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Conserved domains on  [gi|1958789092|ref|XP_038934920|]
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ADAMTS-like protein 5 isoform X5 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ADAMTS_spacer1 super family cl20316
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 377-473 2.76e-28

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.


The actual alignment was detected with superfamily member pfam05986:

Pssm-ID: 461796  Cd Length: 115  Bit Score: 109.20  E-value: 2.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789092 377 GYWNVTLIPEGARHIRVTQR--SHNHLALVTRDGHYVLNGDGVLSL-PGTYEAAGTRVVYTRSAGPEETLQATGPTSQEL 453
Cdd:pfam05986  13 GYVTFVTIPAGATHIHIVNRkpSFTHLAVKNVQGKYILNGKGSISLnPTYPSLLGTVLEYRRSLPALEELHAPGPTQEDL 92

                          90       100
                  ....*....|....*....|...
gi 1958789092 454 LLQVLLR---EPNPGVHFEFWLP 473
Cdd:pfam05986  93 EIQVLRQygkGTNPGITYEYFIP 115
NTR_like cd03523
NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in ...
 540-639 5.50e-26

NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in netrins, complement proteins, tissue inhibitors of metalloproteases (TIMP), and procollagen C-proteinase enhancers (PCOLCE), amongst others. In netrins, the domain plays a role in controlling axon branching in neural development, while the common function of these modules in TIMPs appears to be binding to metzincins. A subset of this family is also known as the C345C domain because it occurs as a C-terminal domain in complement C3, C4 and C5. In C5, the domain interacts with various partners during the formation of the membrane attack complex.


:

Pssm-ID: 239600  Cd Length: 105  Bit Score: 102.55  E-value: 5.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789092 540 HYCGSDFVFQARVLGRHRLAQETRYEVRVLLIYKNRSPL----RSREYVWAPGHCPC-PPLAPHREYLLATRRHVSpdgt 614
Cdd:cd03523     2 AFCKSDYVVRAKIKEIKEENDDVKYEVKIIKIYKTGKAKadkaDLRFYYTAPACCPChPILNPGREYLIMGKEEDS---- 77

                          90       100
                  ....*....|....*....|....*
gi 1958789092 615 QDRLLLPQAGYARLWSPAEDSRVRL 639
Cdd:cd03523    78 QGGLVLDPLSFVEPWSPLSLRQDRR 102
ADAMTS_CR_3 super family cl41950
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 263-362 4.39e-13

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: 65.89  E-value: 4.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789092 263 IPFRDLQCSLYNGHPVL---GTQKTYQW---VPFHGAPNLCDLNCLAEGHAFYHSFG-RVLDGTPCTP------GTQGLC 329
Cdd:pfam19236   3 LEFMSQQCARTDGQPLRsspGGASFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGdSFLDGTRCMPsgpredGTLSLC 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958789092 330 VAGRCLSAGCDGLLGSGTLEDRCGLCGGANDSC 362
Cdd:pfam19236  83 VLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 200-246 3.56e-09

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: 52.97  E-value: 3.56e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958789092  200 WTLWGSWSRCSSSCGRGVSVRRRHCVRLPE---EELCWGDSHEYRVCQLP 246
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPqngGGPCTGEDVETRACNEQ 50
 
Name Accession Description Interval E-value
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 377-473 2.76e-28

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: 109.20  E-value: 2.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789092 377 GYWNVTLIPEGARHIRVTQR--SHNHLALVTRDGHYVLNGDGVLSL-PGTYEAAGTRVVYTRSAGPEETLQATGPTSQEL 453
Cdd:pfam05986  13 GYVTFVTIPAGATHIHIVNRkpSFTHLAVKNVQGKYILNGKGSISLnPTYPSLLGTVLEYRRSLPALEELHAPGPTQEDL 92

                          90       100
                  ....*....|....*....|...
gi 1958789092 454 LLQVLLR---EPNPGVHFEFWLP 473
Cdd:pfam05986  93 EIQVLRQygkGTNPGITYEYFIP 115
NTR_like cd03523
NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in ...
 540-639 5.50e-26

NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in netrins, complement proteins, tissue inhibitors of metalloproteases (TIMP), and procollagen C-proteinase enhancers (PCOLCE), amongst others. In netrins, the domain plays a role in controlling axon branching in neural development, while the common function of these modules in TIMPs appears to be binding to metzincins. A subset of this family is also known as the C345C domain because it occurs as a C-terminal domain in complement C3, C4 and C5. In C5, the domain interacts with various partners during the formation of the membrane attack complex.


Pssm-ID: 239600  Cd Length: 105  Bit Score: 102.55  E-value: 5.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789092 540 HYCGSDFVFQARVLGRHRLAQETRYEVRVLLIYKNRSPL----RSREYVWAPGHCPC-PPLAPHREYLLATRRHVSpdgt 614
Cdd:cd03523     2 AFCKSDYVVRAKIKEIKEENDDVKYEVKIIKIYKTGKAKadkaDLRFYYTAPACCPChPILNPGREYLIMGKEEDS---- 77

                          90       100
                  ....*....|....*....|....*
gi 1958789092 615 QDRLLLPQAGYARLWSPAEDSRVRL 639
Cdd:cd03523    78 QGGLVLDPLSFVEPWSPLSLRQDRR 102
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
 540-638 2.85e-18

UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein family members, and hence the existence of the UNC-6 module, was first reported in. Subsequently, many additional members of the family were identified on the basis of sequence similarity between the C-terminal domains of netrins, complement proteins C3, C4, C5, secreted frizzled-related proteins, and type I pro-collagen C-proteinase enhancer proteins (PCOLCEs), which are homologous with the N-terminal domains of tissue inhibitors of metalloproteinases (TIMPs). The TIMPs are classified as a separate family in Pfam (pfam00965). This expanded domain family has been named as the NTR module.


Pssm-ID: 396359  Cd Length: 106  Bit Score: 80.46  E-value: 2.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789092 540 HYC-GSDFVFQARVLGRHRLAQETRYEVRVLLIYK--NRSPLRSREYVWAP-GHCPCPPLAPHREYLLATrrHVSPDGTQ 615
Cdd:pfam01759   2 KACkGSDYVYKVKVLSVEEEGSFDKYTVKVKEVLKegTDKIQRGKVRLFLKrGDCRCPQLRLGKEYLIMG--KVGDLEGR 79

                          90       100
                  ....*....|....*....|...
gi 1958789092 616 DRLLLPQAGYARLWSPAEDSRVR 638
Cdd:pfam01759  80 GRYVLDKNSWVEPWPTKWECKLR 102
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 263-362 4.39e-13

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: 65.89  E-value: 4.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789092 263 IPFRDLQCSLYNGHPVL---GTQKTYQW---VPFHGAPNLCDLNCLAEGHAFYHSFG-RVLDGTPCTP------GTQGLC 329
Cdd:pfam19236   3 LEFMSQQCARTDGQPLRsspGGASFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGdSFLDGTRCMPsgpredGTLSLC 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958789092 330 VAGRCLSAGCDGLLGSGTLEDRCGLCGGANDSC 362
Cdd:pfam19236  83 VLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 200-246 3.56e-09

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: 52.97  E-value: 3.56e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958789092  200 WTLWGSWSRCSSSCGRGVSVRRRHCVRLPE---EELCWGDSHEYRVCQLP 246
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPqngGGPCTGEDVETRACNEQ 50
C345C smart00643
Netrin C-terminal Domain;
540-603 6.12e-06

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 45.44  E-value: 6.12e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958789092  540 HYCGS--DFVFQARVLGRHRLAQETRYEVRVLLIYK-----NRSPLRSREYVWAPGHCPCPP-LAPHREYLL 603
Cdd:smart00643   3 KACKSdvDYVYKVKVLSVEEEGGFDKYTVKILEVIKsgtdeLVRGKNKLRVFISRASCRCPLlLKLGKSYLI 74
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 203-246 2.18e-05

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: 42.27  E-value: 2.18e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958789092 203 WGSWSRCSSSCGRGVSVRRRHCVRLPEE--ELCwGDSHEYRVCQLP 246
Cdd:pfam19028   6 WSEWSECSVTCGGGVQTRTRTVIVEPQNggRPC-PELLERRPCNLP 50
PTZ00087 PTZ00087
thrombosponding-related protein; Provisional
 200-249 1.38e-04

thrombosponding-related protein; Provisional


Pssm-ID: 185438  Cd Length: 340  Bit Score: 44.55  E-value: 1.38e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958789092 200 WTLWGSWSRCSSSCGR--GVSVRRRHCVRlPEEELCWGDSHEYRVCQLPFYP 249
Cdd:PTZ00087  233 YTEWGEWSNCSMECDHpdNVQIRERKCAH-PSGDCFKGDLKETRPCQVPLPP 283
 
Name Accession Description Interval E-value
ADAMTS_spacer1 pfam05986
ADAM-TS Spacer 1; This domain represents the Spacer-1 region from the ADAM-TS and ADAM-TS-like ...
 377-473 2.76e-28

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: 109.20  E-value: 2.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789092 377 GYWNVTLIPEGARHIRVTQR--SHNHLALVTRDGHYVLNGDGVLSL-PGTYEAAGTRVVYTRSAGPEETLQATGPTSQEL 453
Cdd:pfam05986  13 GYVTFVTIPAGATHIHIVNRkpSFTHLAVKNVQGKYILNGKGSISLnPTYPSLLGTVLEYRRSLPALEELHAPGPTQEDL 92

                          90       100
                  ....*....|....*....|...
gi 1958789092 454 LLQVLLR---EPNPGVHFEFWLP 473
Cdd:pfam05986  93 EIQVLRQygkGTNPGITYEYFIP 115
NTR_like cd03523
NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in ...
 540-639 5.50e-26

NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in netrins, complement proteins, tissue inhibitors of metalloproteases (TIMP), and procollagen C-proteinase enhancers (PCOLCE), amongst others. In netrins, the domain plays a role in controlling axon branching in neural development, while the common function of these modules in TIMPs appears to be binding to metzincins. A subset of this family is also known as the C345C domain because it occurs as a C-terminal domain in complement C3, C4 and C5. In C5, the domain interacts with various partners during the formation of the membrane attack complex.


Pssm-ID: 239600  Cd Length: 105  Bit Score: 102.55  E-value: 5.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789092 540 HYCGSDFVFQARVLGRHRLAQETRYEVRVLLIYKNRSPL----RSREYVWAPGHCPC-PPLAPHREYLLATRRHVSpdgt 614
Cdd:cd03523     2 AFCKSDYVVRAKIKEIKEENDDVKYEVKIIKIYKTGKAKadkaDLRFYYTAPACCPChPILNPGREYLIMGKEEDS---- 77

                          90       100
                  ....*....|....*....|....*
gi 1958789092 615 QDRLLLPQAGYARLWSPAEDSRVRL 639
Cdd:cd03523    78 QGGLVLDPLSFVEPWSPLSLRQDRR 102
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
 540-638 2.85e-18

UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein family members, and hence the existence of the UNC-6 module, was first reported in. Subsequently, many additional members of the family were identified on the basis of sequence similarity between the C-terminal domains of netrins, complement proteins C3, C4, C5, secreted frizzled-related proteins, and type I pro-collagen C-proteinase enhancer proteins (PCOLCEs), which are homologous with the N-terminal domains of tissue inhibitors of metalloproteinases (TIMPs). The TIMPs are classified as a separate family in Pfam (pfam00965). This expanded domain family has been named as the NTR module.


Pssm-ID: 396359  Cd Length: 106  Bit Score: 80.46  E-value: 2.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789092 540 HYC-GSDFVFQARVLGRHRLAQETRYEVRVLLIYK--NRSPLRSREYVWAP-GHCPCPPLAPHREYLLATrrHVSPDGTQ 615
Cdd:pfam01759   2 KACkGSDYVYKVKVLSVEEEGSFDKYTVKVKEVLKegTDKIQRGKVRLFLKrGDCRCPQLRLGKEYLIMG--KVGDLEGR 79

                          90       100
                  ....*....|....*....|...
gi 1958789092 616 DRLLLPQAGYARLWSPAEDSRVR 638
Cdd:pfam01759  80 GRYVLDKNSWVEPWPTKWECKLR 102
ADAMTS_CR_3 pfam19236
ADAMTS cysteine-rich domain; This cysteine rich domain is found in a variety of ADAMTS and ...
 263-362 4.39e-13

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: 65.89  E-value: 4.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789092 263 IPFRDLQCSLYNGHPVL---GTQKTYQW---VPFHGAPNLCDLNCLAEGHAFYHSFG-RVLDGTPCTP------GTQGLC 329
Cdd:pfam19236   3 LEFMSQQCARTDGQPLRsspGGASFYHWgaaVPHSQGDALCRHMCRAIGESFIMKRGdSFLDGTRCMPsgpredGTLSLC 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958789092 330 VAGRCLSAGCDGLLGSGTLEDRCGLCGGANDSC 362
Cdd:pfam19236  83 VLGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTC 115
NTR_netrin-1_like cd03579
NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called ...
 538-643 4.16e-12

NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called domain C in the context of C. elegans netrin UNC-6. Netrins are secreted proteins that function as tropic cues in the direction of axon growth and cell migration during neural development. These proteins may be chemoattractive to some neurons and chemorepellant for others. In the case of netrin-1, attraction and repulsion responses are mediated by the DCC and UNC-5 receptor families. The biological activities of C. elegans UNC-6, which may either attract or repel migrating cells or axons, are mediated by its different domains. The C-terminal NTR domain of UNC-6 has been shown to inhibit axon branching activity.


Pssm-ID: 239634  Cd Length: 115  Bit Score: 63.03  E-value: 4.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789092 538 LLHYCGSDFVFQARVLGRHRLAQETRYEVRVLLIYK-NRSPLRSRE-YVWAPGH---CPCPPLAPHREYLLATRRHVSPD 612
Cdd:cd03579     1 LKKYCKKDYAVQAQVLSRETAGEWAKFTVNVQTVYKrGTSRLRRGDqPLWVPRKdlaCKCPKLKVGKSYLLLGKDEDSPE 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958789092 613 gtQDRLLLPQAGYARLWSPAEDSRVRLAARR 643
Cdd:cd03579    81 --RGGLILDKRSLVIEWRDEWARRLRRFQRR 109
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 200-246 3.56e-09

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: 52.97  E-value: 3.56e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958789092  200 WTLWGSWSRCSSSCGRGVSVRRRHCVRLPE---EELCWGDSHEYRVCQLP 246
Cdd:smart00209   1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPqngGGPCTGEDVETRACNEQ 50
C345C smart00643
Netrin C-terminal Domain;
540-603 6.12e-06

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 45.44  E-value: 6.12e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958789092  540 HYCGS--DFVFQARVLGRHRLAQETRYEVRVLLIYK-----NRSPLRSREYVWAPGHCPCPP-LAPHREYLL 603
Cdd:smart00643   3 KACKSdvDYVYKVKVLSVEEEGGFDKYTVKILEVIKsgtdeLVRGKNKLRVFISRASCRCPLlLKLGKSYLI 74
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 203-246 2.18e-05

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: 42.27  E-value: 2.18e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958789092 203 WGSWSRCSSSCGRGVSVRRRHCVRLPEE--ELCwGDSHEYRVCQLP 246
Cdd:pfam19028   6 WSEWSECSVTCGGGVQTRTRTVIVEPQNggRPC-PELLERRPCNLP 50
TSP_1 pfam00090
Thrombospondin type 1 domain;
201-246 2.37e-05

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 42.02  E-value: 2.37e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1958789092 201 TLWGSWSRCSSSCGRGVSVRRRHCV-RLPEEELCWGDSHEYRVCQLP 246
Cdd:pfam00090   1 SPWSPWSPCSVTCGKGIQVRQRTCKsPFPGGEPCTGDDIETQACKMD 47
PTZ00087 PTZ00087
thrombosponding-related protein; Provisional
 200-249 1.38e-04

thrombosponding-related protein; Provisional


Pssm-ID: 185438  Cd Length: 340  Bit Score: 44.55  E-value: 1.38e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958789092 200 WTLWGSWSRCSSSCGR--GVSVRRRHCVRlPEEELCWGDSHEYRVCQLPFYP 249
Cdd:PTZ00087  233 YTEWGEWSNCSMECDHpdNVQIRERKCAH-PSGDCFKGDLKETRPCQVPLPP 283
NTR_TIMP_like cd03577
NTR domain, TIMP-like subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ...
 540-606 9.23e-04

NTR domain, TIMP-like subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential regulators of extracellular matrix turnover and remodeling. They form complexes with matrix metalloproteases (MMPs) and inactivate them irreversibly by non-covalently binding their active zinc-binding sites. This group contains domains similar to the TIMP NTR domain, which binds MMPs. Members of this group may or may not function as MMP inhibitors.


Pssm-ID: 239632  Cd Length: 116  Bit Score: 39.26  E-value: 9.23e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958789092 540 HYCGSDFVFQARVLGRHRLAQ--ETRYEVRVLLIYKNRSPLRSREYVWAPGHCP-C-PPLAPHREYLLATR 606
Cdd:cd03577    11 KYCQADFVIKVKVLKKKLDGAglNIRYTIEIKKVYKGSEKSLLPITIYTPSDDSaCgIPLLEGKEYLIAGK 81
NTR_Sfrp1_like cd03580
NTR domain, Secreted frizzled-related protein (Sfrp) 1-like subfamily; composed of proteins ...
 522-608 1.04e-03

NTR domain, Secreted frizzled-related protein (Sfrp) 1-like subfamily; composed of proteins similar to human Sfrp1, Sfrp2 and Sfrp5. Sfrps are soluble proteins containing an NTR domain C-terminal to a cysteine-rich Frizzled domain. They show diverse functions and are thought to work in Wnt signaling indirectly, as modulators or antagonists by binding Wnt ligands, and directly, via the Wnt receptor, Frizzled. They participate in regulating the patterning along the anteroposterior axis in vertebrates. Human Sfrp1 has been found frequently to be downregulated in breast cancer and is associated with disease progression and poor prognosis.


Pssm-ID: 239635  Cd Length: 126  Bit Score: 39.59  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789092 522 PDPCGPCPDSRGRAHRLL-HYCGSDFVFQARVLGRHRLAQETRYEVRVLL-IYKNRSPLRS-----REYVWAPGHCPCPP 594
Cdd:cd03580     1 PKVCPPCENEEESAKTLLdNFCASDFALKVKIKEISYENGDRKVIGEKKKeILKQGPLKKKdlkklVLWLKNGANCPCPQ 80

                          90
                  ....*....|....*
gi 1958789092 595 LAPHRE-YLLATRRH 608
Cdd:cd03580    81 LDNLNGvYLVMGRKV 95
NTR_complement_C345C cd03574
NTR/C345C domain; The NTR domains that are found in the C-termini of complement C3, C4 and C5, ...
 525-603 1.16e-03

NTR/C345C domain; The NTR domains that are found in the C-termini of complement C3, C4 and C5, are also called C345C domains. In C5, the domain interacts with various partners during the formation of the membrane attack complex, a fundamental process in the mammalian defense against infection. It's role in component C3 and C4 is not well understood.


Pssm-ID: 239629  Cd Length: 147  Bit Score: 39.68  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789092 525 CGPC--PDSRGRAHRLLHYCGS-DFVFQARVLGRHRLAQETRYEVRVLLIYK----NRSPLRSREYVWAPGHCPCPP-LA 596
Cdd:cd03574     1 CPICkrELSDTCENLLDKACTSvDYVYKVKVTSVEEEAGFRIYKARVTEVIKsgsdDVQNGNARRTFIIRESCDCPLrLK 80


                  ....*..
gi 1958789092 597 PHREYLL 603
Cdd:cd03574    81 EGRHYLI 87
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 204-246 1.81e-03

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


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 37.05  E-value: 1.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958789092 204 GSWSRCSSSCGRGVSVRRRHCVR-----LPEEELCWGDS--HEYRVCQLP 246
Cdd:pfam19030   4 GPWGECSVTCGGGVQTRLVQCVQkgggsIVPDSECSAQKkpPETQSCNLK 53
NTR_Sfrp3_like cd03581
NTR domain, Secreted frizzled-related protein (Sfrp) 3-like subfamily; composed of proteins ...
 546-629 5.80e-03

NTR domain, Secreted frizzled-related protein (Sfrp) 3-like subfamily; composed of proteins similar to human Sfrp3 and Sfrp4. Sfrps are soluble proteins containing an NTR domain C-terminal to a cysteine-rich Frizzled domain. They show diverse functions and are thought to work in Wnt signaling indirectly, as modulators or antagonists by binding Wnt ligands, and directly, via the Wnt receptor, Frizzled. They participate in regulating the patterning along the anteroposterior axis in vertebrates. Human Sfrp3 may suppress the growth and invasiveness of androgen-independent prostate cancer cells.


Pssm-ID: 239636  Cd Length: 111  Bit Score: 37.06  E-value: 5.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789092 546 FVFQARVLGRHRLAQETRYEVRVLLIYKNRSPLRSREYV--WAPGHCPCPPLAPHREYLLATRRhvspDGTQDRLLLPQA 623
Cdd:cd03581    10 YVIRAKVKEVKRGCHEVTAVVEVKEILKSSLVNIPRDTVtlYTNSGCLCPPLTPNEEYIIMGYE----DEERSRLLLVEG 85


                  ....*.
gi 1958789092 624 GYARLW 629
Cdd:cd03581    86 SLAEKW 91
 
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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