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Conserved domains on  [gi|1719556011|ref|WP_145840192|]
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type I secretion C-terminal target domain-containing protein, partial [Shewanella algae]

Protein Classification

calcium-binding protein; M10 family metallopeptidase( domain architecture ID 10956076)

calcium-binding protein such as serralysin, an M10 family metallopeptidase that contains a glycine-rich C-terminal domain Gly-Gly-Xaa-Gly-Asn-Asp which has a role in binding calcium ions| 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG2931 COG2931
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ...
 306-550 1.78e-11

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


:

Pssm-ID: 442175 [Multi-domain]  Cd Length: 252  Bit Score: 64.93  E-value: 1.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719556011 306 TINGITFIVLLADPVDSVEQTWFYDADSGLMKASISYDQIVQESDNSVTLADYLTLNPAQAGDLWTITYFDNDGGSYQAR 385
Cdd:COG2931     8 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGGGGGGDDT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719556011 386 YVQAVFTHELLPDDAITVTGTDDIDNLIFGSTQSDSLTGANQSDEIVGREGNDTIYGLEGDDQLLGGAGNDYIFGGTGAD 465
Cdd:COG2931    88 DGGGDGGDGGGGGTGDDTGDGGGGNDTLTGGDGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTLYGGAGND 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719556011 466 YLVGGPGSDRLDAGIDNDRDILIWDAGSADGSTDEVYNFNPNTDALDLSDILVNEENGVLDDYLDFSFVGGNTIISVDTT 545
Cdd:COG2931   168 TLDGGAGNDTLTGGAGNDTLTGGAGNDTLDGGGGDDTLGGGGGDDGLDGGDGDDGLGGGGGDDTLGGGGGGDGGGGGGGD 247


                  ....*
gi 1719556011 546 GAGGD 550
Cdd:COG2931   248 DGLGG 252
VCBS_repeat super family cl11690
VCBS repeat; This domain of about 100 residues is found multiple (up to 35) copies in long ...
 34-88 1.72e-07

VCBS repeat; This domain of about 100 residues is found multiple (up to 35) copies in long proteins from several species of Vibrio, Colwellia, Bradyrhizobium, and Shewanella (hence the name VCBS) and in smaller copy numbers in proteins from several other bacteria. The large protein size and repeat copy numbers, species distribution, and suggested activities of several member proteins suggests a role for this domain in adhesion.


The actual alignment was detected with superfamily member TIGR01965:

Pssm-ID: 273899 [Multi-domain]  Cd Length: 99  Bit Score: 49.64  E-value: 1.72e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1719556011  34 FSVDNAG-WSYDIANSL--VQFLAVGETITLSFDVTVDDGNggtdTETVTITINGTND 88
Cdd:TIGR01965  29 FSIDADGqWTYQADNSQtaVQALKAGETLTDTFTVTSADGT----SQTVTITITGAND 82
 
Name Accession Description Interval E-value
COG2931 COG2931
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ...
 306-550 1.78e-11

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


Pssm-ID: 442175 [Multi-domain]  Cd Length: 252  Bit Score: 64.93  E-value: 1.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719556011 306 TINGITFIVLLADPVDSVEQTWFYDADSGLMKASISYDQIVQESDNSVTLADYLTLNPAQAGDLWTITYFDNDGGSYQAR 385
Cdd:COG2931     8 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGGGGGGDDT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719556011 386 YVQAVFTHELLPDDAITVTGTDDIDNLIFGSTQSDSLTGANQSDEIVGREGNDTIYGLEGDDQLLGGAGNDYIFGGTGAD 465
Cdd:COG2931    88 DGGGDGGDGGGGGTGDDTGDGGGGNDTLTGGDGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTLYGGAGND 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719556011 466 YLVGGPGSDRLDAGIDNDRDILIWDAGSADGSTDEVYNFNPNTDALDLSDILVNEENGVLDDYLDFSFVGGNTIISVDTT 545
Cdd:COG2931   168 TLDGGAGNDTLTGGAGNDTLTGGAGNDTLDGGGGDDTLGGGGGDDGLDGGDGDDGLGGGGGDDTLGGGGGGDGGGGGGGD 247


                  ....*
gi 1719556011 546 GAGGD 550
Cdd:COG2931   248 DGLGG 252
Peptidase_M10_C pfam08548
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ...
 432-522 1.11e-07

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: 52.76  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719556011 432 VGREGNDTIYGLEGDDQLLGGAGNDYIFGGTGADYLVGGPGsdrldagidndRDILIWDAG--SADGSTDEVYNFNPNTD 509
Cdd:pfam08548  85 IGGSGNDVLIGNDADNILKGGAGNDILYGGGGADQLWGGAG-----------NDIFVYASAkdSLTAAPDTIRDFVSGID 153

                          90
                  ....*....|...
gi 1719556011 510 ALDLSDILVNEEN 522
Cdd:pfam08548 154 KIDLSALNNNSDG 166
VCBS_repeat TIGR01965
VCBS repeat; This domain of about 100 residues is found multiple (up to 35) copies in long ...
 34-88 1.72e-07

VCBS repeat; This domain of about 100 residues is found multiple (up to 35) copies in long proteins from several species of Vibrio, Colwellia, Bradyrhizobium, and Shewanella (hence the name VCBS) and in smaller copy numbers in proteins from several other bacteria. The large protein size and repeat copy numbers, species distribution, and suggested activities of several member proteins suggests a role for this domain in adhesion.


Pssm-ID: 273899 [Multi-domain]  Cd Length: 99  Bit Score: 49.64  E-value: 1.72e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1719556011  34 FSVDNAG-WSYDIANSL--VQFLAVGETITLSFDVTVDDGNggtdTETVTITINGTND 88
Cdd:TIGR01965  29 FSIDADGqWTYQADNSQtaVQALKAGETLTDTFTVTSADGT----SQTVTITITGAND 82
T1SS_VCA0849 TIGR03661
type I secretion C-terminal target domain (VC_A0849 subclass); This model represents a ...
 499-584 3.74e-07

type I secretion C-terminal target domain (VC_A0849 subclass); This model represents a C-terminal domain associated with secretion by type 1 secretion systems (T1SS). Members of this subclass do not include the RtxA toxin of Vibrio cholerae and its homologs, although the two classes of proteins share large size, occurrence in genomes with T1SS, regions with long tandem repeats, and regions with the glycine-rich repeat modeled by pfam00353. [Cellular processes, Pathogenesis]


Pssm-ID: 274707  Cd Length: 88  Bit Score: 48.11  E-value: 3.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719556011 499 DEVYNFNPNTDALDLSDILVNEENGV--LDDYLDFSFVG--GNTIISVDTTGAGGDSV---TIVLNGVDLSAEYGTtdeg 571
Cdd:TIGR03661   1 DTITDFTLGEDKLDLSDLLSGEGVSSanLDQYLNVTTSGedGNTVISVDSDGSAGSAAvtqTITLEGVDLSSTSAD---- 76

                          90
                  ....*....|...
gi 1719556011 572 vIIQSLISDGALL 584
Cdd:TIGR03661  77 -IINQLLDNNQLI 88
 
Name Accession Description Interval E-value
COG2931 COG2931
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ...
 306-550 1.78e-11

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


Pssm-ID: 442175 [Multi-domain]  Cd Length: 252  Bit Score: 64.93  E-value: 1.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719556011 306 TINGITFIVLLADPVDSVEQTWFYDADSGLMKASISYDQIVQESDNSVTLADYLTLNPAQAGDLWTITYFDNDGGSYQAR 385
Cdd:COG2931     8 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGGGGGGDDT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719556011 386 YVQAVFTHELLPDDAITVTGTDDIDNLIFGSTQSDSLTGANQSDEIVGREGNDTIYGLEGDDQLLGGAGNDYIFGGTGAD 465
Cdd:COG2931    88 DGGGDGGDGGGGGTGDDTGDGGGGNDTLTGGDGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTLYGGAGND 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719556011 466 YLVGGPGSDRLDAGIDNDRDILIWDAGSADGSTDEVYNFNPNTDALDLSDILVNEENGVLDDYLDFSFVGGNTIISVDTT 545
Cdd:COG2931   168 TLDGGAGNDTLTGGAGNDTLTGGAGNDTLDGGGGDDTLGGGGGDDGLDGGDGDDGLGGGGGDDTLGGGGGGDGGGGGGGD 247


                  ....*
gi 1719556011 546 GAGGD 550
Cdd:COG2931   248 DGLGG 252
COG2931 COG2931
Ca2+-binding protein, RTX toxin-related [Secondary metabolites biosynthesis, transport and ...
 308-559 5.22e-10

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


Pssm-ID: 442175 [Multi-domain]  Cd Length: 252  Bit Score: 60.30  E-value: 5.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719556011 308 NGITFIVLLADPVDSVEQTWFYDADSGLMKASISYDQIVQESDNSVTLADYLTLNPAQAGDLWTITYFDNDGGSYQARYV 387
Cdd:COG2931     1 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGDGGGGGGGGGGGGGGGGLDGGGGGGGGDGGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719556011 388 QAVFTHELLPDDAITVTGTDDIDNLIFGSTQSDSLTGANQSDEIVGREGNDTIYGLEGDDQLLGGAGNDYIFGGTGADYL 467
Cdd:COG2931    81 GGGGDDTDGGGDGGDGGGGGTGDDTGDGGGGNDTLTGGDGNDTLTGGAGDDTLYGGAGNDTLTGGAGNDTLYGGAGNDTL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719556011 468 VGGPGSDRLDAGIDNDRDILIWDAGSADGSTDEVYNFNPNTDALDLSDILVNEENGVLDDYLDFSFVGGNTIISVDTTGA 547
Cdd:COG2931   161 YGGAGNDTLDGGAGNDTLTGGAGNDTLTGGAGNDTLDGGGGDDTLGGGGGDDGLDGGDGDDGLGGGGGDDTLGGGGGGDG 240

                         250
                  ....*....|..
gi 1719556011 548 GGDSVTIVLNGV 559
Cdd:COG2931   241 GGGGGGDDGLGG 252
Peptidase_M10_C pfam08548
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ...
 432-522 1.11e-07

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: 52.76  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719556011 432 VGREGNDTIYGLEGDDQLLGGAGNDYIFGGTGADYLVGGPGsdrldagidndRDILIWDAG--SADGSTDEVYNFNPNTD 509
Cdd:pfam08548  85 IGGSGNDVLIGNDADNILKGGAGNDILYGGGGADQLWGGAG-----------NDIFVYASAkdSLTAAPDTIRDFVSGID 153

                          90
                  ....*....|...
gi 1719556011 510 ALDLSDILVNEEN 522
Cdd:pfam08548 154 KIDLSALNNNSDG 166
VCBS_repeat TIGR01965
VCBS repeat; This domain of about 100 residues is found multiple (up to 35) copies in long ...
 34-88 1.72e-07

VCBS repeat; This domain of about 100 residues is found multiple (up to 35) copies in long proteins from several species of Vibrio, Colwellia, Bradyrhizobium, and Shewanella (hence the name VCBS) and in smaller copy numbers in proteins from several other bacteria. The large protein size and repeat copy numbers, species distribution, and suggested activities of several member proteins suggests a role for this domain in adhesion.


Pssm-ID: 273899 [Multi-domain]  Cd Length: 99  Bit Score: 49.64  E-value: 1.72e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1719556011  34 FSVDNAG-WSYDIANSL--VQFLAVGETITLSFDVTVDDGNggtdTETVTITINGTND 88
Cdd:TIGR01965  29 FSIDADGqWTYQADNSQtaVQALKAGETLTDTFTVTSADGT----SQTVTITITGAND 82
T1SS_VCA0849 TIGR03661
type I secretion C-terminal target domain (VC_A0849 subclass); This model represents a ...
 499-584 3.74e-07

type I secretion C-terminal target domain (VC_A0849 subclass); This model represents a C-terminal domain associated with secretion by type 1 secretion systems (T1SS). Members of this subclass do not include the RtxA toxin of Vibrio cholerae and its homologs, although the two classes of proteins share large size, occurrence in genomes with T1SS, regions with long tandem repeats, and regions with the glycine-rich repeat modeled by pfam00353. [Cellular processes, Pathogenesis]


Pssm-ID: 274707  Cd Length: 88  Bit Score: 48.11  E-value: 3.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719556011 499 DEVYNFNPNTDALDLSDILVNEENGV--LDDYLDFSFVG--GNTIISVDTTGAGGDSV---TIVLNGVDLSAEYGTtdeg 571
Cdd:TIGR03661   1 DTITDFTLGEDKLDLSDLLSGEGVSSanLDQYLNVTTSGedGNTVISVDSDGSAGSAAvtqTITLEGVDLSSTSAD---- 76

                          90
                  ....*....|...
gi 1719556011 572 vIIQSLISDGALL 584
Cdd:TIGR03661  77 -IINQLLDNNQLI 88
HemolysinCabind pfam00353
RTX calcium-binding nonapeptide repeat (4 copies);
432-467 8.15e-06

RTX calcium-binding nonapeptide repeat (4 copies);


Pssm-ID: 459777 [Multi-domain]  Cd Length: 36  Bit Score: 42.81  E-value: 8.15e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1719556011 432 VGREGNDTIYGLEGDDQLLGGAGNDYIFGGTGADYL 467
Cdd:pfam00353   1 YGGDGNDTLVGGAGNDTIYGGAGNDTLDGGAGNDTL 36
HemolysinCabind pfam00353
RTX calcium-binding nonapeptide repeat (4 copies);
441-476 2.35e-05

RTX calcium-binding nonapeptide repeat (4 copies);


Pssm-ID: 459777 [Multi-domain]  Cd Length: 36  Bit Score: 41.65  E-value: 2.35e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1719556011 441 YGLEGDDQLLGGAGNDYIFGGTGADYLVGGPGSDRL 476
Cdd:pfam00353   1 YGGDGNDTLVGGAGNDTIYGGAGNDTLDGGAGNDTL 36
Peptidase_M10_C pfam08548
Peptidase M10 serralysin C terminal; Serralysins are peptidases related to mammalian matrix ...
 424-528 8.10e-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: 44.29  E-value: 8.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719556011 424 GANQSDEIVGREGNDTIYGLEGDDQLLGGAGNDYIFGGTGADYLVGGPGSDRLDAGIDNdrdilIWDAGSADGSTDeVYN 503
Cdd:pfam08548  86 GGSGNDVLIGNDADNILKGGAGNDILYGGGGADQLWGGAGNDIFVYASAKDSLTAAPDT-----IRDFVSGIDKID-LSA 159

                          90       100
                  ....*....|....*....|....*
gi 1719556011 504 FNPNTDALDLSDILVNEENGVLDDY 528
Cdd:pfam08548 160 LNNNSDGLQFVDRFSGKAGEALLRY 184
HemolysinCabind pfam00353
RTX calcium-binding nonapeptide repeat (4 copies);
423-458 2.94e-04

RTX calcium-binding nonapeptide repeat (4 copies);


Pssm-ID: 459777 [Multi-domain]  Cd Length: 36  Bit Score: 38.57  E-value: 2.94e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1719556011 423 TGANQSDEIVGREGNDTIYGLEGDDQLLGGAGNDYI 458
Cdd:pfam00353   1 YGGDGNDTLVGGAGNDTIYGGAGNDTLDGGAGNDTL 36
HemolysinCabind pfam00353
RTX calcium-binding nonapeptide repeat (4 copies);
451-484 3.18e-04

RTX calcium-binding nonapeptide repeat (4 copies);


Pssm-ID: 459777 [Multi-domain]  Cd Length: 36  Bit Score: 38.19  E-value: 3.18e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1719556011 451 GGAGNDYIFGGTGADYLVGGPGSDRLDAGIDNDR 484
Cdd:pfam00353   2 GGDGNDTLVGGAGNDTIYGGAGNDTLDGGAGNDT 35
 
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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