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Conserved domains on  [gi|1062846830|ref|XP_013820675|]
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PREDICTED: A disintegrin and metalloproteinase with thrombospondin motifs 5 [Capra hircus]

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) ...
 273-477 8.09e-97

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: 302.62  E-value: 8.09e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 273 VELLLVADASMARMY-GRGLQHYLLTLASIANKLYSHASIENHIRLVVVKVVVLGDKDKSLEVSKNAATTLKNFCKWQHQ 351
Cdd:cd04273     3 VETLVVADSKMVEFHhGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQKK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 352 HNQLGDDHEEHYDAAILFTREDLCG-HHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSHDDS-KF 429
Cdd:cd04273    83 LNPPNDSDPEHHDHAILLTRQDICRsNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDgNS 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1062846830 430 CEENFgstEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLL 477
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 ...
 737-856 2.94e-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: 124.23  E-value: 2.94e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 737 KVVGTFNK-KSKGYTDVVRIPEGATHIKVRQFKAKdqtrFTaYLALKKKNGEYLINGKYMISTSETIIDINGTVMNYSGW 815
Cdd:pfam05986   1 TVSGSFTEgRAKGYVTFVTIPAGATHIHIVNRKPS----FT-HLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1062846830 816 SHRDDFLHGMGysATKEILIVQIL-----ATDPtkalDVRYSFFVP 856
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 ...
 491-558 3.57e-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: 93.56  E-value: 3.57e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 491 PGQTYDASQQCNLTFGPEYSVCPGM--DVCARLWCAVvrQGQMVCLTKKLPAVEGTPCGKGRICLQGKCV 558
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGdeDVCSKLWCSN--PGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 62-185 5.79e-16

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: 75.04  E-value: 5.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830  62 HPHPLAPQRGSRGL---VQNIDQLYsgggkvgYLVYAGGRRFLLDLERDDSVGAAGLV-----PAGGGPNATRRHRGHCF 133
Cdd:pfam01562   4 IPVRLDPSRRRRSLaseSTYLDTLS-------YRLAAFGKKFHLHLTPNRLLLAPGFTvtyylDGGTGVESPPVQTDHCY 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1062846830 134 YRGTVDGSPRSLAVFDLCGGLDGFFAVKRARYTLQPLLRGPWAEAEDDARVY 185
Cdd:pfam01562  77 YQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGHPHVVY 128
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 574-626 1.15e-15

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: 71.85  E-value: 1.15e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1062846830  574 WGSWGSWGQCSRSCGGGVQFAYRHCNNPAPRNNGRYCTGKRAIYRSCSVTPCP 626
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 883-934 4.90e-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: 64.40  E-value: 4.90e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1062846830 883 WVTGPWLACSRTCDTGWHTRTVQCQ--DGNRKLA-KGCLLSQRPSAFKQCLLKKC 934
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 ...
 632-735 5.39e-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: 63.57  E-value: 5.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 632 FRHEQCEAKNGYQ-SDAKGVKTFVEW---VPKYAGvlpGDVCKLACRAKGTGYYVVFSPKVTDGTECRPY------SNSV 701
Cdd:pfam19236   5 FMSQQCARTDGQPlRSSPGGASFYHWgaaVPHSQG---DALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1062846830 702 CVRGKCVRTGCDGIIGSKLQYDKCGICGGDNSSC 735
Cdd:pfam19236  82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
COG3899 super family cl28481
Predicted ATPase [General function prediction only];
3-289 5.13e-03

Predicted ATPase [General function prediction only];


The actual alignment was detected with superfamily member COG3899:

Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 40.61  E-value: 5.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830    3 LGWASLMLCALRLPPVAAGPAAAPAQDKAGQPRAAAVATAAQPRGWRGEEAQEPAEPPGHPHPLAPQRGSRGLVqnidqL 82
Cdd:COG3899      7 GLRLAVARLRGLLLALAAALALLAAALLLLLLLALRLALLLLALALLLLLLLALLLLLALLLALLLLALLLLAL-----A 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830   83 YSGGGKVGYLVYAGGRRFLLDLERDDSVGAAGLVPAGGGPNATRRHRGHCFYRGTVDGSPRSLAVFDLCGGLDGFFAVKR 162
Cdd:COG3899     82 LLRLLAAERLALLLALALALLAALLLLLALALLLLALLALALLALLLALLLAAGVLGLLLGGLLLAALAALLALAALAAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830  163 ARYTLQPLLRGPWAEAEDDARVYGDGSPRILHVYTREGFSFEALPPRTSCETHASPPGARERPPAPRRQDGRW----ALA 238
Cdd:COG3899    162 AAAAAAAAAARAARLRRARAARLAALALRALLLLVLLLLLLLLLLGLLLAAAAALAAAAAAAAAAAPAAPVVLvaalLLA 241

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1062846830  239 PQQLPGQSAPSSDGSQGPRTWWRRRRRSISRARQVELLLVADASMARMYGR 289
Cdd:COG3899    242 LAALLALLLLAARLLGLAGAAALLLLGLLAAAAAGRRLLARRLIPQPLVGR 292
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 273-477 8.09e-97

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: 302.62  E-value: 8.09e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 273 VELLLVADASMARMY-GRGLQHYLLTLASIANKLYSHASIENHIRLVVVKVVVLGDKDKSLEVSKNAATTLKNFCKWQHQ 351
Cdd:cd04273     3 VETLVVADSKMVEFHhGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQKK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 352 HNQLGDDHEEHYDAAILFTREDLCG-HHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSHDDS-KF 429
Cdd:cd04273    83 LNPPNDSDPEHHDHAILLTRQDICRsNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDgNS 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1062846830 430 CEENFgstEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLL 477
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 ...
 737-856 2.94e-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: 124.23  E-value: 2.94e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 737 KVVGTFNK-KSKGYTDVVRIPEGATHIKVRQFKAKdqtrFTaYLALKKKNGEYLINGKYMISTSETIIDINGTVMNYSGW 815
Cdd:pfam05986   1 TVSGSFTEgRAKGYVTFVTIPAGATHIHIVNRKPS----FT-HLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1062846830 816 SHRDDFLHGMGysATKEILIVQIL-----ATDPtkalDVRYSFFVP 856
Cdd:pfam05986  76 LPALEELHAPG--PTQEDLEIQVLrqygkGTNP----GITYEYFIP 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 273-480 5.88e-27

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: 108.93  E-value: 5.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 273 VELLLVADASMARMYGRGLQH---YLLTLASIANKLYShaSIENHIRLVVVKVVVLGDKdksLEVSKNAATTLKNFCKWQ 349
Cdd:pfam01421   3 IELFIVVDKQLFQKMGSDTTVvrqRVFQVVNLVNSIYK--ELNIRVVLVGLEIWTDEDK---IDVSGDANDTLRNFLKWR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 350 HQHNQLGDDHeehyDAAILFTREDLCGHhscdTLGMADVGTICSPERSCAVIED---DGLHAAFTVAHEIGHLLGLSHDD 426
Cdd:pfam01421  78 QEYLKKRKPH----DVAQLLSGVEFGGT----TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQHDD 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1062846830 427 SK---FCEENFGStedkrLMSSILTSIDASKpWSKCTSATITEFLDDGHGNCLLDLP 480
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 ...
 491-558 3.57e-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: 93.56  E-value: 3.57e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 491 PGQTYDASQQCNLTFGPEYSVCPGM--DVCARLWCAVvrQGQMVCLTKKLPAVEGTPCGKGRICLQGKCV 558
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGdeDVCSKLWCSN--PGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 62-185 5.79e-16

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: 75.04  E-value: 5.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830  62 HPHPLAPQRGSRGL---VQNIDQLYsgggkvgYLVYAGGRRFLLDLERDDSVGAAGLV-----PAGGGPNATRRHRGHCF 133
Cdd:pfam01562   4 IPVRLDPSRRRRSLaseSTYLDTLS-------YRLAAFGKKFHLHLTPNRLLLAPGFTvtyylDGGTGVESPPVQTDHCY 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1062846830 134 YRGTVDGSPRSLAVFDLCGGLDGFFAVKRARYTLQPLLRGPWAEAEDDARVY 185
Cdd:pfam01562  77 YQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGHPHVVY 128
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 574-626 1.15e-15

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: 71.85  E-value: 1.15e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1062846830  574 WGSWGSWGQCSRSCGGGVQFAYRHCNNPAPRNNGRYCTGKRAIYRSCSVTPCP 626
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 883-934 4.90e-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: 64.40  E-value: 4.90e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1062846830 883 WVTGPWLACSRTCDTGWHTRTVQCQ--DGNRKLA-KGCLLSQRPSAFKQCLLKKC 934
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 ...
 632-735 5.39e-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: 63.57  E-value: 5.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 632 FRHEQCEAKNGYQ-SDAKGVKTFVEW---VPKYAGvlpGDVCKLACRAKGTGYYVVFSPKVTDGTECRPY------SNSV 701
Cdd:pfam19236   5 FMSQQCARTDGQPlRSSPGGASFYHWgaaVPHSQG---DALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1062846830 702 CVRGKCVRTGCDGIIGSKLQYDKCGICGGDNSSC 735
Cdd:pfam19236  82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 575-625 2.56e-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: 45.35  E-value: 2.56e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1062846830 575 GSWGSWGQCSRSCGGGVQFAYRHCNNPaPRNNGRYCTGKRAIyRSCSVTPC 625
Cdd:pfam19028   4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELLER-RPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 883-934 3.45e-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: 36.41  E-value: 3.45e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1062846830  883 WVTGPWLACSRTCDTGWHTRTVQCQDGNRKlAKGCLLSQRPSAFKQCLLKKC 934
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQ-NGGGPCTGEDVETRACNEQPC 52
COG3899 COG3899
Predicted ATPase [General function prediction only];
3-289 5.13e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 40.61  E-value: 5.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830    3 LGWASLMLCALRLPPVAAGPAAAPAQDKAGQPRAAAVATAAQPRGWRGEEAQEPAEPPGHPHPLAPQRGSRGLVqnidqL 82
Cdd:COG3899      7 GLRLAVARLRGLLLALAAALALLAAALLLLLLLALRLALLLLALALLLLLLLALLLLLALLLALLLLALLLLAL-----A 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830   83 YSGGGKVGYLVYAGGRRFLLDLERDDSVGAAGLVPAGGGPNATRRHRGHCFYRGTVDGSPRSLAVFDLCGGLDGFFAVKR 162
Cdd:COG3899     82 LLRLLAAERLALLLALALALLAALLLLLALALLLLALLALALLALLLALLLAAGVLGLLLGGLLLAALAALLALAALAAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830  163 ARYTLQPLLRGPWAEAEDDARVYGDGSPRILHVYTREGFSFEALPPRTSCETHASPPGARERPPAPRRQDGRW----ALA 238
Cdd:COG3899    162 AAAAAAAAAARAARLRRARAARLAALALRALLLLVLLLLLLLLLLGLLLAAAAALAAAAAAAAAAAPAAPVVLvaalLLA 241

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1062846830  239 PQQLPGQSAPSSDGSQGPRTWWRRRRRSISRARQVELLLVADASMARMYGR 289
Cdd:COG3899    242 LAALLALLLLAARLLGLAGAAALLLLGLLAAAAAGRRLLARRLIPQPLVGR 292
SVAGG NF038115
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) ...
 404-452 6.12e-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: 6.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1062846830 404 DGLHAAFTVAHEIGHLLGLSHD--DSKFCEEN----------------FGSTEDKRLMSSILTSIDA 452
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) ...
 273-477 8.09e-97

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: 302.62  E-value: 8.09e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 273 VELLLVADASMARMY-GRGLQHYLLTLASIANKLYSHASIENHIRLVVVKVVVLGDKDKSLEVSKNAATTLKNFCKWQHQ 351
Cdd:cd04273     3 VETLVVADSKMVEFHhGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQKK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 352 HNQLGDDHEEHYDAAILFTREDLCG-HHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSHDDS-KF 429
Cdd:cd04273    83 LNPPNDSDPEHHDHAILLTRQDICRsNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDgNS 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1062846830 430 CEENFgstEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLL 477
Cdd:cd04273   163 CGPEG---KDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 273-469 2.90e-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: 127.15  E-value: 2.90e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 273 VELLLVADASMaRMYGRG----LQHYLLTLASIANKLYSHASIENHIRLVVVKVVVLGDKDKSLEVSKNAATTLKNFCKW 348
Cdd:cd04267     3 IELVVVADHRM-VSYFNSdeniLQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 349 QHQHNQlgddheeHYDAAILFTREDLCGhhsCDTLGMADVGTICSPERSCAVIEDDG--LHAAFTVAHEIGHLLGLSHDD 426
Cdd:cd04267    82 RAEGPI-------RHDNAVLLTAQDFIE---GDILGLAYVGSMCNPYSSVGVVEDTGftLLTALTMAHELGHNLGAEHDG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1062846830 427 SKFCEENFGStEDKRLMSSILTSIDaSKPWSKCTSATITEFLD 469
Cdd:cd04267   152 GDELAFECDG-GGNYIMAPVDSGLN-SYRFSQCSIGSIREFLD 192
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 737-856 2.94e-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: 124.23  E-value: 2.94e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 737 KVVGTFNK-KSKGYTDVVRIPEGATHIKVRQFKAKdqtrFTaYLALKKKNGEYLINGKYMISTSETIIDINGTVMNYSGW 815
Cdd:pfam05986   1 TVSGSFTEgRAKGYVTFVTIPAGATHIHIVNRKPS----FT-HLAVKNVQGKYILNGKGSISLNPTYPSLLGTVLEYRRS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1062846830 816 SHRDDFLHGMGysATKEILIVQIL-----ATDPtkalDVRYSFFVP 856
Cdd:pfam05986  76 LPALEELHAPG--PTQEDLEIQVLrqygkGTNP----GITYEYFIP 115
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 273-478 2.80e-31

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: 121.18  E-value: 2.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 273 VELLLVADASMARMYGRGL---QHYLLTLASIANKLYSHASIenHIRLvvvkvvvLG-----DKDKsLEVSKNAATTLKN 344
Cdd:cd04269     3 VELVVVVDNSLYKKYGSNLskvRQRVIEIVNIVDSIYRPLNI--RVVL-------VGleiwtDKDK-ISVSGDAGETLNR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 345 FCKWQHqhNQLGDDHeeHYDAAILFTREDLCGHhscdTLGMADVGTICSPERSCAVIEDDGLH---AAFTVAHEIGHLLG 421
Cdd:cd04269    73 FLDWKR--SNLLPRK--PHDNAQLLTGRDFDGN----TVGLAYVGGMCSPKYSGGVVQDHSRNlllFAVTMAHELGHNLG 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1062846830 422 LSHDDSK-FCEENFGstedkrLMSSILTSIdaSKPWSKCTSATITEFLDDGHGNCLLD 478
Cdd:cd04269   145 MEHDDGGcTCGRSTC------IMAPSPSSL--TDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 273-480 5.88e-27

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: 108.93  E-value: 5.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 273 VELLLVADASMARMYGRGLQH---YLLTLASIANKLYShaSIENHIRLVVVKVVVLGDKdksLEVSKNAATTLKNFCKWQ 349
Cdd:pfam01421   3 IELFIVVDKQLFQKMGSDTTVvrqRVFQVVNLVNSIYK--ELNIRVVLVGLEIWTDEDK---IDVSGDANDTLRNFLKWR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 350 HQHNQLGDDHeehyDAAILFTREDLCGHhscdTLGMADVGTICSPERSCAVIED---DGLHAAFTVAHEIGHLLGLSHDD 426
Cdd:pfam01421  78 QEYLKKRKPH----DVAQLLSGVEFGGT----TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQHDD 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1062846830 427 SK---FCEENFGStedkrLMSSILTSIDASKpWSKCTSATITEFLDDGHGNCLLDLP 480
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 ...
 491-558 3.57e-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: 93.56  E-value: 3.57e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 491 PGQTYDASQQCNLTFGPEYSVCPGM--DVCARLWCAVvrQGQMVCLTKKLPAVEGTPCGKGRICLQGKCV 558
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGdeDVCSKLWCSN--PGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 62-185 5.79e-16

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: 75.04  E-value: 5.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830  62 HPHPLAPQRGSRGL---VQNIDQLYsgggkvgYLVYAGGRRFLLDLERDDSVGAAGLV-----PAGGGPNATRRHRGHCF 133
Cdd:pfam01562   4 IPVRLDPSRRRRSLaseSTYLDTLS-------YRLAAFGKKFHLHLTPNRLLLAPGFTvtyylDGGTGVESPPVQTDHCY 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1062846830 134 YRGTVDGSPRSLAVFDLCGGLDGFFAVKRARYTLQPLLRGPWAEAEDDARVY 185
Cdd:pfam01562  77 YQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGHPHVVY 128
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 574-626 1.15e-15

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: 71.85  E-value: 1.15e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1062846830  574 WGSWGSWGQCSRSCGGGVQFAYRHCNNPAPRNNGRYCTGKRAIYRSCSVTPCP 626
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 364-468 2.58e-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: 68.70  E-value: 2.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 364 DAAILFTREDlcghHSCDTLGMADVGTICSPERSCAVIEDDGLH---AAFTVAHEIGHLLGLSHDDSKFCEENFGSTEDK 440
Cdd:cd00203    53 DIAILVTRQD----FDGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDRKDRDDYPTIDDT 128

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1062846830 441 R---------LMSSILTSIDA--SKPWSKCTSATITEFL 468
Cdd:cd00203   129 LnaedddyysVMSYTKGSFSDgqRKDFSQCDIDQINKLY 167
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 883-934 4.90e-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: 64.40  E-value: 4.90e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1062846830 883 WVTGPWLACSRTCDTGWHTRTVQCQ--DGNRKLA-KGCLLSQRPSAFKQCLLKKC 934
Cdd:pfam19030   1 WVAGPWGECSVTCGGGVQTRLVQCVqkGGGSIVPdSECSAQKKPPETQSCNLKPC 55
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 337-468 4.54e-12

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 66.61  E-value: 4.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 337 NAATTLKNFckwqhQHNQLGDDHEEHYDAAILFTREDLC----GHHSCDTLGMADVGTICSpERSCAVIED-----DGLH 407
Cdd:cd04272    74 DAAETLENF-----NEYVKKKRDYFNPDVVFLVTGLDMStysgGSLQTGTGGYAYVGGACT-ENRVAMGEDtpgsyYGVY 147

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1062846830 408 aafTVAHEIGHLLGLSHDDS---KFCEENFGST----EDKRLMSSILTSIDASKpWSKCTSATITEFL 468
Cdd:cd04272   148 ---TMTHELAHLLGAPHDGSpppSWVKGHPGSLdcpwDDGYIMSYVVNGERQYR-FSQCSQRQIRNVF 211
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 632-735 5.39e-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: 63.57  E-value: 5.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 632 FRHEQCEAKNGYQ-SDAKGVKTFVEW---VPKYAGvlpGDVCKLACRAKGTGYYVVFSPKVTDGTECRPY------SNSV 701
Cdd:pfam19236   5 FMSQQCARTDGQPlRSSPGGASFYHWgaaVPHSQG---DALCRHMCRAIGESFIMKRGDSFLDGTRCMPSgpredgTLSL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1062846830 702 CVRGKCVRTGCDGIIGSKLQYDKCGICGGDNSSC 735
Cdd:pfam19236  82 CVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 327-425 4.59e-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: 4.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 327 DKDKSLEVSKNAATTLKNFCKWQHQHNQLGDdheehYDAAILFTREDLCGhhscdTLGMADVGTICSPERSCAVIEDD-- 404
Cdd:pfam13582  31 TSADTPYTSSDALEILDELQEVNDTRIGQYG-----YDLGHLFTGRDGGG-----GGGIAYVGGVCNSGSKFGVNSGSgp 100

                          90       100
                  ....*....|....*....|..
gi 1062846830 405 -GLHAAFTVAHEIGHLLGLSHD 425
Cdd:pfam13582 101 vGDTGADTFAHEIGHNFGLNHT 122
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
272-425 5.65e-09

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 56.66  E-value: 5.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 272 QVELLLVADAS-MARMYGRGLQHYLLTL-ASIANKLYSHASIenHIRLVVVKVVVLGDKDKSLEVSK-NAATTLKNFC-- 346
Cdd:pfam13688   4 TVALLVAADCSyVAAFGGDAAQANIINMvNTASNVYERDFNI--SLGLVNLTISDSTCPYTPPACSTgDSSDRLSEFQdf 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 347 -KWQHQHNqlgddheehYDAAILFTredlcgHHSCDTLGMADVGTICSPERSCAVIEDDGLH--------AAFTVAHEIG 417
Cdd:pfam13688  82 sAWRGTQN---------DDLAYLFL------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQVFAHEIG 146


                  ....*...
gi 1062846830 418 HLLGLSHD 425
Cdd:pfam13688 147 HNFGAVHD 154
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 575-625 2.56e-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: 45.35  E-value: 2.56e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1062846830 575 GSWGSWGQCSRSCGGGVQFAYRHCNNPaPRNNGRYCTGKRAIyRSCSVTPC 625
Cdd:pfam19028   4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELLER-RPCNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
577-625 4.64e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 44.33  E-value: 4.64e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1062846830 577 WGSWGQCSRSCGGGVQFAYRHCNNPAPrnNGRYCTGKRAIYRSCSVTPC 625
Cdd:pfam00090   3 WSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 578-625 1.28e-04

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: 40.51  E-value: 1.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1062846830 578 GSWGQCSRSCGGGVQfaYR--HCNNPAPR--NNGRYCTGKRA--IYRSCSVTPC 625
Cdd:pfam19030   4 GPWGECSVTCGGGVQ--TRlvQCVQKGGGsiVPDSECSAQKKppETQSCNLKPC 55
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 360-468 6.17e-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: 41.85  E-value: 6.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 360 EEHYDAAILFTREDLCGhhscDTLGMADVGTICSPERSCaVIEDDGLHAAFT-------------VAHEIGHLLGLSHD- 425
Cdd:pfam13574  68 EQDYCLAHLVTMGTFSG----GELGLAYVGQICQKGASS-PKTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDc 142

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1062846830 426 -----DSKFCEENFGSTEDKRLMSSIL--TSIDASKPWSKCTSATITEFL 468
Cdd:pfam13574 143 dgsqyASSGCERNAATSVCSANGSFIMnpASKSNNDLFSPCSISLICDVL 192
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 883-934 3.45e-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: 36.41  E-value: 3.45e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1062846830  883 WVTGPWLACSRTCDTGWHTRTVQCQDGNRKlAKGCLLSQRPSAFKQCLLKKC 934
Cdd:smart00209   2 SEWSEWSPCSVTCGGGVQTRTRSCCSPPPQ-NGGGPCTGEDVETRACNEQPC 52
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 360-464 4.74e-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: 39.52  E-value: 4.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830 360 EEHYDAAILFtREDLCGHHSCdtlGMADVGTICSPER-----SCAVIEDDGLHaafTVAHEIGHLLGLSHDDSKFCEENF 434
Cdd:pfam13583  89 SLNYDLAYLT-LMTGPSGQNV---GVAWVGALCSSARqnakaSGVARSRDEWD---IFAHEIGHTFGAVHDCSSQGEGLS 161

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1062846830 435 GSTEDKRlMSSILT--SIDASKPWSKCTSATI 464
Cdd:pfam13583 162 SSTEDGS-GQTIMSyaSTASQTAFSPCTIRNI 192
COG3899 COG3899
Predicted ATPase [General function prediction only];
3-289 5.13e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 40.61  E-value: 5.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830    3 LGWASLMLCALRLPPVAAGPAAAPAQDKAGQPRAAAVATAAQPRGWRGEEAQEPAEPPGHPHPLAPQRGSRGLVqnidqL 82
Cdd:COG3899      7 GLRLAVARLRGLLLALAAALALLAAALLLLLLLALRLALLLLALALLLLLLLALLLLLALLLALLLLALLLLAL-----A 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830   83 YSGGGKVGYLVYAGGRRFLLDLERDDSVGAAGLVPAGGGPNATRRHRGHCFYRGTVDGSPRSLAVFDLCGGLDGFFAVKR 162
Cdd:COG3899     82 LLRLLAAERLALLLALALALLAALLLLLALALLLLALLALALLALLLALLLAAGVLGLLLGGLLLAALAALLALAALAAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062846830  163 ARYTLQPLLRGPWAEAEDDARVYGDGSPRILHVYTREGFSFEALPPRTSCETHASPPGARERPPAPRRQDGRW----ALA 238
Cdd:COG3899    162 AAAAAAAAAARAARLRRARAARLAALALRALLLLVLLLLLLLLLLGLLLAAAAALAAAAAAAAAAAPAAPVVLvaalLLA 241

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1062846830  239 PQQLPGQSAPSSDGSQGPRTWWRRRRRSISRARQVELLLVADASMARMYGR 289
Cdd:COG3899    242 LAALLALLLLAARLLGLAGAAALLLLGLLAAAAAGRRLLARRLIPQPLVGR 292
SVAGG NF038115
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) ...
 404-452 6.12e-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: 6.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1062846830 404 DGLHAAFTVAHEIGHLLGLSHD--DSKFCEEN----------------FGSTEDKRLMSSILTSIDA 452
Cdd:NF038115  170 DLYVATQTLAHELGHLFGLYNGhaESAECSEGgyrlmcgslaenfenlFGSSELQRFYNNADSTLDD 236
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 410-424 6.94e-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: 6.94e-03
                          10
                  ....*....|....*.
gi 1062846830 410 FTVA-HEIGHLLGLSH 424
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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