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Conserved domains on  [gi|1958650793|ref|XP_038950266|]
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A disintegrin and metalloproteinase with thrombospondin motifs 17 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) ...
 230-447 7.42e-91

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: 286.44  E-value: 7.42e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 230 HTVETLVVADADMVQYHGAEAAQRFILTVMNMVYNMFQHQSLGIKINIQVTKLVLLRQRPAKLSIGHHGERSLESFCHWQ 309
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 310 NEeyggarylgnnQVPGGKDDTPPVDAAVFVTRTDFCvHKDEPCDTVGIAYLGGVCSAKRKCVLAEDNGLNLAFTIAHEL 389
Cdd:cd04273    81 KK-----------LNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHEL 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958650793 390 GHNLGMNHDDDHSSCAGRS---HIMSGEWvkGRNPSDLSWSSCSRDDLENFLKSKVSTCLL 447
Cdd:cd04273   149 GHVLGMPHDGDGNSCGPEGkdgHIMSPTL--GANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 699-808 1.84e-29

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: 113.06  E-value: 1.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 699 VVKGDFSHSRGTGYIEAVVIPAGARRIRVVEDKPAHSFLALKDSSKRSI-NSDWKIEL-PGEFQIAGTIVRYVRR-GLWE 775
Cdd:pfam05986   1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYIlNGKGSISLnPTYPSLLGTVLEYRRSlPALE 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958650793 776 KFSAKGPTTVPLHLMVL--LFHDQNYGIHYEYTIP 808
Cdd:pfam05986  81 ELHAPGPTQEDLEIQVLrqYGKGTNPGITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 464-531 1.50e-26

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: 103.19  E-value: 1.50e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958650793 464 PGMHYSANEQCQILFGTNATFCKNMEHLMCAGLWCLVEGDTSCKTKLDPPLDGTECGADKWCRAGECV 531
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDEDVCSKLWCSNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 35-179 2.48e-22

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: 93.15  E-value: 2.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793  35 EVVLPRRLRPDdvhlqllpgaaglrqwRRPRaSPGDPRAGPGEraLLLHLPAFGRDLYLQLRRDLRFLSPGFEVEE--AG 112
Cdd:pfam01562   1 EVVIPVRLDPS----------------RRRR-SLASESTYLDT--LSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYylDG 61

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958650793 113 VSGRSGHPA--ELCFYSGQVLGHPGSLVSLSACgaaGGLVGLIQLEQELVFIQPLNNSGGPFSRREHLI 179
Cdd:pfam01562  62 GTGVESPPVqtDHCYYQGHVEGHPDSSVALSTC---SGLRGFIRTENEEYLIEPLEKYSREEGGHPHVV 127
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 544-596 1.51e-17

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


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 77.24  E-value: 1.51e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958650793  544 WSPWSAWSMCSRTCGTGARFRQRKCDNPPPGPGGTHCQGASVEHAACENLPCP 596
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 628-697 7.46e-10

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: 57.41  E-value: 7.46e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958650793 628 DKPCELYCSPLGKESPLLVADRVLDGTPC---GPYET---DLCVYGRCQKIGCDGIIGSAAKEDRCGVCSGDGKTC 697
Cdd:pfam19236  40 DALCRHMCRAIGESFIMKRGDSFLDGTRCmpsGPREDgtlSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS super family cl40597
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 834-886 3.41e-09

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: 53.61  E-value: 3.41e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958650793 834 WEGCSVQCGGGERRTIVSCTRIVNKTTtlVNDSDCPQASRPePQVRRCNSHPC 886
Cdd:pfam19030   6 WGECSVTCGGGVQTRLVQCVQKGGGSI--VPDSECSAQKKP-PETQSCNLKPC 55
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 230-447 7.42e-91

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: 286.44  E-value: 7.42e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 230 HTVETLVVADADMVQYHGAEAAQRFILTVMNMVYNMFQHQSLGIKINIQVTKLVLLRQRPAKLSIGHHGERSLESFCHWQ 309
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 310 NEeyggarylgnnQVPGGKDDTPPVDAAVFVTRTDFCvHKDEPCDTVGIAYLGGVCSAKRKCVLAEDNGLNLAFTIAHEL 389
Cdd:cd04273    81 KK-----------LNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHEL 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958650793 390 GHNLGMNHDDDHSSCAGRS---HIMSGEWvkGRNPSDLSWSSCSRDDLENFLKSKVSTCLL 447
Cdd:cd04273   149 GHVLGMPHDGDGNSCGPEGkdgHIMSPTL--GANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 699-808 1.84e-29

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: 113.06  E-value: 1.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 699 VVKGDFSHSRGTGYIEAVVIPAGARRIRVVEDKPAHSFLALKDSSKRSI-NSDWKIEL-PGEFQIAGTIVRYVRR-GLWE 775
Cdd:pfam05986   1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYIlNGKGSISLnPTYPSLLGTVLEYRRSlPALE 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958650793 776 KFSAKGPTTVPLHLMVL--LFHDQNYGIHYEYTIP 808
Cdd:pfam05986  81 ELHAPGPTQEDLEIQVLrqYGKGTNPGITYEYFIP 115
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 464-531 1.50e-26

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: 103.19  E-value: 1.50e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958650793 464 PGMHYSANEQCQILFGTNATFCKNMEHLMCAGLWCLVEGDTSCKTKLDPPLDGTECGADKWCRAGECV 531
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDEDVCSKLWCSNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 232-447 1.66e-24

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: 101.99  E-value: 1.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 232 VETLVVADADMVQYHGA--EAAQRFILTVMNMVYNMFQhqslgiKINIQVTkLVllrqrpaKLSIGHHGER--------- 300
Cdd:pfam01421   3 IELFIVVDKQLFQKMGSdtTVVRQRVFQVVNLVNSIYK------ELNIRVV-LV-------GLEIWTDEDKidvsgdand 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 301 SLESFCHWQnEEYGGARYlgnnqvpggkddtpPVDAAVFVTRTDFcvhkdePCDTVGIAYLGGVCSAKRKCVLAEDNGLN 380
Cdd:pfam01421  69 TLRNFLKWR-QEYLKKRK--------------PHDVAQLLSGVEF------GGTTVGAAYVGGMCSLEYSGGVNEDHSKN 127

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958650793 381 ---LAFTIAHELGHNLGMNHDDDHSSC---AGRSHIMSGEWVKgrnPSDLSWSSCSRDDLENFLKSKVSTCLL 447
Cdd:pfam01421 128 lesFAVTMAHELGHNLGMQHDDFNGGCkcpPGGGCIMNPSAGS---SFPRKFSNCSQEDFEQFLTKQKGACLF 197
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 35-179 2.48e-22

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: 93.15  E-value: 2.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793  35 EVVLPRRLRPDdvhlqllpgaaglrqwRRPRaSPGDPRAGPGEraLLLHLPAFGRDLYLQLRRDLRFLSPGFEVEE--AG 112
Cdd:pfam01562   1 EVVIPVRLDPS----------------RRRR-SLASESTYLDT--LSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYylDG 61

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958650793 113 VSGRSGHPA--ELCFYSGQVLGHPGSLVSLSACgaaGGLVGLIQLEQELVFIQPLNNSGGPFSRREHLI 179
Cdd:pfam01562  62 GTGVESPPVqtDHCYYQGHVEGHPDSSVALSTC---SGLRGFIRTENEEYLIEPLEKYSREEGGHPHVV 127
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 544-596 1.51e-17

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 77.24  E-value: 1.51e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958650793  544 WSPWSAWSMCSRTCGTGARFRQRKCDNPPPGPGGTHCQGASVEHAACENLPCP 596
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
545-595 8.30e-11

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 57.81  E-value: 8.30e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958650793 545 SPWSAWSMCSRTCGTGARFRQRKCDNPPpgPGGTHCQGASVEHAACENLPC 595
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPF--PGGEPCTGDDIETQACKMDKC 49
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 628-697 7.46e-10

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: 57.41  E-value: 7.46e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958650793 628 DKPCELYCSPLGKESPLLVADRVLDGTPC---GPYET---DLCVYGRCQKIGCDGIIGSAAKEDRCGVCSGDGKTC 697
Cdd:pfam19236  40 DALCRHMCRAIGESFIMKRGDSFLDGTRCmpsGPREDgtlSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 834-886 3.41e-09

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: 53.61  E-value: 3.41e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958650793 834 WEGCSVQCGGGERRTIVSCTRIVNKTTtlVNDSDCPQASRPePQVRRCNSHPC 886
Cdd:pfam19030   6 WGECSVTCGGGVQTRLVQCVQKGGGSI--VPDSECSAQKKP-PETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 832-886 4.93e-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: 36.03  E-value: 4.93e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958650793  832 SGWEGCSVQCGGGERRTIVSCTRIVNKtttlVNDSDCPqasRPEPQVRRCNSHPC 886
Cdd:smart00209   5 SEWSPCSVTCGGGVQTRTRSCCSPPPQ----NGGGPCT---GEDVETRACNEQPC 52
 
Name Accession Description Interval E-value
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 230-447 7.42e-91

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: 286.44  E-value: 7.42e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 230 HTVETLVVADADMVQYHGAEAAQRFILTVMNMVYNMFQHQSLGIKINIQVTKLVLLRQRPAKLSIGHHGERSLESFCHWQ 309
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDLEHYILTLMNIVASLYKDPSLGNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFCRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 310 NEeyggarylgnnQVPGGKDDTPPVDAAVFVTRTDFCvHKDEPCDTVGIAYLGGVCSAKRKCVLAEDNGLNLAFTIAHEL 389
Cdd:cd04273    81 KK-----------LNPPNDSDPEHHDHAILLTRQDIC-RSNGNCDTLGLAPVGGMCSPSRSCSINEDTGLSSAFTIAHEL 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958650793 390 GHNLGMNHDDDHSSCAGRS---HIMSGEWvkGRNPSDLSWSSCSRDDLENFLKSKVSTCLL 447
Cdd:cd04273   149 GHVLGMPHDGDGNSCGPEGkdgHIMSPTL--GANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 232-447 1.86e-33

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: 127.35  E-value: 1.86e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 232 VETLVVADADMVQYHG--AEAAQRFILTVMNMVYNMFQhqslgiKINIQVTkLVLL-----RQrpaKLSIGHHGERSLES 304
Cdd:cd04269     3 VELVVVVDNSLYKKYGsnLSKVRQRVIEIVNIVDSIYR------PLNIRVV-LVGLeiwtdKD---KISVSGDAGETLNR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 305 FCHWQNeeyggaRYLGNNQvpggkddtpPVDAAVFVTRTDFCVHkdepcdTVGIAYLGGVCSAKRKCVLAED---NGLNL 381
Cdd:cd04269    73 FLDWKR------SNLLPRK---------PHDNAQLLTGRDFDGN------TVGLAYVGGMCSPKYSGGVVQDhsrNLLLF 131

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958650793 382 AFTIAHELGHNLGMNHDDDHSSCAGRSHIMSgewvkgRNPSDLS--WSSCSRDDLENFLKSKVSTCLL 447
Cdd:cd04269   132 AVTMAHELGHNLGMEHDDGGCTCGRSTCIMA------PSPSSLTdaFSNCSYEDYQKFLSRGGGQCLL 193
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 699-808 1.84e-29

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: 113.06  E-value: 1.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 699 VVKGDFSHSRGTGYIEAVVIPAGARRIRVVEDKPAHSFLALKDSSKRSI-NSDWKIEL-PGEFQIAGTIVRYVRR-GLWE 775
Cdd:pfam05986   1 TVSGSFTEGRAKGYVTFVTIPAGATHIHIVNRKPSFTHLAVKNVQGKYIlNGKGSISLnPTYPSLLGTVLEYRRSlPALE 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958650793 776 KFSAKGPTTVPLHLMVL--LFHDQNYGIHYEYTIP 808
Cdd:pfam05986  81 ELHAPGPTQEDLEIQVLrqYGKGTNPGITYEYFIP 115
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 231-439 5.27e-27

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: 109.05  E-value: 5.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 231 TVETLVVADADMVQYHGA--EAAQRFILTVMNMVYNMFQHQSLGIKINIQVTKLVLLRQRPAKLSIGHHGERSLESFCHW 308
Cdd:cd04267     2 EIELVVVADHRMVSYFNSdeNILQAYITELINIANSIYRSTNLRLGIRISLEGLQILKGEQFAPPIDSDASNTLNSFSFW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 309 QNEeyGGARylgnnqvpggkddtppVDAAVFVTRTDFcvhkdEPCDTVGIAYLGGVCSAKRKCVLAEDNGLNL--AFTIA 386
Cdd:cd04267    82 RAE--GPIR----------------HDNAVLLTAQDF-----IEGDILGLAYVGSMCNPYSSVGVVEDTGFTLltALTMA 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958650793 387 HELGHNLGMNHDDD----HSSCAGRSHIMSGEWVKGRNpsdLSWSSCSRDDLENFLK 439
Cdd:cd04267   139 HELGHNLGAEHDGGdelaFECDGGGNYIMAPVDSGLNS---YRFSQCSIGSIREFLD 192
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 464-531 1.50e-26

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: 103.19  E-value: 1.50e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958650793 464 PGMHYSANEQCQILFGTNATFCKNMEHLMCAGLWCLVEGDTSCKTKLDPPLDGTECGADKWCRAGECV 531
Cdd:pfam17771   1 PGQLYSADEQCRLIFGPGSTFCPNGDEDVCSKLWCSNPGGSTCTTKNLPAADGTPCGNKKWCLNGKCV 68
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 232-447 1.66e-24

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: 101.99  E-value: 1.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 232 VETLVVADADMVQYHGA--EAAQRFILTVMNMVYNMFQhqslgiKINIQVTkLVllrqrpaKLSIGHHGER--------- 300
Cdd:pfam01421   3 IELFIVVDKQLFQKMGSdtTVVRQRVFQVVNLVNSIYK------ELNIRVV-LV-------GLEIWTDEDKidvsgdand 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 301 SLESFCHWQnEEYGGARYlgnnqvpggkddtpPVDAAVFVTRTDFcvhkdePCDTVGIAYLGGVCSAKRKCVLAEDNGLN 380
Cdd:pfam01421  69 TLRNFLKWR-QEYLKKRK--------------PHDVAQLLSGVEF------GGTTVGAAYVGGMCSLEYSGGVNEDHSKN 127

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958650793 381 ---LAFTIAHELGHNLGMNHDDDHSSC---AGRSHIMSGEWVKgrnPSDLSWSSCSRDDLENFLKSKVSTCLL 447
Cdd:pfam01421 128 lesFAVTMAHELGHNLGMQHDDFNGGCkcpPGGGCIMNPSAGS---SFPRKFSNCSQEDFEQFLTKQKGACLF 197
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 35-179 2.48e-22

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: 93.15  E-value: 2.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793  35 EVVLPRRLRPDdvhlqllpgaaglrqwRRPRaSPGDPRAGPGEraLLLHLPAFGRDLYLQLRRDLRFLSPGFEVEE--AG 112
Cdd:pfam01562   1 EVVIPVRLDPS----------------RRRR-SLASESTYLDT--LSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYylDG 61

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958650793 113 VSGRSGHPA--ELCFYSGQVLGHPGSLVSLSACgaaGGLVGLIQLEQELVFIQPLNNSGGPFSRREHLI 179
Cdd:pfam01562  62 GTGVESPPVqtDHCYYQGHVEGHPDSSVALSTC---SGLRGFIRTENEEYLIEPLEKYSREEGGHPHVV 127
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 544-596 1.51e-17

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


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 77.24  E-value: 1.51e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958650793  544 WSPWSAWSMCSRTCGTGARFRQRKCDNPPPGPGGTHCQGASVEHAACENLPCP 596
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNGGGPCTGEDVETRACNEQPCP 53
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 231-446 1.09e-16

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 80.09  E-value: 1.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 231 TVETLVVADADMVQYHGA-EAAQRFILTVMNMVyNMFQHQSLGIKINIQVTKLVLLRQRPAKLSIGHHGER------SLE 303
Cdd:cd04272     2 YPELFVVVDYDHQSEFFSnEQLIRYLAVMVNAA-NLRYRDLKSPRIRLLLVGITISKDPDFEPYIHPINYGyidaaeTLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 304 SFchwqneeyggarylgnNQVPGGKDDTPPVDAAVFVTRTDFCVHKDEPCDTV--GIAYLGGVCSaKRKCVLAEDNG--L 379
Cdd:cd04272    81 NF----------------NEYVKKKRDYFNPDVVFLVTGLDMSTYSGGSLQTGtgGYAYVGGACT-ENRVAMGEDTPgsY 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958650793 380 NLAFTIAHELGHNLGMNHDDDH--SSCAGRS----------HIMSgeWVKGrNPSDLSWSSCSRDDLENFLKSKVSTCL 446
Cdd:cd04272   144 YGVYTMTHELAHLLGAPHDGSPppSWVKGHPgsldcpwddgYIMS--YVVN-GERQYRFSQCSQRQIRNVFRRLGASCL 219
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 333-438 3.93e-16

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


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 76.79  E-value: 3.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 333 PVDAAVFVTRTDFcvhkdePCDTVGIAYLGGVCSAKRKCVLAEDNGLN---LAFTIAHELGHNLGMNHDDDHSSCA---- 405
Cdd:cd00203    51 KADIAILVTRQDF------DGGTGGWAYLGRVCDSLRGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDRKDRDdypt 124

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958650793 406 ----------GRSHIMSGEWVKGRNPSDLSWSSCSRDDLENFL 438
Cdd:cd00203   125 iddtlnaeddDYYSVMSYTKGSFSDGQRKDFSQCDIDQINKLY 167
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
231-403 3.78e-11

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 63.21  E-value: 3.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 231 TVETLVVADADMVQYHGAEAAQRFILTVMNMVYNMFQHqslgiKINIQVtklvllrqRPAKLSIGHHGERSLESFCHWQN 310
Cdd:pfam13688   4 TVALLVAADCSYVAAFGGDAAQANIINMVNTASNVYER-----DFNISL--------GLVNLTISDSTCPYTPPACSTGD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 311 -----EEYGGARYLGNNQvpggKDDtppvdaAVFVTRtdfcvhkDEPCDTVGIAYLGGVCSAKRKCVLAEDNGLN----- 380
Cdd:pfam13688  71 ssdrlSEFQDFSAWRGTQ----NDD------LAYLFL-------MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvs 133

                         170       180
                  ....*....|....*....|....*.
gi 1958650793 381 ---LAFTIAHELGHNLGMNHDDDHSS 403
Cdd:pfam13688 134 tatEWQVFAHEIGHNFGAVHDCDSST 159
TSP_1 pfam00090
Thrombospondin type 1 domain;
545-595 8.30e-11

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 57.81  E-value: 8.30e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958650793 545 SPWSAWSMCSRTCGTGARFRQRKCDNPPpgPGGTHCQGASVEHAACENLPC 595
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKSPF--PGGEPCTGDDIETQACKMDKC 49
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 628-697 7.46e-10

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: 57.41  E-value: 7.46e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958650793 628 DKPCELYCSPLGKESPLLVADRVLDGTPC---GPYET---DLCVYGRCQKIGCDGIIGSAAKEDRCGVCSGDGKTC 697
Cdd:pfam19236  40 DALCRHMCRAIGESFIMKRGDSFLDGTRCmpsGPREDgtlSLCVLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 255-398 1.24e-09

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


Pssm-ID: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 56.99  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 255 ILTVMNMVYNMFQHQsLGIKINIQVTKLVLLRQRPaklSIGHHGERSLESFCHWQNEEYGGARYlgnnqvpggkddtppv 334
Cdd:pfam13582   3 IVSLVNRANTIYERD-LGIRLQLAAIIITTSADTP---YTSSDALEILDELQEVNDTRIGQYGY---------------- 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958650793 335 DAAVFVTRTDFCvhkdepcDTVGIAYLGGVCSAKRKCVLAED---NGLNLAFTIAHELGHNLGMNHD 398
Cdd:pfam13582  63 DLGHLFTGRDGG-------GGGGIAYVGGVCNSGSKFGVNSGsgpVGDTGADTFAHEIGHNFGLNHT 122
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 834-886 3.41e-09

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: 53.61  E-value: 3.41e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958650793 834 WEGCSVQCGGGERRTIVSCTRIVNKTTtlVNDSDCPQASRPePQVRRCNSHPC 886
Cdd:pfam19030   6 WGECSVTCGGGVQTRLVQCVQKGGGSI--VPDSECSAQKKP-PETQSCNLKPC 55
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 250-408 5.22e-09

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


Pssm-ID: 372637  Cd Length: 193  Bit Score: 56.87  E-value: 5.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 250 AAQRFILTVMNMVYNMFQHQSLGIKINIQVTKLVLLRQrPAKLSighhgerslesfchWQNEEYGGARYLGNN----QVP 325
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEPDDININGGLVNPGEIPATT-SASDS--------------GNNYCNSPTTIVRRLnflsQWR 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 326 GGKDDtppvDAAVFVTRTDFCVhkdepcDTVGIAYLGGVCSAKRKCVlAEDNGLNLAFT-------------IAHELGHN 392
Cdd:pfam13574  67 GEQDY----CLAHLVTMGTFSG------GELGLAYVGQICQKGASSP-KTNTGLSTTTNygsfnyptqewdvVAHEVGHN 135

                         170
                  ....*....|....*.
gi 1958650793 393 LGMNHDDDHSSCAGRS 408
Cdd:pfam13574 136 FGATHDCDGSQYASSG 151
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 545-595 2.18e-08

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


Pssm-ID: 465948  Cd Length: 52  Bit Score: 51.13  E-value: 2.18e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958650793 545 SPWSAWSMCSRTCGTGARFRQRKCDNPPPGpGGTHCqGASVEHAACENLPC 595
Cdd:pfam19028   4 SEWSEWSECSVTCGGGVQTRTRTVIVEPQN-GGRPC-PELLERRPCNLPPC 52
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 384-445 2.85e-07

Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha converting enzyme, releases soluble TNF-alpha from transmembrane pro-TNF-alpha.


Pssm-ID: 239798 [Multi-domain]  Cd Length: 244  Bit Score: 52.76  E-value: 2.85e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958650793 384 TIAHELGHNLGMNHDDDHSSCA-----GRSHIMSGEWVKGRNPSDLSWSSCSRDDLENFLKSKVSTC 445
Cdd:cd04270   170 VTAHELGHNFGSPHDPDIAECApgesqGGNYIMYARATSGDKENNKKFSPCSKKSISKVLEVKSNSC 236
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 332-431 5.90e-04

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


Pssm-ID: 213029  Cd Length: 173  Bit Score: 41.51  E-value: 5.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958650793 332 PPVDAAVFVTRTDFCVHKDEPCdtVGIAYLG---GVCSAKR----KCVLAEDNGLNL---AFTIAHELGHNLGMNHdddh 401
Cdd:cd11375    66 PDADCVLGVTDVDLYEPGLNFV--FGLADGGsgvAVVSTARlrpeFYGLPPDEGLFLerlLKEAVHELGHLFGLDH---- 139

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958650793 402 ssCAGRSHIMSG-----EWVkgRNPSDLsWSSCSR 431
Cdd:cd11375   140 --CPYYACVMNFsnsleETD--RKPPYL-CPVCLR 169
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 355-405 3.97e-03

Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A Disintegrin And Metalloprotease) family of metalloproteases are integral membrane proteases acting on a variety of extracellular targets. They are involved in shedding soluble peptides or proteins from the cell surface. This subfamily contains fungal ADAMs, whose precise function has yet to be determined.


Pssm-ID: 239799 [Multi-domain]  Cd Length: 228  Bit Score: 39.71  E-value: 3.97e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958650793 355 TVGIAYLGGVC----SAKRKCVLAEDNGLNLAFT----IAHELGHNLGMNHDDDHSSCA 405
Cdd:cd04271   111 EVGVAWLGQLCrtgaSDQGNETVAGTNVVVRTSNewqvFAHEIGHTFGAVHDCTSGTCS 169
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 832-886 4.93e-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: 36.03  E-value: 4.93e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958650793  832 SGWEGCSVQCGGGERRTIVSCTRIVNKtttlVNDSDCPqasRPEPQVRRCNSHPC 886
Cdd:smart00209   5 SEWSPCSVTCGGGVQTRTRSCCSPPPQ----NGGGPCT---GEDVETRACNEQPC 52
 
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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