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Conserved domains on  [gi|1907102146|ref|XP_036014600|]
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LIM domain only protein 7 isoform X7 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_LMO7 cd21277
calponin homology (CH) domain found in LIM domain only protein 7; LIM domain only protein 7 ...
14-129 3.67e-74

calponin homology (CH) domain found in LIM domain only protein 7; LIM domain only protein 7 (LMO-7), also called F-box only protein 20, or LOMP, is a transcription regulator for expression of many Emery-Dreifuss muscular dystrophy (EDMD)-relevant genes. It binds to alpha-actinin and AF6/afadin at adherens junctions for epithelial cell-cell adhesion. It contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


:

Pssm-ID: 409126  Cd Length: 116  Bit Score: 242.05  E-value: 3.67e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   14 AFAEAQRWVEAVTEKNFETTDFRASLENGVLLCDLINKLKPGVVKKINRLSTPIAGLDNINVFLRACEQIGLKEAQLFHP 93
Cdd:cd21277      1 AFSEAQRWIEAVTGKNFGNKDFRSALENGVLLCDLINKIKPGIIKKINRLSTPIAGLDNINVFLKACEKLGLKEAQLFHP 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1907102146   94 GDLQDLSNRVTVKQEETDRRLKNVLITLYWLGRKAQ 129
Cdd:cd21277     81 GDLQDLSTRVTVKQEETDRRLKNVLITLYWLGRKAQ 116
DUF4757 pfam15949
Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. ...
655-802 8.39e-43

Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is typically between 145 and 166 amino acids in length. The family is found in association with pfam00412. There are two completely conserved residues (W and L) that may be functionally important.


:

Pssm-ID: 435034  Cd Length: 170  Bit Score: 154.53  E-value: 8.39e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146  655 MLARKIQSWKLGTAVP----------PISFKPGPCSEADLQKWEAIWE-------ASRLRHRKRLMVERLFQKIYGENGS 717
Cdd:pfam15949    1 MSARRTSSSEPKSSVPfnqflpnksnQSSYVPAPLRKKRAEKEEDIRRswvtrtqPSKVAYPPRQFVQRLFQKVSDDLGS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146  718 KSMSDVSAEDV-QNLRQVRYEEMQKIKSQLKEQDQKWQDDLAKWKNRRKSYTSDLQKKKEEREEIEKQALEK----SDRS 792
Cdd:pfam15949   81 KSMSDIRCEEEaQPLSQVRYEELQKIRNQLKEEEDKWQDDLARWKSRRRSASQDLIKKEEERKKIEKLMSGEggdsNRRK 160
                          170
                   ....*....|
gi 1907102146  793 SKTFREMLQD 802
Cdd:pfam15949  161 SKTFKEMVEE 170
DUF4757 super family cl24502
Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. ...
242-304 3.23e-17

Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is typically between 145 and 166 amino acids in length. The family is found in association with pfam00412. There are two completely conserved residues (W and L) that may be functionally important.


The actual alignment was detected with superfamily member pfam15949:

Pssm-ID: 435034  Cd Length: 170  Bit Score: 80.95  E-value: 3.23e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907102146  242 MSYRRISAIEPKSALPFNRFLPNKSKQPSYVPAPLRKKRPDKHEDNRRSW-----ASPVYTETDGTFS 304
Cdd:pfam15949    1 MSARRTSSSEPKSSVPFNQFLPNKSNQSSYVPAPLRKKRAEKEEDIRRSWvtrtqPSKVAYPPRQFVQ 68
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
1114-1183 1.67e-13

PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. Heterodimerization through PDZ-PDZ domain interactions adds to the domain's versatility, and PDZ domain-mediated interactions may be modulated dynamically through target phosphorylation. Some PDZ domains play a role in scaffolding supramolecular complexes. PDZ domains are found in diverse signaling proteins in bacteria, archebacteria, and eurkayotes. This CD contains two distinct structural subgroups with either a N- or C-terminal beta-strand forming the peptide-binding groove base. The circular permutation placing the strand on the N-terminus appears to be found in Eumetazoa only, while the C-terminal variant is found in all three kingdoms of life, and seems to co-occur with protease domains. PDZ domains have been named after PSD95(post synaptic density protein), DlgA (Drosophila disc large tumor suppressor), and ZO1, a mammalian tight junction protein.


:

Pssm-ID: 238080 [Multi-domain]  Cd Length: 70  Bit Score: 66.95  E-value: 1.67e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907102146 1114 PVFGFTIKWDI-SGIFVASVEQGSPAEFSQLQVDDEILAINNTKFSYKDTKKWEEVMANAQEtGNLVMDVR 1183
Cdd:cd00136      1 GGLGFSIRGGTeGGVVVLSVEPGSPAERAGLQAGDVILAVNGTDVKNLTLEDVAELLKKEVG-EKVTLTVR 70
 
Name Accession Description Interval E-value
CH_LMO7 cd21277
calponin homology (CH) domain found in LIM domain only protein 7; LIM domain only protein 7 ...
14-129 3.67e-74

calponin homology (CH) domain found in LIM domain only protein 7; LIM domain only protein 7 (LMO-7), also called F-box only protein 20, or LOMP, is a transcription regulator for expression of many Emery-Dreifuss muscular dystrophy (EDMD)-relevant genes. It binds to alpha-actinin and AF6/afadin at adherens junctions for epithelial cell-cell adhesion. It contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409126  Cd Length: 116  Bit Score: 242.05  E-value: 3.67e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   14 AFAEAQRWVEAVTEKNFETTDFRASLENGVLLCDLINKLKPGVVKKINRLSTPIAGLDNINVFLRACEQIGLKEAQLFHP 93
Cdd:cd21277      1 AFSEAQRWIEAVTGKNFGNKDFRSALENGVLLCDLINKIKPGIIKKINRLSTPIAGLDNINVFLKACEKLGLKEAQLFHP 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1907102146   94 GDLQDLSNRVTVKQEETDRRLKNVLITLYWLGRKAQ 129
Cdd:cd21277     81 GDLQDLSTRVTVKQEETDRRLKNVLITLYWLGRKAQ 116
DUF4757 pfam15949
Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. ...
655-802 8.39e-43

Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is typically between 145 and 166 amino acids in length. The family is found in association with pfam00412. There are two completely conserved residues (W and L) that may be functionally important.


Pssm-ID: 435034  Cd Length: 170  Bit Score: 154.53  E-value: 8.39e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146  655 MLARKIQSWKLGTAVP----------PISFKPGPCSEADLQKWEAIWE-------ASRLRHRKRLMVERLFQKIYGENGS 717
Cdd:pfam15949    1 MSARRTSSSEPKSSVPfnqflpnksnQSSYVPAPLRKKRAEKEEDIRRswvtrtqPSKVAYPPRQFVQRLFQKVSDDLGS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146  718 KSMSDVSAEDV-QNLRQVRYEEMQKIKSQLKEQDQKWQDDLAKWKNRRKSYTSDLQKKKEEREEIEKQALEK----SDRS 792
Cdd:pfam15949   81 KSMSDIRCEEEaQPLSQVRYEELQKIRNQLKEEEDKWQDDLARWKSRRRSASQDLIKKEEERKKIEKLMSGEggdsNRRK 160
                          170
                   ....*....|
gi 1907102146  793 SKTFREMLQD 802
Cdd:pfam15949  161 SKTFKEMVEE 170
DUF4757 pfam15949
Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. ...
242-304 3.23e-17

Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is typically between 145 and 166 amino acids in length. The family is found in association with pfam00412. There are two completely conserved residues (W and L) that may be functionally important.


Pssm-ID: 435034  Cd Length: 170  Bit Score: 80.95  E-value: 3.23e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907102146  242 MSYRRISAIEPKSALPFNRFLPNKSKQPSYVPAPLRKKRPDKHEDNRRSW-----ASPVYTETDGTFS 304
Cdd:pfam15949    1 MSARRTSSSEPKSSVPFNQFLPNKSNQSSYVPAPLRKKRAEKEEDIRRSWvtrtqPSKVAYPPRQFVQ 68
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
1114-1183 1.67e-13

PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. Heterodimerization through PDZ-PDZ domain interactions adds to the domain's versatility, and PDZ domain-mediated interactions may be modulated dynamically through target phosphorylation. Some PDZ domains play a role in scaffolding supramolecular complexes. PDZ domains are found in diverse signaling proteins in bacteria, archebacteria, and eurkayotes. This CD contains two distinct structural subgroups with either a N- or C-terminal beta-strand forming the peptide-binding groove base. The circular permutation placing the strand on the N-terminus appears to be found in Eumetazoa only, while the C-terminal variant is found in all three kingdoms of life, and seems to co-occur with protease domains. PDZ domains have been named after PSD95(post synaptic density protein), DlgA (Drosophila disc large tumor suppressor), and ZO1, a mammalian tight junction protein.


Pssm-ID: 238080 [Multi-domain]  Cd Length: 70  Bit Score: 66.95  E-value: 1.67e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907102146 1114 PVFGFTIKWDI-SGIFVASVEQGSPAEFSQLQVDDEILAINNTKFSYKDTKKWEEVMANAQEtGNLVMDVR 1183
Cdd:cd00136      1 GGLGFSIRGGTeGGVVVLSVEPGSPAERAGLQAGDVILAVNGTDVKNLTLEDVAELLKKEVG-EKVTLTVR 70
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
17-98 1.89e-13

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 67.73  E-value: 1.89e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146    17 EAQRWVEAVTEKNFE--TTDFRASLENGVLLCDLINKLKPGVV--KKINRLSTPIAGLDNINVFLRACEQIGLKEaQLFH 92
Cdd:smart00033    2 TLLRWVNSLLAEYDKppVTNFSSDLKDGVALCALLNSLSPGLVdkKKVAASLSRFKKIENINLALSFAEKLGGKV-VLFE 80

                    ....*.
gi 1907102146    93 PGDLQD 98
Cdd:smart00033   81 PEDLVE 86
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
20-130 3.08e-12

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596  Cd Length: 109  Bit Score: 64.62  E-value: 3.08e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   20 RWVEAVTEKNFET---TDFRASLENGVLLCDLINKLKPGVVKKINRLSTPIAGLDNINVFLRACEQ-IGLKEAQLfhpgD 95
Cdd:pfam00307    9 RWINSHLAEYGPGvrvTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKkLGVPKVLI----E 84
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1907102146   96 LQDLsnrvtvkqeeTDRRLKNVLITLYWLGRKAQS 130
Cdd:pfam00307   85 PEDL----------VEGDNKSVLTYLASLFRRFQA 109
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
1116-1184 3.44e-09

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 55.08  E-value: 3.44e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907102146  1116 FGFTI---KWDISGIFVASVEQGSPAEFSQLQVDDEILAINNTKFSYKDTKkwEEVMANAQETGNLVMDVRR 1184
Cdd:smart00228   14 LGFSLvggKDEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHL--EAVDLLKKAGGKVTLTVLR 83
SCP1 COG5199
Calponin [Cytoskeleton];
17-139 8.24e-07

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 51.07  E-value: 8.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   17 EAQRWVEAVTEKNFETT-DFRASLENGVLLCDLINKLKPGVVKkINRLSTPIAGLDNINVFLRACEQIGLKEAQLFHPGD 95
Cdd:COG5199     17 EVTLWIETVLGEKFEPPgDLLSLLKDGVRLCRILNEASPLDIK-YKESKMPFVQMENISSFINGLKKLRVPEYELFQTND 95
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907102146   96 LQDLSNrvtvkqeetdrrLKNVLITLYWLGRKAQSNPYYNGPYL 139
Cdd:COG5199     96 LFEAKD------------LRQVVICLYSLSRYAQKERMFSGPFL 127
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
1116-1158 1.50e-06

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 47.66  E-value: 1.50e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1907102146 1116 FGFTIK----WDISGIFVASVEQGSPAEFSQLQVDDEILAINNTKFS 1158
Cdd:pfam00595   12 LGFSLKggsdQGDPGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVE 58
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
1085-1184 1.38e-04

periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 46.45  E-value: 1.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146 1085 RGSPLREVSRSLDQFSDmrvsiNQTPGNKPVFGFT-------------IKWDISGIFVASVEQGSPAEFSQLQVDDEILA 1151
Cdd:TIGR02037  314 RKGKEKTITVTLGASPE-----EQASSSNPFLGLTvanlspeirkelrLKGDVKGVVVTKVVSGSPAARAGLQPGDVILS 388
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1907102146 1152 INNTkfSYKDTKKWEEVMANAQETGNLVMDVRR 1184
Cdd:TIGR02037  389 VNQQ--PVSSVAELRKVLARAKKGGRVALLILR 419
 
Name Accession Description Interval E-value
CH_LMO7 cd21277
calponin homology (CH) domain found in LIM domain only protein 7; LIM domain only protein 7 ...
14-129 3.67e-74

calponin homology (CH) domain found in LIM domain only protein 7; LIM domain only protein 7 (LMO-7), also called F-box only protein 20, or LOMP, is a transcription regulator for expression of many Emery-Dreifuss muscular dystrophy (EDMD)-relevant genes. It binds to alpha-actinin and AF6/afadin at adherens junctions for epithelial cell-cell adhesion. It contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409126  Cd Length: 116  Bit Score: 242.05  E-value: 3.67e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   14 AFAEAQRWVEAVTEKNFETTDFRASLENGVLLCDLINKLKPGVVKKINRLSTPIAGLDNINVFLRACEQIGLKEAQLFHP 93
Cdd:cd21277      1 AFSEAQRWIEAVTGKNFGNKDFRSALENGVLLCDLINKIKPGIIKKINRLSTPIAGLDNINVFLKACEKLGLKEAQLFHP 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1907102146   94 GDLQDLSNRVTVKQEETDRRLKNVLITLYWLGRKAQ 129
Cdd:cd21277     81 GDLQDLSTRVTVKQEETDRRLKNVLITLYWLGRKAQ 116
CH_LMO7-like cd21208
calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...
14-129 2.81e-62

calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This family includes LIM domain only protein 7 (LMO-7) and LIM and calponin homology domains-containing protein 1 (LIMCH1), and similar proteins. LMO-7, also called F-box only protein 20, or LOMP, is a transcription regulator for expression of many Emery-Dreifuss muscular dystrophy (EDMD)-relevant genes. It binds to alpha-actinin and AF6/afadin at adherens junctions for epithelial cell-cell adhesion. LIMCH1 acts as an actin stress fiber-associated protein that activates the non-muscle myosin IIa complex by promoting the phosphorylation of its regulatory subunit MRLC/MYL9. It positively regulates actin stress fiber assembly and stabilizes focal adhesions, and therefore negatively regulates cell spreading and cell migration. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409057 [Multi-domain]  Cd Length: 119  Bit Score: 207.96  E-value: 2.81e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   14 AFAEAQRWVEAVTEKNFETTDFRASLENGVLLCDLINKLKPGVVKKINRLSTPIAGLDNINVFLRACEQIGLKEAQLFHP 93
Cdd:cd21208      1 ALKEARTWIEAVTGKKFPSDDFRESLEDGILLCELINAIKPGSIKKINRLPTPIAGLDNLNLFLKACEDLGLKDSQLFDP 80
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907102146   94 GDLQDLSNRVT---VKQEETDRRLKNVLITLYWLGRKAQ 129
Cdd:cd21208     81 TDLQDLSNRRIathVRKKEDERRLKNVAITLYWLGRAAR 119
CH_LIMCH1 cd21278
calponin homology (CH) domain found in LIM and calponin homology domains-containing protein 1; ...
14-130 9.08e-55

calponin homology (CH) domain found in LIM and calponin homology domains-containing protein 1; LIM and calponin homology domains-containing protein 1 (LIMCH1) acts as an actin stress fiber-associated protein that activates the non-muscle myosin IIa complex by promoting the phosphorylation of its regulatory subunit MRLC/MYL9. It positively regulates actin stress fiber assembly and stabilizes focal adhesions, and therefore negatively regulates cell spreading and cell migration. LIMCH1 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409127  Cd Length: 118  Bit Score: 186.61  E-value: 9.08e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   14 AFAEAQRWVEAVTEKNFETTDFRASLENGVLLCDLINKLKPGVVKKINRLSTPIAGLDNINVFLRACEQIGLKEAQLFHP 93
Cdd:cd21278      1 AFTEAQKWIEQVTGRSFGDKDFRSGLENGILLCELLNAIKPGLVKKINRLPTPIAGLDNITLFLRGCKELGLKESQLFDP 80
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907102146   94 GDLQDLSNRVTVKQEETDRRLKNVLITLYWLGRKAQS 130
Cdd:cd21278     81 GDLQDTSNRVTIKSSDCSRKLKNVLITIYWLGKAANS 117
DUF4757 pfam15949
Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. ...
655-802 8.39e-43

Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is typically between 145 and 166 amino acids in length. The family is found in association with pfam00412. There are two completely conserved residues (W and L) that may be functionally important.


Pssm-ID: 435034  Cd Length: 170  Bit Score: 154.53  E-value: 8.39e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146  655 MLARKIQSWKLGTAVP----------PISFKPGPCSEADLQKWEAIWE-------ASRLRHRKRLMVERLFQKIYGENGS 717
Cdd:pfam15949    1 MSARRTSSSEPKSSVPfnqflpnksnQSSYVPAPLRKKRAEKEEDIRRswvtrtqPSKVAYPPRQFVQRLFQKVSDDLGS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146  718 KSMSDVSAEDV-QNLRQVRYEEMQKIKSQLKEQDQKWQDDLAKWKNRRKSYTSDLQKKKEEREEIEKQALEK----SDRS 792
Cdd:pfam15949   81 KSMSDIRCEEEaQPLSQVRYEELQKIRNQLKEEEDKWQDDLARWKSRRRSASQDLIKKEEERKKIEKLMSGEggdsNRRK 160
                          170
                   ....*....|
gi 1907102146  793 SKTFREMLQD 802
Cdd:pfam15949  161 SKTFKEMVEE 170
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
16-126 2.32e-23

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 409031  Cd Length: 103  Bit Score: 96.25  E-value: 2.32e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   16 AEAQRWVEAVTEKNF--ETTDFRASLENGVLLCDLINKLKPGVVKKINRLS-TPIAGLDNINVFLRACEQIGLKEAQLFH 92
Cdd:cd00014      2 EELLKWINEVLGEELpvSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPkSPFKKRENINLFLNACKKLGLPELDLFE 81
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1907102146   93 PGDLQDlsnrvtvkqeetDRRLKNVLITLYWLGR 126
Cdd:cd00014     82 PEDLYE------------KGNLKKVLGTLWALAL 103
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
16-126 4.06e-23

calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 (dMP20) and similar domains; This subfamily contains Drosophila melanogaster muscle-specific protein 20 (dMP20), Echinococcus granulosus myophilin, Dictyostelium discoideum Rac guanine nucleotide exchange factor B (also called Trix), and similar proteins. dMP20 is present only in the synchronous muscles of D. melanogaster. It may be involved in the system linking the nerve impulse with the contraction or the relaxation process. Trix is involved in the regulation of the late steps of the endocytic pathway. dMP20 contains a single copy of the CH domain, while Trix (triple CH-domain array exchange factor) contains three, two type 3 CH domains which are included in this model, and one type 1 CH domain that is not included in this subfamily, but is part of the superfamily. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409056  Cd Length: 107  Bit Score: 95.45  E-value: 4.06e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   16 AEAQRWVEAVTEKNFET-TDFRASLENGVLLCDLINKLKPGVVKKINRLSTPIAGLDNINVFLRACEQIGLKEAQLFHPG 94
Cdd:cd21207      8 AEALDWIEAVTGEKLDDgKDYEDVLKDGVILCKLINILKPGSVKKINTSKMAFKLMENIENFLTACKGYGVPKTDLFQTV 87
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1907102146   95 DLQDLSNrvtvkqeetdrrLKNVLITLYWLGR 126
Cdd:cd21207     88 DLYEKKN------------IPQVTNCLFALGR 107
DUF4757 pfam15949
Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. ...
242-304 3.23e-17

Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is typically between 145 and 166 amino acids in length. The family is found in association with pfam00412. There are two completely conserved residues (W and L) that may be functionally important.


Pssm-ID: 435034  Cd Length: 170  Bit Score: 80.95  E-value: 3.23e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907102146  242 MSYRRISAIEPKSALPFNRFLPNKSKQPSYVPAPLRKKRPDKHEDNRRSW-----ASPVYTETDGTFS 304
Cdd:pfam15949    1 MSARRTSSSEPKSSVPFNQFLPNKSNQSSYVPAPLRKKRAEKEEDIRRSWvtrtqPSKVAYPPRQFVQ 68
CH_SCP1-like cd21210
calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar ...
16-126 3.26e-17

calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar proteins; The family includes transgelins from Saccharomyces cerevisiae and Schizosaccharomyces pombe, which are also called SCP1 and STG1, respectively. Transgelin, also called calponin homolog 1, has actin-binding and actin-bundling activity. It stabilizes actin filaments against disassembly. Transgelin contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409059  Cd Length: 101  Bit Score: 78.56  E-value: 3.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   16 AEAQRWVEAVTEKNFETTDFRASLENGVLLCDLINKLKPGVVKKINRLSTPIAGLDNINVFLRACEQIGLKEAQLFHPGD 95
Cdd:cd21210      3 QEAREWIEEVLGEKLAQGDLLDALKDGVVLCKLANRILPADIRKYKESKMPFVQMENISAFLNAARKLGVPENDLFQTVD 82
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1907102146   96 LQDlsnrvtvkqeetDRRLKNVLITLYWLGR 126
Cdd:cd21210     83 LFE------------RKNPAQVLQCLHALSR 101
CH_CNN cd21211
calponin homology (CH) domain found in the calponin family; Calponin is an actin ...
16-106 7.72e-15

calponin homology (CH) domain found in the calponin family; Calponin is an actin filament-associated regulatory protein expressed in smooth muscle and many types of non-muscle cells. There are three calponin isoforms, calponin-1, -2, -3. All of them are actin-binding proteins with functions in inhibiting actin-activated myosin ATPase and stabilizing the actin cytoskeleton. Calponin-1 is specifically expressed in smooth muscle cells and plays a role in fine-tuning smooth muscle contractility. Calponin-2 is expressed in both smooth muscle and non-muscle cells and regulates multiple actin cytoskeleton-based functions. Calponin-3 is expressed in the brain and participates in actin cytoskeleton-based activities in embryonic development and myogenesis. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409060  Cd Length: 108  Bit Score: 71.96  E-value: 7.72e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   16 AEAQRWVEAVTEKNFeTTDFRASLENGVLLCDLINKLKPGVVKKINRLSTPIAGLDNINVFLRACEQIGLKEAQLFHPGD 95
Cdd:cd21211      6 AELRTWIEGVTGLSI-GPNFQKGLKDGIILCELINKLQPGSVKKINESMQNWHQLENIGNFIKAIVSYGMKPHDIFEAND 84
                           90
                   ....*....|.
gi 1907102146   96 LQDLSNRVTVK 106
Cdd:cd21211     85 LFENGNMTQVQ 95
CH_CNN2 cd21283
calponin homology (CH) domain found in calponin-2; Calponin-2 (CNN2), also called neutral ...
16-106 9.28e-15

calponin homology (CH) domain found in calponin-2; Calponin-2 (CNN2), also called neutral calponin, or smooth muscle calponin H2, is an actin cytoskeleton-associated regulatory protein that inhibits the activity of myosin-ATPase and cytoskeleton dynamics. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409132  Cd Length: 109  Bit Score: 71.89  E-value: 9.28e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   16 AEAQRWVEAVTEKNFeTTDFRASLENGVLLCDLINKLKPGVVKKINRLSTPIAGLDNINVFLRACEQIGLKEAQLFHPGD 95
Cdd:cd21283      6 AELRTWIEGLTGRSI-GPDFQKGLKDGVILCELMNKLQPGSVPKINRSMQNWHQLENLSNFIKAMVSYGMKPVDLFEAND 84
                           90
                   ....*....|.
gi 1907102146   96 LQDLSNRVTVK 106
Cdd:cd21283     85 LFESGNMTQVQ 95
CH_CNN1 cd21282
calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), ...
16-106 3.63e-14

calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), also called basic calponin, or smooth muscle calponin H1, is a thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C, and tropomyosin. Calponin-1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409131  Cd Length: 108  Bit Score: 70.29  E-value: 3.63e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   16 AEAQRWVEAVTEKNFeTTDFRASLENGVLLCDLINKLKPGVVKKINRLSTPIAGLDNINVFLRACEQIGLKEAQLFHPGD 95
Cdd:cd21282      6 EELRVWIEGVTGRRI-GDNFMDGLKDGVILCELINKLQPGSVRKINESTQNWHKLENIGNFIKAIMHYGVKPHDIFEAND 84
                           90
                   ....*....|.
gi 1907102146   96 LQDLSNRVTVK 106
Cdd:cd21282     85 LFENTNHTQVQ 95
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
1114-1183 1.67e-13

PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. Heterodimerization through PDZ-PDZ domain interactions adds to the domain's versatility, and PDZ domain-mediated interactions may be modulated dynamically through target phosphorylation. Some PDZ domains play a role in scaffolding supramolecular complexes. PDZ domains are found in diverse signaling proteins in bacteria, archebacteria, and eurkayotes. This CD contains two distinct structural subgroups with either a N- or C-terminal beta-strand forming the peptide-binding groove base. The circular permutation placing the strand on the N-terminus appears to be found in Eumetazoa only, while the C-terminal variant is found in all three kingdoms of life, and seems to co-occur with protease domains. PDZ domains have been named after PSD95(post synaptic density protein), DlgA (Drosophila disc large tumor suppressor), and ZO1, a mammalian tight junction protein.


Pssm-ID: 238080 [Multi-domain]  Cd Length: 70  Bit Score: 66.95  E-value: 1.67e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907102146 1114 PVFGFTIKWDI-SGIFVASVEQGSPAEFSQLQVDDEILAINNTKFSYKDTKKWEEVMANAQEtGNLVMDVR 1183
Cdd:cd00136      1 GGLGFSIRGGTeGGVVVLSVEPGSPAERAGLQAGDVILAVNGTDVKNLTLEDVAELLKKEVG-EKVTLTVR 70
CH_CNN3 cd21284
calponin homology (CH) domain found in calponin-3; Calponin-3 (CNN3), also called acidic ...
17-106 1.76e-13

calponin homology (CH) domain found in calponin-3; Calponin-3 (CNN3), also called acidic isoform calponin, is an F-actin-binding protein that is expressed in the brain and has been shown to control dendritic spine morphology, density, and plasticity by regulating actin cytoskeletal reorganization and dynamics. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409133  Cd Length: 111  Bit Score: 68.39  E-value: 1.76e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   17 EAQRWVEAVTEKNFeTTDFRASLENGVLLCDLINKLKPGVVKKINRLSTPIAGLDNINVFLRACEQIGLKEAQLFHPGDL 96
Cdd:cd21284      9 ELRNWIEEVTGMSI-GENFQKGLKDGVILCELINKLQPGSIRKINESKLNWHQLENIGNFIKAIQAYGMKPHDIFEANDL 87
                           90
                   ....*....|
gi 1907102146   97 QDLSNRVTVK 106
Cdd:cd21284     88 FENGNMTQVQ 97
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
17-98 1.89e-13

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 67.73  E-value: 1.89e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146    17 EAQRWVEAVTEKNFE--TTDFRASLENGVLLCDLINKLKPGVV--KKINRLSTPIAGLDNINVFLRACEQIGLKEaQLFH 92
Cdd:smart00033    2 TLLRWVNSLLAEYDKppVTNFSSDLKDGVALCALLNSLSPGLVdkKKVAASLSRFKKIENINLALSFAEKLGGKV-VLFE 80

                    ....*.
gi 1907102146    93 PGDLQD 98
Cdd:smart00033   81 PEDLVE 86
CH_IQGAP cd21206
calponin homology (CH) domain found in the IQ motif containing GTPase activating protein ...
16-101 6.79e-13

calponin homology (CH) domain found in the IQ motif containing GTPase activating protein family; Members of the IQ motif containing GTPase activating protein (IQGAP) family are associated with the Ras GTP-binding protein and act as essential regulators of cytoskeletal function. There are three known IQGAP family members: IQGAP1, IQGAP2, and IQGAP3. They are multi-domain molecules having a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeats, a single WW domain, four IQ motifs that mediate interactions with calmodulin, and a RasGAP related domain that binds active Rho family GTPases. IQGAP1 negatively regulates Ras family GTPases by stimulating their intrinsic GTPase activity. It lacks GAP activity. Both IQGAP1 and IQGAP2 specifically bind to Cdc42 and Rac1, but not to RhoA. Despite similarities to part of the sequence of RasGAP, neither IQGAP1 nor IQGAP2 interacts with Ras. IQGAP3 regulates the organization of the cytoskeleton under the regulation of Rac1 and Cdc42 in neuronal cells. The depletion of IQGAP3 is shown to impair neurite or axon outgrowth in neuronal cells with disorganized cytoskeleton.


Pssm-ID: 409055  Cd Length: 118  Bit Score: 66.87  E-value: 6.79e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   16 AEAQRWVEAVTEKNFE-TTDFRASLENGVLLCDLINKLKPGVVKKINrlsTPIAGL-----DNINVFLRACEQIGLKEAQ 89
Cdd:cd21206     11 EEAKQWIEACLNEELPpTTEFEEELRNGVVLAKLANKFAPKLVPLKK---IYDVGLqfrhtDNINHFLRALKKIGLPKIF 87
                           90
                   ....*....|..
gi 1907102146   90 LFHPGDLQDLSN 101
Cdd:cd21206     88 HFETTDLYEKKN 99
CH_VAV cd21201
calponin homology (CH) domain found in VAV proteins; VAV proteins function both as cytoplasmic ...
34-101 1.07e-12

calponin homology (CH) domain found in VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and as scaffold proteins, and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the CH domain, an actin-binding domain which is present as a single copy in VAV proteins.


Pssm-ID: 409050  Cd Length: 117  Bit Score: 66.12  E-value: 1.07e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907102146   34 DFRASLENGVLLCDLINKLKPGVVKKINRLSTP----IAGLDNINVFLRAC-EQIGLKEAQLFHPGDLQDLSN 101
Cdd:cd21201     31 DLAQALRDGVLLCQLLNRLSPGSVDDREINLRPqmsqFLCLKNIRTFLQACrTVFGLRSADLFEPEDLYDVTN 103
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
20-130 3.08e-12

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596  Cd Length: 109  Bit Score: 64.62  E-value: 3.08e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   20 RWVEAVTEKNFET---TDFRASLENGVLLCDLINKLKPGVVKKINRLSTPIAGLDNINVFLRACEQ-IGLKEAQLfhpgD 95
Cdd:pfam00307    9 RWINSHLAEYGPGvrvTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKkLGVPKVLI----E 84
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1907102146   96 LQDLsnrvtvkqeeTDRRLKNVLITLYWLGRKAQS 130
Cdd:pfam00307   85 PEDL----------VEGDNKSVLTYLASLFRRFQA 109
CH_PIX cd21202
calponin homology (CH) domain found in the Pak Interactive eXchange factor family; Pak ...
36-96 6.04e-11

calponin homology (CH) domain found in the Pak Interactive eXchange factor family; Pak Interactive eXchange factor (PIX) proteins are Rho guanine nucleotide exchange factors (GEFs), which activate small GTPases by exchanging bound GDP for free GTP. They act as GEFs for both Cdc42 and Rac1, and have been implicated in cell motility, adhesion, neurite outgrowth, and cell polarity. Vertebrates contain two proteins from the PIX family, alpha-PIX and beta-PIX. Alpha-PIX, also called Rho guanine nucleotide exchange factor 6 (ARHGEF6), is localized in dendritic spines where it regulates spine morphogenesis. It controls dendritic length and spine density in the hippocampus. Mutations in the ARHGEF6 gene cause X-linked intellectual disability in humans. Beta-PIX, also called Rho guanine nucleotide exchange factor 7 (ARHGEF7), plays important roles in regulating neuroendocrine exocytosis, focal adhesion maturation, cell migration, synaptic vesicle localization, and insulin secretion. Both alpha-PIX and beta-PIX contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409051  Cd Length: 114  Bit Score: 61.01  E-value: 6.04e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907102146   36 RASLENGVLLCDLINKLKPGVVKKInrLSTPIAG---LDNINVFLRACEQIGLKEAQLFHPGDL 96
Cdd:cd21202     31 SESLKNGVVLCRLVNRLKPGTVEKI--YDEPTTEeecLYNFESFLKACQELGILAEEIFDPNDL 92
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
1116-1184 3.44e-09

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 55.08  E-value: 3.44e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907102146  1116 FGFTI---KWDISGIFVASVEQGSPAEFSQLQVDDEILAINNTKFSYKDTKkwEEVMANAQETGNLVMDVRR 1184
Cdd:smart00228   14 LGFSLvggKDEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHL--EAVDLLKKAGGKVTLTVLR 83
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
1116-1179 4.14e-08

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 52.18  E-value: 4.14e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907102146 1116 FGFTI---KWDISGIFVASVEQGSPAEFSQLQVDDEILAINNTKFSYKDTKKWEEVMANAQETGNLV 1179
Cdd:cd00992     14 LGFSLrggKDSGGGIFVSRVEPGGPAERGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTLT 80
CH_GAS2-like cd21204
calponin homology (CH) domain found in the growth arrest-specific protein 2 family; The growth ...
20-130 1.23e-07

calponin homology (CH) domain found in the growth arrest-specific protein 2 family; The growth arrest-specific protein 2 (GAS-2) family includes GAS-2, and GAS-2 like proteins, GAS2L1-3. GAS-2 may play a role in apoptosis by acting as a cell death substrate for caspases. GAS2L1 (also called GAS2-related protein on chromosome 22 or growth arrest-specific protein 2-like 1) and GAS2L2 (also called GAS2-related protein on chromosome 17 or growth arrest-specific protein 2-like 2) may be involved in the cross-linking of microtubules and microfilaments. GAS2L3, also called GAS2-like protein 3, is a cytoskeletal linker protein that may promote and stabilize the formation of the actin and microtubule network. Members of this family contain a single copy of the CH domain at the N-terminal region. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409053  Cd Length: 131  Bit Score: 52.27  E-value: 1.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   20 RWVEAVTEKNFETTDFRASLENGVLLCDLINKL--------------KPGVVKKI----NRLSTPIAGLDNINVFLRACE 81
Cdd:cd21204     13 EWLNDLLGDDLTPDNFLDELRNGVVLCQLAQKIqeaaekareagkknGPPPSYKLkcneNAKPGSFFARDNVANFLRWCR 92
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1907102146   82 QIGLKEAQLFHPGDLqdlsnrVTVKQEetdrrlKNVLITLYWLGRKAQS 130
Cdd:cd21204     93 KLGVDEVLLFESEDL------VLHKNP------RQVLLCLLELARIAAR 129
CH_LRCH cd21205
calponin homology (CH) domain found in the leucine-rich repeat and calponin homology ...
34-114 1.63e-07

calponin homology (CH) domain found in the leucine-rich repeat and calponin homology domain-containing protein family; The leucine-rich repeat and calponin homology domain-containing protein (LRCH) family includes LRCH1-4. LRCH1, also called calponin homology domain-containing protein 1, or neuronal protein 81 (NP81), acts as a negative regulator of GTPase Cdc42 by sequestering Cdc42-guanine exchange factor DOCK8. LRCH2 may play a role in the organization of the cytoskeleton. LRCH3 is part of the DISP complex and may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. LRCH4, also called leucine-rich repeat neuronal protein 4, or leucine-rich neuronal protein, acts as a novel Toll-like receptor (TLR) accessory protein that regulates the innate immune response. Members of this family contain a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409054  Cd Length: 107  Bit Score: 51.15  E-value: 1.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   34 DFRASLENGVLLCDLINKLKPGVVKKINRLS------TPIAGLDNINVFLRACEQIGLKEAQLFHPGDLqdLSNRVTVKQ 107
Cdd:cd21205     21 DLGEALMDGVVLCHLANHVRPRSVPSIHVPSpavpklSMAKCRRNVENFLEACRKLGVPEERLCSPGDI--LEEKGLVRV 98

                   ....*..
gi 1907102146  108 EETDRRL 114
Cdd:cd21205     99 AVTVQAL 105
CH_AtKIN14-like cd21203
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ...
34-97 2.03e-07

calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. This family includes a group of kinesin-like proteins belonging to KIN-14 protein family. They all contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409052  Cd Length: 112  Bit Score: 50.88  E-value: 2.03e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907102146   34 DFRASLENGVLLCDLINKLKPGVVKKI--------NRLSTPIAGLDNINVFLRACEQIGLKeaqLFHPGDLQ 97
Cdd:cd21203     25 EFRLCLRDGVVLCKLLNKLQPGAVPKVvespddpdGAAGSAFQYFENVRNFLVAIEEMGLP---TFEASDLE 93
CH_VAV3 cd21264
calponin homology (CH) domain found in VAV3 protein and similar proteins; VAV3 is ubiquitously ...
25-101 5.32e-07

calponin homology (CH) domain found in VAV3 protein and similar proteins; VAV3 is ubiquitously expressed and functions as a phosphorylation-dependent guanine nucleotide exchange factor (GEF) for RhoA, RhoG, and Rac1. Its function has been implicated in the hematopoietic, bone, cerebellar, and cardiovascular systems. VAV3 is essential in axon guidance in neurons that control blood pressure and respiration. It is overexpressed in prostate cancer cells and it plays a role in regulating androgen receptor transcriptional activity. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The model corresponds to CH domain, an actin-binding domain which is present as a single copy in VAV3 protein.


Pssm-ID: 409113  Cd Length: 117  Bit Score: 49.96  E-value: 5.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   25 VTEKNFETTDFRASLENGVLLCDLINKLKPGVV--KKIN---RLSTPIAgLDNINVFLRA-CEQIGLKEAQLFHPGDLQD 98
Cdd:cd21264     22 VTWDTAQVFDLAQTLRDGVLLCQLLNNLRPHSInlKEINlrpQMSQFLC-LKNIRTFLSAcCETFGMRKSELFEAFDLFD 100

                   ...
gi 1907102146   99 LSN 101
Cdd:cd21264    101 VRD 103
SCP1 COG5199
Calponin [Cytoskeleton];
17-139 8.24e-07

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 51.07  E-value: 8.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   17 EAQRWVEAVTEKNFETT-DFRASLENGVLLCDLINKLKPGVVKkINRLSTPIAGLDNINVFLRACEQIGLKEAQLFHPGD 95
Cdd:COG5199     17 EVTLWIETVLGEKFEPPgDLLSLLKDGVRLCRILNEASPLDIK-YKESKMPFVQMENISSFINGLKKLRVPEYELFQTND 95
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907102146   96 LQDLSNrvtvkqeetdrrLKNVLITLYWLGRKAQSNPYYNGPYL 139
Cdd:COG5199     96 LFEAKD------------LRQVVICLYSLSRYAQKERMFSGPFL 127
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
17-102 8.61e-07

Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and chromosome partitioning / Signal transduction mechanisms];


Pssm-ID: 227586 [Multi-domain]  Cd Length: 1054  Bit Score: 54.12  E-value: 8.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   17 EAQRWVEAVTEKNFETTDFRASLENGVLLCDLINKLKPGVVKKINRLST-PIAGLDNINVFLRACEQIGLKEaqLFHpGD 95
Cdd:COG5261     48 EAKIWIEEVIEEALPELCFEDSLRNGVFLAKLTQRFNPDLTTVIFPADKlQFRHTDNINAFLDLIEHVGLPE--SFH-FE 124

                   ....*..
gi 1907102146   96 LQDLSNR 102
Cdd:COG5261    125 LQDLYEK 131
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
1116-1158 1.50e-06

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 47.66  E-value: 1.50e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1907102146 1116 FGFTIK----WDISGIFVASVEQGSPAEFSQLQVDDEILAINNTKFS 1158
Cdd:pfam00595   12 LGFSLKggsdQGDPGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVE 58
PDZ_metalloprotease cd00989
PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or ...
1115-1187 1.67e-06

PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or integral membrane proteases, which may be involved in signalling and regulatory mechanisms. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238489 [Multi-domain]  Cd Length: 79  Bit Score: 47.23  E-value: 1.67e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907102146 1115 VFGFTIKWDISGIFVASVEQGSPAEFSQLQVDDEILAINNTKfsykdTKKWEEVMANAQE--TGNLVMDVRRYGK 1187
Cdd:cd00989      2 ILGFVPGGPPIEPVIGEVVPGSPAAKAGLKAGDRILAINGQK-----IKSWEDLVDAVQEnpGKPLTLTVERNGE 71
CH_alphaPIX cd21265
calponin homology (CH) domain found in alpha-Pak Interactive eXchange factor; Alpha-Pak ...
36-96 1.95e-06

calponin homology (CH) domain found in alpha-Pak Interactive eXchange factor; Alpha-Pak Interactive eXchange factor (alpha-PIX), also called PAK-interacting exchange factor alpha, Rho guanine nucleotide exchange factor 6 (ARHGEF6), Rac/Cdc42 guanine nucleotide exchange factor 6, or Cool (Cloned out of Library)-2, activates small GTPases by exchanging bound GDP for free GTP. It acts as a GEF for both Cdc42 and Rac1, and is localized in dendritic spines where it regulates spine morphogenesis. It controls dendritic length and spine density in the hippocampus. Mutations in the ARHGEF6 gene cause X-linked intellectual disability in humans. Alpha-PIX contains a single copy of the CH domain at its N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409114  Cd Length: 117  Bit Score: 48.28  E-value: 1.95e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907102146   36 RASLENGVLLCDLINKLKPGVVKKI-NRLSTPIAGLDNINVFLRACEQIGLkeaQLFHPGDL 96
Cdd:cd21265     32 KSSLKDGVVLCKLIERLLPGSVEKYcLEPKTEADCIGNIKEFLKGCAALKV---ETFEPDDL 90
CH_VAV1 cd21262
calponin homology (CH) domain found in VAV1 protein; VAV1 is expressed predominantly in the ...
25-99 2.78e-06

calponin homology (CH) domain found in VAV1 protein; VAV1 is expressed predominantly in the hematopoietic system and it plays an important role in the development and activation of B and T cells. It is activated by tyrosine phosphorylation to function as a guanine nucleotide exchange factor (GEF) for Rho GTPases following cell surface receptor activation, triggering various effects such as cytoskeletal reorganization, transcription regulation, cell cycle progression, and calcium mobilization. It also serves as a scaffold protein and has been shown to interact with Ku70, Socs1, Janus kinase 2, SIAH2, S100B, Abl gene, ZAP-70, SLP76, and Syk, among others. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the CH domain, an actin-binding domain which is present as a single copy in VAV1 protein.


Pssm-ID: 409111  Cd Length: 120  Bit Score: 48.01  E-value: 2.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   25 VTEKNFETTDFRASLENGVLLCDLINKLKPGVV--KKIN---RLSTPIAgLDNINVFLRAC-EQIGLKEAQLFHPGDLQD 98
Cdd:cd21262     22 VTWDSAQVCDLAQALRDGVLLCQLLNNLLPHAVnlREINlrpQMSQFLC-LKNIRTFLSTCcEKFGLRKSELFEAFDLFD 100

                   .
gi 1907102146   99 L 99
Cdd:cd21262    101 V 101
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
34-86 3.05e-06

first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409066  Cd Length: 114  Bit Score: 47.57  E-value: 3.05e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907102146   34 DFRASLENGVLLCDLINKLKPGVV--KKINRLS--TPIAGLDNINVFLRACEQIGLK 86
Cdd:cd21217     32 DLFEALRDGVLLCKLINKIVPGTIdeRKLNKKKpkNIFEATENLNLALNAAKKIGCK 88
CH_IQGAP3 cd21276
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP3; IQ motif ...
17-101 5.09e-06

calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP3; IQ motif containing GTPase activating protein 3 (IQGAP3) associates with Ras GTP-binding proteins. It regulates the organization of the cytoskeleton under the regulation of Rac1 and Cdc42 in neuronal cells. The depletion of IQGAP3 is shown to impair neurite or axon outgrowth in neuronal cells with disorganized cytoskeleton. It belongs to the IQGAP family, which consists of multi-domain proteins having a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeats, a single WW domain, four IQ motifs that mediate interactions with calmodulin, and a RasGAP related domain that binds active Rho family GTPases. IQGAP3 contains a single copy of the CH domain at the N-terminus.


Pssm-ID: 409125  Cd Length: 152  Bit Score: 48.05  E-value: 5.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   17 EAQRWVEAVTEKNFET-TDFRASLENGVLLCDLINKLKPGVV--KKI---NRLSTPIAGL-----DNINVFLRACEQIGL 85
Cdd:cd21276     12 EAKRWMEACLKEELPPpTELEESLRNGVYLAKLGHCFAPRVVplKKIydlEQMRYQATGLhfrhtDNINHWRNAMMHIGL 91
                           90
                   ....*....|....*...
gi 1907102146   86 keAQLFHP--GDLQDLSN 101
Cdd:cd21276     92 --PSIFHPetTDIYDKKN 107
CH_TAGLN-like cd21209
calponin homology (CH) domain found in the transgelin family; The transgelin (TAGLN) family ...
33-107 8.25e-06

calponin homology (CH) domain found in the transgelin family; The transgelin (TAGLN) family includes transgelin, transgelin-2 and transgelin-3. Transgelin, also called 22 kDa actin-binding protein, protein WS3-10, or smooth muscle protein 22-alpha (SM22-alpha), acts as an actin cross-linking/gelling protein that may be involved in calcium interactions and in regulating contractile properties of the cell. Transgelin-2, also called epididymis tissue protein Li 7e, or SM22-alpha homolog, acts as an actin-binding protein that induces actin gelation and regulates actin cytoskeleton. It may participate in the development and progression of multiple cancers. Transgelin-3, also called neuronal protein 22 (NP22), or neuronal protein NP25, may have a role in alcohol-related adaptations and may mediate regulatory signal transduction pathways in neurons. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409058  Cd Length: 119  Bit Score: 46.74  E-value: 8.25e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907102146   33 TDFRASLENGVLLCDLINKLKP---GVVKKINRLSTPIAGLDNINVFLRACEQIGLKEAQLFHPGDLQDLSNRVTVKQ 107
Cdd:cd21209     28 LGFQKWLKDGTVLCKLINSLYPegsKPVKKIQSSKMAFKQMEQISQFLKAAEDYGVRTTDIFQTVDLWEGKDMAAVQR 105
CH_VAV2 cd21263
calponin homology (CH) domain found in VAV2 protein and similar proteins; VAV2 is widely ...
34-101 2.74e-05

calponin homology (CH) domain found in VAV2 protein and similar proteins; VAV2 is widely expressed and functions as a guanine nucleotide exchange factor (GEF) for RhoA, RhoB and RhoG and also activates Rac1 and Cdc42. It is implicated in many cellular and physiological functions including blood pressure control, eye development, neurite outgrowth and branching, EGFR endocytosis and degradation, and cell cluster morphology, among others. It has been reported to associate with Nek3. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The model corresponds to CH domain, an actin-binding domain which is present as a single copy in VAV2 protein.


Pssm-ID: 409112  Cd Length: 119  Bit Score: 45.33  E-value: 2.74e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907102146   34 DFRASLENGVLLCDLINKLKPGVV--KKIN---RLSTPIAgLDNINVFLRAC-EQIGLKEAQLFHPGDLQDLSN 101
Cdd:cd21263     31 DLAQALRDGVLLCQLLHNLSPGSIdlKDINfrpQMSQFLC-LKNIRTFLKVChDKFGLRNSELFDPFDLFDVRD 103
CH_LRCH3 cd21272
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
27-93 3.72e-05

calponin homology (CH) domain found in leucine-rich repeat and calponin homology domain-containing protein 3; Leucine-rich repeat and calponin homology domain-containing protein 3 (LRCH3) is part of the DISP (DOCK7-Induced Septin disPlacement) complex. It may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. LRCH3 contains a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409121  Cd Length: 109  Bit Score: 44.60  E-value: 3.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   27 EKNFET-------TDFRASLENGVLLCDLINKLKPGVVKKINRLSTPIAGLD------NINVFLRACEQIGLKEAQLFHP 93
Cdd:cd21272      7 RKNIESrlkvslpSDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTmakcrrNVENFLEACRRIGVPQEQLCLP 86
CH_LRCH1 cd21270
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
34-110 5.21e-05

calponin homology (CH) domain found in leucine-rich repeat and calponin homology domain-containing protein 1; Leucine-rich repeat and calponin homology domain-containing protein 1 (LRCH1), also called calponin homology domain-containing protein 1, or neuronal protein 81 (NP81), acts as a negative regulator of GTPase CDC42 by sequestering CDC42-guanine exchange factor DOCK8. LRCH1 contains a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409119  Cd Length: 112  Bit Score: 44.07  E-value: 5.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   34 DFRASLENGVLLCDLINKLKPGVVKKINRLSTPIAGLD------NINVFLRACEQIGLKEAQLFHPGDLQDLSNRVTVKQ 107
Cdd:cd21270     24 DLGAALMDGVVLCHLVNHVRPRSVASIHVPSPAVPKLSmakcrrNVENFLEACRKIGVPEADLCSPYDILQLNLRGIRKT 103

                   ...
gi 1907102146  108 EET 110
Cdd:cd21270    104 VET 106
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
1117-1158 8.25e-05

PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in posttranslational protein processing, maturation, and disassembly or degradation, in Bacteria, Archaea, and plant chloroplasts. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238488 [Multi-domain]  Cd Length: 85  Bit Score: 42.60  E-value: 8.25e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907102146 1117 GFTIKWDISGIFVASVEQGSPAEFSQLQVDDEILAINNTKFS 1158
Cdd:cd00988      5 GLELKYDDGGLVITSVLPGSPAAKAGIKAGDIIVAIDGEPVD 46
CH_IQGAP2 cd21275
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP2; IQ motif ...
17-101 1.34e-04

calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP2; IQ motif containing GTPase activating protein 2 (IQGAP2) is a member of the IQGAP family, which consists of multi-domain proteins having a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeats, a single WW domain, four IQ motifs that mediate interactions with calmodulin, and a RasGAP related domain that binds active Rho family GTPases. IQGAP2 binds to activated Cdc42 and Rac1 but does not seem to stimulate their GTPase activity. It associates with calmodulin. IQGAP2 contains a single copy of the CH domain at the N-terminus.


Pssm-ID: 409124  Cd Length: 156  Bit Score: 44.24  E-value: 1.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   17 EAQRWVEAVTEKNFE-TTDFRASLENGVLLCDLINKLKPGVV--KKI---NRLSTPIAGL-----DNINVFLRACEQIGL 85
Cdd:cd21275     36 EAKQWIEACLNEELPpTTELEEGLRNGVYLVKLAKFFAPKLVseKKIydvDQVRYKRSGLhfrhtDNTVQWLRAMESIGL 115
                           90
                   ....*....|....*...
gi 1907102146   86 keAQLFHP--GDLQDLSN 101
Cdd:cd21275    116 --PKIFYPetTDVYDRKN 131
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
1085-1184 1.38e-04

periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 46.45  E-value: 1.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146 1085 RGSPLREVSRSLDQFSDmrvsiNQTPGNKPVFGFT-------------IKWDISGIFVASVEQGSPAEFSQLQVDDEILA 1151
Cdd:TIGR02037  314 RKGKEKTITVTLGASPE-----EQASSSNPFLGLTvanlspeirkelrLKGDVKGVVVTKVVSGSPAARAGLQPGDVILS 388
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1907102146 1152 INNTkfSYKDTKKWEEVMANAQETGNLVMDVRR 1184
Cdd:TIGR02037  389 VNQQ--PVSSVAELRKVLARAKKGGRVALLILR 419
CH_TAGLN2 cd21280
calponin homology (CH) domain found in transgelin-2; Transgelin-2, also called epididymis ...
21-107 2.00e-04

calponin homology (CH) domain found in transgelin-2; Transgelin-2, also called epididymis tissue protein Li 7e, or SM22-alpha homolog, acts as an actin-binding protein that induces actin gelation and regulates the actin cytoskeleton. It may participate in the development and progression of multiple cancers. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409129  Cd Length: 137  Bit Score: 43.33  E-value: 2.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   21 WVEAVTEKNFETTD-----FRASLENGVLLCDLINKLKP---GVVKKINRLSTPIAGLDNINVFLRACEQIGLKEAQLFH 92
Cdd:cd21280     16 WITAQCGKQVGRPQpgrenFQNWLKDGTVLCHLINSLYPkgqAPVKKIQASTMAFKQMEQISQFLQAAERYGINTTDIFQ 95
                           90
                   ....*....|....*
gi 1907102146   93 PGDLQDLSNRVTVKQ 107
Cdd:cd21280     96 TVDLWEGKNMASVQR 110
CH_LRCH4 cd21273
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
34-96 4.35e-04

calponin homology (CH) domain found in leucine-rich repeat and calponin homology domain-containing protein 4; Leucine-rich repeat and calponin homology domain-containing protein 4 (LRCH4), also called leucine-rich repeat neuronal protein 4, or leucine-rich neuronal protein, acts as a novel Toll-like receptor (TLR) accessory protein that regulates the innate immune response. LRCH4 contains a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409122  Cd Length: 109  Bit Score: 41.42  E-value: 4.35e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907102146   34 DFRASLENGVLLCDLINKLKPGVVKKINRLSTPIAGLD------NINVFLRACEQIGLKEAQLFHPGDL 96
Cdd:cd21273     24 DLAEALSNGAVLCQLANQLRPRSVSIIHVPSPAVPKLSkakcrkNVENFIEACRKMGVPEVDLCSPSDV 92
CH_LRCH2 cd21271
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
34-93 7.53e-04

calponin homology (CH) domain found in leucine-rich repeat and calponin homology domain-containing protein 2; Leucine-rich repeat and calponin homology domain-containing protein 2 (LRCH2) may play a role in the organization of the cytoskeleton. It contains a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409120  Cd Length: 111  Bit Score: 40.68  E-value: 7.53e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907102146   34 DFRASLENGVLLCDLINKLKPGVVKKINRLSTPIAGLD------NINVFLRACEQIGLKEAQLFHP 93
Cdd:cd21271     25 DLGAALMDGVVLCHLANHIRPRSVGSIHVPSPAVPKLSmakcrrNVENFLDACRKLGVPEDKLCLP 90
PDZ_serine_protease cd00987
PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins ...
1123-1188 8.76e-04

PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins involved in heat-shock response, chaperone function, and apoptosis. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238487 [Multi-domain]  Cd Length: 90  Bit Score: 39.93  E-value: 8.76e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907102146 1123 DISGIFVASVEQGSPAEFSQLQVDDEILAINNTKFsyKDTKKWEEVMANAQETGNLVMDVRRYGKS 1188
Cdd:cd00987     22 DTKGVLVASVDPGSPAAKAGLKPGDVILAVNGKPV--KSVADLRRALAELKPGDKVTLTVLRGGKE 85
CH_betaPIX cd21266
calponin homology (CH) domain found in beta-Pak Interactive eXchange factor; Beta-Pak ...
35-96 1.09e-03

calponin homology (CH) domain found in beta-Pak Interactive eXchange factor; Beta-Pak Interactive eXchange factor (beta-PIX), also called PAK-interacting exchange factor beta, Rho guanine nucleotide exchange factor 7 (ARHGEF7), p85, or Cool (Cloned out of Library)-1, activates small GTPases by exchanging bound GDP for free GTP. It acts as a GEF for both Cdc42 and Rac1, and plays important roles in regulating neuroendocrine exocytosis, focal adhesion maturation, cell migration, synaptic vesicle localization, and insulin secretion. Beta-PIX contains a single copy of the CH domain at its N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409115  Cd Length: 112  Bit Score: 40.29  E-value: 1.09e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907102146   35 FRASLENGVLLCDLINKLKPGVVKKI-NRLSTPIAGLDNINVFLRACeqiGLKEAQLFHPGDL 96
Cdd:cd21266     29 LQASLKDGVVLCRLLERLLPGSIDKVyPEPRTESECLSNIREFLRGC---GALRLETFDANDL 88
CH_IQGAP1 cd21274
calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif ...
17-101 1.78e-03

calponin homology (CH) domain found in Ras GTPase-activating-like protein IQGAP1; IQ motif containing GTPase activating protein 1 (IQGAP1), also called p195, is a homodimeric protein that is widely expressed among vertebrate cell types from early embryogenesis. It plays a crucial role in regulating the dynamics and assembly of the actin cytoskeleton. It belongs to the IQGAP family, which consists of multi-domain proteins having a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeats, a single WW domain, four IQ motifs that mediate interactions with calmodulin, and a RasGAP related domain that binds active Rho family GTPases. IQGAP1 negatively regulates Ras family GTPases by stimulating their intrinsic GTPase activity. It lacks GAP activity. Both, IQGAP1 and IQGAP2, specifically bind to Cdc42 and Rac1, but not to RhoA. Despite similarities to part of the sequence of RasGAP, neither IQGAP1 nor IQGAP2 interacts with Ras. IQGAP1 contains a single copy of the CH domain at the N-terminus.


Pssm-ID: 409123  Cd Length: 154  Bit Score: 40.75  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907102146   17 EAQRWVEAVTEKNFE-TTDFRASLENGVLLCDLINKLKPGVV--KKI-NRLST--PIAGL-----DNINVFLRACEQIGL 85
Cdd:cd21274     13 EAKRWMEACLGEDLPpTTELEEGLRNGVYLAKLGNFFSPKVVslKKIyDREQTryKATGLhfrhtDNVIQWLNAMDEIGL 92
                           90
                   ....*....|....*...
gi 1907102146   86 keAQLFHP--GDLQDLSN 101
Cdd:cd21274     93 --PKIFYPetTDIYDRKN 108
CH_TAGLN3 cd21281
calponin homology (CH) domain found in transgelin-3; Transgelin-3, also called neuronal ...
34-96 2.64e-03

calponin homology (CH) domain found in transgelin-3; Transgelin-3, also called neuronal protein 22 (NP22), or neuronal protein NP25, may have a role in alcohol-related adaptations and may mediate regulatory signal transduction pathways in neurons. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409130  Cd Length: 119  Bit Score: 39.56  E-value: 2.64e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907102146   34 DFRASLENGVLLCDLINKLKP---GVVKKINRLSTPIAGLDNINVFLRACEQIGLKEAQLFHPGDL 96
Cdd:cd21281     29 NFQKWLMDGTILCRLINSLYPpgkEPIKKISETKMAFKQMEKISQFLQAAEAYGVITTDIFQTVDL 94
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
1128-1184 7.86e-03

PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 36.35  E-value: 7.86e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907102146 1128 FVASVEQGSPAEFSQLQVDDEILAINNTkfSYKDTKKWEEVMANAQETgNLVMDVRR 1184
Cdd:pfam17820    1 VVTAVVPGSPAERAGLRVGDVILAVNGK--PVRSLEDVARLLQGSAGE-SVTLTVRR 54
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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