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Conserved domains on  [gi|392925753|ref|NP_508681|]
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Peptidase M12B domain-containing protein [Caenorhabditis elegans]

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) ...
 201-416 1.82e-77

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: 251.39  E-value: 1.82e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925753 201 LTVELAVFADDAMWDHFkkmygkaAEENMHTFIMAVVNNIDVLYTQRLLQPRINIKIVRYEILKNIPHLMNarkhSNGDV 280
Cdd:cd04273    1 RYVETLVVADSKMVEFH-------HGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLL----ISGNA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925753 281 DRLLDAFCQYQNEINPPNDADPRHWDHALLFSGYDLHR-NGVKTVAGYAPVKGMCSGVRSCTINEGLDFGSVFVVTHEMG 359
Cdd:cd04273   70 QKSLKSFCRWQKKLNPPNDSDPEHHDHAILLTRQDICRsNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELG 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392925753 360 HSLGMYHDGD-NECD---LRCCIMSPSVGS--GKTHWSQCSVNEMATFVGHLGddfrpPNCLQ 416
Cdd:cd04273  150 HVLGMPHDGDgNSCGpegKDGHIMSPTLGAntGPFTWSKCSRRYLTSFLDTGD-----GNCLL 207
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 434-502 3.40e-16

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: 73.92  E-value: 3.40e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392925753  434 PGQLFTLDEQCEIFHGECWKHELKDGQtmqNICQMVWC--GNGEGVIRTAHPALEGTYCGFGMICRQGQCV 502
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDE---DVCSKLWCsnPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 836-881 2.27e-10

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: 56.83  E-value: 2.27e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 392925753   836 WTEWSQWSDCSVNCGEGVQFRKRACFA-------AFCRGKDSDVRNCYGQRCS 881
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSpppqnggGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 896-940 3.65e-09

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: 53.36  E-value: 3.65e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 392925753   896 WTGWSSWSSCSTKCGIGQRTRRRRCY-------QGSCLGDDNEKERCIGSQC 940
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCspppqngGGPCTGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 791-829 3.41e-07

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: 47.97  E-value: 3.41e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 392925753   791 WGPWSACSVTCGTGQKLRRRENC------IGQECA----ETGPCVMQSC 829
Cdd:smart00209   4 WSEWSPCSVTCGGGVQTRTRSCCspppqnGGGPCTgedvETRACNEQPC 52
TSP1 super family cl15278
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 699-751 1.21e-03

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


The actual alignment was detected with superfamily member PTZ00087:

Pssm-ID: 472794  Cd Length: 340  Bit Score: 42.24  E-value: 1.21e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 392925753 699 KKTPFLNEWSGwsvWSECvTYDC-HTQGVKVRVRRCL--AGVC-AGALRERQPCTRP 751
Cdd:PTZ00087 228 KKNMFYTEWGE---WSNC-SMECdHPDNVQIRERKCAhpSGDCfKGDLKETRPCQVP 280
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 201-416 1.82e-77

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: 251.39  E-value: 1.82e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925753 201 LTVELAVFADDAMWDHFkkmygkaAEENMHTFIMAVVNNIDVLYTQRLLQPRINIKIVRYEILKNIPHLMNarkhSNGDV 280
Cdd:cd04273    1 RYVETLVVADSKMVEFH-------HGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLL----ISGNA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925753 281 DRLLDAFCQYQNEINPPNDADPRHWDHALLFSGYDLHR-NGVKTVAGYAPVKGMCSGVRSCTINEGLDFGSVFVVTHEMG 359
Cdd:cd04273   70 QKSLKSFCRWQKKLNPPNDSDPEHHDHAILLTRQDICRsNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELG 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392925753 360 HSLGMYHDGD-NECD---LRCCIMSPSVGS--GKTHWSQCSVNEMATFVGHLGddfrpPNCLQ 416
Cdd:cd04273  150 HVLGMPHDGDgNSCGpegKDGHIMSPTLGAntGPFTWSKCSRRYLTSFLDTGD-----GNCLL 207
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 434-502 3.40e-16

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: 73.92  E-value: 3.40e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392925753  434 PGQLFTLDEQCEIFHGECWKHELKDGQtmqNICQMVWC--GNGEGVIRTAHPALEGTYCGFGMICRQGQCV 502
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDE---DVCSKLWCsnPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 203-418 3.21e-15

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: 75.03  E-value: 3.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925753  203 VELAVFADDAMwdhFKKMygKAAEENMHTFIMAVVNNIDVLYTQrllqprINIKIVryeiLKNIPHLMNARK-HSNGDVD 281
Cdd:pfam01421   3 IELFIVVDKQL---FQKM--GSDTTVVRQRVFQVVNLVNSIYKE------LNIRVV----LVGLEIWTDEDKiDVSGDAN 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925753  282 RLLDAFCQYQNEINPPndadPRHWDHALLFSGYDLHrngvKTVAGYAPVKGMCSGVRSCTINEgldFGSV----FVVT-- 355
Cdd:pfam01421  68 DTLRNFLKWRQEYLKK----RKPHDVAQLLSGVEFG----GTTVGAAYVGGMCSLEYSGGVNE---DHSKnlesFAVTma 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925753  356 HEMGHSLGMYHDGDN-ECdlRC-----CIMSPSVG-SGKTHWSQCSVNEMATFVGHLGddfrpPNCLQDA 418
Cdd:pfam01421 137 HELGHNLGMQHDDFNgGC--KCppgggCIMNPSAGsSFPRKFSNCSQEDFEQFLTKQK-----GACLFNK 199
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 836-881 2.27e-10

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: 56.83  E-value: 2.27e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 392925753   836 WTEWSQWSDCSVNCGEGVQFRKRACFA-------AFCRGKDSDVRNCYGQRCS 881
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSpppqnggGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 896-940 3.65e-09

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: 53.36  E-value: 3.65e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 392925753   896 WTGWSSWSSCSTKCGIGQRTRRRRCY-------QGSCLGDDNEKERCIGSQC 940
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCspppqngGGPCTGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 791-829 3.41e-07

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: 47.97  E-value: 3.41e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 392925753   791 WGPWSACSVTCGTGQKLRRRENC------IGQECA----ETGPCVMQSC 829
Cdd:smart00209   4 WSEWSPCSVTCGGGVQTRTRSCCspppqnGGGPCTgedvETRACNEQPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
790-829 5.44e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 47.03  E-value: 5.44e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 392925753  790 HWGPWSACSVTCGTGQKLRRR---------ENCIGqECAETGPCVMQSC 829
Cdd:pfam00090   2 PWSPWSPCSVTCGKGIQVRQRtckspfpggEPCTG-DDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
837-880 7.75e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 46.64  E-value: 7.75e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 392925753  837 TEWSQWSDCSVNCGEGVQFRKRACFA-----AFCRGKDSDVRNCYGQRC 880
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSpfpggEPCTGDDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
899-940 1.14e-05

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 43.18  E-value: 1.14e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 392925753  899 WSSWSSCSTKCGIGQRTRRRRCYQ-----GSCLGDDNEKERCIGSQC 940
Cdd:pfam00090   3 WSPWSPCSVTCGKGIQVRQRTCKSpfpggEPCTGDDIETQACKMDKC 49
PTZ00087 PTZ00087
thrombosponding-related protein; Provisional
 699-751 1.21e-03

thrombosponding-related protein; Provisional


Pssm-ID: 185438  Cd Length: 340  Bit Score: 42.24  E-value: 1.21e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 392925753 699 KKTPFLNEWSGwsvWSECvTYDC-HTQGVKVRVRRCL--AGVC-AGALRERQPCTRP 751
Cdd:PTZ00087 228 KKNMFYTEWGE---WSNC-SMECdHPDNVQIRERKCAhpSGDCfKGDLKETRPCQVP 280
PTZ00087 PTZ00087
thrombosponding-related protein; Provisional
 831-860 2.79e-03

thrombosponding-related protein; Provisional


Pssm-ID: 185438  Cd Length: 340  Bit Score: 41.08  E-value: 2.79e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 392925753 831 ENKNT-WTEWSQWSDCSVNCG--EGVQFRKRAC 860
Cdd:PTZ00087 227 EKKNMfYTEWGEWSNCSMECDhpDNVQIRERKC 259
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 201-416 1.82e-77

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: 251.39  E-value: 1.82e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925753 201 LTVELAVFADDAMWDHFkkmygkaAEENMHTFIMAVVNNIDVLYTQRLLQPRINIKIVRYEILKNIPHLMNarkhSNGDV 280
Cdd:cd04273    1 RYVETLVVADSKMVEFH-------HGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLL----ISGNA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925753 281 DRLLDAFCQYQNEINPPNDADPRHWDHALLFSGYDLHR-NGVKTVAGYAPVKGMCSGVRSCTINEGLDFGSVFVVTHEMG 359
Cdd:cd04273   70 QKSLKSFCRWQKKLNPPNDSDPEHHDHAILLTRQDICRsNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELG 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392925753 360 HSLGMYHDGD-NECD---LRCCIMSPSVGS--GKTHWSQCSVNEMATFVGHLGddfrpPNCLQ 416
Cdd:cd04273  150 HVLGMPHDGDgNSCGpegKDGHIMSPTLGAntGPFTWSKCSRRYLTSFLDTGD-----GNCLL 207
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 203-417 4.16e-26

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: 106.55  E-value: 4.16e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925753 203 VELAVFADDAMwdhFKKMYGKaaEENMHTFIMAVVNNIDVLYTQrllqprINIKIVryeiLKNIPHLMNARKHS-NGDVD 281
Cdd:cd04269    3 VELVVVVDNSL---YKKYGSN--LSKVRQRVIEIVNIVDSIYRP------LNIRVV----LVGLEIWTDKDKISvSGDAG 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925753 282 RLLDAFCQYQNeinppNDADPRHW-DHALLFSGYDLHRNgvktVAGYAPVKGMCSGVRSCTINEGLD---FGSVFVVTHE 357
Cdd:cd04269   68 ETLNRFLDWKR-----SNLLPRKPhDNAQLLTGRDFDGN----TVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHE 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392925753 358 MGHSLGMYHDgDNECdlRC----CIMSPSVGSGKTHWSQCSVNEMATFVGHLGddfrpPNCLQD 417
Cdd:cd04269  139 LGHNLGMEHD-DGGC--TCgrstCIMAPSPSSLTDAFSNCSYEDYQKFLSRGG-----GQCLLN 194
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 202-403 1.88e-24

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: 101.73  E-value: 1.88e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925753 202 TVELAVFADdamWDHFKKMYGKaaEENMHTFIMAVVNNIDVLYTQRLLQPRINIKIVRYEILKNIPHLmnarKHSNGDVD 281
Cdd:cd04267    2 EIELVVVAD---HRMVSYFNSD--ENILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFA----PPIDSDAS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925753 282 RLLDAFCQYQNEinppndaDPRHWDHALLFSGYDLhrNGVKTVaGYAPVKGMCSGVRSCTINE--GLDFGSVFVVTHEMG 359
Cdd:cd04267   73 NTLNSFSFWRAE-------GPIRHDNAVLLTAQDF--IEGDIL-GLAYVGSMCNPYSSVGVVEdtGFTLLTALTMAHELG 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 392925753 360 HSLGMYHDGDNECDLRC-----CIMSPSVGS-GKTHWSQCSVNEMATFVG 403
Cdd:cd04267  143 HNLGAEHDGGDELAFECdgggnYIMAPVDSGlNSYRFSQCSIGSIREFLD 192
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 434-502 3.40e-16

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: 73.92  E-value: 3.40e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392925753  434 PGQLFTLDEQCEIFHGECWKHELKDGQtmqNICQMVWC--GNGEGVIRTAHPALEGTYCGFGMICRQGQCV 502
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDE---DVCSKLWCsnPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 203-418 3.21e-15

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: 75.03  E-value: 3.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925753  203 VELAVFADDAMwdhFKKMygKAAEENMHTFIMAVVNNIDVLYTQrllqprINIKIVryeiLKNIPHLMNARK-HSNGDVD 281
Cdd:pfam01421   3 IELFIVVDKQL---FQKM--GSDTTVVRQRVFQVVNLVNSIYKE------LNIRVV----LVGLEIWTDEDKiDVSGDAN 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925753  282 RLLDAFCQYQNEINPPndadPRHWDHALLFSGYDLHrngvKTVAGYAPVKGMCSGVRSCTINEgldFGSV----FVVT-- 355
Cdd:pfam01421  68 DTLRNFLKWRQEYLKK----RKPHDVAQLLSGVEFG----GTTVGAAYVGGMCSLEYSGGVNE---DHSKnlesFAVTma 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925753  356 HEMGHSLGMYHDGDN-ECdlRC-----CIMSPSVG-SGKTHWSQCSVNEMATFVGHLGddfrpPNCLQDA 418
Cdd:pfam01421 137 HELGHNLGMQHDDFNgGC--KCppgggCIMNPSAGsSFPRKFSNCSQEDFEQFLTKQK-----GACLFNK 199
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 234-416 7.34e-12

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 65.84  E-value: 7.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925753 234 MAV-VNNIDVLYTQrLLQPRINIKIVRYEILKNIPHLMNARKHSNGDVD--RLLDAFCQYQNEINppndaDPRHWDHALL 310
Cdd:cd04272   27 LAVmVNAANLRYRD-LKSPRIRLLLVGITISKDPDFEPYIHPINYGYIDaaETLENFNEYVKKKR-----DYFNPDVVFL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925753 311 FSGYDLHR--NGVKT--VAGYAPVKGMCS--GVRSCTINEGLdFGSVFVVTHEMGHSLGMYHDGDNECD--------LRC 376
Cdd:cd04272  101 VTGLDMSTysGGSLQtgTGGYAYVGGACTenRVAMGEDTPGS-YYGVYTMTHELAHLLGAPHDGSPPPSwvkghpgsLDC 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 392925753 377 -----CIMSPSVGSGKTH-WSQCSVNEMATFVGHLGddfrpPNCLQ 416
Cdd:cd04272  180 pwddgYIMSYVVNGERQYrFSQCSQRQIRNVFRRLG-----ASCLH 220
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 836-881 2.27e-10

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: 56.83  E-value: 2.27e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 392925753   836 WTEWSQWSDCSVNCGEGVQFRKRACFA-------AFCRGKDSDVRNCYGQRCS 881
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSpppqnggGPCTGEDVETRACNEQPCP 53
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
229-391 1.66e-09

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 58.20  E-value: 1.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925753  229 MHTFIMAVVNNIDVLYTQRLlqpRINIKIVRYEILKNiPHLMNARKHSNGDVDRLLDAFCQYQNEINPPNDadprhwDHA 308
Cdd:pfam13688  24 AQANIINMVNTASNVYERDF---NISLGLVNLTISDS-TCPYTPPACSTGDSSDRLSEFQDFSAWRGTQND------DLA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925753  309 LLFSGYDLHRNGVKTVAGYAP--VKGMCSGVRSCTINEGLDFGSVFVVTHEMGHSLGMYHDGDNECDLRCC--------- 377
Cdd:pfam13688  94 YLFLMTNCSGGGLAWLGQLCNsgSAGSVSTRVSGNNVVVSTATEWQVFAHEIGHNFGAVHDCDSSTSSQCCppsnstcpa 173

                         170
                  ....*....|....*...
gi 392925753  378 ----IMSPSVGSGKTHWS 391
Cdd:pfam13688 174 ggryIMNPSSSPNSTDFS 191
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 896-940 3.65e-09

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: 53.36  E-value: 3.65e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 392925753   896 WTGWSSWSSCSTKCGIGQRTRRRRCY-------QGSCLGDDNEKERCIGSQC 940
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCspppqngGGPCTGEDVETRACNEQPC 52
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 306-396 1.51e-08

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: 54.84  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925753 306 DHALLFSGYDLHRNGvktvAGYAPVKGMCSGVRSCTI---NEGLDFGSVFVVTHEMGHSLGMYHDGD------------- 369
Cdd:cd00203   53 DIAILVTRQDFDGGT----GGWAYLGRVCDSLRGVGVlqdNQSGTKEGAQTIAHELGHALGFYHDHDrkdrddyptiddt 128

                         90       100       110
                 ....*....|....*....|....*....|...
gi 392925753 370 --NECDLRCCIMSPSVGSG----KTHWSQCSVN 396
Cdd:cd00203  129 lnAEDDDYYSVMSYTKGSFsdgqRKDFSQCDID 161
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 791-829 3.41e-07

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: 47.97  E-value: 3.41e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 392925753   791 WGPWSACSVTCGTGQKLRRRENC------IGQECA----ETGPCVMQSC 829
Cdd:smart00209   4 WSEWSPCSVTCGGGVQTRTRSCCspppqnGGGPCTgedvETRACNEQPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
790-829 5.44e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 47.03  E-value: 5.44e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 392925753  790 HWGPWSACSVTCGTGQKLRRR---------ENCIGqECAETGPCVMQSC 829
Cdd:pfam00090   2 PWSPWSPCSVTCGKGIQVRQRtckspfpggEPCTG-DDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
837-880 7.75e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 46.64  E-value: 7.75e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 392925753  837 TEWSQWSDCSVNCGEGVQFRKRACFA-----AFCRGKDSDVRNCYGQRC 880
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSpfpggEPCTGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 787-829 1.94e-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: 45.73  E-value: 1.94e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392925753  787 KVDHWGPWSACSVTCGTGQKLRRREncI-------GQEC---AETGPCVMQSC 829
Cdd:pfam19028   2 VVSEWSEWSECSVTCGGGVQTRTRT--VivepqngGRPCpelLERRPCNLPPC 52
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 298-367 3.99e-06

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: 46.98  E-value: 3.99e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392925753  298 NDADPRHWDHALLFSGYDLH----RNGVKTVAGYAPVKGMCSGVRSCTINEGL----DFGsVFVVTHEMGHSLGMYHD 367
Cdd:pfam13582  46 LDELQEVNDTRIGQYGYDLGhlftGRDGGGGGGIAYVGGVCNSGSKFGVNSGSgpvgDTG-ADTFAHEIGHNFGLNHT 122
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 353-403 6.87e-06

Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A Disintegrin And Metalloprotease) family of metalloproteases are integral membrane proteases acting on a variety of extracellular targets. They are involved in shedding soluble peptides or proteins from the cell surface. This subfamily contains fungal ADAMs, whose precise function has yet to be determined.


Pssm-ID: 239799 [Multi-domain]  Cd Length: 228  Bit Score: 48.19  E-value: 6.87e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392925753 353 VVTHEMGHSLGMYHDGDNEC-------DLRCC-------------IMSPSVGSGKTHWSQCSVNEMATFVG 403
Cdd:cd04271  148 VFAHEIGHTFGAVHDCTSGTcsdgsvgSQQCCplststcdangqyIMNPSSSSGITEFSPCTIGNICSLLG 218
TSP_1 pfam00090
Thrombospondin type 1 domain;
899-940 1.14e-05

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 43.18  E-value: 1.14e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 392925753  899 WSSWSSCSTKCGIGQRTRRRRCYQ-----GSCLGDDNEKERCIGSQC 940
Cdd:pfam00090   3 WSPWSPCSVTCGKGIQVRQRTCKSpfpggEPCTGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 837-880 2.75e-05

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: 42.27  E-value: 2.75e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392925753  837 TEWSQWSDCSVNCGEGVQFRKRA-----------CfaafcrGKDSDVRNCYGQRC 880
Cdd:pfam19028   4 SEWSEWSECSVTCGGGVQTRTRTvivepqnggrpC------PELLERRPCNLPPC 52
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 897-918 1.09e-04

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: 40.73  E-value: 1.09e-04
                          10        20
                  ....*....|....*....|..
gi 392925753  897 TGWSSWSSCSTKCGIGQRTRRR 918
Cdd:pfam19028   4 SEWSEWSECSVTCGGGVQTRTR 25
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 792-831 6.35e-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: 38.59  E-value: 6.35e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 392925753  792 GPWSACSVTCGTGQKlRRRENCI---------GQEC-AETGPCVMQSCRE 831
Cdd:pfam19030   4 GPWGECSVTCGGGVQ-TRLVQCVqkgggsivpDSECsAQKKPPETQSCNL 52
PTZ00087 PTZ00087
thrombosponding-related protein; Provisional
 699-751 1.21e-03

thrombosponding-related protein; Provisional


Pssm-ID: 185438  Cd Length: 340  Bit Score: 42.24  E-value: 1.21e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 392925753 699 KKTPFLNEWSGwsvWSECvTYDC-HTQGVKVRVRRCL--AGVC-AGALRERQPCTRP 751
Cdd:PTZ00087 228 KKNMFYTEWGE---WSNC-SMECdHPDNVQIRERKCAhpSGDCfKGDLKETRPCQVP 280
PTZ00087 PTZ00087
thrombosponding-related protein; Provisional
 831-860 2.79e-03

thrombosponding-related protein; Provisional


Pssm-ID: 185438  Cd Length: 340  Bit Score: 41.08  E-value: 2.79e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 392925753 831 ENKNT-WTEWSQWSDCSVNCG--EGVQFRKRAC 860
Cdd:PTZ00087 227 EKKNMfYTEWGEWSNCSMECDhpDNVQIRERKC 259
 
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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