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Conserved domains on  [gi|5902004|ref|NP_008914|]
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matrix metalloproteinase-23 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 87-254 8.19e-68

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


:

Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 211.29  E-value: 8.19e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902004   87 RWDHFNLTYRILSFPRNLlSPRETRRALAAAFRMWSDVSPFSFREVAPEQPSDLRIGFYPINHTDclvsalHHCFDGPTG 166
Cdd:cd04278   1 KWSKTNLTYRILNYPPDL-PRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGD------GYPFDGPGG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902004  167 ELAHAFFP--PHGGIHFDDSEYWVLGPtryswkkGVWLTDLVHVAAHEIGHALGLMHSQHGRALMHLNATLR-GWKALSQ 243
Cdd:cd04278  74 TLAHAFFPggIGGDIHFDDDEQWTLGS-------DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPvPKFKLSQ 146

                       170
                ....*....|.
gi 5902004  244 DELWGLHRLYG 254
Cdd:cd04278 147 DDIRGIQALYG 157
ShKT smart00254
ShK toxin domain; ShK toxin domain
 255-289 1.03e-04

ShK toxin domain; ShK toxin domain


:

Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 39.28  E-value: 1.03e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 5902004     255 CLDRLFVCASWARrGFCDaRRRLMKRLCPSSCDFC 289
Cdd:smart00254   1 CVDRHPDCAAWAK-GFCT-NPFYMKSNCPKTCGFC 33
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 311-373 2.18e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 36.77  E-value: 2.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5902004    311 VPEGRNVTFRC---GqkilHKKGKVYWYKDQEPL--EFSYPGYLALGEAHLSII-ANAVNEGTYTCVVR 373
Cdd:pfam13927  13 VREGETVTLTCeatG----SPPPTITWYKNGEPIssGSTRSRSLSGSNSTLTISnVTRSDAGTYTCVAS 77
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 87-254 8.19e-68

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 211.29  E-value: 8.19e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902004   87 RWDHFNLTYRILSFPRNLlSPRETRRALAAAFRMWSDVSPFSFREVAPEQPSDLRIGFYPINHTDclvsalHHCFDGPTG 166
Cdd:cd04278   1 KWSKTNLTYRILNYPPDL-PRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGD------GYPFDGPGG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902004  167 ELAHAFFP--PHGGIHFDDSEYWVLGPtryswkkGVWLTDLVHVAAHEIGHALGLMHSQHGRALMHLNATLR-GWKALSQ 243
Cdd:cd04278  74 TLAHAFFPggIGGDIHFDDDEQWTLGS-------DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPvPKFKLSQ 146

                       170
                ....*....|.
gi 5902004  244 DELWGLHRLYG 254
Cdd:cd04278 147 DDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 87-254 9.70e-46

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 154.31  E-value: 9.70e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902004     87 RWDHFNLTYRILSFPrNLLSPRETRRALAAAFRMWSDVSPFSFREVaPEQPSDLRIGFYPINHTDCLVsalhhcFDGPTG 166
Cdd:pfam00413   1 KWRKKNLTYRILNYT-PDLPRAEVRRAIRRAFKVWSEVTPLTFTEV-STGEADIMIGFGRGDHGDGYP------FDGPGG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902004    167 ELAHAFFP---PHGGIHFDDSEYWVLGPTRYSwkkGvwlTDLVHVAAHEIGHALGLMHSQHGRALMHlnATLRGWKA--- 240
Cdd:pfam00413  73 VLAHAFFPgpgLGGDIHFDDDETWTVGSDPPH---G---INLFLVAAHEIGHALGLGHSSDPGAIMY--PTYSPLDSkkf 144

                         170
                  ....*....|....*
gi 5902004    241 -LSQDELWGLHRLYG 254
Cdd:pfam00413 145 rLSQDDIKGIQQLYG 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 84-254 6.92e-28

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 106.67  E-value: 6.92e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902004      84 ARLRWDHFNLTYRILSfprNLLSPREtRRALAAAFRMWSDVSPFSFREVAPEQpsDLRIGFYPINHtdclvsalhHCFdg 163
Cdd:smart00235   1 GSKKWPKGTVPYVIDS---SSLSPEE-REAIAKALAEWSDVTCIRFVERTGTA--DIYISFGSGDS---------GCT-- 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902004     164 ptgeLAHAFFPpHGGIHFDDsEYWVLGptryswkkgvwltdlVHVAAHEIGHALGLMHSQH---GRALMHLNAT--LRGW 238
Cdd:smart00235  64 ----LSHAGRP-GGDQHLSL-GNGCIN---------------TGVAAHELGHALGLYHEQSrsdRDNYMYINYTniDTRN 122

                          170
                   ....*....|....*.
gi 5902004     239 KALSQDELWGLHRLYG 254
Cdd:smart00235 123 FDLSEDDSLGIPYDYG 138
ShKT smart00254
ShK toxin domain; ShK toxin domain
 255-289 1.03e-04

ShK toxin domain; ShK toxin domain


Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 39.28  E-value: 1.03e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 5902004     255 CLDRLFVCASWARrGFCDaRRRLMKRLCPSSCDFC 289
Cdd:smart00254   1 CVDRHPDCAAWAK-GFCT-NPFYMKSNCPKTCGFC 33
ShK pfam01549
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 ...
 254-289 2.06e-04

ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 amino acids long and rich in cysteine residues. There are 6 conserved cysteine positions in the domain that form three disulphide bridges. The domain is found in the potassium channel inhibitor ShK in sea anemone.


Pssm-ID: 426319  Cd Length: 37  Bit Score: 38.53  E-value: 2.06e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 5902004    254 GCLDRLFVCASWARRGfCDAR--RRLMKRLCPSSCDFC 289
Cdd:pfam01549   1 SCVDPHSDCASWAALG-CTSPfyQDFMKENCPKTCGFC 37
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 311-373 2.18e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 36.77  E-value: 2.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5902004    311 VPEGRNVTFRC---GqkilHKKGKVYWYKDQEPL--EFSYPGYLALGEAHLSII-ANAVNEGTYTCVVR 373
Cdd:pfam13927  13 VREGETVTLTCeatG----SPPPTITWYKNGEPIssGSTRSRSLSGSNSTLTISnVTRSDAGTYTCVAS 77
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 317-373 2.97e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 36.15  E-value: 2.97e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5902004  317 VTFRC---GqkilHKKGKVYWYKDQEPLEFS--YPGYLALGEAHLSII-ANAVNEGTYTCVVR 373
Cdd:cd00096   1 VTLTCsasG----NPPPTITWYKNGKPLPPSsrDSRRSELGNGTLTISnVTLEDSGTYTCVAS 59
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 87-254 8.19e-68

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 211.29  E-value: 8.19e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902004   87 RWDHFNLTYRILSFPRNLlSPRETRRALAAAFRMWSDVSPFSFREVAPEQPSDLRIGFYPINHTDclvsalHHCFDGPTG 166
Cdd:cd04278   1 KWSKTNLTYRILNYPPDL-PRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGD------GYPFDGPGG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902004  167 ELAHAFFP--PHGGIHFDDSEYWVLGPtryswkkGVWLTDLVHVAAHEIGHALGLMHSQHGRALMHLNATLR-GWKALSQ 243
Cdd:cd04278  74 TLAHAFFPggIGGDIHFDDDEQWTLGS-------DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPvPKFKLSQ 146

                       170
                ....*....|.
gi 5902004  244 DELWGLHRLYG 254
Cdd:cd04278 147 DDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 87-254 9.70e-46

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 154.31  E-value: 9.70e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902004     87 RWDHFNLTYRILSFPrNLLSPRETRRALAAAFRMWSDVSPFSFREVaPEQPSDLRIGFYPINHTDCLVsalhhcFDGPTG 166
Cdd:pfam00413   1 KWRKKNLTYRILNYT-PDLPRAEVRRAIRRAFKVWSEVTPLTFTEV-STGEADIMIGFGRGDHGDGYP------FDGPGG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902004    167 ELAHAFFP---PHGGIHFDDSEYWVLGPTRYSwkkGvwlTDLVHVAAHEIGHALGLMHSQHGRALMHlnATLRGWKA--- 240
Cdd:pfam00413  73 VLAHAFFPgpgLGGDIHFDDDETWTVGSDPPH---G---INLFLVAAHEIGHALGLGHSSDPGAIMY--PTYSPLDSkkf 144

                         170
                  ....*....|....*
gi 5902004    241 -LSQDELWGLHRLYG 254
Cdd:pfam00413 145 rLSQDDIKGIQQLYG 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 84-254 6.92e-28

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 106.67  E-value: 6.92e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902004      84 ARLRWDHFNLTYRILSfprNLLSPREtRRALAAAFRMWSDVSPFSFREVAPEQpsDLRIGFYPINHtdclvsalhHCFdg 163
Cdd:smart00235   1 GSKKWPKGTVPYVIDS---SSLSPEE-REAIAKALAEWSDVTCIRFVERTGTA--DIYISFGSGDS---------GCT-- 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902004     164 ptgeLAHAFFPpHGGIHFDDsEYWVLGptryswkkgvwltdlVHVAAHEIGHALGLMHSQH---GRALMHLNAT--LRGW 238
Cdd:smart00235  64 ----LSHAGRP-GGDQHLSL-GNGCIN---------------TGVAAHELGHALGLYHEQSrsdRDNYMYINYTniDTRN 122

                          170
                   ....*....|....*.
gi 5902004     239 KALSQDELWGLHRLYG 254
Cdd:smart00235 123 FDLSEDDSLGIPYDYG 138
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 91-240 1.17e-10

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 59.82  E-value: 1.17e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902004   91 FNLTYRILSfprnlLSPRETRRALAAAFRMWSDVSPFSFREVAPEQPSDLRIGFYPINHTDCLVSALHHCFDGP-TGELA 169
Cdd:cd04268   2 KPITYYIDD-----SVPDKLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYSVIRWIPYNDGTWSYGPSQVDPlTGEIL 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5902004  170 HAFFpphggihfddseywvlgpTRYSWKKGVWLTDLVHVAAHEIGHALGLMHSQHGRALMHLNATLRGWKA 240
Cdd:cd04268  77 LARV------------------YLYSSFVEYSGARLRNTAEHELGHALGLRHNFAASDRDDNVDLLAEKGD 129
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 109-223 4.78e-08

Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 52.42  E-value: 4.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902004  109 ETRRALAAAFRMWSDVSPFSFREVAPEQPSDLRIGFYPinhtdclvsalhhcfDGPTGELAHAFFPPHGG-------IHF 181
Cdd:cd04277  34 AQQAAARDALEAWEDVADIDFVEVSDNSGADIRFGNSS---------------DPDGNTAGYAYYPGSGSgtayggdIWF 98

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 5902004  182 DDSEYwvlgpTRYSWKKGVWLtdlvHVAAHEIGHALGLMHSQ 223
Cdd:cd04277  99 NSSYD-----TNSDSPGSYGY----QTIIHEIGHALGLEHPG 131
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 93-223 5.58e-07

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: 49.06  E-value: 5.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902004   93 LTYRILSFPR---NLLSPRETRRALAAAFRMWSDVSPFSFREVAPE-QPSDLRIGFYpinHTDclvsalhhcFDGPTGel 168
Cdd:cd00203   3 IPYVVVADDRdveEENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEiDKADIAILVT---RQD---------FDGGTG-- 68

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902004  169 AHAFFP----PHGG-IHFDDSEYWvlgpTRYSWKkgvwltdlvhVAAHEIGHALGLMHSQ 223
Cdd:cd00203  69 GWAYLGrvcdSLRGvGVLQDNQSG----TKEGAQ----------TIAHELGHALGFYHDH 114
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 107-248 8.22e-06

Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239803  Cd Length: 197  Bit Score: 46.16  E-value: 8.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902004  107 PRETRRALAAAFRMWS-----DVSPFSFR-EVAPEQ--PSDLRIGFYPINHTDCLVSALHHCFDGP-TGELAHAF-FPPH 176
Cdd:cd04276  19 PEKYRDAIREGVLYWNkafekAGFKNAIIvKVLPDDadPGDIRYNVIRWIHSPNGGWAYGPSVVDPrTGEILKADvILYS 98

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5902004  177 GGIHFDDSEYWVLGPTRYSwkkgvwltdlvHVAAHEIGHALGLMHSQHGRAlMHLNATLRGWKALSQDELWG 248
Cdd:cd04276  99 GFLRQDQLWYEDLLAASLR-----------YLLAHEVGHTLGLRHNFKASS-DGSNEELEDPLGTKEKGATS 158
ShKT smart00254
ShK toxin domain; ShK toxin domain
 255-289 1.03e-04

ShK toxin domain; ShK toxin domain


Pssm-ID: 214586 [Multi-domain]  Cd Length: 33  Bit Score: 39.28  E-value: 1.03e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 5902004     255 CLDRLFVCASWARrGFCDaRRRLMKRLCPSSCDFC 289
Cdd:smart00254   1 CVDRHPDCAAWAK-GFCT-NPFYMKSNCPKTCGFC 33
ShK pfam01549
ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 ...
 254-289 2.06e-04

ShK domain-like; This domain of is found in several C. elegans proteins. The domain is 30 amino acids long and rich in cysteine residues. There are 6 conserved cysteine positions in the domain that form three disulphide bridges. The domain is found in the potassium channel inhibitor ShK in sea anemone.


Pssm-ID: 426319  Cd Length: 37  Bit Score: 38.53  E-value: 2.06e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 5902004    254 GCLDRLFVCASWARRGfCDAR--RRLMKRLCPSSCDFC 289
Cdd:pfam01549   1 SCVDPHSDCASWAALG-CTSPfyQDFMKENCPKTCGFC 37
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 113-254 3.14e-04

Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239806 [Multi-domain]  Cd Length: 156  Bit Score: 40.90  E-value: 3.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902004  113 ALAAAFRMWSDVSPFSFREVAPEQP-SDLRIGFypinHTDCLVsalhhcfDGPTGELAHAFFPPHGGIHFDDSEYW--VL 189
Cdd:cd04279  25 AVKQAAAEWENVGPLKFVYNPEEDNdADIVIFF----DRPPPV-------GGAGGGLARAGFPLISDGNRKLFNRTdiNL 93

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5902004  190 GPTRYSWKKGVWLTdlvhvAAHEIGHALGLMHSQ-HGRALM--HLNATLRGWKALSQDELWGLHRLYG 254
Cdd:cd04279  94 GPGQPRGAENLQAI-----ALHELGHALGLWHHSdRPEDAMypSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 106-227 5.77e-04

Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239819 [Multi-domain]  Cd Length: 198  Bit Score: 40.83  E-value: 5.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5902004  106 SPRETRRALAAAFRMWSDVSPFSFREVAPEqPSDLRIGFYPINH------TDCLVSALHHcfdgPTGELAhaffpphggi 179
Cdd:cd04327  17 PDAFLKDKVRAAAREWLPYANLKFKFVTDA-DADIRISFTPGDGywsyvgTDALLIGADA----PTMNLG---------- 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 5902004  180 hfddseyWVLGPTRYSwkkgvwltDLVHVAAHEIGHALGLMHS-QHGRA 227
Cdd:cd04327  82 -------WFTDDTPDP--------EFSRVVLHEFGHALGFIHEhQSPAA 115
DUF4953 pfam16313
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
 208-221 9.66e-04

Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic met-zincin mmotif HExxHxxGxxH, the extended zinc-binding domain of metallopeptidases.


Pssm-ID: 435269  Cd Length: 319  Bit Score: 40.70  E-value: 9.66e-04
                          10
                  ....*....|....
gi 5902004    208 VAAHEIGHALGLMH 221
Cdd:pfam16313  16 VSAHEVGHTLGLRH 29
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 311-373 2.18e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 36.77  E-value: 2.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5902004    311 VPEGRNVTFRC---GqkilHKKGKVYWYKDQEPL--EFSYPGYLALGEAHLSII-ANAVNEGTYTCVVR 373
Cdd:pfam13927  13 VREGETVTLTCeatG----SPPPTITWYKNGEPIssGSTRSRSLSGSNSTLTISnVTRSDAGTYTCVAS 77
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 317-373 2.97e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 36.15  E-value: 2.97e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5902004  317 VTFRC---GqkilHKKGKVYWYKDQEPLEFS--YPGYLALGEAHLSII-ANAVNEGTYTCVVR 373
Cdd:cd00096   1 VTLTCsasG----NPPPTITWYKNGKPLPPSsrDSRRSELGNGTLTISnVTLEDSGTYTCVAS 59
 
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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