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Conserved domains on  [gi|453232819|ref|NP_001024532|]
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A disintegrin and metalloproteinase with thrombospondin motifs adt-2 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc super family cl00064
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 211-417 7.18e-70

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.


The actual alignment was detected with superfamily member cd04273:

Pssm-ID: 469599  Cd Length: 207  Bit Score: 231.36  E-value: 7.18e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453232819  211 LIVELAVFVDENLWRHFsskhggmADRKLQDYTLTLLNNIQIMYYQPTASPPLTFRVIRYEVLTRQPSALAgylhNHGNA 290
Cdd:cd04273     1 RYVETLVVADSKMVEFH-------HGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLL----ISGNA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453232819  291 QMYLDRFCRYQRNLAVRD------WDHAIMLTGYDIHRGAGSRSISGIARLDGMCDPWNTCTLAEGLDFTSAFIGTHELG 364
Cdd:cd04273    70 QKSLKSFCRWQKKLNPPNdsdpehHDHAILLTRQDICRSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELG 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 453232819  365 HSVGMRHD------EPYCQSKHIMSSSLGP--GKVTWSTCSLRDYHQFLQRLDGrgkNCLR 417
Cdd:cd04273   150 HVLGMPHDgdgnscGPEGKDGHIMSPTLGAntGPFTWSKCSRRYLTSFLDTGDG---NCLL 207
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 433-502 1.75e-17

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: 77.39  E-value: 1.75e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 453232819   433 PGQIYDANLQCELMHGNGYqqvTPRQDSYDGICYMMWCGQSSFGRIIT-SHPALEGTFCGPSKWCQLGRCV 502
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGS---TFCPNGDEDVCSKLWCSNPGGSTCTTkNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 969-1015 1.18e-11

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: 60.68  E-value: 1.18e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 453232819    969 WGGWGYWSSCSETCGDGVRKRVRKC------YGSGNCDGQQYEKQYCNLRVCD 1015
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcspppqNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 866-910 2.45e-11

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: 59.52  E-value: 2.45e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 453232819    866 WSLWNEWSDCSRVCGKGLRSRSRSCF-------GSGCMGASSEQQFCNEQAC 910
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCspppqngGGPCTGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 918-963 7.54e-11

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: 58.37  E-value: 7.54e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 453232819    918 WGTWSGWSQCSVSCGAGVKRRTRTCRTGN-------CPGNYKESAICNDRDCE 963
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPpqngggpCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 760-810 7.99e-11

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: 57.98  E-value: 7.99e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 453232819    760 WSTWTEWNHCSVSCGRGSQARYRKCLSPHRTLAF-DCPEKNIEVRSCDNGPC 810
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGgPCTGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 705-751 2.91e-10

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 56.44  E-value: 2.91e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 453232819    705 WGTWSLWTSCTATCGGGYRKRNRACS------ITGQCEGNEDETEVCSSESCP 751
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCspppqnGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 816-860 8.69e-10

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 55.29  E-value: 8.69e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 453232819    816 WGTWGGWSTCSTSCGPGTLVRQRTCNR-------EPCDGSAHERRSCNVATC 860
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSpppqnggGPCTGEDVETRACNEQPC 52
Pep_M12B_propep super family cl03265
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 46-163 4.25e-06

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.


The actual alignment was detected with superfamily member pfam01562:

Pssm-ID: 460254  Cd Length: 128  Bit Score: 46.92  E-value: 4.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453232819    46 DPVPYYHQngsLHkLEFMAFNKKYNLSLEPTlAKLLSSGVTVVKKNEKKGGSLDFGSTLDSCHYHHY--GEKVY-AAISN 122
Cdd:pfam01562   19 SESTYLDT---LS-YRLAAFGKKFHLHLTPN-RLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHveGHPDSsVALST 93

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 453232819   123 CDGrIKGTVIDDGEIIVVHPFPDHHAHRSKRatengAHVVY 163
Cdd:pfam01562   94 CSG-LRGFIRTENEEYLIEPLEKYSREEGGH-----PHVVY 128
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 211-417 7.18e-70

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: 231.36  E-value: 7.18e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453232819  211 LIVELAVFVDENLWRHFsskhggmADRKLQDYTLTLLNNIQIMYYQPTASPPLTFRVIRYEVLTRQPSALAgylhNHGNA 290
Cdd:cd04273     1 RYVETLVVADSKMVEFH-------HGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLL----ISGNA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453232819  291 QMYLDRFCRYQRNLAVRD------WDHAIMLTGYDIHRGAGSRSISGIARLDGMCDPWNTCTLAEGLDFTSAFIGTHELG 364
Cdd:cd04273    70 QKSLKSFCRWQKKLNPPNdsdpehHDHAILLTRQDICRSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELG 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 453232819  365 HSVGMRHD------EPYCQSKHIMSSSLGP--GKVTWSTCSLRDYHQFLQRLDGrgkNCLR 417
Cdd:cd04273   150 HVLGMPHDgdgnscGPEGKDGHIMSPTLGAntGPFTWSKCSRRYLTSFLDTGDG---NCLL 207
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 287-422 1.27e-18

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: 85.04  E-value: 1.27e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453232819   287 HGNAQMYLDRFCRY-QRNLAVR-DWDHAIMLTGYDIHrgaGSRSisGIARLDGMCDPWNTCTLAE-GLDFTSAFIGT--H 361
Cdd:pfam01421   63 SGDANDTLRNFLKWrQEYLKKRkPHDVAQLLSGVEFG---GTTV--GAAYVGGMCSLEYSGGVNEdHSKNLESFAVTmaH 137

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 453232819   362 ELGHSVGMRHDEP----YCQSKH--IMSSSLG-PGKVTWSTCSLRDYHQFLQRLDGRgknCLrvSNMP 422
Cdd:pfam01421  138 ELGHNLGMQHDDFnggcKCPPGGgcIMNPSAGsSFPRKFSNCSQEDFEQFLTKQKGA---CL--FNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 433-502 1.75e-17

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: 77.39  E-value: 1.75e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 453232819   433 PGQIYDANLQCELMHGNGYqqvTPRQDSYDGICYMMWCGQSSFGRIIT-SHPALEGTFCGPSKWCQLGRCV 502
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGS---TFCPNGDEDVCSKLWCSNPGGSTCTTkNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 969-1015 1.18e-11

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: 60.68  E-value: 1.18e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 453232819    969 WGGWGYWSSCSETCGDGVRKRVRKC------YGSGNCDGQQYEKQYCNLRVCD 1015
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcspppqNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 866-910 2.45e-11

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: 59.52  E-value: 2.45e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 453232819    866 WSLWNEWSDCSRVCGKGLRSRSRSCF-------GSGCMGASSEQQFCNEQAC 910
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCspppqngGGPCTGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 918-963 7.54e-11

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: 58.37  E-value: 7.54e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 453232819    918 WGTWSGWSQCSVSCGAGVKRRTRTCRTGN-------CPGNYKESAICNDRDCE 963
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPpqngggpCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 760-810 7.99e-11

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: 57.98  E-value: 7.99e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 453232819    760 WSTWTEWNHCSVSCGRGSQARYRKCLSPHRTLAF-DCPEKNIEVRSCDNGPC 810
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGgPCTGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 705-751 2.91e-10

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 56.44  E-value: 2.91e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 453232819    705 WGTWSLWTSCTATCGGGYRKRNRACS------ITGQCEGNEDETEVCSSESCP 751
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCspppqnGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 816-860 8.69e-10

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 55.29  E-value: 8.69e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 453232819    816 WGTWGGWSTCSTSCGPGTLVRQRTCNR-------EPCDGSAHERRSCNVATC 860
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSpppqnggGPCTGEDVETRACNEQPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
708-750 4.45e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 47.41  E-value: 4.45e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 453232819   708 WSLWTSCTATCGGGYRKRNRACSIT----GQCEGNEDETEVCSSESC 750
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCKSPfpggEPCTGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 819-860 6.29e-07

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: 46.89  E-value: 6.29e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 453232819   819 WGGWSTCSTSCGPGTLVRQRTCNREPCDGSAH-----ERRSCNVATC 860
Cdd:pfam19028    6 WSEWSECSVTCGGGVQTRTRTVIVEPQNGGRPcpellERRPCNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
761-810 1.00e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 46.26  E-value: 1.00e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 453232819   761 STWTEWNHCSVSCGRGSQARYRKCLSPHRTLAfDCPEKNIEVRSCDNGPC 810
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGE-PCTGDDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
921-962 2.14e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 45.49  E-value: 2.14e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 453232819   921 WSGWSQCSVSCGAGVKRRTRTCRT-----GNCPGNYKESAICNDRDC 962
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCKSpfpggEPCTGDDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
970-1014 3.26e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 45.10  E-value: 3.26e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 453232819   970 GGWGYWSSCSETCGDGVRKRVRKC----YGSGNCDGQQYEKQYCNLRVC 1014
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCkspfPGGEPCTGDDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
867-910 3.32e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 45.10  E-value: 3.32e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 453232819   867 SLWNEWSDCSRVCGKGLRSRSRSC-----FGSGCMGASSEQQFCNEQAC 910
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCkspfpGGEPCTGDDIETQACKMDKC 49
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 46-163 4.25e-06

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: 46.92  E-value: 4.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453232819    46 DPVPYYHQngsLHkLEFMAFNKKYNLSLEPTlAKLLSSGVTVVKKNEKKGGSLDFGSTLDSCHYHHY--GEKVY-AAISN 122
Cdd:pfam01562   19 SESTYLDT---LS-YRLAAFGKKFHLHLTPN-RLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHveGHPDSsVALST 93

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 453232819   123 CDGrIKGTVIDDGEIIVVHPFPDHHAHRSKRatengAHVVY 163
Cdd:pfam01562   94 CSG-LRGFIRTENEEYLIEPLEKYSREEGGH-----PHVVY 128
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 869-910 1.07e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 49.19  E-value: 1.07e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 453232819  869 WNEWSDCSRVCGKGLRSRSRSCFGSGCMGASSEQqfCNEQAC 910
Cdd:PTZ00441  243 WDEWTPCSVTCGKGTHSRSRPILHEGCTTHMVEE--CEEEEC 282
PTZ00087 PTZ00087
thrombosponding-related protein; Provisional
 963-1009 5.05e-03

thrombosponding-related protein; Provisional


Pssm-ID: 185438  Cd Length: 340  Bit Score: 40.31  E-value: 5.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 453232819  963 ENKNAAWGGWGYWSSCSETCG--DGVRKRVRKC-YGSGNC-DGQQYEKQYC 1009
Cdd:PTZ00087  227 EKKNMFYTEWGEWSNCSMECDhpDNVQIRERKCaHPSGDCfKGDLKETRPC 277
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 211-417 7.18e-70

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: 231.36  E-value: 7.18e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453232819  211 LIVELAVFVDENLWRHFsskhggmADRKLQDYTLTLLNNIQIMYYQPTASPPLTFRVIRYEVLTRQPSALAgylhNHGNA 290
Cdd:cd04273     1 RYVETLVVADSKMVEFH-------HGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLL----ISGNA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453232819  291 QMYLDRFCRYQRNLAVRD------WDHAIMLTGYDIHRGAGSRSISGIARLDGMCDPWNTCTLAEGLDFTSAFIGTHELG 364
Cdd:cd04273    70 QKSLKSFCRWQKKLNPPNdsdpehHDHAILLTRQDICRSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELG 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 453232819  365 HSVGMRHD------EPYCQSKHIMSSSLGP--GKVTWSTCSLRDYHQFLQRLDGrgkNCLR 417
Cdd:cd04273   150 HVLGMPHDgdgnscGPEGKDGHIMSPTLGAntGPFTWSKCSRRYLTSFLDTGDG---NCLL 207
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 294-416 7.44e-19

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: 85.74  E-value: 7.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453232819  294 LDRFCRYQRNLAVRDW--DHAIMLTGYDIHRGagsrsISGIARLDGMCDPWNTCTLAEGLD---FTSAFIGTHELGHSVG 368
Cdd:cd04269    70 LNRFLDWKRSNLLPRKphDNAQLLTGRDFDGN-----TVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHNLG 144

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 453232819  369 MRHDEPYCQ---SKHIMSSSLGPGKVTWSTCSLRDYHQFLQRldgRGKNCL 416
Cdd:cd04269   145 MEHDDGGCTcgrSTCIMAPSPSSLTDAFSNCSYEDYQKFLSR---GGGQCL 192
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 287-422 1.27e-18

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: 85.04  E-value: 1.27e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453232819   287 HGNAQMYLDRFCRY-QRNLAVR-DWDHAIMLTGYDIHrgaGSRSisGIARLDGMCDPWNTCTLAE-GLDFTSAFIGT--H 361
Cdd:pfam01421   63 SGDANDTLRNFLKWrQEYLKKRkPHDVAQLLSGVEFG---GTTV--GAAYVGGMCSLEYSGGVNEdHSKNLESFAVTmaH 137

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 453232819   362 ELGHSVGMRHDEP----YCQSKH--IMSSSLG-PGKVTWSTCSLRDYHQFLQRLDGRgknCLrvSNMP 422
Cdd:pfam01421  138 ELGHNLGMQHDDFnggcKCPPGGgcIMNPSAGsSFPRKFSNCSQEDFEQFLTKQKGA---CL--FNKP 200
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 433-502 1.75e-17

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: 77.39  E-value: 1.75e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 453232819   433 PGQIYDANLQCELMHGNGYqqvTPRQDSYDGICYMMWCGQSSFGRIIT-SHPALEGTFCGPSKWCQLGRCV 502
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGS---TFCPNGDEDVCSKLWCSNPGGSTCTTkNLPAADGTPCGNKKWCLNGKCV 68
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 213-405 2.25e-13

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: 69.76  E-value: 2.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453232819  213 VELAVFVDenlWRHFSSKHGGMADrkLQDYTLTLLNNIQIMYYQPTASPPLTFRVIRYEVLTRQPSALAgylhNHGNAQM 292
Cdd:cd04267     3 IELVVVAD---HRMVSYFNSDENI--LQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPP----IDSDASN 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453232819  293 YLDRFCRYQRNLAVRDwDHAIMLTGYDIHRGAgsrsISGIARLDGMCDPWNTCTLAE--GLDFTSAFIGTHELGHSVGMR 370
Cdd:cd04267    74 TLNSFSFWRAEGPIRH-DNAVLLTAQDFIEGD----ILGLAYVGSMCNPYSSVGVVEdtGFTLLTALTMAHELGHNLGAE 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 453232819  371 HDEPYC-------QSKHIMSSSLGP-GKVTWSTCSLRDYHQFL 405
Cdd:cd04267   149 HDGGDElafecdgGGNYIMAPVDSGlNSYRFSQCSIGSIREFL 191
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 969-1015 1.18e-11

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: 60.68  E-value: 1.18e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 453232819    969 WGGWGYWSSCSETCGDGVRKRVRKC------YGSGNCDGQQYEKQYCNLRVCD 1015
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcspppqNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 866-910 2.45e-11

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: 59.52  E-value: 2.45e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 453232819    866 WSLWNEWSDCSRVCGKGLRSRSRSCF-------GSGCMGASSEQQFCNEQAC 910
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCspppqngGGPCTGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 918-963 7.54e-11

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: 58.37  E-value: 7.54e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 453232819    918 WGTWSGWSQCSVSCGAGVKRRTRTCRTGN-------CPGNYKESAICNDRDCE 963
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPpqngggpCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 760-810 7.99e-11

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: 57.98  E-value: 7.99e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 453232819    760 WSTWTEWNHCSVSCGRGSQARYRKCLSPHRTLAF-DCPEKNIEVRSCDNGPC 810
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGgPCTGEDVETRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 705-751 2.91e-10

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 56.44  E-value: 2.91e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 453232819    705 WGTWSLWTSCTATCGGGYRKRNRACS------ITGQCEGNEDETEVCSSESCP 751
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCspppqnGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 816-860 8.69e-10

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 55.29  E-value: 8.69e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 453232819    816 WGTWGGWSTCSTSCGPGTLVRQRTCNR-------EPCDGSAHERRSCNVATC 860
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSpppqnggGPCTGEDVETRACNEQPC 52
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 213-417 9.76e-09

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 56.98  E-value: 9.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453232819  213 VELAVFVDENLWRHFSSkhggmaDRKLQDYTLTLLNNIQIMYYQpTASPPLTFRVIRYEVLTRQPSALagYLHNHGNAQM 292
Cdd:cd04272     3 PELFVVVDYDHQSEFFS------NEQLIRYLAVMVNAANLRYRD-LKSPRIRLLLVGITISKDPDFEP--YIHPINYGYI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453232819  293 Y----LDRFCRY--QRNLAVRdWDHAIMLTGYDI---HRGAGSRSISGIARLDGMCDPWNtctLAEGLDFTSAFIG---- 359
Cdd:cd04272    74 DaaetLENFNEYvkKKRDYFN-PDVVFLVTGLDMstySGGSLQTGTGGYAYVGGACTENR---VAMGEDTPGSYYGvytm 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 453232819  360 THELGHSVGMRHDE----PYCQSK-----------HIMSSSL-GPGKVTWSTCSLRDYHQFLQRLDGRgknCLR 417
Cdd:cd04272   150 THELAHLLGAPHDGspppSWVKGHpgsldcpwddgYIMSYVVnGERQYRFSQCSQRQIRNVFRRLGAS---CLH 220
TSP_1 pfam00090
Thrombospondin type 1 domain;
708-750 4.45e-07

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 47.41  E-value: 4.45e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 453232819   708 WSLWTSCTATCGGGYRKRNRACSIT----GQCEGNEDETEVCSSESC 750
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCKSPfpggEPCTGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 819-860 6.29e-07

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: 46.89  E-value: 6.29e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 453232819   819 WGGWSTCSTSCGPGTLVRQRTCNREPCDGSAH-----ERRSCNVATC 860
Cdd:pfam19028    6 WSEWSECSVTCGGGVQTRTRTVIVEPQNGGRPcpellERRPCNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
761-810 1.00e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 46.26  E-value: 1.00e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 453232819   761 STWTEWNHCSVSCGRGSQARYRKCLSPHRTLAfDCPEKNIEVRSCDNGPC 810
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGE-PCTGDDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
921-962 2.14e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 45.49  E-value: 2.14e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 453232819   921 WSGWSQCSVSCGAGVKRRTRTCRT-----GNCPGNYKESAICNDRDC 962
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCKSpfpggEPCTGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 761-810 2.37e-06

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 45.35  E-value: 2.37e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 453232819   761 STWTEWNHCSVSCGRGSQARYRKCLSPHRTLAFDCPEKNiEVRSCDNGPC 810
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVEPQNGGRPCPELL-ERRPCNLPPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
970-1014 3.26e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 45.10  E-value: 3.26e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 453232819   970 GGWGYWSSCSETCGDGVRKRVRKC----YGSGNCDGQQYEKQYCNLRVC 1014
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCkspfPGGEPCTGDDIETQACKMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
867-910 3.32e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 45.10  E-value: 3.32e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 453232819   867 SLWNEWSDCSRVCGKGLRSRSRSC-----FGSGCMGASSEQQFCNEQAC 910
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCkspfpGGEPCTGDDIETQACKMDKC 49
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 46-163 4.25e-06

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: 46.92  E-value: 4.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453232819    46 DPVPYYHQngsLHkLEFMAFNKKYNLSLEPTlAKLLSSGVTVVKKNEKKGGSLDFGSTLDSCHYHHY--GEKVY-AAISN 122
Cdd:pfam01562   19 SESTYLDT---LS-YRLAAFGKKFHLHLTPN-RLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHveGHPDSsVALST 93

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 453232819   123 CDGrIKGTVIDDGEIIVVHPFPDHHAHRSKRatengAHVVY 163
Cdd:pfam01562   94 CSG-LRGFIRTENEEYLIEPLEKYSREEGGH-----PHVVY 128
TSP_1 pfam00090
Thrombospondin type 1 domain;
819-860 8.61e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 43.95  E-value: 8.61e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 453232819   819 WGGWSTCSTSCGPGTLVRQRTCN-----REPCDGSAHERRSCNVATC 860
Cdd:pfam00090    3 WSPWSPCSVTCGKGIQVRQRTCKspfpgGEPCTGDDIETQACKMDKC 49
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 869-910 1.07e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 49.19  E-value: 1.07e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 453232819  869 WNEWSDCSRVCGKGLRSRSRSCFGSGCMGASSEQqfCNEQAC 910
Cdd:PTZ00441  243 WDEWTPCSVTCGKGTHSRSRPILHEGCTTHMVEE--CEEEEC 282
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 924-962 8.49e-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: 41.28  E-value: 8.49e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 453232819   924 WSQCSVSCGAGVKRRTRTCRTG---------NCPGNYKESAI--CNDRDC 962
Cdd:pfam19030    6 WGECSVTCGGGVQTRLVQCVQKgggsivpdsECSAQKKPPETqsCNLKPC 55
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 921-941 1.17e-04

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 40.73  E-value: 1.17e-04
                           10        20
                   ....*....|....*....|.
gi 453232819   921 WSGWSQCSVSCGAGVKRRTRT 941
Cdd:pfam19028    6 WSEWSECSVTCGGGVQTRTRT 26
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 973-1014 2.34e-04

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 39.74  E-value: 2.34e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 453232819   973 GYWSSCSETCGDGVRKRVRKC--------YGSGNCDGQQ--YEKQYCNLRVC 1014
Cdd:pfam19030    4 GPWGECSVTCGGGVQTRLVQCvqkgggsiVPDSECSAQKkpPETQSCNLKPC 55
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 970-1014 2.44e-04

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 39.57  E-value: 2.44e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 453232819   970 GGWGYWSSCSETCGDGVRKRVRKC-----YGSGNCdGQQYEKQYCNLRVC 1014
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVivepqNGGRPC-PELLERRPCNLPPC 52
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
212-394 4.14e-04

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 42.41  E-value: 4.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453232819   212 IVELAVFVDENlwrhFSSKHGGMAdrkLQDYTLTLLNNIQIMYYQPTaspPLTFRVIRYEVLTRQPSALAGYlHNHGNAQ 291
Cdd:pfam13688    4 TVALLVAADCS----YVAAFGGDA---AQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCPYTPPA-CSTGDSS 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453232819   292 MYLDRFcryqrnLAVRDWDHAImltGYDI-----HRGAGSRsisGIARLDGMC--------DPWNTCTLAEGLDFTSAFI 358
Cdd:pfam13688   73 DRLSEF------QDFSAWRGTQ---NDDLaylflMTNCSGG---GLAWLGQLCnsgsagsvSTRVSGNNVVVSTATEWQV 140

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 453232819   359 GTHELGHSVGMRHD------EPYCQS---------KHIMSSSLGPGKVTWS 394
Cdd:pfam13688  141 FAHEIGHNFGAVHDcdsstsSQCCPPsnstcpaggRYIMNPSSSPNSTDFS 191
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 867-889 1.47e-03

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: 37.64  E-value: 1.47e-03
                           10        20
                   ....*....|....*....|...
gi 453232819   867 SLWNEWSDCSRVCGKGLRSRSRS 889
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRT 26
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 711-750 2.51e-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: 37.05  E-value: 2.51e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 453232819   711 WTSCTATCGGGYRKRNRACSITG--------QCEGNE--DETEVCSSESC 750
Cdd:pfam19030    6 WGECSVTCGGGVQTRLVQCVQKGggsivpdsECSAQKkpPETQSCNLKPC 55
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 262-397 4.22e-03

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: 39.04  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453232819  262 PLTFRVIRYEVLTRQpSALAGYLHNHGNA--QMYLDRFC-RYQ-RNLAVRDWDHAIMLTGYDIHRGAGsrsisGIARLDG 337
Cdd:cd00203     2 VIPYVVVADDRDVEE-ENLSAQIQSLILIamQIWRDYLNiRFVlVGVEIDKADIAILVTRQDFDGGTG-----GWAYLGR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453232819  338 MCDPWNTCTLAEglDFTS-----AFIGTHELGHSVGMRHDEPYC-----------------QSKHIMSSSLGPGKVT--- 392
Cdd:cd00203    76 VCDSLRGVGVLQ--DNQSgtkegAQTIAHELGHALGFYHDHDRKdrddyptiddtlnaeddDYYSVMSYTKGSFSDGqrk 153


                  ....*.
gi 453232819  393 -WSTCS 397
Cdd:cd00203   154 dFSQCD 159
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 872-910 4.85e-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: 36.28  E-value: 4.85e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 453232819   872 WSDCSRVCGKGLRSRSRSCF---------GSGCMGAS--SEQQFCNEQAC 910
Cdd:pfam19030    6 WGECSVTCGGGVQTRLVQCVqkgggsivpDSECSAQKkpPETQSCNLKPC 55
PTZ00087 PTZ00087
thrombosponding-related protein; Provisional
 963-1009 5.05e-03

thrombosponding-related protein; Provisional


Pssm-ID: 185438  Cd Length: 340  Bit Score: 40.31  E-value: 5.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 453232819  963 ENKNAAWGGWGYWSSCSETCG--DGVRKRVRKC-YGSGNC-DGQQYEKQYC 1009
Cdd:PTZ00087  227 EKKNMFYTEWGEWSNCSMECDhpDNVQIRERKCaHPSGDCfKGDLKETRPC 277
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 263-372 8.02e-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: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 37.35  E-value: 8.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453232819   263 LTFRVIRYEVLTrqpsaLAGYLHNHGNAQMYLDRFcryqrnlaVRDWDHAIMLTGYDIH---RGAGSRSISGIARLDGMC 339
Cdd:pfam13582   20 IRLQLAAIIITT-----SADTPYTSSDALEILDEL--------QEVNDTRIGQYGYDLGhlfTGRDGGGGGGIAYVGGVC 86

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 453232819   340 DPWNTCTLAEGLD---FTSAFIGTHELGHSVGMRHD 372
Cdd:pfam13582   87 NSGSKFGVNSGSGpvgDTGADTFAHEIGHNFGLNHT 122
 
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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