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Conserved domains on  [gi|564364873|ref|XP_006243588|]
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A disintegrin and metalloproteinase with thrombospondin motifs 7 isoform X2 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 223-431 9.18e-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: 357.32  E-value: 9.18e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873  223 KWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLYHDPSIGNPIHITVVRLIILEDEEKDLKITHHADDTLKNFCRWQ 302
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873  303 KNVNMKGDDHPQHHDTAILLTRKDLCaTMNHPCETLGLSHVAGLCHPQLSCSVSEDTGLPLAFTVAHELGHSFGIQHDGT 382
Cdd:cd04273    81 KKLNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 564364873  383 GNDCESIGKRPFIMSPQLLYDRGiPLTWSRCSREYITRFLDRGWGLCLD 431
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 6.01e-37

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: 135.90  E-value: 6.01e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873    34 DIVHPVRVDAGgsflsyelwpRVLRKRDVSAAQASSAFYQLQYQGRELLFNLTTNPYLLAPGFVSEIRRRSNLSNVHIQT 113
Cdd:pfam01562    1 EVVIPVRLDPS----------RRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPV 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564364873   114 SVPTCHLLGDVQDpeLEGGFAAISACDGLRGVFQLSNEDYFIEPLdEVPAQPGHAQPHMVY 174
Cdd:pfam01562   71 QTDHCYYQGHVEG--HPDSSVALSTCSGLRGFIRTENEEYLIEPL-EKYSREEGGHPHVVY 128
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 681-790 1.99e-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: 122.30  E-value: 1.99e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873   681 TVSRTFKEAEGMGYVDVGLIPAGAREILIEEVAEAANFLALRSeDPDKYFLNGGWTIQ-WNGDYQVAGTTFTYTRKGN-W 758
Cdd:pfam05986    1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPaL 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 564364873   759 ETLTSPGPTTEPVWIQLLFQ---ERNPGVHYKYTI 790
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 ...
 446-510 8.42e-25

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


:

Pssm-ID: 465496  Cd Length: 68  Bit Score: 98.96  E-value: 8.42e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564364873   446 PGVLYDVNHQCRLQYGPSSAYCEDV-DNVCYTLWCSVGT--TCHSKMDAAVDGTSCGKNKWCLNGECV 510
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGgsTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 523-575 2.79e-14

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: 68.38  E-value: 2.79e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 564364873    523 WSGWSAWSVCSRSCGVGVRSSERQCTQPVPKNKGKYCVGERKRYRLCNLQACP 575
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1440-1495 4.49e-14

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: 67.86  E-value: 4.49e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 564364873  1440 WVVGPWGQCSAPCGGGVQRRLVKCVNTqTGLAEEDSDLCSHEAWPESSRPCATEDC 1495
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQK-GGGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 805-859 5.91e-14

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: 67.48  E-value: 5.91e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 564364873   805 WHYGPWSKCPVTCGTGVQRQSLYCMEKQAGIVDEGH-CDHLSRPRDRKRkCNEEPC 859
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSeCSAQKKPPETQS-CNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1333-1388 5.17e-12

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: 62.09  E-value: 5.17e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 564364873  1333 WRAGNWSKCSRNCGGGSATRDVQCVDTRDLRPLRPFHCqPGPTKPPTRQLCGTQPC 1388
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSEC-SAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1282-1330 3.30e-10

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: 57.08  E-value: 3.30e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 564364873  1282 WQVGNWSQCSTTCGLGAIWRLVRCSSG------NDEDCTLSSRPQPARHCHLRPC 1330
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKgggsivPDSECSAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 581-679 2.94e-08

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


The actual alignment was detected with superfamily member pfam19236:

Pssm-ID: 437068  Cd Length: 115  Bit Score: 53.56  E-value: 2.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873   581 FRHTQCSQFDSMLYK-----GKLHKW---VPVLNDENPCELHCRPFNYSNREKLRDAVMDGTPCYQGRISRD----ICID 648
Cdd:pfam19236    5 FMSQQCARTDGQPLRsspggASFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDgtlsLCVL 84

                           90       100       110
                   ....*....|....*....|....*....|.
gi 564364873   649 GICKKVGCDFELDSGAEEDRCGVCRGDGSTC 679
Cdd:pfam19236   85 GSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1391-1437 3.45e-08

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: 51.30  E-value: 3.45e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 564364873  1391 WYTSSWRECSEACGGGEQQRLVTCPEPG--------LCEESLRPNNTRPCNTHPC 1437
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggsivpdsECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 863-916 6.98e-08

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: 50.53  E-value: 6.98e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 564364873   863 WWVGDWQPCSRSCGpGGFFRRAVFCTRSVGLDEQRalePSACGHLPRPLAEIPC 916
Cdd:pfam19030    1 WVAGPWGECSVTCG-GGVQTRLVQCVQKGGGSIVP---DSECSAQKKPPETQSC 50
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 1031-1270 1.67e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.49  E-value: 1.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873 1031 GQTVPPHIRPTEPPSDSPvPTAGAPGAEEEGiQGSWSPSPllseashsPPVLLENTPVNPLANFLTEEESPIGAPELGLP 1110
Cdd:PHA03247 2610 GPAPPSPLPPDTHAPDPP-PPSPSPAANEPD-PHPPPTVP--------PPERPRDDPAPGRVSRPRRARRLGRAAQASSP 2679

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873 1111 SVSW-PPASVD--GMVTSVA----PGNPDELLVREDTQSQPSTPWSDRNKLSKDGNPLGPTSPALPKSPF----PTQPSS 1179
Cdd:PHA03247 2680 PQRPrRRAARPtvGSLTSLAdpppPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAtpggPARPAR 2759

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873 1180 PSNSTTQASLSPDAVEVS------TGWNVALDPVLEADLKPVHAPTDPGLLDQIQTPHTEGTQSP-GLLPRPAQETQTNS 1252
Cdd:PHA03247 2760 PPTTAGPPAPAPPAAPAAgpprrlTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPaGPLPPPTSAQPTAP 2839

                         250
                  ....*....|....*...
gi 564364873 1253 SKDPAvqPLQPSLVEDGA 1270
Cdd:PHA03247 2840 PPPPG--PPPPSLPLGGS 2855
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 223-431 9.18e-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: 357.32  E-value: 9.18e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873  223 KWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLYHDPSIGNPIHITVVRLIILEDEEKDLKITHHADDTLKNFCRWQ 302
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873  303 KNVNMKGDDHPQHHDTAILLTRKDLCaTMNHPCETLGLSHVAGLCHPQLSCSVSEDTGLPLAFTVAHELGHSFGIQHDGT 382
Cdd:cd04273    81 KKLNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 564364873  383 GNDCESIGKRPFIMSPQLLYDRGiPLTWSRCSREYITRFLDRGWGLCLD 431
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 6.01e-37

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: 135.90  E-value: 6.01e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873    34 DIVHPVRVDAGgsflsyelwpRVLRKRDVSAAQASSAFYQLQYQGRELLFNLTTNPYLLAPGFVSEIRRRSNLSNVHIQT 113
Cdd:pfam01562    1 EVVIPVRLDPS----------RRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPV 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564364873   114 SVPTCHLLGDVQDpeLEGGFAAISACDGLRGVFQLSNEDYFIEPLdEVPAQPGHAQPHMVY 174
Cdd:pfam01562   71 QTDHCYYQGHVEG--HPDSSVALSTCSGLRGFIRTENEEYLIEPL-EKYSREEGGHPHVVY 128
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 681-790 1.99e-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: 122.30  E-value: 1.99e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873   681 TVSRTFKEAEGMGYVDVGLIPAGAREILIEEVAEAANFLALRSeDPDKYFLNGGWTIQ-WNGDYQVAGTTFTYTRKGN-W 758
Cdd:pfam05986    1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPaL 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 564364873   759 ETLTSPGPTTEPVWIQLLFQ---ERNPGVHYKYTI 790
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFI 114
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 223-434 2.90e-31

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: 122.02  E-value: 2.90e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873   223 KWVETLVVADSKMVEYHGQPQ--VESYVLTIMNMVAGLYhdpsigNPIHITVVrLIILE---DEEKdLKITHHADDTLKN 297
Cdd:pfam01421    1 KYIELFIVVDKQLFQKMGSDTtvVRQRVFQVVNLVNSIY------KELNIRVV-LVGLEiwtDEDK-IDVSGDANDTLRN 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873   298 FCRWQKNVNMKgddhPQHHDTAILLTRKDLCATmnhpceTLGLSHVAGLCHPQLSCSVSED---TGLPLAFTVAHELGHS 374
Cdd:pfam01421   73 FLKWRQEYLKK----RKPHDVAQLLSGVEFGGT------TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHN 142

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873   375 FGIQHDGTGNDCESIGKRPFIMSPQLLYDrgIPLTWSRCSREYITRFLDRGWGLCLDDRP 434
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 ...
 446-510 8.42e-25

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


Pssm-ID: 465496  Cd Length: 68  Bit Score: 98.96  E-value: 8.42e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564364873   446 PGVLYDVNHQCRLQYGPSSAYCEDV-DNVCYTLWCSVGT--TCHSKMDAAVDGTSCGKNKWCLNGECV 510
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGgsTCTTKNLPAADGTPCGNKKWCLNGKCV 68
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 523-575 2.79e-14

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: 68.38  E-value: 2.79e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 564364873    523 WSGWSAWSVCSRSCGVGVRSSERQCTQPVPKNKGKYCVGERKRYRLCNLQACP 575
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1440-1495 4.49e-14

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: 67.86  E-value: 4.49e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 564364873  1440 WVVGPWGQCSAPCGGGVQRRLVKCVNTqTGLAEEDSDLCSHEAWPESSRPCATEDC 1495
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQK-GGGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 805-859 5.91e-14

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: 67.48  E-value: 5.91e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 564364873   805 WHYGPWSKCPVTCGTGVQRQSLYCMEKQAGIVDEGH-CDHLSRPRDRKRkCNEEPC 859
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSeCSAQKKPPETQS-CNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1333-1388 5.17e-12

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: 62.09  E-value: 5.17e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 564364873  1333 WRAGNWSKCSRNCGGGSATRDVQCVDTRDLRPLRPFHCqPGPTKPPTRQLCGTQPC 1388
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSEC-SAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1282-1330 3.30e-10

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: 57.08  E-value: 3.30e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 564364873  1282 WQVGNWSQCSTTCGLGAIWRLVRCSSG------NDEDCTLSSRPQPARHCHLRPC 1330
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKgggsivPDSECSAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 581-679 2.94e-08

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


Pssm-ID: 437068  Cd Length: 115  Bit Score: 53.56  E-value: 2.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873   581 FRHTQCSQFDSMLYK-----GKLHKW---VPVLNDENPCELHCRPFNYSNREKLRDAVMDGTPCYQGRISRD----ICID 648
Cdd:pfam19236    5 FMSQQCARTDGQPLRsspggASFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDgtlsLCVL 84

                           90       100       110
                   ....*....|....*....|....*....|.
gi 564364873   649 GICKKVGCDFELDSGAEEDRCGVCRGDGSTC 679
Cdd:pfam19236   85 GSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1391-1437 3.45e-08

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: 51.30  E-value: 3.45e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 564364873  1391 WYTSSWRECSEACGGGEQQRLVTCPEPG--------LCEESLRPNNTRPCNTHPC 1437
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggsivpdsECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 863-916 6.98e-08

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: 50.53  E-value: 6.98e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 564364873   863 WWVGDWQPCSRSCGpGGFFRRAVFCTRSVGLDEQRalePSACGHLPRPLAEIPC 916
Cdd:pfam19030    1 WVAGPWGECSVTCG-GGVQTRLVQCVQKGGGSIVP---DSECSAQKKPPETQSC 50
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1031-1270 1.67e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.49  E-value: 1.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873 1031 GQTVPPHIRPTEPPSDSPvPTAGAPGAEEEGiQGSWSPSPllseashsPPVLLENTPVNPLANFLTEEESPIGAPELGLP 1110
Cdd:PHA03247 2610 GPAPPSPLPPDTHAPDPP-PPSPSPAANEPD-PHPPPTVP--------PPERPRDDPAPGRVSRPRRARRLGRAAQASSP 2679

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873 1111 SVSW-PPASVD--GMVTSVA----PGNPDELLVREDTQSQPSTPWSDRNKLSKDGNPLGPTSPALPKSPF----PTQPSS 1179
Cdd:PHA03247 2680 PQRPrRRAARPtvGSLTSLAdpppPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAtpggPARPAR 2759

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873 1180 PSNSTTQASLSPDAVEVS------TGWNVALDPVLEADLKPVHAPTDPGLLDQIQTPHTEGTQSP-GLLPRPAQETQTNS 1252
Cdd:PHA03247 2760 PPTTAGPPAPAPPAAPAAgpprrlTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPaGPLPPPTSAQPTAP 2839

                         250
                  ....*....|....*...
gi 564364873 1253 SKDPAvqPLQPSLVEDGA 1270
Cdd:PHA03247 2840 PPPPG--PPPPSLPLGGS 2855
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 805-860 4.61e-06

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: 45.27  E-value: 4.61e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 564364873    805 WHYGPWSKCPVTCGTGVQRQSLYCmEKQAGIVDEGHCDHlsrPRDRKRKCNEEPCP 860
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSC-CSPPPQNGGGPCTG---EDVETRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
524-574 4.69e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 45.10  E-value: 4.69e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 564364873   524 SGWSAWSVCSRSCGVGVRSSERQCTQPVPknKGKYCVGERKRYRLCNLQAC 574
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1437-1496 3.89e-05

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: 42.57  E-value: 3.89e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873   1437 CTQWvvGPWGQCSAPCGGGVQRRLVKCVNtqtGLAEEDSDLCSHEAwpESSRPCATEDCE 1496
Cdd:smart00209    1 WSEW--SEWSPCSVTCGGGVQTRTRSCCS---PPPQNGGGPCTGED--VETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1393-1437 3.77e-03

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 37.18  E-value: 3.77e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 564364873   1393 TSSWRECSEACGGGEQQRLVTC--PEPGLCEESLRPNN--TRPCNTHPC 1437
Cdd:smart00209    4 WSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTGEDveTRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1336-1388 4.29e-03

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 36.80  E-value: 4.29e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 564364873   1336 GNWSKCSRNCGGGSATRDVQCVDtrdlrPLRPFHCQPGPTKPPTRQLCGTQPC 1388
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSCCS-----PPPQNGGGPCTGEDVETRACNEQPC 52
ACR smart00608
ADAM Cysteine-Rich Domain;
477-511 8.88e-03

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 38.11  E-value: 8.88e-03
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 564364873    477 LWCsVGTTCHSKMDAAV----DGTSCGKNKWCLNGECVP 511
Cdd:smart00608   99 LVC-WSLDYHLGTDPDIgmvkDGTKCGPGKVCINGQCVD 136
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 223-431 9.18e-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: 357.32  E-value: 9.18e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873  223 KWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLYHDPSIGNPIHITVVRLIILEDEEKDLKITHHADDTLKNFCRWQ 302
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873  303 KNVNMKGDDHPQHHDTAILLTRKDLCaTMNHPCETLGLSHVAGLCHPQLSCSVSEDTGLPLAFTVAHELGHSFGIQHDGT 382
Cdd:cd04273    81 KKLNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHELGHVLGMPHDGD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 564364873  383 GNDCESIGKRPFIMSPQLLYDRGiPLTWSRCSREYITRFLDRGWGLCLD 431
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 6.01e-37

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: 135.90  E-value: 6.01e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873    34 DIVHPVRVDAGgsflsyelwpRVLRKRDVSAAQASSAFYQLQYQGRELLFNLTTNPYLLAPGFVSEIRRRSNLSNVHIQT 113
Cdd:pfam01562    1 EVVIPVRLDPS----------RRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPV 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564364873   114 SVPTCHLLGDVQDpeLEGGFAAISACDGLRGVFQLSNEDYFIEPLdEVPAQPGHAQPHMVY 174
Cdd:pfam01562   71 QTDHCYYQGHVEG--HPDSSVALSTCSGLRGFIRTENEEYLIEPL-EKYSREEGGHPHVVY 128
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 225-423 4.54e-36

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: 135.63  E-value: 4.54e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873  225 VETLVVADSKMVEYHgQPQVES---YVLTIMNMVAGLYHDPSIGNPIHITVVRLIILEDEEKDLKITHHADDTLKNFCRW 301
Cdd:cd04267     3 IELVVVADHRMVSYF-NSDENIlqaYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873  302 QKNVnmkgddhPQHHDTAILLTRKDLCAtmnhpCETLGLSHVAGLCHPQLSCSVSEDTGLPL--AFTVAHELGHSFGIQH 379
Cdd:cd04267    82 RAEG-------PIRHDNAVLLTAQDFIE-----GDILGLAYVGSMCNPYSSVGVVEDTGFTLltALTMAHELGHNLGAEH 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 564364873  380 DGTGNDCESIGKRP-FIMSPQLlyDRGIPLTWSRCSREYITRFLD 423
Cdd:cd04267   150 DGGDELAFECDGGGnYIMAPVD--SGLNSYRFSQCSIGSIREFLD 192
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 223-430 6.29e-34

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: 129.66  E-value: 6.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873  223 KWVETLVVADSKMVEYHGQ--PQVESYVLTIMNMVAGLYHdpsignPIHITVVrLIILE---DEEKdLKITHHADDTLKN 297
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSnlSKVRQRVIEIVNIVDSIYR------PLNIRVV-LVGLEiwtDKDK-ISVSGDAGETLNR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873  298 FCRWQKNVNmkgdDHPQHHDTAILLTRKDLCATmnhpceTLGLSHVAGLCHPQLSCSVSEDTG---LPLAFTVAHELGHS 374
Cdd:cd04269    73 FLDWKRSNL----LPRKPHDNAQLLTGRDFDGN------TVGLAYVGGMCSPKYSGGVVQDHSrnlLLFAVTMAHELGHN 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564364873  375 FGIQHDGTGNDCESigkRPFIMSPQLLYdrgIPLTWSRCSREYITRFLDRGWGLCL 430
Cdd:cd04269   143 LGMEHDDGGCTCGR---STCIMAPSPSS---LTDAFSNCSYEDYQKFLSRGGGQCL 192
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 681-790 1.99e-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: 122.30  E-value: 1.99e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873   681 TVSRTFKEAEGMGYVDVGLIPAGAREILIEEVAEAANFLALRSeDPDKYFLNGGWTIQ-WNGDYQVAGTTFTYTRKGN-W 758
Cdd:pfam05986    1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKN-VQGKYILNGKGSISlNPTYPSLLGTVLEYRRSLPaL 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 564364873   759 ETLTSPGPTTEPVWIQLLFQ---ERNPGVHYKYTI 790
Cdd:pfam05986   80 EELHAPGPTQEDLEIQVLRQygkGTNPGITYEYFI 114
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 223-434 2.90e-31

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: 122.02  E-value: 2.90e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873   223 KWVETLVVADSKMVEYHGQPQ--VESYVLTIMNMVAGLYhdpsigNPIHITVVrLIILE---DEEKdLKITHHADDTLKN 297
Cdd:pfam01421    1 KYIELFIVVDKQLFQKMGSDTtvVRQRVFQVVNLVNSIY------KELNIRVV-LVGLEiwtDEDK-IDVSGDANDTLRN 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873   298 FCRWQKNVNMKgddhPQHHDTAILLTRKDLCATmnhpceTLGLSHVAGLCHPQLSCSVSED---TGLPLAFTVAHELGHS 374
Cdd:pfam01421   73 FLKWRQEYLKK----RKPHDVAQLLSGVEFGGT------TVGAAYVGGMCSLEYSGGVNEDhskNLESFAVTMAHELGHN 142

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873   375 FGIQHDGTGNDCESIGKRPFIMSPQLLYDrgIPLTWSRCSREYITRFLDRGWGLCLDDRP 434
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 ...
 446-510 8.42e-25

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


Pssm-ID: 465496  Cd Length: 68  Bit Score: 98.96  E-value: 8.42e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564364873   446 PGVLYDVNHQCRLQYGPSSAYCEDV-DNVCYTLWCSVGT--TCHSKMDAAVDGTSCGKNKWCLNGECV 510
Cdd:pfam17771    1 PGQLYSADEQCRLIFGPGSTFCPNGdEDVCSKLWCSNPGgsTCTTKNLPAADGTPCGNKKWCLNGKCV 68
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 225-430 6.43e-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: 6.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873  225 VETLVVADSKMVEYHGQ-PQVESYVLTIMNMVAGLYHDpsIGNP-IHITVVRLIILEDEEKDLKITHHADD------TLK 296
Cdd:cd04272     3 PELFVVVDYDHQSEFFSnEQLIRYLAVMVNAANLRYRD--LKSPrIRLLLVGITISKDPDFEPYIHPINYGyidaaeTLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873  297 NFcrwqkNVNMKGDDHPQHHDTAILLTRKDLCATMNHPCET--LGLSHVAGLCHpQLSCSVSEDTGLPL--AFTVAHELG 372
Cdd:cd04272    81 NF-----NEYVKKKRDYFNPDVVFLVTGLDMSTYSGGSLQTgtGGYAYVGGACT-ENRVAMGEDTPGSYygVYTMTHELA 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873  373 HSFGIQHDGTGnDCESIGKRP----------FIMSpqllYDRGIP--LTWSRCSREYITRFLDRGWGLCL 430
Cdd:cd04272   155 HLLGAPHDGSP-PPSWVKGHPgsldcpwddgYIMS----YVVNGErqYRFSQCSQRQIRNVFRRLGASCL 219
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 313-422 8.75e-15

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: 73.71  E-value: 8.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873  313 PQHHDTAILLTRKDlcatmnHPCETLGLSHVAGLCHPQLSCSVSEDTGLP---LAFTVAHELGHSFGIQHDGTGNDCESI 389
Cdd:cd00203    49 IDKADIAILVTRQD------FDGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDRKDRDDY 122

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 564364873  390 GKRP-----------FIMSPQLL-YDRGIPLTWSRCSREYITRFL 422
Cdd:cd00203   123 PTIDdtlnaedddyySVMSYTKGsFSDGQRKDFSQCDIDQINKLY 167
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 523-575 2.79e-14

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: 68.38  E-value: 2.79e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 564364873    523 WSGWSAWSVCSRSCGVGVRSSERQCTQPVPKNKGKYCVGERKRYRLCNLQACP 575
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1440-1495 4.49e-14

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: 67.86  E-value: 4.49e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 564364873  1440 WVVGPWGQCSAPCGGGVQRRLVKCVNTqTGLAEEDSDLCSHEAWPESSRPCATEDC 1495
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQK-GGGSIVPDSECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 805-859 5.91e-14

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: 67.48  E-value: 5.91e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 564364873   805 WHYGPWSKCPVTCGTGVQRQSLYCMEKQAGIVDEGH-CDHLSRPRDRKRkCNEEPC 859
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSeCSAQKKPPETQS-CNLKPC 55
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
221-399 5.25e-13

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 69.37  E-value: 5.25e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873   221 KEKWVETLVVADSKMVEYHGQPQVESYVLTIMNMVAGLYHDPSignPIHITVVRLIILEDEEKDLKI---THHADDTLKN 297
Cdd:pfam13688    1 STRTVALLVAADCSYVAAFGGDAAQANIINMVNTASNVYERDF---NISLGLVNLTISDSTCPYTPPacsTGDSSDRLSE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873   298 FCRWQKNvnmkgdDHPQHHDTAILLTRKDlcatmnhpCETLGLSHVAGLCHPQLSCSVSEDTGLP--------LAFTVAH 369
Cdd:pfam13688   78 FQDFSAW------RGTQNDDLAYLFLMTN--------CSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvstatEWQVFAH 143

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 564364873   370 ELGHSFGIQHDGT----------GNDCESIGKRpFIMSPQ 399
Cdd:pfam13688  144 EIGHNFGAVHDCDsstssqccppSNSTCPAGGR-YIMNPS 182
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1333-1388 5.17e-12

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: 62.09  E-value: 5.17e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 564364873  1333 WRAGNWSKCSRNCGGGSATRDVQCVDTRDLRPLRPFHCqPGPTKPPTRQLCGTQPC 1388
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGGGSIVPDSEC-SAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1282-1330 3.30e-10

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: 57.08  E-value: 3.30e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 564364873  1282 WQVGNWSQCSTTCGLGAIWRLVRCSSG------NDEDCTLSSRPQPARHCHLRPC 1330
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKgggsivPDSECSAQKKPPETQSCNLKPC 55
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 581-679 2.94e-08

ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ADAMTS-like endopeptidases widely spread in animals. It is a well-conserved cysteine-rich sequence containing 10 cysteine residues. ADAM-TS (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) is closely related to the ADAM family (A Disintegrin and Metalloproteinase, pfam08516) and consists of at least 20 members sharing a high degree of sequence similarity and conserved domain organization. Members of the ADAMTS family have been implicated in a range of diseases.


Pssm-ID: 437068  Cd Length: 115  Bit Score: 53.56  E-value: 2.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873   581 FRHTQCSQFDSMLYK-----GKLHKW---VPVLNDENPCELHCRPFNYSNREKLRDAVMDGTPCYQGRISRD----ICID 648
Cdd:pfam19236    5 FMSQQCARTDGQPLRsspggASFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDgtlsLCVL 84

                           90       100       110
                   ....*....|....*....|....*....|.
gi 564364873   649 GICKKVGCDFELDSGAEEDRCGVCRGDGSTC 679
Cdd:pfam19236   85 GSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1391-1437 3.45e-08

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: 51.30  E-value: 3.45e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 564364873  1391 WYTSSWRECSEACGGGEQQRLVTCPEPG--------LCEESLRPNNTRPCNTHPC 1437
Cdd:pfam19030    1 WVAGPWGECSVTCGGGVQTRLVQCVQKGggsivpdsECSAQKKPPETQSCNLKPC 55
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 863-916 6.98e-08

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: 50.53  E-value: 6.98e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 564364873   863 WWVGDWQPCSRSCGpGGFFRRAVFCTRSVGLDEQRalePSACGHLPRPLAEIPC 916
Cdd:pfam19030    1 WVAGPWGECSVTCG-GGVQTRLVQCVQKGGGSIVP---DSECSAQKKPPETQSC 50
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1031-1270 1.67e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.49  E-value: 1.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873 1031 GQTVPPHIRPTEPPSDSPvPTAGAPGAEEEGiQGSWSPSPllseashsPPVLLENTPVNPLANFLTEEESPIGAPELGLP 1110
Cdd:PHA03247 2610 GPAPPSPLPPDTHAPDPP-PPSPSPAANEPD-PHPPPTVP--------PPERPRDDPAPGRVSRPRRARRLGRAAQASSP 2679

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873 1111 SVSW-PPASVD--GMVTSVA----PGNPDELLVREDTQSQPSTPWSDRNKLSKDGNPLGPTSPALPKSPF----PTQPSS 1179
Cdd:PHA03247 2680 PQRPrRRAARPtvGSLTSLAdpppPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAtpggPARPAR 2759

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873 1180 PSNSTTQASLSPDAVEVS------TGWNVALDPVLEADLKPVHAPTDPGLLDQIQTPHTEGTQSP-GLLPRPAQETQTNS 1252
Cdd:PHA03247 2760 PPTTAGPPAPAPPAAPAAgpprrlTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPaGPLPPPTSAQPTAP 2839

                         250
                  ....*....|....*...
gi 564364873 1253 SKDPAvqPLQPSLVEDGA 1270
Cdd:PHA03247 2840 PPPPG--PPPPSLPLGGS 2855
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 805-860 4.61e-06

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: 45.27  E-value: 4.61e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 564364873    805 WHYGPWSKCPVTCGTGVQRQSLYCmEKQAGIVDEGHCDHlsrPRDRKRKCNEEPCP 860
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTRSC-CSPPPQNGGGPCTG---EDVETRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
524-574 4.69e-06

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 45.10  E-value: 4.69e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 564364873   524 SGWSAWSVCSRSCGVGVRSSERQCTQPVPknKGKYCVGERKRYRLCNLQAC 574
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFP--GGEPCTGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 524-574 4.85e-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: 44.96  E-value: 4.85e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 564364873   524 SGWSAWSVCSRSCGVGVRSSERQCTQPvPKNKGKYCVGERKRyRLCNLQAC 574
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVIVE-PQNGGRPCPELLER-RPCNLPPC 52
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 337-419 1.26e-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: 372637  Cd Length: 193  Bit Score: 47.62  E-value: 1.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873   337 TLGLSHVAGLCHPQLSCsVSEDTGLPLAFT-------------VAHELGHSFGIQHDGTG--NDCESI----------GK 391
Cdd:pfam13574   86 ELGLAYVGQICQKGASS-PKTNTGLSTTTNygsfnyptqewdvVAHEVGHNFGATHDCDGsqYASSGCernaatsvcsAN 164

                           90       100
                   ....*....|....*....|....*...
gi 564364873   392 RPFIMSPQllYDRGIPLtWSRCSREYIT 419
Cdd:pfam13574  165 GSFIMNPA--SKSNNDL-FSPCSISLIC 189
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1022-1333 1.28e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873 1022 SHSDLVDIGGQTVPPHIRPTEPPSDSPVPTAGAPGaeeegiqGSWSPSPLLSEASHSPPV-----LLENTPVNPLANFLT 1096
Cdd:PHA03247 2694 SLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAA-------RQASPALPAAPAPPAVPAgpatpGGPARPARPPTTAGP 2766

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873 1097 EEESPIGAPELGLPSVSWPPASVDGMV-TSVAPGNPDEllvrEDTQSQPSTPWSDRNKLSKDGNPLGPTSPALPKSPFPT 1175
Cdd:PHA03247 2767 PAPAPPAAPAAGPPRRLTRPAVASLSEsRESLPSPWDP----ADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPP 2842

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873 1176 QPSSPSNSTTQASLSPdavevstGWNVALDPVLEADLKPVHAPTDPGLLDQIQTPHTEGTQS-------PGLLPRPAQET 1248
Cdd:PHA03247 2843 PGPPPPSLPLGGSVAP-------GGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESfalppdqPERPPQPQAPP 2915

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873 1249 QTNSSKDPAVQPL-QPSLVEDGAP-------TDLLPAKNASWQVGNWSQCSTTCGLGAIWRLvRCSSGNDEDCTLSSRPQ 1320
Cdd:PHA03247 2916 PPQPQPQPPPPPQpQPPPPPPPRPqpplaptTDPAGAGEPSGAVPQPWLGALVPGRVAVPRF-RVPQPAPSREAPASSTP 2994

                         330
                  ....*....|...
gi 564364873 1321 PARHCHLRPCAAW 1333
Cdd:PHA03247 2995 PLTGHSLSRVSSW 3007
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 268-380 2.48e-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: 2.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873   268 IHITVVRLIILED-EEKDLKIThhADDTLKNFCRWqknvNMKGDDHPQHhDTAILLTRKDlcatmnhPCETLGLSHVAGL 346
Cdd:pfam13582   20 IRLQLAAIIITTSaDTPYTSSD--ALEILDELQEV----NDTRIGQYGY-DLGHLFTGRD-------GGGGGGIAYVGGV 85

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 564364873   347 CHPQLSCSVSED---TGLPLAFTVAHELGHSFGIQHD 380
Cdd:pfam13582   86 CNSGSKFGVNSGsgpVGDTGADTFAHEIGHNFGLNHT 122
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1437-1496 3.89e-05

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: 42.57  E-value: 3.89e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873   1437 CTQWvvGPWGQCSAPCGGGVQRRLVKCVNtqtGLAEEDSDLCSHEAwpESSRPCATEDCE 1496
Cdd:smart00209    1 WSEW--SEWSPCSVTCGGGVQTRTRSCCS---PPPQNGGGPCTGED--VETRACNEQPCP 53
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 228-436 4.11e-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: 4.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873  228 LVVADSKMVEYHGQPQVESYVLTIMNMVAG---LYHDPSIGNP----IHITVVRLIIL-EDEEKDLKITHHAddtlKNFC 299
Cdd:cd04270     6 LLVADHRFYKYMGRGEEETTINYLISHIDRvddIYRNTDWDGGgfkgIGFQIKRIRIHtTPDEVDPGNKFYN----KSFP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873  300 RWQKNVNMKGDDHPQHHD---TAILLTRKDLcaTMNhpceTLGLSHVA--------GLCHPQLSCSV----SEDTGLPLA 364
Cdd:cd04270    82 NWGVEKFLVKLLLEQFSDdvcLAHLFTYRDF--DMG----TLGLAYVGsprdnsagGICEKAYYYSNgkkkYLNTGLTTT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873  365 F-------------TVAHELGHSFGIQHDGTGNDC---ESIGKRpFIMSPQLLY-DRGIPLTWSRCSREYITRFLDRGWG 427
Cdd:cd04270   156 VnygkrvptkesdlVTAHELGHNFGSPHDPDIAECapgESQGGN-YIMYARATSgDKENNKKFSPCSKKSISKVLEVKSN 234


                  ....*....
gi 564364873  428 LCLDDRPSK 436
Cdd:cd04270   235 SCFVERSQS 243
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1032-1280 9.71e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 9.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873 1032 QTVPPH---IRPTEP--------PSDSPVPTAG-APGAEEEGIQGSWSPSPLLSEASHSPPVLLENTPvnplANFLTEEE 1099
Cdd:PHA03247 2566 RSVPPPrpaPRPSEPavtsrarrPDAPPQSARPrAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSP----AANEPDPH 2641

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873 1100 SPIGAPELGLPSVSWPPASVDGMVTSVAPGNPdellvredtqSQPSTPwsdrnklskdgnPLGPTSPALPKS-------- 1171
Cdd:PHA03247 2642 PPPTVPPPERPRDDPAPGRVSRPRRARRLGRA----------AQASSP------------PQRPRRRAARPTvgsltsla 2699

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564364873 1172 ---PFPTQPSSPSNSTTQASLSPDAVEVSTGWNVALdPVLEADLKPVHAPTDPGLLDQIQTPHTEGTQSPGLLPRPAQET 1248
Cdd:PHA03247 2700 dppPPPPTPEPAPHALVSATPLPPGPAAARQASPAL-PAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAG 2778

                         250       260       270
                  ....*....|....*....|....*....|..
gi 564364873 1249 QTNSSKDPAVQPLQPSLVEDGAPTDLLPAKNA 1280
Cdd:PHA03247 2779 PPRRLTRPAVASLSESRESLPSPWDPADPPAA 2810
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 526-574 1.18e-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: 38.59  E-value: 1.18e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 564364873   526 WSA--WSVCSRSCGVGVRSSERQCTQPVPK--NKGKYCVGERK--RYRLCNLQAC 574
Cdd:pfam19030    1 WVAgpWGECSVTCGGGVQTRLVQCVQKGGGsiVPDSECSAQKKppETQSCNLKPC 55
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 1390-1437 3.01e-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: 37.26  E-value: 3.01e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 564364873  1390 PWytSSWRECSEACGGGEQQR---LVTCPEPG--LCEESLRpnnTRPCNTHPC 1437
Cdd:pfam19028    5 EW--SEWSECSVTCGGGVQTRtrtVIVEPQNGgrPCPELLE---RRPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1393-1437 3.77e-03

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 37.18  E-value: 3.77e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 564364873   1393 TSSWRECSEACGGGEQQRLVTC--PEPGLCEESLRPNN--TRPCNTHPC 1437
Cdd:smart00209    4 WSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTGEDveTRACNEQPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1336-1388 4.29e-03

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 36.80  E-value: 4.29e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 564364873   1336 GNWSKCSRNCGGGSATRDVQCVDtrdlrPLRPFHCQPGPTKPPTRQLCGTQPC 1388
Cdd:smart00209    5 SEWSPCSVTCGGGVQTRTRSCCS-----PPPQNGGGPCTGEDVETRACNEQPC 52
TSP_1 pfam00090
Thrombospondin type 1 domain;
1390-1437 4.67e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 36.63  E-value: 4.67e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 564364873  1390 PWytSSWRECSEACGGGEQQRLVTC----PEPGLCEESLRPnnTRPCNTHPC 1437
Cdd:pfam00090    2 PW--SPWSPCSVTCGKGIQVRQRTCkspfPGGEPCTGDDIE--TQACKMDKC 49
TSP1_CCN pfam19035
CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in ...
 1283-1330 4.69e-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: 36.54  E-value: 4.69e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 564364873  1283 QVGNWSQCSTTCGLGAIwrlVRCSSGNDEdCTLSsrpQPARHCHLRPC 1330
Cdd:pfam19035    4 QSTEWSPCSKTCGMGVS---TRVSNDNAE-CKLV---TETRLCQLRPC 44
ACR smart00608
ADAM Cysteine-Rich Domain;
477-511 8.88e-03

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 38.11  E-value: 8.88e-03
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 564364873    477 LWCsVGTTCHSKMDAAV----DGTSCGKNKWCLNGECVP 511
Cdd:smart00608   99 LVC-WSLDYHLGTDPDIgmvkDGTKCGPGKVCINGQCVD 136
 
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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