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Conserved domains on  [gi|1907194498|ref|XP_036010447|]
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A disintegrin and metalloproteinase with thrombospondin motifs 7 isoform X6 [Mus musculus]

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) ...
 226-434 6.63e-114

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: 344.99  E-value: 6.63e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 226 KWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLFHDPSIGNPIHISIVRLIILEDEEKDLKITHHAEETLKNFCRWQ 305
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 306 KNINIKGDDHPQHHDTAILLTRKDLCaSMNQPCETLGLSHVSGLCHPQLSCSVSEDTGMPLAFTVAHELGHSFGIQHDGT 385
Cdd:cd04273    81 KKLNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1907194498 386 GNDCESIGKRPFIMSPQLLYDRGiPLTWSRCSREYITRFLDRGWGLCLD 434
Cdd:cd04273   160 GNSCGPEGKDGHIMSPTLGANTG-PFTWSKCSRRYLTSFLDTGDGNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 34-174 3.26e-36

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: 132.82  E-value: 3.26e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498  34 DIVHPVRVDAGgsflsyelwpRVLRKRDVSTTQASSAFYQLQYQGRELLFNLTTNPYLMAPGFVSEIRRHSTLGHAHIQT 113
Cdd:pfam01562   1 EVVIPVRLDPS----------RRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPV 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907194498 114 SVPTCHLLGDVQDpeLEGGFAAISACDGLRGVFQLSNEDYFIEPLDGvSAQPGHAQPHVVY 174
Cdd:pfam01562  71 QTDHCYYQGHVEG--HPDSSVALSTCSGLRGFIRTENEEYLIEPLEK-YSREEGGHPHVVY 128
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 684-793 1.80e-32

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: 121.53  E-value: 1.80e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 684 TVSRTFKETEGQGYVDIGLIPAGAREILIEEVAEAANFLALRSeDPDKYFLNGGWTIQ-WNGDYRVAGTTFTYARKGN-W 761
Cdd:pfam05986   1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPaL 79

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907194498 762 ENLTSPGPTSEPVWIQLLFQ---EKNPGVHYQYTI 793
Cdd:pfam05986  80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFI 114
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 449-513 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: 99.73  E-value: 2.47e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907194498 449 PGVLYDVNHQCRLQYGSHSAYCEDM-DDVCHTLWCSVGT--TCHSKLDAAVDGTSCGKNKWCLKGECV 513
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGgsTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 526-578 1.07e-15

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.85  E-value: 1.07e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907194498  526 WSGWSAWSDCSRSCGVGVRSSERQCTQPVPKNRGKYCVGERKRSQLCNLPACP 578
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 ...
 584-682 8.66e-11

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: 59.72  E-value: 8.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 584 FRHTQCSQFDGMLYK-----GKLHKW---VPVPNDDNPCELHCRPSNSSNTEKLRDAVVDGTPCYQSRISRD----ICLN 651
Cdd:pfam19236   5 FMSQQCARTDGQPLRsspggASFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDgtlsLCVL 84

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907194498 652 GICKNVGCDFVIDSGAEEDRCGVCRGDGSTC 682
Cdd:pfam19236  85 GSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 808-821 6.32e-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: 35.51  E-value: 6.32e-03
                          10
                  ....*....|....
gi 1907194498 808 WHYGPWSKCTVTCG 821
Cdd:pfam19030   1 WVAGPWGECSVTCG 14
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 226-434 6.63e-114

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: 344.99  E-value: 6.63e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 226 KWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLFHDPSIGNPIHISIVRLIILEDEEKDLKITHHAEETLKNFCRWQ 305
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 306 KNINIKGDDHPQHHDTAILLTRKDLCaSMNQPCETLGLSHVSGLCHPQLSCSVSEDTGMPLAFTVAHELGHSFGIQHDGT 385
Cdd:cd04273    81 KKLNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1907194498 386 GNDCESIGKRPFIMSPQLLYDRGiPLTWSRCSREYITRFLDRGWGLCLD 434
Cdd:cd04273   160 GNSCGPEGKDGHIMSPTLGANTG-PFTWSKCSRRYLTSFLDTGDGNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 34-174 3.26e-36

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: 132.82  E-value: 3.26e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498  34 DIVHPVRVDAGgsflsyelwpRVLRKRDVSTTQASSAFYQLQYQGRELLFNLTTNPYLMAPGFVSEIRRHSTLGHAHIQT 113
Cdd:pfam01562   1 EVVIPVRLDPS----------RRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPV 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907194498 114 SVPTCHLLGDVQDpeLEGGFAAISACDGLRGVFQLSNEDYFIEPLDGvSAQPGHAQPHVVY 174
Cdd:pfam01562  71 QTDHCYYQGHVEG--HPDSSVALSTCSGLRGFIRTENEEYLIEPLEK-YSREEGGHPHVVY 128
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 684-793 1.80e-32

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: 121.53  E-value: 1.80e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 684 TVSRTFKETEGQGYVDIGLIPAGAREILIEEVAEAANFLALRSeDPDKYFLNGGWTIQ-WNGDYRVAGTTFTYARKGN-W 761
Cdd:pfam05986   1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPaL 79

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907194498 762 ENLTSPGPTSEPVWIQLLFQ---EKNPGVHYQYTI 793
Cdd:pfam05986  80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFI 114
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 226-437 1.57e-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: 116.25  E-value: 1.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 226 KWVETLVVADSKMVEYHGQPQ--VESYVLTIMNMVAglfhdpSIGNPIHISIVrLIILE---DEEKdLKITHHAEETLKN 300
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTtvVRQRVFQVVNLVN------SIYKELNIRVV-LVGLEiwtDEDK-IDVSGDANDTLRN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 301 FCRWQKNiNIKgddHPQHHDTAILLTRKDLCASmnqpceTLGLSHVSGLCHPQLSCSVSED---TGMPLAFTVAHELGHS 377
Cdd:pfam01421  73 FLKWRQE-YLK---KRKPHDVAQLLSGVEFGGT------TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHN 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 378 FGIQHDGTGNDCESIGKRPFIMSPQLLYDrgIPLTWSRCSREYITRFLDRGWGLCLDDRP 437
Cdd:pfam01421 143 LGMQHDDFNGGCKCPPGGGCIMNPSAGSS--FPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 449-513 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: 99.73  E-value: 2.47e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907194498 449 PGVLYDVNHQCRLQYGSHSAYCEDM-DDVCHTLWCSVGT--TCHSKLDAAVDGTSCGKNKWCLKGECV 513
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGgsTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 526-578 1.07e-15

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.85  E-value: 1.07e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907194498  526 WSGWSAWSDCSRSCGVGVRSSERQCTQPVPKNRGKYCVGERKRSQLCNLPACP 578
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 584-682 8.66e-11

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: 59.72  E-value: 8.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 584 FRHTQCSQFDGMLYK-----GKLHKW---VPVPNDDNPCELHCRPSNSSNTEKLRDAVVDGTPCYQSRISRD----ICLN 651
Cdd:pfam19236   5 FMSQQCARTDGQPLRsspggASFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDgtlsLCVL 84

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907194498 652 GICKNVGCDFVIDSGAEEDRCGVCRGDGSTC 682
Cdd:pfam19236  85 GSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP_1 pfam00090
Thrombospondin type 1 domain;
527-577 1.62e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 51.26  E-value: 1.62e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907194498 527 SGWSAWSDCSRSCGVGVRSSERQCTQPVPKnrGKYCVGERKRSQLCNLPAC 577
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPG--GEPCTGDDIETQACKMDKC 49
PTZ00087 PTZ00087
thrombosponding-related protein; Provisional
 526-592 6.19e-03

thrombosponding-related protein; Provisional


Pssm-ID: 185438  Cd Length: 340  Bit Score: 39.54  E-value: 6.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907194498 526 WSGWSAWSDCSRSC----GVGVRssERQCTQPvpknRGKYCVGERKRSQLCNLPaCPPDRPSFRHTQCSQF 592
Cdd:PTZ00087  233 YTEWGEWSNCSMECdhpdNVQIR--ERKCAHP----SGDCFKGDLKETRPCQVP-LPPCNSLFEHKESSTF 296
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 808-821 6.32e-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: 35.51  E-value: 6.32e-03
                          10
                  ....*....|....
gi 1907194498 808 WHYGPWSKCTVTCG 821
Cdd:pfam19030   1 WVAGPWGECSVTCG 14
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 226-434 6.63e-114

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: 344.99  E-value: 6.63e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 226 KWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLFHDPSIGNPIHISIVRLIILEDEEKDLKITHHAEETLKNFCRWQ 305
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 306 KNINIKGDDHPQHHDTAILLTRKDLCaSMNQPCETLGLSHVSGLCHPQLSCSVSEDTGMPLAFTVAHELGHSFGIQHDGT 385
Cdd:cd04273    81 KKLNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1907194498 386 GNDCESIGKRPFIMSPQLLYDRGiPLTWSRCSREYITRFLDRGWGLCLD 434
Cdd:cd04273   160 GNSCGPEGKDGHIMSPTLGANTG-PFTWSKCSRRYLTSFLDTGDGNCLL 207
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 34-174 3.26e-36

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: 132.82  E-value: 3.26e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498  34 DIVHPVRVDAGgsflsyelwpRVLRKRDVSTTQASSAFYQLQYQGRELLFNLTTNPYLMAPGFVSEIRRHSTLGHAHIQT 113
Cdd:pfam01562   1 EVVIPVRLDPS----------RRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPV 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907194498 114 SVPTCHLLGDVQDpeLEGGFAAISACDGLRGVFQLSNEDYFIEPLDGvSAQPGHAQPHVVY 174
Cdd:pfam01562  71 QTDHCYYQGHVEG--HPDSSVALSTCSGLRGFIRTENEEYLIEPLEK-YSREEGGHPHVVY 128
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 228-426 3.77e-35

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: 132.16  E-value: 3.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 228 VETLVVADSKMVEYHgQPQVES---YVLTIMNMVAGLFHDPSIGNPIHISIVRLIILEDEEKDLKITHHAEETLKNFCRW 304
Cdd:cd04267     3 IELVVVADHRMVSYF-NSDENIlqaYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 305 QKninikgdDHPQHHDTAILLTRKDLCAsmnqpCETLGLSHVSGLCHPQLSCSVSEDTGMPL--AFTVAHELGHSFGIQH 382
Cdd:cd04267    82 RA-------EGPIRHDNAVLLTAQDFIE-----GDILGLAYVGSMCNPYSSVGVVEDTGFTLltALTMAHELGHNLGAEH 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907194498 383 DGTGNDCESIGKRP-FIMSPQLlyDRGIPLTWSRCSREYITRFLD 426
Cdd:cd04267   150 DGGDELAFECDGGGnYIMAPVD--SGLNSYRFSQCSIGSIREFLD 192
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 684-793 1.80e-32

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: 121.53  E-value: 1.80e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 684 TVSRTFKETEGQGYVDIGLIPAGAREILIEEVAEAANFLALRSeDPDKYFLNGGWTIQ-WNGDYRVAGTTFTYARKGN-W 761
Cdd:pfam05986   1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPaL 79

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907194498 762 ENLTSPGPTSEPVWIQLLFQ---EKNPGVHYQYTI 793
Cdd:pfam05986  80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFI 114
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 226-433 8.00e-32

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: 122.72  E-value: 8.00e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 226 KWVETLVVADSKMVEYHGQ--PQVESYVLTIMNMVAGLFHdpSIGnpIHISIVRLIILEDEEKdLKITHHAEETLKNFCR 303
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSnlSKVRQRVIEIVNIVDSIYR--PLN--IRVVLVGLEIWTDKDK-ISVSGDAGETLNRFLD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 304 W-QKNINikgddHPQHHDTAILLTRKDLCAsmnqpcETLGLSHVSGLCHPQLSCSVSEDTGMPL---AFTVAHELGHSFG 379
Cdd:cd04269    76 WkRSNLL-----PRKPHDNAQLLTGRDFDG------NTVGLAYVGGMCSPKYSGGVVQDHSRNLllfAVTMAHELGHNLG 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907194498 380 IQHDGTGNDCESigkRPFIMSPQLLYdrgIPLTWSRCSREYITRFLDRGWGLCL 433
Cdd:cd04269   145 MEHDDGGCTCGR---STCIMAPSPSS---LTDAFSNCSYEDYQKFLSRGGGQCL 192
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 226-437 1.57e-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: 116.25  E-value: 1.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 226 KWVETLVVADSKMVEYHGQPQ--VESYVLTIMNMVAglfhdpSIGNPIHISIVrLIILE---DEEKdLKITHHAEETLKN 300
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTtvVRQRVFQVVNLVN------SIYKELNIRVV-LVGLEiwtDEDK-IDVSGDANDTLRN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 301 FCRWQKNiNIKgddHPQHHDTAILLTRKDLCASmnqpceTLGLSHVSGLCHPQLSCSVSED---TGMPLAFTVAHELGHS 377
Cdd:pfam01421  73 FLKWRQE-YLK---KRKPHDVAQLLSGVEFGGT------TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHN 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 378 FGIQHDGTGNDCESIGKRPFIMSPQLLYDrgIPLTWSRCSREYITRFLDRGWGLCLDDRP 437
Cdd:pfam01421 143 LGMQHDDFNGGCKCPPGGGCIMNPSAGSS--FPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 449-513 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: 99.73  E-value: 2.47e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907194498 449 PGVLYDVNHQCRLQYGSHSAYCEDM-DDVCHTLWCSVGT--TCHSKLDAAVDGTSCGKNKWCLKGECV 513
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGgsTCTTKNLPAADGTPCGNKKWCLNGKCV 68
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 228-433 2.75e-19

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 87.41  E-value: 2.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 228 VETLVVADSKMVEYHGQ-PQVESYVLTIMNMVAGLFHDpsIGNP-IHISIVRLIILEDEEKDLKITHH------AEETLK 299
Cdd:cd04272     3 PELFVVVDYDHQSEFFSnEQLIRYLAVMVNAANLRYRD--LKSPrIRLLLVGITISKDPDFEPYIHPInygyidAAETLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 300 NFcrwqkNINIKGDDHPQHHDTAILLTRKDLCASMNQPCET--LGLSHVSGLCHpQLSCSVSEDTGMPL--AFTVAHELG 375
Cdd:cd04272    81 NF-----NEYVKKKRDYFNPDVVFLVTGLDMSTYSGGSLQTgtGGYAYVGGACT-ENRVAMGEDTPGSYygVYTMTHELA 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 376 HSFGIQHDGTGnDCESIGKRP----------FIMSpqllYDRGIP--LTWSRCSREYITRFLDRGWGLCL 433
Cdd:cd04272   155 HLLGAPHDGSP-PPSWVKGHPgsldcpwddgYIMS----YVVNGErqYRFSQCSQRQIRNVFRRLGASCL 219
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 526-578 1.07e-15

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.85  E-value: 1.07e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907194498  526 WSGWSAWSDCSRSCGVGVRSSERQCTQPVPKNRGKYCVGERKRSQLCNLPACP 578
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 316-425 3.89e-14

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: 71.01  E-value: 3.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 316 PQHHDTAILLTRKDLcasmnqPCETLGLSHVSGLCHPQLSCSVSEDTGMP---LAFTVAHELGHSFGIQHDGTGNDCESI 392
Cdd:cd00203    49 IDKADIAILVTRQDF------DGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDRKDRDDY 122

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907194498 393 GKRP-----------FIMSPQLL-YDRGIPLTWSRCSREYITRFL 425
Cdd:cd00203   123 PTIDdtlnaedddyySVMSYTKGsFSDGQRKDFSQCDIDQINKLY 167
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
224-402 5.02e-13

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 68.60  E-value: 5.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 224 KEKWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLFHDPSignPIHISIVRLIILEDEEKDlkiTHHAEETLKNFCR 303
Cdd:pfam13688   1 STRTVALLVAADCSYVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCPY---TPPACSTGDSSDR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 304 WQKNINIKGDDHPQHHDTAILLTrkdlcasmNQPCETLGLSHVSGLCHPQLSCSVSEDTGMP--------LAFTVAHELG 375
Cdd:pfam13688  75 LSEFQDFSAWRGTQNDDLAYLFL--------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQVFAHEIG 146

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907194498 376 HSFGIQHDGT----------GNDCESIGKRpFIMSPQ 402
Cdd:pfam13688 147 HNFGAVHDCDsstssqccppSNSTCPAGGR-YIMNPS 182
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 584-682 8.66e-11

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: 59.72  E-value: 8.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 584 FRHTQCSQFDGMLYK-----GKLHKW---VPVPNDDNPCELHCRPSNSSNTEKLRDAVVDGTPCYQSRISRD----ICLN 651
Cdd:pfam19236   5 FMSQQCARTDGQPLRsspggASFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDgtlsLCVL 84

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907194498 652 GICKNVGCDFVIDSGAEEDRCGVCRGDGSTC 682
Cdd:pfam19236  85 GSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP_1 pfam00090
Thrombospondin type 1 domain;
527-577 1.62e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 51.26  E-value: 1.62e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907194498 527 SGWSAWSDCSRSCGVGVRSSERQCTQPVPKnrGKYCVGERKRSQLCNLPAC 577
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPG--GEPCTGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 527-577 9.75e-08

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: 49.20  E-value: 9.75e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907194498 527 SGWSAWSDCSRSCGVGVRSSERQCTQPvPKNRGKYCvGERKRSQLCNLPAC 577
Cdd:pfam19028   4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPC-PELLERRPCNLPPC 52
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 340-422 4.62e-06

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 372637  Cd Length: 193  Bit Score: 48.01  E-value: 4.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 340 TLGLSHVSGLCHPQLSCsVSEDTGMPLAFT-------------VAHELGHSFGIQHDGTG--NDCESI----------GK 394
Cdd:pfam13574  86 ELGLAYVGQICQKGASS-PKTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDCDGsqYASSGCernaatsvcsAN 164

                          90       100
                  ....*....|....*....|....*...
gi 1907194498 395 RPFIMSPQllYDRGIPLtWSRCSREYIT 422
Cdd:pfam13574 165 GSFIMNPA--SKSNNDL-FSPCSISLIC 189
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 529-577 1.50e-05

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: 43.21  E-value: 1.50e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907194498 529 WSA--WSDCSRSCGVGVRSSERQCTQPVPK--NRGKYCVGERK--RSQLCNLPAC 577
Cdd:pfam19030   1 WVAgpWGECSVTCGGGVQTRLVQCVQKGGGsiVPDSECSAQKKppETQSCNLKPC 55
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 271-383 1.64e-05

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: 45.05  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 271 IHISIVRLIILED-EEKDLKIThhAEETLKNFCRWQKNiNIKGDDHPQHHdtaiLLTRKDlcasmnqPCETLGLSHVSGL 349
Cdd:pfam13582  20 IRLQLAAIIITTSaDTPYTSSD--ALEILDELQEVNDT-RIGQYGYDLGH----LFTGRD-------GGGGGGIAYVGGV 85

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907194498 350 CHPQLSCSVSEDTGMP---LAFTVAHELGHSFGIQHD 383
Cdd:pfam13582  86 CNSGSKFGVNSGSGPVgdtGADTFAHEIGHNFGLNHT 122
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 231-439 2.01e-05

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: 46.98  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 231 LVVADSKMVEYHGQPQVESYVLTIMNMVAGL--------FHDPSIGNpIHISIVRLIIL-EDEEKDLKITHHaeetlkNF 301
Cdd:cd04270     6 LLVADHRFYKYMGRGEEETTINYLISHIDRVddiyrntdWDGGGFKG-IGFQIKRIRIHtTPDEVDPGNKFY------NK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 302 C-------RWQKNINIKgddhpQHHD---TAILLTRKDLcaSMNqpceTLGLSHVS--------GLCHPQLSCSV----S 359
Cdd:cd04270    79 SfpnwgveKFLVKLLLE-----QFSDdvcLAHLFTYRDF--DMG----TLGLAYVGsprdnsagGICEKAYYYSNgkkkY 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194498 360 EDTGMPLAF-------------TVAHELGHSFGIQHDGTGNDC---ESIGKRpFIMSPQLLY-DRGIPLTWSRCSREYIT 422
Cdd:cd04270   148 LNTGLTTTVnygkrvptkesdlVTAHELGHNFGSPHDPDIAECapgESQGGN-YIMYARATSgDKENNKKFSPCSKKSIS 226

                         250
                  ....*....|....*..
gi 1907194498 423 RFLDRGWGLCLDDRPSK 439
Cdd:cd04270   227 KVLEVKSNSCFVERSQS 243
PTZ00087 PTZ00087
thrombosponding-related protein; Provisional
 526-592 6.19e-03

thrombosponding-related protein; Provisional


Pssm-ID: 185438  Cd Length: 340  Bit Score: 39.54  E-value: 6.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907194498 526 WSGWSAWSDCSRSC----GVGVRssERQCTQPvpknRGKYCVGERKRSQLCNLPaCPPDRPSFRHTQCSQF 592
Cdd:PTZ00087  233 YTEWGEWSNCSMECdhpdNVQIR--ERKCAHP----SGDCFKGDLKETRPCQVP-LPPCNSLFEHKESSTF 296
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 808-821 6.32e-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: 35.51  E-value: 6.32e-03
                          10
                  ....*....|....
gi 1907194498 808 WHYGPWSKCTVTCG 821
Cdd:pfam19030   1 WVAGPWGECSVTCG 14
TSP1_CCN pfam19035
CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in ...
 530-577 6.65e-03

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: 35.39  E-value: 6.65e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907194498 530 SAWSDCSRSCGVGVrsSERQctqpvpKNRGKYCvGERKRSQLCNLPAC 577
Cdd:pfam19035   6 TEWSPCSKTCGMGV--STRV------SNDNAEC-KLVTETRLCQLRPC 44
 
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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