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Conserved domains on  [gi|1034589927|ref|XP_016877473|]
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A disintegrin and metalloproteinase with thrombospondin motifs 17 isoform X13 [Homo sapiens]

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) ...
 1-206 1.61e-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: 262.17  E-value: 1.61e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589927   1 MVQYHGAEAAQRFILTVMNMVYNMFQHQSLGIKINIQVTKLVLLRQRPAKLSIGHHGERSLESFCHWQNEeyggarylgn 80
Cdd:cd04273    13 MVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQKK---------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589927  81 nQVPGGKDDPPLVDAAVFVTRTDFCvHKDEPCDTVGIAYLGGVCSAKRKCVLAEDNGLNLAFTIAHELGHNLGMNHDDDH 160
Cdd:cd04273    83 -LNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034589927 161 SSCAGRS---HIMSGEWvkGRNPSDLSWSSCSRDDLENFLKSKVSTCLL 206
Cdd:cd04273   161 NSCGPEGkdgHIMSPTL--GANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 223-290 2.47e-25

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: 98.57  E-value: 2.47e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034589927 223 PGMHYSANEQCQILFGMNATFCRNMEHLMCAGLWCLVEGDTSCKTKLDPPLDGTECGADKWCRAGECV 290
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDEDVCSKLWCSNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 303-355 6.84e-17

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: 74.55  E-value: 6.84e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034589927  303 WSPWGAWSMCSRTCGTGARFRQRKCDNPPPGPGGTHCPGASVEHAVCENLPCP 355
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 387-456 2.03e-09

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: 55.10  E-value: 2.03e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034589927 387 DKPCELYCSPLGKESPLLVADRVLDGT---PCGPYET---DLCVHGKCQKIGCDGIIGSAAKEDRCGVCSGDGKTC 456
Cdd:pfam19236  40 DALCRHMCRAIGESFIMKRGDSFLDGTrcmPSGPREDgtlSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
ADAMTS_spacer1 super family cl20316
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 458-496 3.77e-07

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.


The actual alignment was detected with superfamily member pfam05986:

Pssm-ID: 461796  Cd Length: 115  Bit Score: 48.73  E-value: 3.77e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1034589927 458 LVKGDFSHARGTGYIEAAVIPAGARRIRVVEDKPAHSFL 496
Cdd:pfam05986   1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHL 39
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 1-206 1.61e-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: 262.17  E-value: 1.61e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589927   1 MVQYHGAEAAQRFILTVMNMVYNMFQHQSLGIKINIQVTKLVLLRQRPAKLSIGHHGERSLESFCHWQNEeyggarylgn 80
Cdd:cd04273    13 MVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQKK---------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589927  81 nQVPGGKDDPPLVDAAVFVTRTDFCvHKDEPCDTVGIAYLGGVCSAKRKCVLAEDNGLNLAFTIAHELGHNLGMNHDDDH 160
Cdd:cd04273    83 -LNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034589927 161 SSCAGRS---HIMSGEWvkGRNPSDLSWSSCSRDDLENFLKSKVSTCLL 206
Cdd:cd04273   161 NSCGPEGkdgHIMSPTL--GANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 223-290 2.47e-25

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: 98.57  E-value: 2.47e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034589927 223 PGMHYSANEQCQILFGMNATFCRNMEHLMCAGLWCLVEGDTSCKTKLDPPLDGTECGADKWCRAGECV 290
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDEDVCSKLWCSNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 1-206 2.69e-20

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: 88.90  E-value: 2.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589927   1 MVQYHGA--EAAQRFILTVMNMVYNMFQhqslgiKINIQVTkLVLLR--QRPAKLSIGHHGERSLESFCHWQneeyggAR 76
Cdd:pfam01421  13 LFQKMGSdtTVVRQRVFQVVNLVNSIYK------ELNIRVV-LVGLEiwTDEDKIDVSGDANDTLRNFLKWR------QE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589927  77 YLGNnqvpggkddPPLVDAAVFVTRTDFcvhkdePCDTVGIAYLGGVCSAKRKCVLAEDNGLN---LAFTIAHELGHNLG 153
Cdd:pfam01421  80 YLKK---------RKPHDVAQLLSGVEF------GGTTVGAAYVGGMCSLEYSGGVNEDHSKNlesFAVTMAHELGHNLG 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034589927 154 MNHDDDHSSC---AGRSHIMSGEWVKgrnPSDLSWSSCSRDDLENFLKSKVSTCLL 206
Cdd:pfam01421 145 MQHDDFNGGCkcpPGGGCIMNPSAGS---SFPRKFSNCSQEDFEQFLTKQKGACLF 197
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 303-355 6.84e-17

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: 74.55  E-value: 6.84e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034589927  303 WSPWGAWSMCSRTCGTGARFRQRKCDNPPPGPGGTHCPGASVEHAVCENLPCP 355
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
304-354 2.37e-10

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 55.89  E-value: 2.37e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034589927 304 SPWGAWSMCSRTCGTGARFRQRKCDNPPpgPGGTHCPGASVEHAVCENLPC 354
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPF--PGGEPCTGDDIETQACKMDKC 49
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 387-456 2.03e-09

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: 55.10  E-value: 2.03e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034589927 387 DKPCELYCSPLGKESPLLVADRVLDGT---PCGPYET---DLCVHGKCQKIGCDGIIGSAAKEDRCGVCSGDGKTC 456
Cdd:pfam19236  40 DALCRHMCRAIGESFIMKRGDSFLDGTrcmPSGPREDgtlSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 458-496 3.77e-07

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: 48.73  E-value: 3.77e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1034589927 458 LVKGDFSHARGTGYIEAAVIPAGARRIRVVEDKPAHSFL 496
Cdd:pfam05986   1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHL 39
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 1-206 1.61e-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: 262.17  E-value: 1.61e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589927   1 MVQYHGAEAAQRFILTVMNMVYNMFQHQSLGIKINIQVTKLVLLRQRPAKLSIGHHGERSLESFCHWQNEeyggarylgn 80
Cdd:cd04273    13 MVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQKK---------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589927  81 nQVPGGKDDPPLVDAAVFVTRTDFCvHKDEPCDTVGIAYLGGVCSAKRKCVLAEDNGLNLAFTIAHELGHNLGMNHDDDH 160
Cdd:cd04273    83 -LNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGDG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034589927 161 SSCAGRS---HIMSGEWvkGRNPSDLSWSSCSRDDLENFLKSKVSTCLL 206
Cdd:cd04273   161 NSCGPEGkdgHIMSPTL--GANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 1-206 2.45e-29

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


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 113.86  E-value: 2.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589927   1 MVQYHG--AEAAQRFILTVMNMVYNMFQhqslgiKINIQVTkLVLL-----RQrpaKLSIGHHGERSLESFCHWQNeeyg 73
Cdd:cd04269    13 LYKKYGsnLSKVRQRVIEIVNIVDSIYR------PLNIRVV-LVGLeiwtdKD---KISVSGDAGETLNRFLDWKR---- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589927  74 gaRYLGNNQVPggkddpplvDAAVFVTRTDFCVHkdepcdTVGIAYLGGVCSAKRKCVLAED---NGLNLAFTIAHELGH 150
Cdd:cd04269    79 --SNLLPRKPH---------DNAQLLTGRDFDGN------TVGLAYVGGMCSPKYSGGVVQDhsrNLLLFAVTMAHELGH 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034589927 151 NLGMNHDDDHSSCAGRSHIMSgewvkgRNPSDLS--WSSCSRDDLENFLKSKVSTCLL 206
Cdd:cd04269   142 NLGMEHDDGGCTCGRSTCIMA------PSPSSLTdaFSNCSYEDYQKFLSRGGGQCLL 193
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 223-290 2.47e-25

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: 98.57  E-value: 2.47e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034589927 223 PGMHYSANEQCQILFGMNATFCRNMEHLMCAGLWCLVEGDTSCKTKLDPPLDGTECGADKWCRAGECV 290
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDEDVCSKLWCSNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 8-198 6.73e-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: 101.73  E-value: 6.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589927   8 EAAQRFILTVMNMVYNMFQHQSLGIKINIQVTKLVLLRQRPAKLSIGHHGERSLESFCHWQNEEyggarylgnnqvpggk 87
Cdd:cd04267    22 NILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFWRAEG---------------- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589927  88 ddPPLVDAAVFVTRTDFcvhkdEPCDTVGIAYLGGVCSAKRKCVLAEDNGLNL--AFTIAHELGHNLGMNHDDD----HS 161
Cdd:cd04267    86 --PIRHDNAVLLTAQDF-----IEGDILGLAYVGSMCNPYSSVGVVEDTGFTLltALTMAHELGHNLGAEHDGGdelaFE 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1034589927 162 SCAGRSHIMSGEWVKGRNpsdLSWSSCSRDDLENFLK 198
Cdd:cd04267   159 CDGGGNYIMAPVDSGLNS---YRFSQCSIGSIREFLD 192
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 1-206 2.69e-20

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: 88.90  E-value: 2.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589927   1 MVQYHGA--EAAQRFILTVMNMVYNMFQhqslgiKINIQVTkLVLLR--QRPAKLSIGHHGERSLESFCHWQneeyggAR 76
Cdd:pfam01421  13 LFQKMGSdtTVVRQRVFQVVNLVNSIYK------ELNIRVV-LVGLEiwTDEDKIDVSGDANDTLRNFLKWR------QE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589927  77 YLGNnqvpggkddPPLVDAAVFVTRTDFcvhkdePCDTVGIAYLGGVCSAKRKCVLAEDNGLN---LAFTIAHELGHNLG 153
Cdd:pfam01421  80 YLKK---------RKPHDVAQLLSGVEF------GGTTVGAAYVGGMCSLEYSGGVNEDHSKNlesFAVTMAHELGHNLG 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034589927 154 MNHDDDHSSC---AGRSHIMSGEWVKgrnPSDLSWSSCSRDDLENFLKSKVSTCLL 206
Cdd:pfam01421 145 MQHDDFNGGCkcpPGGGCIMNPSAGS---SFPRKFSNCSQEDFEQFLTKQKGACLF 197
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 303-355 6.84e-17

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: 74.55  E-value: 6.84e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034589927  303 WSPWGAWSMCSRTCGTGARFRQRKCDNPPPGPGGTHCPGASVEHAVCENLPCP 355
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 86-205 2.57e-16

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 77.78  E-value: 2.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589927  86 GKDDPPLVDAAVFVTRTDFCVHKDEPCDTV--GIAYLGGVCSaKRKCVLAEDNG--LNLAFTIAHELGHNLGMNHDDDH- 160
Cdd:cd04272    88 KKRDYFNPDVVFLVTGLDMSTYSGGSLQTGtgGYAYVGGACT-ENRVAMGEDTPgsYYGVYTMTHELAHLLGAPHDGSPp 166

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034589927 161 -SSCAGRS----------HIMSgeWVKGrNPSDLSWSSCSRDDLENFLKSKVSTCL 205
Cdd:cd04272   167 pSWVKGHPgsldcpwddgYIMS--YVVN-GERQYRFSQCSQRQIRNVFRRLGASCL 219
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 94-197 3.48e-16

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: 76.02  E-value: 3.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589927  94 DAAVFVTRTDFcvhkdePCDTVGIAYLGGVCSAKRKCVLAEDNGLN---LAFTIAHELGHNLGMNHDDDHSSCA------ 164
Cdd:cd00203    53 DIAILVTRQDF------DGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDRKDRDdyptid 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1034589927 165 --------GRSHIMSGEWVKGRNPSDLSWSSCSRDDLENFL 197
Cdd:cd00203   127 dtlnaeddDYYSVMSYTKGSFSDGQRKDFSQCDIDQINKLY 167
TSP_1 pfam00090
Thrombospondin type 1 domain;
304-354 2.37e-10

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 55.89  E-value: 2.37e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034589927 304 SPWGAWSMCSRTCGTGARFRQRKCDNPPpgPGGTHCPGASVEHAVCENLPC 354
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPF--PGGEPCTGDDIETQACKMDKC 49
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 14-157 6.51e-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: 56.99  E-value: 6.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589927  14 ILTVMNMVYNMFQHQsLGIKINIQVTKLVLLRQRPaklSIGHHGERSLESFCHWQNEEYGGARYlgnnqvpggkddpplv 93
Cdd:pfam13582   3 IVSLVNRANTIYERD-LGIRLQLAAIIITTSADTP---YTSSDALEILDELQEVNDTRIGQYGY---------------- 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034589927  94 DAAVFVTRTDFCvhkdepcDTVGIAYLGGVCSAKRKCVLAED---NGLNLAFTIAHELGHNLGMNHD 157
Cdd:pfam13582  63 DLGHLFTGRDGG-------GGGGIAYVGGVCNSGSKFGVNSGsgpVGDTGADTFAHEIGHNFGLNHT 122
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 387-456 2.03e-09

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: 55.10  E-value: 2.03e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034589927 387 DKPCELYCSPLGKESPLLVADRVLDGT---PCGPYET---DLCVHGKCQKIGCDGIIGSAAKEDRCGVCSGDGKTC 456
Cdd:pfam19236  40 DALCRHMCRAIGESFIMKRGDSFLDGTrcmPSGPREDgtlSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 9-167 2.56e-09

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: 56.87  E-value: 2.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589927   9 AAQRFILTVMNMVYNMFQHQSLGIKINIQVTKLVLLRQrPAKLSighhgerslesfchWQNEEYGGARYLGNN----QVP 84
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEPDDININGGLVNPGEIPATT-SASDS--------------GNNYCNSPTTIVRRLnflsQWR 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589927  85 GGKDDpplvDAAVFVTRTDFCVhkdepcDTVGIAYLGGVCSAKRKCVlAEDNGLNLAFT-------------IAHELGHN 151
Cdd:pfam13574  67 GEQDY----CLAHLVTMGTFSG------GELGLAYVGQICQKGASSP-KTNTGLSTTTNygsfnyptqewdvVAHEVGHN 135

                         170
                  ....*....|....*.
gi 1034589927 152 LGMNHDDDHSSCAGRS 167
Cdd:pfam13574 136 FGATHDCDGSQYASSG 151
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 304-354 8.19e-09

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: 51.51  E-value: 8.19e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034589927 304 SPWGAWSMCSRTCGTGARFRQRKCDNPPPGpGGTHCPgASVEHAVCENLPC 354
Cdd:pfam19028   4 SEWSEWSECSVTCGGGVQTRTRTVIVEPQN-GGRPCP-ELLERRPCNLPPC 52
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
2-162 1.02e-08

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 55.12  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589927   2 VQYHGAEAAQRFILTVMNMVYNMFQHqslgiKINIQVtklvllrqRPAKLSIGHHGERSLESFCHWQN-----EEYGGAR 76
Cdd:pfam13688  16 VAAFGGDAAQANIINMVNTASNVYER-----DFNISL--------GLVNLTISDSTCPYTPPACSTGDssdrlSEFQDFS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589927  77 YLGNNQvpggKDDpplvdaAVFVTRtdfcvhkDEPCDTVGIAYLGGVCSAKRKCVLAEDNGLN--------LAFTIAHEL 148
Cdd:pfam13688  83 AWRGTQ----NDD------LAYLFL-------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQVFAHEI 145

                         170
                  ....*....|....
gi 1034589927 149 GHNLGMNHDDDHSS 162
Cdd:pfam13688 146 GHNFGAVHDCDSST 159
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 143-204 1.75e-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: 52.38  E-value: 1.75e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034589927 143 TIAHELGHNLGMNHDDDHSSCA-----GRSHIMSGEWVKGRNPSDLSWSSCSRDDLENFLKSKVSTC 204
Cdd:cd04270   170 VTAHELGHNFGSPHDPDIAECApgesqGGNYIMYARATSGDKENNKKFSPCSKKSISKVLEVKSNSC 236
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 458-496 3.77e-07

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: 48.73  E-value: 3.77e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1034589927 458 LVKGDFSHARGTGYIEAAVIPAGARRIRVVEDKPAHSFL 496
Cdd:pfam05986   1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHL 39
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 90-190 9.58e-04

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


Pssm-ID: 213029  Cd Length: 173  Bit Score: 39.97  E-value: 9.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034589927  90 PPLVDAAVFVTRTDFCVHKDEPCdtVGIAYLG---GVCSAKR----KCVLAEDNGLNL---AFTIAHELGHNLGMNHddd 159
Cdd:cd11375    65 PPDADCVLGVTDVDLYEPGLNFV--FGLADGGsgvAVVSTARlrpeFYGLPPDEGLFLerlLKEAVHELGHLFGLDH--- 139

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034589927 160 hssCAGRSHIMSG-----EWVkgRNPSDLsWSSCSR 190
Cdd:cd11375   140 ---CPYYACVMNFsnsleETD--RKPPYL-CPVCLR 169
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 115-163 2.13e-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: 2.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034589927 115 VGIAYLGGVCSAKRKCvlAEDNGLNLAF----TIAHELGHNLGMNHDDDHSSC 163
Cdd:pfam13583 108 VGVAWVGALCSSARQN--AKASGVARSRdewdIFAHEIGHTFGAVHDCSSQGE 158
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 114-164 3.38e-03

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: 38.94  E-value: 3.38e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034589927 114 TVGIAYLGGVC----SAKRKCVLAEDNGLNLAFT----IAHELGHNLGMNHDDDHSSCA 164
Cdd:cd04271   111 EVGVAWLGQLCrtgaSDQGNETVAGTNVVVRTSNewqvFAHEIGHTFGAVHDCTSGTCS 169
 
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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