|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
331-543 |
4.19e-85 |
|
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: 274.50 E-value: 4.19e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 331 LFIETAIFVDSDLYAHMqknfptnTESKVVSFLLAMINGVQLLYHHPTLGRRINFVLKRLEIWKSWdPPGLVRSRDVENY 410
Cdd:cd04273 1 RYVETLVVADSKMVEFH-------HGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDE-ESGLLISGNAQKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 411 LNSFCKWQEKLNPFSDADPLHYDHALVLTGLDLVTYDKgkaNSQVVGMATVKGMCTSIYSCTINEAKHFESVFVVAHEIG 490
Cdd:cd04273 73 LKSFCRWQKKLNPPNDSDPEHHDHAILLTRQDICRSNG---NCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 386768470 491 HNLGMRHDAKEISCDPT---MHIMSPKLGS--GKVTWSKCSRTYLEDFLMDPQAECLF 543
Cdd:cd04273 150 HVLGMPHDGDGNSCGPEgkdGHIMSPTLGAntGPFTWSKCSRRYLTSFLDTGDGNCLL 207
|
|
| ADAMTS_CR_2 |
pfam17771 |
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ... |
561-625 |
1.51e-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: 75.07 E-value: 1.51e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386768470 561 PGERFNANQQCMLRFGKNFmQASTQSKMEICRDLHCRQDGLP---WTSHPALEGTECGPNMWCRGGTC 625
Cdd:pfam17771 1 PGQLYSADEQCRLIFGPGS-TFCPNGDEDVCSKLWCSNPGGStctTKNLPAADGTPCGNKKWCLNGKC 67
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
683-741 |
6.82e-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: 36.03 E-value: 6.82e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386768470 683 WGEWSEPSACESGClygqsrrllegSTGLRTLNRSCLNFP-----SRCIGRDRRFVTCNTPQCH 741
Cdd:smart00209 1 WSEWSEWSPCSVTC-----------GGGVQTRTRSCCSPPpqnggGPCTGEDVETRACNEQPCP 53
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
331-543 |
4.19e-85 |
|
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: 274.50 E-value: 4.19e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 331 LFIETAIFVDSDLYAHMqknfptnTESKVVSFLLAMINGVQLLYHHPTLGRRINFVLKRLEIWKSWdPPGLVRSRDVENY 410
Cdd:cd04273 1 RYVETLVVADSKMVEFH-------HGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDE-ESGLLISGNAQKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 411 LNSFCKWQEKLNPFSDADPLHYDHALVLTGLDLVTYDKgkaNSQVVGMATVKGMCTSIYSCTINEAKHFESVFVVAHEIG 490
Cdd:cd04273 73 LKSFCRWQKKLNPPNDSDPEHHDHAILLTRQDICRSNG---NCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 386768470 491 HNLGMRHDAKEISCDPT---MHIMSPKLGS--GKVTWSKCSRTYLEDFLMDPQAECLF 543
Cdd:cd04273 150 HVLGMPHDGDGNSCGPEgkdGHIMSPTLGAntGPFTWSKCSRRYLTSFLDTGDGNCLL 207
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
332-545 |
4.02e-29 |
|
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: 115.48 E-value: 4.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 332 FIETAIFVDSDLYAHMQKNfptntESKVVSFLLAMINGVQLLYhhptlgRRINF--VLKRLEIWKSWDPPGLvrSRDVEN 409
Cdd:pfam01421 2 YIELFIVVDKQLFQKMGSD-----TTVVRQRVFQVVNLVNSIY------KELNIrvVLVGLEIWTDEDKIDV--SGDAND 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 410 YLNSFCKW-QEKLNPFSDadplhYDHALVLTGLDLvtydkgkaNSQVVGMATVKGMCTSIYSCTINEAKHFESVFV---V 485
Cdd:pfam01421 69 TLRNFLKWrQEYLKKRKP-----HDVAQLLSGVEF--------GGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFavtM 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386768470 486 AHEIGHNLGMRHDAKEISCD-PTMH--IMSPKLG-SGKVTWSKCSRTYLEDFLMDPQAECLFDR 545
Cdd:pfam01421 136 AHELGHNLGMQHDDFNGGCKcPPGGgcIMNPSAGsSFPRKFSNCSQEDFEQFLTKQKGACLFNK 199
|
|
| ADAMTS_CR_2 |
pfam17771 |
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ... |
561-625 |
1.51e-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: 75.07 E-value: 1.51e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386768470 561 PGERFNANQQCMLRFGKNFmQASTQSKMEICRDLHCRQDGLP---WTSHPALEGTECGPNMWCRGGTC 625
Cdd:pfam17771 1 PGQLYSADEQCRLIFGPGS-TFCPNGDEDVCSKLWCSNPGGStctTKNLPAADGTPCGNKKWCLNGKC 67
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
683-741 |
6.82e-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: 36.03 E-value: 6.82e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386768470 683 WGEWSEPSACESGClygqsrrllegSTGLRTLNRSCLNFP-----SRCIGRDRRFVTCNTPQCH 741
Cdd:smart00209 1 WSEWSEWSPCSVTC-----------GGGVQTRTRSCCSPPpqnggGPCTGEDVETRACNEQPCP 53
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
331-543 |
4.19e-85 |
|
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: 274.50 E-value: 4.19e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 331 LFIETAIFVDSDLYAHMqknfptnTESKVVSFLLAMINGVQLLYHHPTLGRRINFVLKRLEIWKSWdPPGLVRSRDVENY 410
Cdd:cd04273 1 RYVETLVVADSKMVEFH-------HGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDE-ESGLLISGNAQKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 411 LNSFCKWQEKLNPFSDADPLHYDHALVLTGLDLVTYDKgkaNSQVVGMATVKGMCTSIYSCTINEAKHFESVFVVAHEIG 490
Cdd:cd04273 73 LKSFCRWQKKLNPPNDSDPEHHDHAILLTRQDICRSNG---NCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 386768470 491 HNLGMRHDAKEISCDPT---MHIMSPKLGS--GKVTWSKCSRTYLEDFLMDPQAECLF 543
Cdd:cd04273 150 HVLGMPHDGDGNSCGPEgkdGHIMSPTLGAntGPFTWSKCSRRYLTSFLDTGDGNCLL 207
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
332-544 |
1.25e-37 |
|
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: 139.67 E-value: 1.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 332 FIETAIFVDSDLYAHMQKNfptntESKVVSFLLAMINGVQLLYHhpTLGrrINFVLKRLEIWKSWDPpgLVRSRDVENYL 411
Cdd:cd04269 2 YVELVVVVDNSLYKKYGSN-----LSKVRQRVIEIVNIVDSIYR--PLN--IRVVLVGLEIWTDKDK--ISVSGDAGETL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 412 NSFCKW-QEKLNPFsdadpLHYDHALVLTGLDLvtydkgkaNSQVVGMATVKGMCTSIYSCTINE--AKHFESV-FVVAH 487
Cdd:cd04269 71 NRFLDWkRSNLLPR-----KPHDNAQLLTGRDF--------DGNTVGLAYVGGMCSPKYSGGVVQdhSRNLLLFaVTMAH 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 386768470 488 EIGHNLGMRHDAKEISCDPTMHIMSPKLGSGKVTWSKCSRTYLEDFLMDPQAECLFD 544
Cdd:cd04269 138 ELGHNLGMEHDDGGCTCGRSTCIMAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
332-545 |
4.02e-29 |
|
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: 115.48 E-value: 4.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 332 FIETAIFVDSDLYAHMQKNfptntESKVVSFLLAMINGVQLLYhhptlgRRINF--VLKRLEIWKSWDPPGLvrSRDVEN 409
Cdd:pfam01421 2 YIELFIVVDKQLFQKMGSD-----TTVVRQRVFQVVNLVNSIY------KELNIrvVLVGLEIWTDEDKIDV--SGDAND 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 410 YLNSFCKW-QEKLNPFSDadplhYDHALVLTGLDLvtydkgkaNSQVVGMATVKGMCTSIYSCTINEAKHFESVFV---V 485
Cdd:pfam01421 69 TLRNFLKWrQEYLKKRKP-----HDVAQLLSGVEF--------GGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFavtM 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386768470 486 AHEIGHNLGMRHDAKEISCD-PTMH--IMSPKLG-SGKVTWSKCSRTYLEDFLMDPQAECLFDR 545
Cdd:pfam01421 136 AHELGHNLGMQHDDFNGGCKcPPGGgcIMNPSAGsSFPRKFSNCSQEDFEQFLTKQKGACLFNK 199
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
347-534 |
1.17e-25 |
|
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: 105.58 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 347 MQKNFPTNTESkVVSFLLAMINGVQLLYHHPTLGRRINFVLKRLEIWKSwDPPGLVRSRDVENYLNSFCKWQEKlnpfsd 426
Cdd:cd04267 13 MVSYFNSDENI-LQAYITELINIANSIYRSTNLRLGIRISLEGLQILKG-EQFAPPIDSDASNTLNSFSFWRAE------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 427 aDPLHYDHALVLTGLDLVtydkgkaNSQVVGMATVKGMCTSIYSCTINE--AKHFESVFVVAHEIGHNLGMRHD----AK 500
Cdd:cd04267 85 -GPIRHDNAVLLTAQDFI-------EGDILGLAYVGSMCNPYSSVGVVEdtGFTLLTALTMAHELGHNLGAEHDggdeLA 156
|
170 180 190
....*....|....*....|....*....|....*
gi 386768470 501 EISCDPTMHIMSPKLGS-GKVTWSKCSRTYLEDFL 534
Cdd:cd04267 157 FECDGGGNYIMAPVDSGlNSYRFSQCSIGSIREFL 191
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
331-542 |
9.69e-19 |
|
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.
Pssm-ID: 239800 Cd Length: 220 Bit Score: 86.25 E-value: 9.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 331 LFIETAIFVDSDLYAHMQKNfptnteSKVVSFLLAMINGVQLLYHHpTLGRRINFVLKRLEIWKSwDPPGLVRSRDVENY 410
Cdd:cd04272 1 VYPELFVVVDYDHQSEFFSN------EQLIRYLAVMVNAANLRYRD-LKSPRIRLLLVGITISKD-PDFEPYIHPINYGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 411 LNSFcKWQEKLNPF--SDADPLHYDHALVLTGLDLVTYDKGKANSQVVGMATVKGMCTSiYSCTINE--AKHFESVFVVA 486
Cdd:cd04272 73 IDAA-ETLENFNEYvkKKRDYFNPDVVFLVTGLDMSTYSGGSLQTGTGGYAYVGGACTE-NRVAMGEdtPGSYYGVYTMT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386768470 487 HEIGHNLGMRHDAKEISCDPTMH------------IMSPKLGSGK-VTWSKCSRTYLEDFLMDPQAECL 542
Cdd:cd04272 151 HELAHLLGAPHDGSPPPSWVKGHpgsldcpwddgyIMSYVVNGERqYRFSQCSQRQIRNVFRRLGASCL 219
|
|
| ADAMTS_CR_2 |
pfam17771 |
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ... |
561-625 |
1.51e-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: 75.07 E-value: 1.51e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386768470 561 PGERFNANQQCMLRFGKNFmQASTQSKMEICRDLHCRQDGLP---WTSHPALEGTECGPNMWCRGGTC 625
Cdd:pfam17771 1 PGQLYSADEQCRLIFGPGS-TFCPNGDEDVCSKLWCSNPGGStctTKNLPAADGTPCGNKKWCLNGKC 67
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
357-523 |
4.36e-12 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 66.29 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 357 SKVVSFLLAMINGVQLLYHHPTlgrRINFVLKRLEIWKSWDP--PGLVRSRDVENYLNSFckwqeklNPFSDADPLHYDH 434
Cdd:pfam13688 22 DAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCPytPPACSTGDSSDRLSEF-------QDFSAWRGTQNDD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 435 ALVLTgldLVTydkgkaNSQVVGMATVKGMCTSIYSCTINE--------AKHFESVFVVAHEIGHNLGMRHD----AKEI 502
Cdd:pfam13688 92 LAYLF---LMT------NCSGGGLAWLGQLCNSGSAGSVSTrvsgnnvvVSTATEWQVFAHEIGHNFGAVHDcdssTSSQ 162
|
170 180
....*....|....*....|....*....
gi 386768470 503 SCDPTMH--------IMSPKLGSGKVTWS 523
Cdd:pfam13688 163 CCPPSNStcpaggryIMNPSSSPNSTDFS 191
|
|
| ZnMc_TACE_like |
cd04270 |
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ... |
340-547 |
1.29e-07 |
|
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha converting enzyme, releases soluble TNF-alpha from transmembrane pro-TNF-alpha.
Pssm-ID: 239798 [Multi-domain] Cd Length: 244 Bit Score: 53.92 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 340 DSDLYAHMQKNfptnTESKVVSFLLAMINGVQLLYHH----PTLGRRINFVLKRLEIWkswDPPGLVRSRdveNYLNSFC 415
Cdd:cd04270 10 DHRFYKYMGRG----EEETTINYLISHIDRVDDIYRNtdwdGGGFKGIGFQIKRIRIH---TTPDEVDPG---NKFYNKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 416 -------KWQEKLN--PFSDADPLHYdhalVLTGLDlvtYDKGkansqVVGMA--------TVKGMCTSIY--------- 469
Cdd:cd04270 80 fpnwgveKFLVKLLleQFSDDVCLAH----LFTYRD---FDMG-----TLGLAyvgsprdnSAGGICEKAYyysngkkky 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 470 -----SCTINEAKHF---ESVFVVAHEIGHNLGMRHDAKEISCDPTM-----HIMSPKLGSG----KVTWSKCSRTYLED 532
Cdd:cd04270 148 lntglTTTVNYGKRVptkESDLVTAHELGHNFGSPHDPDIAECAPGEsqggnYIMYARATSGdkenNKKFSPCSKKSISK 227
|
250
....*....|....*
gi 386768470 533 FLMDPQAECLFDRDS 547
Cdd:cd04270 228 VLEVKSNSCFVERSQ 242
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
383-498 |
2.51e-07 |
|
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: 50.45 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 383 INFVLKRLEIWKSWDPPGLVRSRDvenylnsfckwqEKLNPFSDADPLHYDHAlvltGLDLVTYDKGKANSQVVGMATVK 462
Cdd:pfam13582 20 IRLQLAAIIITTSADTPYTSSDAL------------EILDELQEVNDTRIGQY----GYDLGHLFTGRDGGGGGGIAYVG 83
|
90 100 110
....*....|....*....|....*....|....*....
gi 386768470 463 GMCTSIYSCTINEAKH---FESVFVVAHEIGHNLGMRHD 498
Cdd:pfam13582 84 GVCNSGSKFGVNSGSGpvgDTGADTFAHEIGHNFGLNHT 122
|
|
| Reprolysin_2 |
pfam13574 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
359-534 |
9.04e-07 |
|
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: 50.71 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 359 VVSFLLAMINGVQLLYHHPTLGRRINFV-----LKRLEIWKSWDPPGLVRSRDVENyLNSFCKWQEKlnpfSDADPLHyd 433
Cdd:pfam13574 3 VTENLVNVVNRVNQIYEPDDININGGLVnpgeiPATTSASDSGNNYCNSPTTIVRR-LNFLSQWRGE----QDYCLAH-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 434 haLVLTGldlvTYDKGkansqVVGMATVKGMCTSIYSC---------TINEAKHFE---SVFVVAHEIGHNLGMRHD-AK 500
Cdd:pfam13574 76 --LVTMG----TFSGG-----ELGLAYVGQICQKGASSpktntglstTTNYGSFNYptqEWDVVAHEVGHNFGATHDcDG 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 386768470 501 EISCDPTMH--------------IMSPKLGSGKVTWSKCSRTYLEDFL 534
Cdd:pfam13574 145 SQYASSGCErnaatsvcsangsfIMNPASKSNNDLFSPCSISLICDVL 192
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
456-534 |
1.11e-05 |
|
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: 46.75 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768470 456 VGMATVKGMCTSIYSCTI---NEAKHFESVFVVAHEIGHNLGMRHD--AKEISCDPTM------------HIMSPKLGSG 518
Cdd:cd00203 68 GGWAYLGRVCDSLRGVGVlqdNQSGTKEGAQTIAHELGHALGFYHDhdRKDRDDYPTIddtlnaedddyySVMSYTKGSF 147
|
90 100
....*....|....*....|
gi 386768470 519 KVT----WSKCSRTYLEDFL 534
Cdd:cd00203 148 SDGqrkdFSQCDIDQINKLY 167
|
|
| ZnMc_MMP_like_2 |
cd04276 |
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ... |
484-523 |
5.05e-03 |
|
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase domains similar to matrix metalloproteinases and astacin.
Pssm-ID: 239803 Cd Length: 197 Bit Score: 39.62 E-value: 5.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 386768470 484 VVAHEIGHNLGMRHDAKEISCDPTMHIMSPKLGSGKVTWS 523
Cdd:cd04276 119 LLAHEVGHTLGLRHNFKASSDGSNEELEDPLGTKEKGATS 158
|
|
| TSP1 |
smart00209 |
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta. |
683-741 |
6.82e-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: 36.03 E-value: 6.82e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386768470 683 WGEWSEPSACESGClygqsrrllegSTGLRTLNRSCLNFP-----SRCIGRDRRFVTCNTPQCH 741
Cdd:smart00209 1 WSEWSEWSPCSVTC-----------GGGVQTRTRSCCSPPpqnggGPCTGEDVETRACNEQPCP 53
|
|
| |
