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Conserved domains on  [gi|1538027407|ref|XP_027268159|]
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A disintegrin and metalloproteinase with thrombospondin motifs 5 [Cricetulus griseus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 268-472 1.04e-95

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


:

Pssm-ID: 239801  Cd Length: 207  Bit Score: 299.54  E-value: 1.04e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 268 VEILLVADSSMARMY-GRGLQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLADKDKSLEVSKNAATTLKNFCKWQHQ 346
Cdd:cd04273     3 VETLVVADSKMVEFHhGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQKK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 347 HNQLGDDHEEHYDAAILFTREDLCG-HHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSHDDS-KF 424
Cdd:cd04273    83 LNPPNDSDPEHHDHAILLTRQDICRsNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDgNS 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1538027407 425 CEENFgstEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLL 472
Cdd:cd04273   163 CGPEG---KDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 732-851 3.52e-33

ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like proteins. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase) and is a subfamily of the metalloprotease family, sharing a high degree of sequence similarity and conserved domain organization among its members. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS-like proteins lack a metalloprotease domain. They resides in the ECM and have regulatory roles. Examples of ADAM-TS-like proteins are papilin and punctin.


:

Pssm-ID: 461796  Cd Length: 115  Bit Score: 123.84  E-value: 3.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 732 KVIGTFNK-KSKGYTDVVRIPEGATHIKVRQFKAKdqtrFTaYLALKKKNGEYLINGKYMISTSETIIDINGTVMNYSGW 810
Cdd:pfam05986   1 TVSGSFTEgRAKGYVTFVTIPAGATHIHIVNRKPS----FT-HLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1538027407 811 SHRDDFLHGMGysATKEILIVQIL-----ATDPtkalDVRYSFFVP 851
Cdd:pfam05986  76 LPALEELHAPG--PTQEDLEIQVLrqygkGTNP----GITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 486-553 1.06e-23

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


:

Pssm-ID: 465496  Cd Length: 68  Bit Score: 95.10  E-value: 1.06e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 486 PGQTYDATQQCNLTFGPEYTVCPGM--DVCARLWCAVvrQGQMVCLTKKLPAVEGTPCGKGRICLQGKCV 553
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGdeDVCSKLWCSN--PGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 569-621 6.79e-16

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 72.62  E-value: 6.79e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1538027407  569 WGSWGPWGQCSRSCGGGVQFAYRHCNNPAPRNSGRYCTGKRAIYRSCSVTPCP 621
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
Pep_M12B_propep super family cl03265
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 64-176 1.58e-13

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


The actual alignment was detected with superfamily member pfam01562:

Pssm-ID: 460254  Cd Length: 128  Bit Score: 68.11  E-value: 1.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407  64 RQRRSSG-LVQNIDQLYsgggkvgYLVYAGSRRFLLDLERDDSVGTAGGILT--AGDGQSASSS--HRGHCFYRGTVDGS 138
Cdd:pfam01562  12 RRRRSLAsESTYLDTLS-------YRLAAFGKKFHLHLTPNRLLLAPGFTVTyyLDGGTGVESPpvQTDHCYYQGHVEGH 84

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1538027407 139 PRSLAVFDLCGGLDGFFAVKHARYTLKPLLRGSWAEAE 176
Cdd:pfam01562  85 PDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGG 122
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 878-929 2.30e-13

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 65.17  E-value: 2.30e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1538027407 878 WVTGPWLSCSRTCDTGWHTRTVQCQ--DGNRKLA-KGCLLSQRPSAFKQCLLKKC 929
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqkGGGSIVPdSECSAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 627-730 3.05e-12

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


The actual alignment was detected with superfamily member pfam19236:

Pssm-ID: 437068  Cd Length: 115  Bit Score: 64.34  E-value: 3.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 627 FRHEQCEAKNGYQ-SDAKGIKTFVEW---VPKYAGvlpGDVCKLTCRAKGTGYYVVFSPKVTDGTECRPY------SNSV 696
Cdd:pfam19236   5 FMSQQCARTDGQPlRSSPGGASFYHWgaaVPHSQG---DALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1538027407 697 CVRGRCVRTGCDGIIGSKLQYDKCGVCGGDNSSC 730
Cdd:pfam19236  82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 268-472 1.04e-95

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 299.54  E-value: 1.04e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 268 VEILLVADSSMARMY-GRGLQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLADKDKSLEVSKNAATTLKNFCKWQHQ 346
Cdd:cd04273     3 VETLVVADSKMVEFHhGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQKK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 347 HNQLGDDHEEHYDAAILFTREDLCG-HHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSHDDS-KF 424
Cdd:cd04273    83 LNPPNDSDPEHHDHAILLTRQDICRsNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDgNS 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1538027407 425 CEENFgstEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLL 472
Cdd:cd04273   163 CGPEG---KDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 732-851 3.52e-33

ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like proteins. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase) and is a subfamily of the metalloprotease family, sharing a high degree of sequence similarity and conserved domain organization among its members. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS-like proteins lack a metalloprotease domain. They resides in the ECM and have regulatory roles. Examples of ADAM-TS-like proteins are papilin and punctin.


Pssm-ID: 461796  Cd Length: 115  Bit Score: 123.84  E-value: 3.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 732 KVIGTFNK-KSKGYTDVVRIPEGATHIKVRQFKAKdqtrFTaYLALKKKNGEYLINGKYMISTSETIIDINGTVMNYSGW 810
Cdd:pfam05986   1 TVSGSFTEgRAKGYVTFVTIPAGATHIHIVNRKPS----FT-HLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1538027407 811 SHRDDFLHGMGysATKEILIVQIL-----ATDPtkalDVRYSFFVP 851
Cdd:pfam05986  76 LPALEELHAPG--PTQEDLEIQVLrqygkGTNP----GITYEYFIP 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 268-475 1.03e-26

Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


Pssm-ID: 426256 [Multi-domain]  Cd Length: 200  Bit Score: 108.54  E-value: 1.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 268 VEILLVADSSMARMYGRGLQH---YLLTLASIANRLYShasiENHIRLAVVKVVVLADKDKsLEVSKNAATTLKNFCKWQ 344
Cdd:pfam01421   3 IELFIVVDKQLFQKMGSDTTVvrqRVFQVVNLVNSIYK----ELNIRVVLVGLEIWTDEDK-IDVSGDANDTLRNFLKWR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 345 HQHNQLGDDHeehyDAAILFTREDLCGHhscdTLGMADVGTICSPERSCAVIED---DGLHAAFTVAHEIGHLLGLSHDD 421
Cdd:pfam01421  78 QEYLKKRKPH----DVAQLLSGVEFGGT----TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQHDD 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1538027407 422 SK---FCEENFGStedkrLMSSILTSIDASKpWSKCTSATITEFLDDGHGNCLLDLP 475
Cdd:pfam01421 150 FNggcKCPPGGGC-----IMNPSAGSSFPRK-FSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 486-553 1.06e-23

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


Pssm-ID: 465496  Cd Length: 68  Bit Score: 95.10  E-value: 1.06e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 486 PGQTYDATQQCNLTFGPEYTVCPGM--DVCARLWCAVvrQGQMVCLTKKLPAVEGTPCGKGRICLQGKCV 553
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGdeDVCSKLWCSN--PGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 569-621 6.79e-16

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 72.62  E-value: 6.79e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1538027407  569 WGSWGPWGQCSRSCGGGVQFAYRHCNNPAPRNSGRYCTGKRAIYRSCSVTPCP 621
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 64-176 1.58e-13

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


Pssm-ID: 460254  Cd Length: 128  Bit Score: 68.11  E-value: 1.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407  64 RQRRSSG-LVQNIDQLYsgggkvgYLVYAGSRRFLLDLERDDSVGTAGGILT--AGDGQSASSS--HRGHCFYRGTVDGS 138
Cdd:pfam01562  12 RRRRSLAsESTYLDTLS-------YRLAAFGKKFHLHLTPNRLLLAPGFTVTyyLDGGTGVESPpvQTDHCYYQGHVEGH 84

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1538027407 139 PRSLAVFDLCGGLDGFFAVKHARYTLKPLLRGSWAEAE 176
Cdd:pfam01562  85 PDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGG 122
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 878-929 2.30e-13

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 65.17  E-value: 2.30e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1538027407 878 WVTGPWLSCSRTCDTGWHTRTVQCQ--DGNRKLA-KGCLLSQRPSAFKQCLLKKC 929
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqkGGGSIVPdSECSAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 627-730 3.05e-12

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


Pssm-ID: 437068  Cd Length: 115  Bit Score: 64.34  E-value: 3.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 627 FRHEQCEAKNGYQ-SDAKGIKTFVEW---VPKYAGvlpGDVCKLTCRAKGTGYYVVFSPKVTDGTECRPY------SNSV 696
Cdd:pfam19236   5 FMSQQCARTDGQPlRSSPGGASFYHWgaaVPHSQG---DALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1538027407 697 CVRGRCVRTGCDGIIGSKLQYDKCGVCGGDNSSC 730
Cdd:pfam19236  82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP_1 pfam00090
Thrombospondin type 1 domain;
572-620 5.07e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 47.03  E-value: 5.07e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1538027407 572 WGPWGQCSRSCGGGVQFAYRHCNNPAPRNSgrYCTGKRAIYRSCSVTPC 620
Cdd:pfam00090   3 WSPWSPCSVTCGKGIQVRQRTCKSPFPGGE--PCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 878-929 2.20e-03

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 37.18  E-value: 2.20e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1538027407  878 WVTGPWLSCSRTCDTGWHTRTVQCQDGNRKlAKGCLLSQRPSAFKQCLLKKC 929
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQ-NGGGPCTGEDVETRACNEQPC 52
SVAGG NF038115
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) ...
 399-447 6.08e-03

SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) family (defined and named here) averages about 420 amino acids in length. Member proteins have a C-terminal GlyGly-CTERM sorting signal, which implies cleavage by rhombosortase, export by a type II secretion system (T2SS), and covalent attachment to the outer membrane.


Pssm-ID: 468358 [Multi-domain]  Cd Length: 407  Bit Score: 40.15  E-value: 6.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1538027407 399 DGLHAAFTVAHEIGHLLGLSHD--DSKFCEEN----------------FGSTEDKRLMSSILTSIDA 447
Cdd:NF038115  170 DLYVATQTLAHELGHLFGLYNGhaESAECSEGgyrlmcgslaenfenlFGSSELQRFYNNADSTLDD 236
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 268-472 1.04e-95

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 299.54  E-value: 1.04e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 268 VEILLVADSSMARMY-GRGLQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLADKDKSLEVSKNAATTLKNFCKWQHQ 346
Cdd:cd04273     3 VETLVVADSKMVEFHhGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQKK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 347 HNQLGDDHEEHYDAAILFTREDLCG-HHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSHDDS-KF 424
Cdd:cd04273    83 LNPPNDSDPEHHDHAILLTRQDICRsNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDgNS 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1538027407 425 CEENFgstEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLL 472
Cdd:cd04273   163 CGPEG---KDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 732-851 3.52e-33

ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like proteins. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase) and is a subfamily of the metalloprotease family, sharing a high degree of sequence similarity and conserved domain organization among its members. Members of the ADAM-TS family have been implicated in a range of diseases. ADAM-TS-like proteins lack a metalloprotease domain. They resides in the ECM and have regulatory roles. Examples of ADAM-TS-like proteins are papilin and punctin.


Pssm-ID: 461796  Cd Length: 115  Bit Score: 123.84  E-value: 3.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 732 KVIGTFNK-KSKGYTDVVRIPEGATHIKVRQFKAKdqtrFTaYLALKKKNGEYLINGKYMISTSETIIDINGTVMNYSGW 810
Cdd:pfam05986   1 TVSGSFTEgRAKGYVTFVTIPAGATHIHIVNRKPS----FT-HLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1538027407 811 SHRDDFLHGMGysATKEILIVQIL-----ATDPtkalDVRYSFFVP 851
Cdd:pfam05986  76 LPALEELHAPG--PTQEDLEIQVLrqygkGTNP----GITYEYFIP 115
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 268-464 6.74e-33

Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ADAM family of metalloproteases contains proteolytic domains from snake venoms, proteases from the mammalian reproductive tract, and the tumor necrosis factor alpha convertase, TACE. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239795  Cd Length: 192  Bit Score: 126.00  E-value: 6.74e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 268 VEILLVADSSMaRMYGRG----LQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLADKDKSLEVSKNAATTLKNFCKW 343
Cdd:cd04267     3 IELVVVADHRM-VSYFNSdeniLQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 344 QHQHNQlgddheeHYDAAILFTREDLCGhhsCDTLGMADVGTICSPERSCAVIEDDG--LHAAFTVAHEIGHLLGLSHDD 421
Cdd:cd04267    82 RAEGPI-------RHDNAVLLTAQDFIE---GDILGLAYVGSMCNPYSSVGVVEDTGftLLTALTMAHELGHNLGAEHDG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1538027407 422 SKFCEENFGStEDKRLMSSILTSIDaSKPWSKCTSATITEFLD 464
Cdd:cd04267   152 GDELAFECDG-GGNYIMAPVDSGLN-SYRFSQCSIGSIREFLD 192
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 268-473 1.92e-29

Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 116.18  E-value: 1.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 268 VEILLVADSSMARMYGRGL---QHYLLTLASIANRLYSHAsienHIRLAVVKVVVLADKDKsLEVSKNAATTLKNFCKWQ 344
Cdd:cd04269     3 VELVVVVDNSLYKKYGSNLskvRQRVIEIVNIVDSIYRPL----NIRVVLVGLEIWTDKDK-ISVSGDAGETLNRFLDWK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 345 HqhNQLGDDHeeHYDAAILFTREDLCGHhscdTLGMADVGTICSPERSCAVIEDDGLH---AAFTVAHEIGHLLGLSHDD 421
Cdd:cd04269    78 R--SNLLPRK--PHDNAQLLTGRDFDGN----TVGLAYVGGMCSPKYSGGVVQDHSRNlllFAVTMAHELGHNLGMEHDD 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1538027407 422 SK-FCEENFGstedkrLMSSILTSIdaSKPWSKCTSATITEFLDDGHGNCLLD 473
Cdd:cd04269   150 GGcTCGRSTC------IMAPSPSSL--TDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 268-475 1.03e-26

Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


Pssm-ID: 426256 [Multi-domain]  Cd Length: 200  Bit Score: 108.54  E-value: 1.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 268 VEILLVADSSMARMYGRGLQH---YLLTLASIANRLYShasiENHIRLAVVKVVVLADKDKsLEVSKNAATTLKNFCKWQ 344
Cdd:pfam01421   3 IELFIVVDKQLFQKMGSDTTVvrqRVFQVVNLVNSIYK----ELNIRVVLVGLEIWTDEDK-IDVSGDANDTLRNFLKWR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 345 HQHNQLGDDHeehyDAAILFTREDLCGHhscdTLGMADVGTICSPERSCAVIED---DGLHAAFTVAHEIGHLLGLSHDD 421
Cdd:pfam01421  78 QEYLKKRKPH----DVAQLLSGVEFGGT----TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQHDD 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1538027407 422 SK---FCEENFGStedkrLMSSILTSIDASKpWSKCTSATITEFLDDGHGNCLLDLP 475
Cdd:pfam01421 150 FNggcKCPPGGGC-----IMNPSAGSSFPRK-FSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 486-553 1.06e-23

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


Pssm-ID: 465496  Cd Length: 68  Bit Score: 95.10  E-value: 1.06e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 486 PGQTYDATQQCNLTFGPEYTVCPGM--DVCARLWCAVvrQGQMVCLTKKLPAVEGTPCGKGRICLQGKCV 553
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGdeDVCSKLWCSN--PGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 569-621 6.79e-16

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 72.62  E-value: 6.79e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1538027407  569 WGSWGPWGQCSRSCGGGVQFAYRHCNNPAPRNSGRYCTGKRAIYRSCSVTPCP 621
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 64-176 1.58e-13

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


Pssm-ID: 460254  Cd Length: 128  Bit Score: 68.11  E-value: 1.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407  64 RQRRSSG-LVQNIDQLYsgggkvgYLVYAGSRRFLLDLERDDSVGTAGGILT--AGDGQSASSS--HRGHCFYRGTVDGS 138
Cdd:pfam01562  12 RRRRSLAsESTYLDTLS-------YRLAAFGKKFHLHLTPNRLLLAPGFTVTyyLDGGTGVESPpvQTDHCYYQGHVEGH 84

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1538027407 139 PRSLAVFDLCGGLDGFFAVKHARYTLKPLLRGSWAEAE 176
Cdd:pfam01562  85 PDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGG 122
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 878-929 2.30e-13

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 65.17  E-value: 2.30e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1538027407 878 WVTGPWLSCSRTCDTGWHTRTVQCQ--DGNRKLA-KGCLLSQRPSAFKQCLLKKC 929
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqkGGGSIVPdSECSAQKKPPETQSCNLKPC 55
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 359-463 3.46e-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: 68.32  E-value: 3.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 359 DAAILFTREDlcghHSCDTLGMADVGTICSPERSCAVIEDDGLH---AAFTVAHEIGHLLGLSHDDSKFCEENFGSTEDK 435
Cdd:cd00203    53 DIAILVTRQD----FDGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDRKDRDDYPTIDDT 128

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1538027407 436 R---------LMSSILTSIDA--SKPWSKCTSATITEFL 463
Cdd:cd00203   129 LnaedddyysVMSYTKGSFSDgqRKDFSQCDIDQINKLY 167
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 268-463 6.33e-13

Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.


Pssm-ID: 239800  Cd Length: 220  Bit Score: 68.92  E-value: 6.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 268 VEILLVADSSMARMYGRGLQ--HYLLTLASIANRLYShaSIEN---HIRLAVVKVVVLADKDKSLEVSKN----AATTLK 338
Cdd:cd04272     3 PELFVVVDYDHQSEFFSNEQliRYLAVMVNAANLRYR--DLKSpriRLLLVGITISKDPDFEPYIHPINYgyidAAETLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 339 NFckwqhQHNQLGDDHEEHYDAAILFTREDLC----GHHSCDTLGMADVGTICSpERSCAVIED-----DGLHaafTVAH 409
Cdd:cd04272    81 NF-----NEYVKKKRDYFNPDVVFLVTGLDMStysgGSLQTGTGGYAYVGGACT-ENRVAMGEDtpgsyYGVY---TMTH 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1538027407 410 EIGHLLGLSHDDS---KFCEENFGST----EDKRLMSSILTSIDASKpWSKCTSATITEFL 463
Cdd:cd04272   152 ELAHLLGAPHDGSpppSWVKGHPGSLdcpwDDGYIMSYVVNGERQYR-FSQCSQRQIRNVF 211
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 627-730 3.05e-12

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


Pssm-ID: 437068  Cd Length: 115  Bit Score: 64.34  E-value: 3.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 627 FRHEQCEAKNGYQ-SDAKGIKTFVEW---VPKYAGvlpGDVCKLTCRAKGTGYYVVFSPKVTDGTECRPY------SNSV 696
Cdd:pfam19236   5 FMSQQCARTDGQPlRSSPGGASFYHWgaaVPHSQG---DALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1538027407 697 CVRGRCVRTGCDGIIGSKLQYDKCGVCGGDNSSC 730
Cdd:pfam19236  82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 322-420 4.56e-10

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 58.15  E-value: 4.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 322 DKDKSLEVSKNAATTLKNFCKWQHQHNQLGDdheehYDAAILFTREDLCGhhscdTLGMADVGTICSPERSCAVIEDD-- 399
Cdd:pfam13582  31 TSADTPYTSSDALEILDELQEVNDTRIGQYG-----YDLGHLFTGRDGGG-----GGGIAYVGGVCNSGSKFGVNSGSgp 100

                          90       100
                  ....*....|....*....|..
gi 1538027407 400 -GLHAAFTVAHEIGHLLGLSHD 420
Cdd:pfam13582 101 vGDTGADTFAHEIGHNFGLNHT 122
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
267-420 6.93e-08

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 53.58  E-value: 6.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 267 QVEILLVADSS-MARMYGRGLQHYLLTL-ASIANRLYSHASIenHIRLAVVKVVVLADKDKSLEVSK-NAATTLKNFC-- 341
Cdd:pfam13688   4 TVALLVAADCSyVAAFGGDAAQANIINMvNTASNVYERDFNI--SLGLVNLTISDSTCPYTPPACSTgDSSDRLSEFQdf 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 342 -KWQHQHNqlgddheehYDAAILFTredlcgHHSCDTLGMADVGTICSPERSCAVIEDDGLH--------AAFTVAHEIG 412
Cdd:pfam13688  82 sAWRGTQN---------DDLAYLFL------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQVFAHEIG 146


                  ....*...
gi 1538027407 413 HLLGLSHD 420
Cdd:pfam13688 147 HNFGAVHD 154
TSP_1 pfam00090
Thrombospondin type 1 domain;
572-620 5.07e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 47.03  E-value: 5.07e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1538027407 572 WGPWGQCSRSCGGGVQFAYRHCNNPAPRNSgrYCTGKRAIYRSCSVTPC 620
Cdd:pfam00090   3 WSPWSPCSVTCGKGIQVRQRTCKSPFPGGE--PCTGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 570-620 3.81e-06

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 44.58  E-value: 3.81e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1538027407 570 GSWGPWGQCSRSCGGGVQFAYRHCNNPaPRNSGRYCTGKRAIyRSCSVTPC 620
Cdd:pfam19028   4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELLER-RPCNLPPC 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 573-620 2.05e-05

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 42.83  E-value: 2.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1538027407 573 GPWGQCSRSCGGGVQfaYR--HCNNPAPR--NSGRYCTGKRA--IYRSCSVTPC 620
Cdd:pfam19030   4 GPWGECSVTCGGGVQ--TRlvQCVQKGGGsiVPDSECSAQKKppETQSCNLKPC 55
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 290-463 4.08e-04

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 372637  Cd Length: 193  Bit Score: 42.62  E-value: 4.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 290 LLTLASIANRLYSHASIENHIRLAvvkvvvladKDKSLEVSKNAATTLKNFCK---WQHQHNQLGDD--HEEHYDAAILF 364
Cdd:pfam13574   7 LVNVVNRVNQIYEPDDININGGLV---------NPGEIPATTSASDSGNNYCNsptTIVRRLNFLSQwrGEQDYCLAHLV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 365 TREDLCGhhscDTLGMADVGTICSPERSCaVIEDDGLHAAFT-------------VAHEIGHLLGLSHD------DSKFC 425
Cdd:pfam13574  78 TMGTFSG----GELGLAYVGQICQKGASS-PKTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDcdgsqyASSGC 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1538027407 426 EENFGSTEDKRLMSSIL--TSIDASKPWSKCTSATITEFL 463
Cdd:pfam13574 153 ERNAATSVCSANGSFIMnpASKSNNDLFSPCSISLICDVL 192
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 878-929 2.20e-03

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 37.18  E-value: 2.20e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1538027407  878 WVTGPWLSCSRTCDTGWHTRTVQCQDGNRKlAKGCLLSQRPSAFKQCLLKKC 929
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQ-NGGGPCTGEDVETRACNEQPC 52
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 268-459 5.98e-03

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 404471  Cd Length: 203  Bit Score: 39.14  E-value: 5.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 268 VEILLVADSSMARMYGR--GLQHYLLTLASIANRLYSHaSIENHIRLAVVKVVVLADKDKSLEVSKNAATTLKN-----F 340
Cdd:pfam13583   5 YRVAVATDCTYSASFGSvdELRANINATVTTANEVYGR-DFNVSLALISDRDVIYTDSSTDSFNADCSGGDLGNwrlatL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538027407 341 CKWQHQHNqlgddheehYDAAILFtREDLCGHHSCdtlGMADVGTICSPER-----SCAVIEDDGLHaafTVAHEIGHLL 415
Cdd:pfam13583  84 TSWRDSLN---------YDLAYLT-LMTGPSGQNV---GVAWVGALCSSARqnakaSGVARSRDEWD---IFAHEIGHTF 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1538027407 416 GLSHDDSKFCEENFGSTEDKRlMSSILT--SIDASKPWSKCTSATI 459
Cdd:pfam13583 148 GAVHDCSSQGEGLSSSTEDGS-GQTIMSyaSTASQTAFSPCTIRNI 192
SVAGG NF038115
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) ...
 399-447 6.08e-03

SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) family (defined and named here) averages about 420 amino acids in length. Member proteins have a C-terminal GlyGly-CTERM sorting signal, which implies cleavage by rhombosortase, export by a type II secretion system (T2SS), and covalent attachment to the outer membrane.


Pssm-ID: 468358 [Multi-domain]  Cd Length: 407  Bit Score: 40.15  E-value: 6.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1538027407 399 DGLHAAFTVAHEIGHLLGLSHD--DSKFCEEN----------------FGSTEDKRLMSSILTSIDA 447
Cdd:NF038115  170 DLYVATQTLAHELGHLFGLYNGhaESAECSEGgyrlmcgslaenfenlFGSSELQRFYNNADSTLDD 236
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 405-419 6.90e-03

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: 38.37  E-value: 6.90e-03
                          10
                  ....*....|....*.
gi 1538027407 405 FTVA-HEIGHLLGLSH 419
Cdd:pfam00413 109 FLVAaHEIGHALGLGH 124
 
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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