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Conserved domains on  [gi|1958644989|ref|XP_038966002|]
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A disintegrin and metalloproteinase with thrombospondin motifs 16 isoform X2 [Rattus norvegicus]

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) ...
 287-488 2.62e-104

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: 323.42  E-value: 2.62e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 287 LNVETLVVVDRKMLQSHGHENITTYVLTILNMVSALFKDGTIGGNINIVIVGLILLEDEQPGLAISHHADRTLTSFCQWQ 366
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 367 SGLMGKDGA---RHDHAILLTGLDICSWkNEPCDTLGFAPISGMCSKYRSCTVNEDSGLGLAFTIAHESGHNFGMVHDGE 443
Cdd:cd04273    81 KKLNPPNDSdpeHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958644989 444 GNMCKKS--EGNIMSPTLAGRNGVFSWSSCSRQYLHKFLSTAQAICL 488
Cdd:cd04273   160 GNSCGPEgkDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 745-855 3.08e-38

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: 138.48  E-value: 3.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 745 HRGLYSKNHpTNQYYHVVTIPSGARSIHIYETNISTSYISVRNSVKKYYLNGHWSVD-WPGRYKFSGTTFNYRRSYKEPE 823
Cdd:pfam05986   2 VSGSFTEGR-AKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPALE 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958644989 824 SLTSTGPTNETLIVELLFQ---GRNPGVAWEFSVP 855
Cdd:pfam05986  81 ELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFIP 115
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 74-202 1.45e-34

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


:

Pssm-ID: 460254  Cd Length: 128  Bit Score: 128.20  E-value: 1.45e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989  74 DIMHHQR----RRRRAVT--QSKGDALHLRLKGPRHDLHLDLKAASNLMAPGFMVQTLGKGGTKSVQMFPAEENCFYQGS 147
Cdd:pfam01562   1 EVVIPVRldpsRRRRSLAseSTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958644989 148 LRSQGNSSVALSTCQGLLGMIRTKDADYFLKPLPPQltsklnrSAQGGSPSHILY 202
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKY-------SREEGGHPHVVY 128
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 505-572 1.04e-19

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: 83.93  E-value: 1.04e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644989 505 PGQLYDANTQCKWQFGEKAKLCmLDFRKDICKALWCHRIGRK-CETKFMPAAEGTLCGQDMWCRGGQCV 572
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFC-PNGDEDVCSKLWCSNPGGStCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 586-638 2.21e-18

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: 79.55  E-value: 2.21e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958644989  586 WSDWSPWSPCSRTCGGGVSHRDRLCTNPRPSHGGKFCQGSARTLKLCNSQKCP 638
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 ...
 644-742 2.22e-08

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: 53.17  E-value: 2.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 644 FRAAQCAEYNSKRFR-----GWLYKW---TPYTQveDQDLCKLYCIAEGFDFFFSLSNKVKDGTPC------SEDSRNVC 709
Cdd:pfam19236   5 FMSQQCARTDGQPLRsspggASFYHWgaaVPHSQ--GDALCRHMCRAIGESFIMKRGDSFLDGTRCmpsgprEDGTLSLC 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958644989 710 IDGMCEKVGCDNVLGSDATEDSCGVCQGNNSDC 742
Cdd:pfam19236  83 VLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 876-924 1.74e-03

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


The actual alignment was detected with superfamily member pfam19030:

Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 37.43  E-value: 1.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958644989 876 SECSVSCGGGKMSSKAGCYRDL-KVLVNASFCNPKTRPvPALVPCKVSAC 924
Cdd:pfam19030   7 GECSVTCGGGVQTRLVQCVQKGgGSIVPDSECSAQKKP-PETQSCNLKPC 55
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 287-488 2.62e-104

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: 323.42  E-value: 2.62e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 287 LNVETLVVVDRKMLQSHGHENITTYVLTILNMVSALFKDGTIGGNINIVIVGLILLEDEQPGLAISHHADRTLTSFCQWQ 366
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 367 SGLMGKDGA---RHDHAILLTGLDICSWkNEPCDTLGFAPISGMCSKYRSCTVNEDSGLGLAFTIAHESGHNFGMVHDGE 443
Cdd:cd04273    81 KKLNPPNDSdpeHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958644989 444 GNMCKKS--EGNIMSPTLAGRNGVFSWSSCSRQYLHKFLSTAQAICL 488
Cdd:cd04273   160 GNSCGPEgkDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 745-855 3.08e-38

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: 138.48  E-value: 3.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 745 HRGLYSKNHpTNQYYHVVTIPSGARSIHIYETNISTSYISVRNSVKKYYLNGHWSVD-WPGRYKFSGTTFNYRRSYKEPE 823
Cdd:pfam05986   2 VSGSFTEGR-AKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPALE 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958644989 824 SLTSTGPTNETLIVELLFQ---GRNPGVAWEFSVP 855
Cdd:pfam05986  81 ELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFIP 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 289-492 2.67e-35

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: 133.19  E-value: 2.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 289 VETLVVVDRKMLQSHG--HENITTYVLTILNMVSALFKdgtiGGNINIVIVGLILLEDEQPgLAISHHADRTLTSFCQW- 365
Cdd:pfam01421   3 IELFIVVDKQLFQKMGsdTTVVRQRVFQVVNLVNSIYK----ELNIRVVLVGLEIWTDEDK-IDVSGDANDTLRNFLKWr 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 366 QSGLMGKdgARHDHAILLTGldicswKNEPCDTLGFAPISGMCSKYRSCTVNED---SGLGLAFTIAHESGHNFGMVHDG 442
Cdd:pfam01421  78 QEYLKKR--KPHDVAQLLSG------VEFGGTTVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQHDD 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958644989 443 EGNMCK--KSEGNIMSPTlAGRNGVFSWSSCSRQYLHKFLSTAQAICLADQP 492
Cdd:pfam01421 150 FNGGCKcpPGGGCIMNPS-AGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 74-202 1.45e-34

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


Pssm-ID: 460254  Cd Length: 128  Bit Score: 128.20  E-value: 1.45e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989  74 DIMHHQR----RRRRAVT--QSKGDALHLRLKGPRHDLHLDLKAASNLMAPGFMVQTLGKGGTKSVQMFPAEENCFYQGS 147
Cdd:pfam01562   1 EVVIPVRldpsRRRRSLAseSTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958644989 148 LRSQGNSSVALSTCQGLLGMIRTKDADYFLKPLPPQltsklnrSAQGGSPSHILY 202
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKY-------SREEGGHPHVVY 128
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 505-572 1.04e-19

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: 83.93  E-value: 1.04e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644989 505 PGQLYDANTQCKWQFGEKAKLCmLDFRKDICKALWCHRIGRK-CETKFMPAAEGTLCGQDMWCRGGQCV 572
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFC-PNGDEDVCSKLWCSNPGGStCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 586-638 2.21e-18

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: 79.55  E-value: 2.21e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958644989  586 WSDWSPWSPCSRTCGGGVSHRDRLCTNPRPSHGGKFCQGSARTLKLCNSQKCP 638
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
587-637 1.23e-11

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 60.12  E-value: 1.23e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958644989 587 SDWSPWSPCSRTCGGGVSHRDRLCTNPRPshGGKFCQGSARTLKLCNSQKC 637
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 644-742 2.22e-08

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: 53.17  E-value: 2.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 644 FRAAQCAEYNSKRFR-----GWLYKW---TPYTQveDQDLCKLYCIAEGFDFFFSLSNKVKDGTPC------SEDSRNVC 709
Cdd:pfam19236   5 FMSQQCARTDGQPLRsspggASFYHWgaaVPHSQ--GDALCRHMCRAIGESFIMKRGDSFLDGTRCmpsgprEDGTLSLC 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958644989 710 IDGMCEKVGCDNVLGSDATEDSCGVCQGNNSDC 742
Cdd:pfam19236  83 VLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 876-924 1.74e-03

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: 37.43  E-value: 1.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958644989 876 SECSVSCGGGKMSSKAGCYRDL-KVLVNASFCNPKTRPvPALVPCKVSAC 924
Cdd:pfam19030   7 GECSVTCGGGVQTRLVQCVQKGgGSIVPDSECSAQKKP-PETQSCNLKPC 55
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 287-488 2.62e-104

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: 323.42  E-value: 2.62e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 287 LNVETLVVVDRKMLQSHGHENITTYVLTILNMVSALFKDGTIGGNINIVIVGLILLEDEQPGLAISHHADRTLTSFCQWQ 366
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 367 SGLMGKDGA---RHDHAILLTGLDICSWkNEPCDTLGFAPISGMCSKYRSCTVNEDSGLGLAFTIAHESGHNFGMVHDGE 443
Cdd:cd04273    81 KKLNPPNDSdpeHHDHAILLTRQDICRS-NGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958644989 444 GNMCKKS--EGNIMSPTLAGRNGVFSWSSCSRQYLHKFLSTAQAICL 488
Cdd:cd04273   160 GNSCGPEgkDGHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCL 206
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 289-481 4.96e-41

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: 149.49  E-value: 4.96e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 289 VETLVVVDRKM-LQSHGHENITT-YVLTILNMVSALFKDGTIGGNINIVIVGLILLEDEQPGLAISHHADRTLTSFCQWQ 366
Cdd:cd04267     3 IELVVVADHRMvSYFNSDENILQaYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFWR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 367 SglmgKDGARHDHAILLTGLDICSwknepCDTLGFAPISGMCSKYRSCTVNEDSGLGL--AFTIAHESGHNFGMVHDGEG 444
Cdd:cd04267    83 A----EGPIRHDNAVLLTAQDFIE-----GDILGLAYVGSMCNPYSSVGVVEDTGFTLltALTMAHELGHNLGAEHDGGD 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958644989 445 ---NMCKKSEGNIMSPTLAGRNGVFsWSSCSRQYLHKFLS 481
Cdd:cd04267   154 elaFECDGGGNYIMAPVDSGLNSYR-FSQCSIGSIREFLD 192
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 745-855 3.08e-38

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: 138.48  E-value: 3.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 745 HRGLYSKNHpTNQYYHVVTIPSGARSIHIYETNISTSYISVRNSVKKYYLNGHWSVD-WPGRYKFSGTTFNYRRSYKEPE 823
Cdd:pfam05986   2 VSGSFTEGR-AKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPALE 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958644989 824 SLTSTGPTNETLIVELLFQ---GRNPGVAWEFSVP 855
Cdd:pfam05986  81 ELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFIP 115
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 288-488 8.58e-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: 137.36  E-value: 8.58e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 288 NVETLVVVDRKMLQSHGH--ENITTYVLTILNMVSALFKdgTIggNINIVIVGLILLEDEQPgLAISHHADRTLTSFCQW 365
Cdd:cd04269     2 YVELVVVVDNSLYKKYGSnlSKVRQRVIEIVNIVDSIYR--PL--NIRVVLVGLEIWTDKDK-ISVSGDAGETLNRFLDW 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 366 QSGLMGKdGARHDHAILLTGLDICSwknepcDTLGFAPISGMCSKYRSCTVNEDSG---LGLAFTIAHESGHNFGMVHDG 442
Cdd:cd04269    77 KRSNLLP-RKPHDNAQLLTGRDFDG------NTVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLGMEHDD 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958644989 443 EGnmCKKSEGN-IMSPTLAgrNGVFSWSSCSRQYLHKFLSTAQAICL 488
Cdd:cd04269   150 GG--CTCGRSTcIMAPSPS--SLTDAFSNCSYEDYQKFLSRGGGQCL 192
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 289-492 2.67e-35

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: 133.19  E-value: 2.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 289 VETLVVVDRKMLQSHG--HENITTYVLTILNMVSALFKdgtiGGNINIVIVGLILLEDEQPgLAISHHADRTLTSFCQW- 365
Cdd:pfam01421   3 IELFIVVDKQLFQKMGsdTTVVRQRVFQVVNLVNSIYK----ELNIRVVLVGLEIWTDEDK-IDVSGDANDTLRNFLKWr 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 366 QSGLMGKdgARHDHAILLTGldicswKNEPCDTLGFAPISGMCSKYRSCTVNED---SGLGLAFTIAHESGHNFGMVHDG 442
Cdd:pfam01421  78 QEYLKKR--KPHDVAQLLSG------VEFGGTTVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHNLGMQHDD 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958644989 443 EGNMCK--KSEGNIMSPTlAGRNGVFSWSSCSRQYLHKFLSTAQAICLADQP 492
Cdd:pfam01421 150 FNGGCKcpPGGGCIMNPS-AGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 74-202 1.45e-34

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


Pssm-ID: 460254  Cd Length: 128  Bit Score: 128.20  E-value: 1.45e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989  74 DIMHHQR----RRRRAVT--QSKGDALHLRLKGPRHDLHLDLKAASNLMAPGFMVQTLGKGGTKSVQMFPAEENCFYQGS 147
Cdd:pfam01562   1 EVVIPVRldpsRRRRSLAseSTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958644989 148 LRSQGNSSVALSTCQGLLGMIRTKDADYFLKPLPPQltsklnrSAQGGSPSHILY 202
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKY-------SREEGGHPHVVY 128
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 505-572 1.04e-19

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: 83.93  E-value: 1.04e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644989 505 PGQLYDANTQCKWQFGEKAKLCmLDFRKDICKALWCHRIGRK-CETKFMPAAEGTLCGQDMWCRGGQCV 572
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFC-PNGDEDVCSKLWCSNPGGStCTTKNLPAADGTPCGNKKWCLNGKCV 68
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 287-488 1.44e-19

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 88.56  E-value: 1.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 287 LNVETLVVVDRKmLQSHG--HENITTYVLTILNMVSALFKDgTIGGNINIVIVGLILLEDEQPGLAISHHADR------T 358
Cdd:cd04272     1 VYPELFVVVDYD-HQSEFfsNEQLIRYLAVMVNAANLRYRD-LKSPRIRLLLVGITISKDPDFEPYIHPINYGyidaaeT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 359 LTSFCQWQSGlmGKDGARHDHAILLTGLDICSWKNEPCDT--LGFAPISGMCSKYRSCTVnEDSG--LGLAFTIAHESGH 434
Cdd:cd04272    79 LENFNEYVKK--KRDYFNPDVVFLVTGLDMSTYSGGSLQTgtGGYAYVGGACTENRVAMG-EDTPgsYYGVYTMTHELAH 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958644989 435 NFGMVHDGEG-----------NMCKKSEGNIMSPTLAGRNGvFSWSSCSRQYLHKFLSTAQAICL 488
Cdd:cd04272   156 LLGAPHDGSPppswvkghpgsLDCPWDDGYIMSYVVNGERQ-YRFSQCSQRQIRNVFRRLGASCL 219
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 586-638 2.21e-18

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: 79.55  E-value: 2.21e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958644989  586 WSDWSPWSPCSRTCGGGVSHRDRLCTNPRPSHGGKFCQGSARTLKLCNSQKCP 638
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 371-480 4.41e-13

Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 68.32  E-value: 4.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 371 GKDGARHDHAILLTGLDIcswknePCDTLGFAPISGMCSKYRSCTVNEDSGLG---LAFTIAHESGHNFGMVHDGEGNMC 447
Cdd:cd00203    46 GVEIDKADIAILVTRQDF------DGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDRKDR 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958644989 448 KK-------------SEGNIMSPTLAGRNGVFS--WSSCSRQYLHKFL 480
Cdd:cd00203   120 DDyptiddtlnaeddDYYSVMSYTKGSFSDGQRkdFSQCDIDQINKLY 167
TSP_1 pfam00090
Thrombospondin type 1 domain;
587-637 1.23e-11

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 60.12  E-value: 1.23e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958644989 587 SDWSPWSPCSRTCGGGVSHRDRLCTNPRPshGGKFCQGSARTLKLCNSQKC 637
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 587-637 4.66e-10

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: 55.75  E-value: 4.66e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958644989 587 SDWSPWSPCSRTCGGGVSHRDRLCTNPrPSHGGKFCQGSARTLKlCNSQKC 637
Cdd:pfam19028   4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELLERRP-CNLPPC 52
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 307-473 8.92e-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: 372637  Cd Length: 193  Bit Score: 59.18  E-value: 8.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 307 NITTYVLTILNMVSALFKDGTIggNINIVIVGLILLEDEQPGLAiSHHAD--------RTLTSFCQWQsglmgkdGARHD 378
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEPDDI--NINGGLVNPGEIPATTSASD-SGNNYcnspttivRRLNFLSQWR-------GEQDY 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 379 HAILLTGLDICSwknEPcdTLGFAPISGMCSKYRSCtVNEDSGLGLAFT-------------IAHESGHNFGMVHD--GE 443
Cdd:pfam13574  72 CLAHLVTMGTFS---GG--ELGLAYVGQICQKGASS-PKTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDcdGS 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958644989 444 GNMCKKSEGN------------IMSPTlaGRNGVFSWSSCSR 473
Cdd:pfam13574 146 QYASSGCERNaatsvcsangsfIMNPA--SKSNNDLFSPCSI 185
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
292-467 1.25e-09

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 58.58  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 292 LVVVDRKMLQSHGHENITTYVLTILNMVSALFKDGTiggNINIVIVGLILLEDEQPGLAISHHADR---TLTSFcQWQSG 368
Cdd:pfam13688   8 LVAADCSYVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCPYTPPACSTGDssdRLSEF-QDFSA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 369 LMGKDgaRHDHAILLTgldicswkNEPCDTLGFAPISGMCSKYRSCTVNEDSG--------LGLAFTIAHESGHNFGMVH 440
Cdd:pfam13688  84 WRGTQ--NDDLAYLFL--------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSgnnvvvstATEWQVFAHEIGHNFGAVH 153

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958644989 441 DGEGNM-----------CKKSEGNIMSPTLAGRNGVFS 467
Cdd:pfam13688 154 DCDSSTssqccppsnstCPAGGRYIMNPSSSPNSTDFS 191
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 644-742 2.22e-08

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: 53.17  E-value: 2.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 644 FRAAQCAEYNSKRFR-----GWLYKW---TPYTQveDQDLCKLYCIAEGFDFFFSLSNKVKDGTPC------SEDSRNVC 709
Cdd:pfam19236   5 FMSQQCARTDGQPLRsspggASFYHWgaaVPHSQ--GDALCRHMCRAIGESFIMKRGDSFLDGTRCmpsgprEDGTLSLC 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958644989 710 IDGMCEKVGCDNVLGSDATEDSCGVCQGNNSDC 742
Cdd:pfam19236  83 VLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 331-441 1.93e-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: 50.83  E-value: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 331 NINIVIVGLILLED-EQPGLAIShhADRTLTSFCQWQSGLMGKDGARHDHAILltgldicswKNEPCDTLGFAPISGMCS 409
Cdd:pfam13582  19 GIRLQLAAIIITTSaDTPYTSSD--ALEILDELQEVNDTRIGQYGYDLGHLFT---------GRDGGGGGGIAYVGGVCN 87

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958644989 410 KYRSCTVNEDS---GLGLAFTIAHESGHNFGMVHD 441
Cdd:pfam13582  88 SGSKFGVNSGSgpvGDTGADTFAHEIGHNFGLNHT 122
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 591-637 2.05e-06

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: 45.52  E-value: 2.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958644989 591 PWSPCSRTCGGGVSHRDRLCTNPRP--SHGGKFCQGSAR--TLKLCNSQKC 637
Cdd:pfam19030   5 PWGECSVTCGGGVQTRLVQCVQKGGgsIVPDSECSAQKKppETQSCNLKPC 55
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 427-487 1.95e-04

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: 44.29  E-value: 1.95e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644989 427 TIAHESGHNFGMVHDGEGNMCKKSE---GN-IMSP-TLAG---RNGVFswSSCSRQYLHKFLSTAQAIC 487
Cdd:cd04270   170 VTAHELGHNFGSPHDPDIAECAPGEsqgGNyIMYArATSGdkeNNKKF--SPCSKKSISKVLEVKSNSC 236
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 312-480 2.68e-04

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: 43.56  E-value: 2.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 312 VLTILNMVSALFKDGTiggNINIVIVGLILLEDEQP---------------GLAIShhaDRtLTSFCQWQSGLMGKDgar 376
Cdd:cd04271    27 ILNNVNSASQLYESSF---NISLGLRNLTISDASCPstavdsapwnlpcnsRIDID---DR-LSIFSQWRGQQPDDG--- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644989 377 hdhAILLTGLDICswKNEPcdTLGFAPISGMCSKYRSCTVNE--DSGLGLAFT------IAHESGHNFGMVHD------- 441
Cdd:cd04271    97 ---NAFWTLMTAC--PSGS--EVGVAWLGQLCRTGASDQGNEtvAGTNVVVRTsnewqvFAHEIGHTFGAVHDctsgtcs 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958644989 442 ----GEGNMCKKSEGN-------IMSPTlaGRNGVFSWSSCSRQYLHKFL 480
Cdd:cd04271   170 dgsvGSQQCCPLSTSTcdangqyIMNPS--SSSGITEFSPCTIGNICSLL 217
TSP1_CCN pfam19035
CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in ...
 590-606 3.67e-04

CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in matricellular CCN proteins that have an alternative disulphide binding pattern compared to the canonical TSP1 domains.


Pssm-ID: 465952  Cd Length: 44  Bit Score: 38.85  E-value: 3.67e-04
                          10
                  ....*....|....*..
gi 1958644989 590 SPWSPCSRTCGGGVSHR 606
Cdd:pfam19035   6 TEWSPCSKTCGMGVSTR 22
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 876-924 1.74e-03

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: 37.43  E-value: 1.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958644989 876 SECSVSCGGGKMSSKAGCYRDL-KVLVNASFCNPKTRPvPALVPCKVSAC 924
Cdd:pfam19030   7 GECSVTCGGGVQTRLVQCVQKGgGSIVPDSECSAQKKP-PETQSCNLKPC 55
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 427-457 2.94e-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: 39.91  E-value: 2.94e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1958644989 427 TIAHESGHNFGMVHD----GEGNMCKKSEGN---IMSP 457
Cdd:pfam13583 138 IFAHEIGHTFGAVHDcssqGEGLSSSTEDGSgqtIMSY 175
 
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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