPPSNStcPAGGRY 177

                          90
                  ....*....|
gi 1668545465 189 LMSYSNDYYN 198
Cdd:pfam13688 178 IMNPSSSPNS 187
Peptidase_M10_C pfam08548
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ...
 583-624 9.02e-05

Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix metallopeptidases (MMPs). The peptidase unit is found at the N terminal while this domain at the C terminal forms a corkscrew and is thought to be important for secretion of the protein through the bacterial cell wall. This domain contains the calcium ion binding domain pfam00353.


Pssm-ID: 430067 [Multi-domain]  Cd Length: 222  Bit Score: 44.67  E-value: 9.02e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1668545465 583 GNTQNNRITGNAGDNWLDGGEGIDTLVGGQGNDTYVVDNLRD 624
Cdd:pfam08548  95 GNDADNILKGGAGNDILYGGGGADQLWGGAGNDIFVYASAKD 136
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 230-715 1.02e-04

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 45.92  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 230 TGNNTYSFKPGQVVFQTIWDAGGTDTLDASNQTAGVLLNLNEGEFSNIGALFYDYARNEMINNGLAIAYGAKIENATGSA 309
Cdd:COG4625    39 GGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGS 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 310 FADTLIGNALDNVLDGRAGADIMRGGLGNDTYIVDNVSDVVIEESTLASEIDTVRASVSYTLSANVENLVLTGKANLNGG 389
Cdd:COG4625   119 AGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGG 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 390 GNALDNVITGNAGINTLVGGAGNDSLYGGAGNDRLEGGEGNDLLDGGVGIDTLIGGRGNDIYYVDNLRDVVIELAGAAEG 469
Cdd:COG4625   199 GGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGG 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 470 RDLVRASVSYVLAANVEDGELLGKASLSLTGNALDNVLTGNDGANVLRGGGGADTLIGGLGNDTYYVDSVDDLIIESGTS 549
Cdd:COG4625   279 GGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGG 358

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 550 AKEIDSVFSSVSWTLSSNLENLTLTGTDNINGTGNTQNNRITGNAGDNWL-DGGEGIDTLVGGQGNDTYVVDNLRDVVTE 628
Cdd:COG4625   359 GGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGGGAGGTgGGGAGGGGGAAGGGGGGTGAGGGGGGGGT 438

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 629 GANAGIDTVRASVNWTLGANFENLTLTGLDNLNGTGNTLNNVIIGNAGNNTLNGGaGNDVLNGGAGNDVLIGGLGTDTMT 708
Cdd:COG4625   439 GAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGNNTYTGTTTVNGG-GNYTQSAGSTLAVEVDAANSDRLV 517


                  ....*..
gi 1668545465 709 GGQGADI 715
Cdd:COG4625   518 VTGTATL 524
HemolysinCabind pfam00353
RTX calcium-binding nonapeptide repeat (4 copies);
390-424 2.41e-04

RTX calcium-binding nonapeptide repeat (4 copies);


Pssm-ID: 459777 [Multi-domain]  Cd Length: 36  Bit Score: 38.96  E-value: 2.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1668545465 390 GNALDNVITGNAGINTLVGGAGNDSLYGGAGNDRL 424
Cdd:pfam00353   2 GGDGNDTLVGGAGNDTIYGGAGNDTLDGGAGNDTL 36
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 73-223 2.55e-04

Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239806 [Multi-domain]  Cd Length: 156  Bit Score: 42.06  E-value: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465  73 QQTAVKGALGAWSAVANIKFTQVTETSTSVGDLRFGGFSGMGNTAAAWAYYPANSPSGGDVWIGP-------ATNQakPV 145
Cdd:cd04279    22 WLQAVKQAAAEWENVGPLKFVYNPEEDNDADIVIFFDRPPPVGGAGGGLARAGFPLISDGNRKLFnrtdinlGPGQ--PR 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1668545465 146 AGTYDYMTFMHEIGHALGLKHpfESASNnsavlpaalDDVRYTLMSYSNDYynaqmtayvePTTPMLYDIAAIQYLYG 223
Cdd:cd04279   100 GAENLQAIALHELGHALGLWH--HSDRP---------EDAMYPSQGQGPDG----------NPTLSARDVATLKRLYG 156
HemolysinCabind pfam00353
RTX calcium-binding nonapeptide repeat (4 copies);
499-533 6.37e-04

RTX calcium-binding nonapeptide repeat (4 copies);


Pssm-ID: 459777 [Multi-domain]  Cd Length: 36  Bit Score: 37.80  E-value: 6.37e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1668545465 499 TGNALDNVLTGNDGANVLRGGGGADTLIGGLGNDT 533
Cdd:pfam00353   1 YGGDGNDTLVGGAGNDTIYGGAGNDTLDGGAGNDT 35
HemolysinCabind pfam00353
RTX calcium-binding nonapeptide repeat (4 copies);
582-616 1.97e-03

RTX calcium-binding nonapeptide repeat (4 copies);


Pssm-ID: 459777 [Multi-domain]  Cd Length: 36  Bit Score: 36.26  E-value: 1.97e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1668545465 582 TGNTQNNRITGNAGDNWLDGGEGIDTLVGGQGNDT 616
Cdd:pfam00353   1 YGGDGNDTLVGGAGNDTIYGGAGNDTLDGGAGNDT 35
AidA COG3468
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ...
 215-594 4.94e-03

Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442691 [Multi-domain]  Cd Length: 846  Bit Score: 40.70  E-value: 4.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 215 IAAIQYLYGANMTWQTGNNTYSFKPGQVVFQTIWDAGGTDTLDASNQTAGVLLNLNEGEFSNIGALFYDYARNEMINNGL 294
Cdd:COG3468    59 GGGGAGGGGGGAGSGGGLAGAGSGGTGGNSTGGGGGNSGTGGTGGGGGGGGSGNGGGGGGGGGGGGTGGGGGGGTGSAGG 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 295 AIAYGAKIENATGSAFADTLIGNALDNVLDGRAGADIMRGGLGNDTYIVDNVSDVVIEESTLASEIDTVRASVSYTLSAN 374
Cdd:COG3468   139 GGGGGGGGTGVGGTGAAAAGGGTGSGGGGSGGGGGAGGGGGGGAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGG 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 375 VENLVLTGKANLNGGGNALDNVITGNAGINTLVGGAGNDSLYGGAGNDRLEGGEGNDLLDGGVGIDTLIGGRGNDIYYVD 454
Cdd:COG3468   219 GGAGGATGGAGSGGNTGGGVGGGGGSAGGTGGGGLTGGGAAGTGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGGGG 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668545465 455 NLRDVVIELAGAAEGRDLVRASVSYVLAANVEDGELLGKASLSLTGNALDNVLTGNDGANVLRGGGGADTLIGGLGNDTY 534
Cdd:COG3468   299 TASTGGGGGGGGGNGGGGGGGSNAGGGSGGGGGGGGGGGGGGTTLNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGG 378

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1668545465 535 YVDSVDDLIIESGTSAKEIDSVFSSVSWTLSSNLE--NLTLTGTDNINGTGNTQNNRITGNA 594
Cdd:COG3468   379 AGGGGANTGSDGVGTGLTTGGTGNNGGGGVGGGGGggLTLTGGTLTVNGNYTGNNGTLVLNT 440
HemolysinCabind pfam00353
RTX calcium-binding nonapeptide repeat (4 copies);
508-543 5.18e-03

RTX calcium-binding nonapeptide repeat (4 copies);


Pssm-ID: 459777 [Multi-domain]  Cd Length: 36  Bit Score: 35.11  E-value: 5.18e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1668545465 508 TGNDGANVLRGGGGADTLIGGLGNDTYYVDSVDDLI 543
Cdd:pfam00353   1 YGGDGNDTLVGGAGNDTIYGGAGNDTLDGGAGNDTL 36
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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