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Conserved domains on  [gi|2195004491|ref|NP_001388494|]
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LIM and calponin homology domains-containing protein 1 isoform f [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_LIMCH1 cd21278
calponin homology (CH) domain found in LIM and calponin homology domains-containing protein 1; ...
 23-140 7.26e-78

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 [Multi-domain]  Cd Length: 118  Bit Score: 252.48  E-value: 7.26e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   23 AFAEAQKWIEQVTGRSFGDKDFRTGLENGILLCELLNAIKPGLVKKINRLPTPIAGLDNTILFLRGCKELGLKESQLFDP 102
Cdd:cd21278      1 AFTEAQKWIEQVTGRSFGDKDFRSGLENGILLCELLNAIKPGLVKKINRLPTPIAGLDNITLFLRGCKELGLKESQLFDP 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2195004491  103 SDLQDTSNRVTVKNFDYSRKLKNVLVTIYWLGKAANSC 140
Cdd:cd21278     81 GDLQDTSNRVTIKSSDCSRKLKNVLITIYWLGKAANSC 118
DUF4757 pfam15949
Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. ...
 736-868 2.61e-40

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: 464950  Cd Length: 170  Bit Score: 147.20  E-value: 2.61e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491  736 QEKEEVIKKEPEML---PRVQRPEgsSGPLYGPRTPVSDDAESTSMFDMRCEEEAAvlPHSRARQEQLQLINNQLREEDD 812
Cdd:pfam15949   40 AEKEEDIRRSWSTRtqpSKVAYPP--RQFVQRLFQKVSDDLGSKSMSDIRCEEEAQ--PLSQVRYEELQKIRNQLKEEED 115

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2195004491  813 KWQDDLARWKSRRRSASQDLIKKEEERKKMEKLMSGEDGTSERRKSiKTYREIVQE 868
Cdd:pfam15949  116 KWQDDLARWKSRRRSASQDLIKKEEERKKIEKLMSGEGGDSNRRKS-KTFKEMVEE 170
DUF4757 super family cl24502
Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. ...
 250-311 6.34e-20

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: 464950  Cd Length: 170  Bit Score: 88.65  E-value: 6.34e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2195004491  250 MSARRTSHGEPKSAVPFNQYLPNKSNQTAYVPAPLRKKKAEREEY-RKSWSTATSPLGGERPF 311
Cdd:pfam15949    1 MLARRTSSSEPKSSVPFNQFLPNKSNQSAYVPAPLRKKRAEKEEDiRRSWSTRTQPSKVAYPP 63
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
 1462-1519 2.01e-06

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


:

Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 46.22  E-value: 2.01e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 2195004491  1462 CSSCGLALGkGAAMIIETLNLYFHIQCFRCGICKGQLgdavSGTDVRIRNGLLNCTDC 1519
Cdd:smart00132    2 CAGCGKPIY-GTERVLRALGKVWHPECFKCATCGKPL----SGDTFFEKDGKLYCKDC 54
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
 276-412 3.81e-03

DNA polymerase III subunits gamma and tau; Validated


The actual alignment was detected with superfamily member PRK07764:

Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 3.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491  276 QTAYVPAPLRKKKAEREEYRKSWSTATSPLGGERPFSYPETIEEEGSEAGSPTEDDPSSQMDPDGKPEcgleAPPSNGKA 355
Cdd:PRK07764   428 APQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPA----APAAPAAP 503

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2195004491  356 QSPEDAAAVPAAIPEDREAVERQKRRRLE----------------QAGIKVMPAAQRFASQKQSSEEKEAIRD 412
Cdd:PRK07764   504 AGADDAATLRERWPEILAAVPKRSRKTWAillpeatvlgvrgdtlVLGFSTGGLARRFASPGNAEVLVTALAE 576
GBP_C super family cl46256
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 1245-1282 8.94e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


The actual alignment was detected with superfamily member cd16269:

Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.87  E-value: 8.94e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2195004491 1245 EEERRRQEKWQQEQERLLQERYQKEQDKLKEEWEKAQK 1282
Cdd:cd16269    218 EEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLK 255
 
Name Accession Description Interval E-value
CH_LIMCH1 cd21278
calponin homology (CH) domain found in LIM and calponin homology domains-containing protein 1; ...
 23-140 7.26e-78

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 [Multi-domain]  Cd Length: 118  Bit Score: 252.48  E-value: 7.26e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   23 AFAEAQKWIEQVTGRSFGDKDFRTGLENGILLCELLNAIKPGLVKKINRLPTPIAGLDNTILFLRGCKELGLKESQLFDP 102
Cdd:cd21278      1 AFTEAQKWIEQVTGRSFGDKDFRSGLENGILLCELLNAIKPGLVKKINRLPTPIAGLDNITLFLRGCKELGLKESQLFDP 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2195004491  103 SDLQDTSNRVTVKNFDYSRKLKNVLVTIYWLGKAANSC 140
Cdd:cd21278     81 GDLQDTSNRVTIKSSDCSRKLKNVLITIYWLGKAANSC 118
DUF4757 pfam15949
Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. ...
 736-868 2.61e-40

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: 464950  Cd Length: 170  Bit Score: 147.20  E-value: 2.61e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491  736 QEKEEVIKKEPEML---PRVQRPEgsSGPLYGPRTPVSDDAESTSMFDMRCEEEAAvlPHSRARQEQLQLINNQLREEDD 812
Cdd:pfam15949   40 AEKEEDIRRSWSTRtqpSKVAYPP--RQFVQRLFQKVSDDLGSKSMSDIRCEEEAQ--PLSQVRYEELQKIRNQLKEEED 115

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2195004491  813 KWQDDLARWKSRRRSASQDLIKKEEERKKMEKLMSGEDGTSERRKSiKTYREIVQE 868
Cdd:pfam15949  116 KWQDDLARWKSRRRSASQDLIKKEEERKKIEKLMSGEGGDSNRRKS-KTFKEMVEE 170
DUF4757 pfam15949
Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. ...
 250-311 6.34e-20

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: 464950  Cd Length: 170  Bit Score: 88.65  E-value: 6.34e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2195004491  250 MSARRTSHGEPKSAVPFNQYLPNKSNQTAYVPAPLRKKKAEREEY-RKSWSTATSPLGGERPF 311
Cdd:pfam15949    1 MLARRTSSSEPKSSVPFNQFLPNKSNQSAYVPAPLRKKRAEKEEDiRRSWSTRTQPSKVAYPP 63
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 26-107 3.46e-12

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: 64.26  E-value: 3.46e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491    26 EAQKWIEQVTGRSFGDK--DFRTGLENGILLCELLNAIKPGLV--KKINRLPTPIAGLDNTILFLRGCKELGLKEsQLFD 101
Cdd:smart00033    2 TLLRWVNSLLAEYDKPPvtNFSSDLKDGVALCALLNSLSPGLVdkKKVAASLSRFKKIENINLALSFAEKLGGKV-VLFE 80


                    ....*.
gi 2195004491   102 PSDLQD 107
Cdd:smart00033   81 PEDLVE 86
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 29-139 4.56e-11

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 [Multi-domain]  Cd Length: 109  Bit Score: 61.15  E-value: 4.56e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   29 KWIEQVTGRSFGD---KDFRTGLENGILLCELLNAIKPGLVKKINRLPTPIAGLDNTILFLRGC-KELGLKEsQLFDPSD 104
Cdd:pfam00307    9 RWINSHLAEYGPGvrvTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAeKKLGVPK-VLIEPED 87

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2195004491  105 LqdtsnrvtvknfdYSRKLKNVLVTIYWLGKAANS 139
Cdd:pfam00307   88 L-------------VEGDNKSVLTYLASLFRRFQA 109
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
 1462-1519 2.01e-06

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 46.22  E-value: 2.01e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 2195004491  1462 CSSCGLALGkGAAMIIETLNLYFHIQCFRCGICKGQLgdavSGTDVRIRNGLLNCTDC 1519
Cdd:smart00132    2 CAGCGKPIY-GTERVLRALGKVWHPECFKCATCGKPL----SGDTFFEKDGKLYCKDC 54
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
 1462-1520 2.81e-06

LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid).


Pssm-ID: 259829 [Multi-domain]  Cd Length: 53  Bit Score: 45.77  E-value: 2.81e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2195004491 1462 CSSCGLALGkgAAMIIETLNLYFHIQCFRCGICKGQLGdavsGTDVRIRNGLLNCTDCY 1520
Cdd:cd08368      1 CAGCGKPIE--GRELLRALGKKWHPECFKCAECGKPLG----GDSFYEKDGKPYCEKCY 53
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
 1462-1524 6.97e-06

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 44.63  E-value: 6.97e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2195004491 1462 CSSCGlalgKG--AAMIIETLNLYFHIQCFRCGICKGQLGDavsgTDVRIRNGLLNCTDCYMRSR 1524
Cdd:pfam00412    1 CAGCN----RPiyDRELVRALGKVWHPECFRCAVCGKPLTT----GDFYEKDGKLYCKHDYYKLF 57
SCP1 COG5199
Calponin [Cytoskeleton];
26-138 8.23e-05

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 44.91  E-value: 8.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   26 EAQKWIEQVTGRSFGDK-DFRTGLENGILLCELLNAIKPGLVK-KINRLPtpIAGLDNTILFLRGCKELGLKESQLFDPS 103
Cdd:COG5199     17 EVTLWIETVLGEKFEPPgDLLSLLKDGVRLCRILNEASPLDIKyKESKMP--FVQMENISSFINGLKKLRVPEYELFQTN 94

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2195004491  104 DLqdtsnrvtvknFDySRKLKNVLVTIYWLGKAAN 138
Cdd:COG5199     95 DL-----------FE-AKDLRQVVICLYSLSRYAQ 117
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 276-412 3.81e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 3.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491  276 QTAYVPAPLRKKKAEREEYRKSWSTATSPLGGERPFSYPETIEEEGSEAGSPTEDDPSSQMDPDGKPEcgleAPPSNGKA 355
Cdd:PRK07764   428 APQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPA----APAAPAAP 503

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2195004491  356 QSPEDAAAVPAAIPEDREAVERQKRRRLE----------------QAGIKVMPAAQRFASQKQSSEEKEAIRD 412
Cdd:PRK07764   504 AGADDAATLRERWPEILAAVPKRSRKTWAillpeatvlgvrgdtlVLGFSTGGLARRFASPGNAEVLVTALAE 576
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 1245-1282 8.94e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.87  E-value: 8.94e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2195004491 1245 EEERRRQEKWQQEQERLLQERYQKEQDKLKEEWEKAQK 1282
Cdd:cd16269    218 EEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLK 255
 
Name Accession Description Interval E-value
CH_LIMCH1 cd21278
calponin homology (CH) domain found in LIM and calponin homology domains-containing protein 1; ...
 23-140 7.26e-78

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 [Multi-domain]  Cd Length: 118  Bit Score: 252.48  E-value: 7.26e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   23 AFAEAQKWIEQVTGRSFGDKDFRTGLENGILLCELLNAIKPGLVKKINRLPTPIAGLDNTILFLRGCKELGLKESQLFDP 102
Cdd:cd21278      1 AFTEAQKWIEQVTGRSFGDKDFRSGLENGILLCELLNAIKPGLVKKINRLPTPIAGLDNITLFLRGCKELGLKESQLFDP 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2195004491  103 SDLQDTSNRVTVKNFDYSRKLKNVLVTIYWLGKAANSC 140
Cdd:cd21278     81 GDLQDTSNRVTIKSSDCSRKLKNVLITIYWLGKAANSC 118
CH_LMO7-like cd21208
calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...
 23-138 1.09e-58

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: 197.56  E-value: 1.09e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   23 AFAEAQKWIEQVTGRSFGDKDFRTGLENGILLCELLNAIKPGLVKKINRLPTPIAGLDNTILFLRGCKELGLKESQLFDP 102
Cdd:cd21208      1 ALKEARTWIEAVTGKKFPSDDFRESLEDGILLCELINAIKPGSIKKINRLPTPIAGLDNLNLFLKACEDLGLKDSQLFDP 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2195004491  103 SDLQDTSNRVT---VKNFDYSRKLKNVLVTIYWLGKAAN 138
Cdd:cd21208     81 TDLQDLSNRRIathVRKKEDERRLKNVAITLYWLGRAAR 119
CH_LMO7 cd21277
calponin homology (CH) domain found in LIM domain only protein 7; LIM domain only protein 7 ...
 23-137 7.95e-56

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 [Multi-domain]  Cd Length: 116  Bit Score: 189.28  E-value: 7.95e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   23 AFAEAQKWIEQVTGRSFGDKDFRTGLENGILLCELLNAIKPGLVKKINRLPTPIAGLDNTILFLRGCKELGLKESQLFDP 102
Cdd:cd21277      1 AFSEAQRWIEAVTGKNFGNKDFRSALENGVLLCDLINKIKPGIIKKINRLSTPIAGLDNINVFLKACEKLGLKEAQLFHP 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2195004491  103 SDLQDTSNRVTVKNFDYSRKLKNVLVTIYWLGKAA 137
Cdd:cd21277     81 GDLQDLSTRVTVKQEETDRRLKNVLITLYWLGRKA 115
DUF4757 pfam15949
Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. ...
 736-868 2.61e-40

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: 464950  Cd Length: 170  Bit Score: 147.20  E-value: 2.61e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491  736 QEKEEVIKKEPEML---PRVQRPEgsSGPLYGPRTPVSDDAESTSMFDMRCEEEAAvlPHSRARQEQLQLINNQLREEDD 812
Cdd:pfam15949   40 AEKEEDIRRSWSTRtqpSKVAYPP--RQFVQRLFQKVSDDLGSKSMSDIRCEEEAQ--PLSQVRYEELQKIRNQLKEEED 115

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2195004491  813 KWQDDLARWKSRRRSASQDLIKKEEERKKMEKLMSGEDGTSERRKSiKTYREIVQE 868
Cdd:pfam15949  116 KWQDDLARWKSRRRSASQDLIKKEEERKKIEKLMSGEGGDSNRRKS-KTFKEMVEE 170
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 25-135 1.27e-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 [Multi-domain]  Cd Length: 103  Bit Score: 96.64  E-value: 1.27e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   25 AEAQKWIEQVTGRSFGD--KDFRTGLENGILLCELLNAIKPGLVKKINRLP-TPIAGLDNTILFLRGCKELGLKESQLFD 101
Cdd:cd00014      2 EELLKWINEVLGEELPVsiTDLFESLRDGVLLCKLINKLSPGSIPKINKKPkSPFKKRENINLFLNACKKLGLPELDLFE 81

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2195004491  102 PSDLQDTSNrvtvknfdysrkLKNVLVTIYWLGK 135
Cdd:cd00014     82 PEDLYEKGN------------LKKVLGTLWALAL 103
DUF4757 pfam15949
Domain of unknown function (DUF4757); This presumed domain is functionally uncharacterized. ...
 250-311 6.34e-20

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: 464950  Cd Length: 170  Bit Score: 88.65  E-value: 6.34e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2195004491  250 MSARRTSHGEPKSAVPFNQYLPNKSNQTAYVPAPLRKKKAEREEY-RKSWSTATSPLGGERPF 311
Cdd:pfam15949    1 MLARRTSSSEPKSSVPFNQFLPNKSNQSAYVPAPLRKKRAEKEEDiRRSWSTRTQPSKVAYPP 63
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
 25-135 2.48e-19

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 [Multi-domain]  Cd Length: 107  Bit Score: 84.67  E-value: 2.48e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   25 AEAQKWIEQVTGRSFGD-KDFRTGLENGILLCELLNAIKPGLVKKINRLPTPIAGLDNTILFLRGCKELGLKESQLFDPS 103
Cdd:cd21207      8 AEALDWIEAVTGEKLDDgKDYEDVLKDGVILCKLINILKPGSVKKINTSKMAFKLMENIENFLTACKGYGVPKTDLFQTV 87

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2195004491  104 DLqdtsnrvtvknfdYSRK-LKNVLVTIYWLGK 135
Cdd:cd21207     88 DL-------------YEKKnIPQVTNCLFALGR 107
CH_CNN2 cd21283
calponin homology (CH) domain found in calponin-2; Calponin-2 (CNN2), also called neutral ...
 25-115 1.78e-17

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 [Multi-domain]  Cd Length: 109  Bit Score: 79.59  E-value: 1.78e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   25 AEAQKWIEQVTGRSFGDkDFRTGLENGILLCELLNAIKPGLVKKINRLPTPIAGLDNTILFLRGCKELGLKESQLFDPSD 104
Cdd:cd21283      6 AELRTWIEGLTGRSIGP-DFQKGLKDGVILCELMNKLQPGSVPKINRSMQNWHQLENLSNFIKAMVSYGMKPVDLFEAND 84

                           90
                   ....*....|.
gi 2195004491  105 LQDTSNRVTVK 115
Cdd:cd21283     85 LFESGNMTQVQ 95
CH_CNN cd21211
calponin homology (CH) domain found in the calponin family; Calponin is an actin ...
 25-115 6.18e-17

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 [Multi-domain]  Cd Length: 108  Bit Score: 78.12  E-value: 6.18e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   25 AEAQKWIEQVTGRSFGDkDFRTGLENGILLCELLNAIKPGLVKKINRLPTPIAGLDNTILFLRGCKELGLKESQLFDPSD 104
Cdd:cd21211      6 AELRTWIEGVTGLSIGP-NFQKGLKDGIILCELINKLQPGSVKKINESMQNWHQLENIGNFIKAIVSYGMKPHDIFEAND 84

                           90
                   ....*....|.
gi 2195004491  105 LQDTSNRVTVK 115
Cdd:cd21211     85 LFENGNMTQVQ 95
CH_CNN1 cd21282
calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), ...
 25-115 2.13e-16

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 [Multi-domain]  Cd Length: 108  Bit Score: 76.45  E-value: 2.13e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   25 AEAQKWIEQVTGRSFGDkDFRTGLENGILLCELLNAIKPGLVKKINRLPTPIAGLDNTILFLRGCKELGLKESQLFDPSD 104
Cdd:cd21282      6 EELRVWIEGVTGRRIGD-NFMDGLKDGVILCELINKLQPGSVRKINESTQNWHKLENIGNFIKAIMHYGVKPHDIFEAND 84

                           90
                   ....*....|.
gi 2195004491  105 LQDTSNRVTVK 115
Cdd:cd21282     85 LFENTNHTQVQ 95
CH_SCP1-like cd21210
calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar ...
 25-135 4.55e-15

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 [Multi-domain]  Cd Length: 101  Bit Score: 72.40  E-value: 4.55e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   25 AEAQKWIEQVTGRSFGDKDFRTGLENGILLCELLNAIKPGLVKKINRLPTPIAGLDNTILFLRGCKELGLKESQLFDPSD 104
Cdd:cd21210      3 QEAREWIEEVLGEKLAQGDLLDALKDGVVLCKLANRILPADIRKYKESKMPFVQMENISAFLNAARKLGVPENDLFQTVD 82

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2195004491  105 LQDTSNrvtvknfdysrkLKNVLVTIYWLGK 135
Cdd:cd21210     83 LFERKN------------PAQVLQCLHALSR 101
CH_CNN3 cd21284
calponin homology (CH) domain found in calponin-3; Calponin-3 (CNN3), also called acidic ...
 26-115 8.68e-15

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 [Multi-domain]  Cd Length: 111  Bit Score: 71.86  E-value: 8.68e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   26 EAQKWIEQVTGRSFGDkDFRTGLENGILLCELLNAIKPGLVKKINRLPTPIAGLDNTILFLRGCKELGLKESQLFDPSDL 105
Cdd:cd21284      9 ELRNWIEEVTGMSIGE-NFQKGLKDGVILCELINKLQPGSIRKINESKLNWHQLENIGNFIKAIQAYGMKPHDIFEANDL 87

                           90
                   ....*....|
gi 2195004491  106 QDTSNRVTVK 115
Cdd:cd21284     88 FENGNMTQVQ 97
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 26-107 3.46e-12

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: 64.26  E-value: 3.46e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491    26 EAQKWIEQVTGRSFGDK--DFRTGLENGILLCELLNAIKPGLV--KKINRLPTPIAGLDNTILFLRGCKELGLKEsQLFD 101
Cdd:smart00033    2 TLLRWVNSLLAEYDKPPvtNFSSDLKDGVALCALLNSLSPGLVdkKKVAASLSRFKKIENINLALSFAEKLGGKV-VLFE 80


                    ....*.
gi 2195004491   102 PSDLQD 107
Cdd:smart00033   81 PEDLVE 86
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 29-139 4.56e-11

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 [Multi-domain]  Cd Length: 109  Bit Score: 61.15  E-value: 4.56e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   29 KWIEQVTGRSFGD---KDFRTGLENGILLCELLNAIKPGLVKKINRLPTPIAGLDNTILFLRGC-KELGLKEsQLFDPSD 104
Cdd:pfam00307    9 RWINSHLAEYGPGvrvTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAeKKLGVPK-VLIEPED 87

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2195004491  105 LqdtsnrvtvknfdYSRKLKNVLVTIYWLGKAANS 139
Cdd:pfam00307   88 L-------------VEGDNKSVLTYLASLFRRFQA 109
CH_AtKIN14-like cd21203
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ...
 26-106 1.00e-09

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 [Multi-domain]  Cd Length: 112  Bit Score: 57.42  E-value: 1.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   26 EAQKWIEQVTGRSFG----DKDFRTGLENGILLCELLNAIKPGLVKKINRLPTPIAG--------LDNTILFLRGCKELG 93
Cdd:cd21203      4 EAAEWIQNVLGVLVLpdpsEEEFRLCLRDGVVLCKLLNKLQPGAVPKVVESPDDPDGaagsafqyFENVRNFLVAIEEMG 83

                           90
                   ....*....|...
gi 2195004491   94 LKesqLFDPSDLQ 106
Cdd:cd21203     84 LP---TFEASDLE 93
CH_IQGAP cd21206
calponin homology (CH) domain found in the IQ motif containing GTPase activating protein ...
 25-110 1.39e-09

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 [Multi-domain]  Cd Length: 118  Bit Score: 57.24  E-value: 1.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   25 AEAQKWIEQVTGRSFGD-KDFRTGLENGILLCELLNAIKPGLVKKINrlpTPIAGL-----DNTILFLRGCKELGLKESQ 98
Cdd:cd21206     11 EEAKQWIEACLNEELPPtTEFEEELRNGVVLAKLANKFAPKLVPLKK---IYDVGLqfrhtDNINHFLRALKKIGLPKIF 87

                           90
                   ....*....|..
gi 2195004491   99 LFDPSDLQDTSN 110
Cdd:cd21206     88 HFETTDLYEKKN 99
CH_PIX cd21202
calponin homology (CH) domain found in the Pak Interactive eXchange factor family; Pak ...
 45-139 3.98e-09

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 [Multi-domain]  Cd Length: 114  Bit Score: 56.00  E-value: 3.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   45 RTGLENGILLCELLNAIKPGLVKKINRLPTPIAG-LDNTILFLRGCKELGLKESQLFDPSDLQDTSNrvtvknfdysrkL 123
Cdd:cd21202     31 SESLKNGVVLCRLVNRLKPGTVEKIYDEPTTEEEcLYNFESFLKACQELGILAEEIFDPNDLYSGGN------------F 98

                           90
                   ....*....|....*.
gi 2195004491  124 KNVLVTIYWLGKAANS 139
Cdd:cd21202     99 QKVLSTLERLEKVAGG 114
CH_VAV cd21201
calponin homology (CH) domain found in VAV proteins; VAV proteins function both as cytoplasmic ...
 43-110 1.93e-08

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: 53.80  E-value: 1.93e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2195004491   43 DFRTGLENGILLCELLNAIKPGLVKKINRLPTP----IAGLDNTILFLRGCKE-LGLKESQLFDPSDLQDTSN 110
Cdd:cd21201     31 DLAQALRDGVLLCQLLNRLSPGSVDDREINLRPqmsqFLCLKNIRTFLQACRTvFGLRSADLFEPEDLYDVTN 103
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
 1462-1519 2.01e-06

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 46.22  E-value: 2.01e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 2195004491  1462 CSSCGLALGkGAAMIIETLNLYFHIQCFRCGICKGQLgdavSGTDVRIRNGLLNCTDC 1519
Cdd:smart00132    2 CAGCGKPIY-GTERVLRALGKVWHPECFKCATCGKPL----SGDTFFEKDGKLYCKDC 54
CH_GAS2-like cd21204
calponin homology (CH) domain found in the growth arrest-specific protein 2 family; The growth ...
 30-105 2.22e-06

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: 48.42  E-value: 2.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   30 WIEQVtgrsFGDKD----FRTGLENGILLCELLNAI--------------KPGLVKKI----NRLPTPIAGLDNTILFLR 87
Cdd:cd21204     14 WLNDL----LGDDLtpdnFLDELRNGVVLCQLAQKIqeaaekareagkknGPPPSYKLkcneNAKPGSFFARDNVANFLR 89

                           90
                   ....*....|....*...
gi 2195004491   88 GCKELGLKESQLFDPSDL 105
Cdd:cd21204     90 WCRKLGVDEVLLFESEDL 107
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
 1462-1520 2.81e-06

LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid).


Pssm-ID: 259829 [Multi-domain]  Cd Length: 53  Bit Score: 45.77  E-value: 2.81e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2195004491 1462 CSSCGLALGkgAAMIIETLNLYFHIQCFRCGICKGQLGdavsGTDVRIRNGLLNCTDCY 1520
Cdd:cd08368      1 CAGCGKPIE--GRELLRALGKKWHPECFKCAECGKPLG----GDSFYEKDGKPYCEKCY 53
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
 1462-1524 6.97e-06

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 44.63  E-value: 6.97e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2195004491 1462 CSSCGlalgKG--AAMIIETLNLYFHIQCFRCGICKGQLGDavsgTDVRIRNGLLNCTDCYMRSR 1524
Cdd:pfam00412    1 CAGCN----RPiyDRELVRALGKVWHPECFRCAVCGKPLTT----GDFYEKDGKLYCKHDYYKLF 57
CH_VAV2 cd21263
calponin homology (CH) domain found in VAV2 protein and similar proteins; VAV2 is widely ...
 43-110 1.01e-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: 46.10  E-value: 1.01e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2195004491   43 DFRTGLENGILLCELLNAIKPGLV--KKINRLP--TPIAGLDNTILFLRGCKE-LGLKESQLFDPSDLQDTSN 110
Cdd:cd21263     31 DLAQALRDGVLLCQLLHNLSPGSIdlKDINFRPqmSQFLCLKNIRTFLKVCHDkFGLRNSELFDPFDLFDVRD 103
CH_VAV3 cd21264
calponin homology (CH) domain found in VAV3 protein and similar proteins; VAV3 is ubiquitously ...
 43-107 2.60e-05

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: 44.95  E-value: 2.60e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   43 DFRTGLENGILLCELLNAIKPGLV--KKINRLP--TPIAGLDNTILFLRG-CKELGLKESQLFDPSDLQD 107
Cdd:cd21264     31 DLAQTLRDGVLLCQLLNNLRPHSInlKEINLRPqmSQFLCLKNIRTFLSAcCETFGMRKSELFEAFDLFD 100
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 48-95 3.52e-05

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 [Multi-domain]  Cd Length: 114  Bit Score: 44.49  E-value: 3.52e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2195004491   48 LENGILLCELLNAIKPGLV--KKINRLP--TPIAGLDNTILFLRGCKELGLK 95
Cdd:cd21217     37 LRDGVLLCKLINKIVPGTIdeRKLNKKKpkNIFEATENLNLALNAAKKIGCK 88
CH_alphaPIX cd21265
calponin homology (CH) domain found in alpha-Pak Interactive eXchange factor; Alpha-Pak ...
 45-105 7.69e-05

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: 43.66  E-value: 7.69e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2195004491   45 RTGLENGILLCELLNAIKPGLVKKINRLP-TPIAGLDNTILFLRGCKELGLkesQLFDPSDL 105
Cdd:cd21265     32 KSSLKDGVVLCKLIERLLPGSVEKYCLEPkTEADCIGNIKEFLKGCAALKV---ETFEPDDL 90
SCP1 COG5199
Calponin [Cytoskeleton];
26-138 8.23e-05

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 44.91  E-value: 8.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   26 EAQKWIEQVTGRSFGDK-DFRTGLENGILLCELLNAIKPGLVK-KINRLPtpIAGLDNTILFLRGCKELGLKESQLFDPS 103
Cdd:COG5199     17 EVTLWIETVLGEKFEPPgDLLSLLKDGVRLCRILNEASPLDIKyKESKMP--FVQMENISSFINGLKKLRVPEYELFQTN 94

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2195004491  104 DLqdtsnrvtvknFDySRKLKNVLVTIYWLGKAAN 138
Cdd:COG5199     95 DL-----------FE-AKDLRQVVICLYSLSRYAQ 117
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
 26-114 1.07e-04

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: 47.19  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   26 EAQKWIEQVTGRSFGDKDFRTGLENGILLCELLNAIKPGLVKKI---NRLptPIAGLDNTILFLRGCKELGLKESQLFDP 102
Cdd:COG5261     48 EAKIWIEEVIEEALPELCFEDSLRNGVFLAKLTQRFNPDLTTVIfpaDKL--QFRHTDNINAFLDLIEHVGLPESFHFEL 125

                           90
                   ....*....|..
gi 2195004491  103 SDLQDTSNRVTV 114
Cdd:COG5261    126 QDLYEKKNIPKV 137
CH_VAV1 cd21262
calponin homology (CH) domain found in VAV1 protein; VAV1 is expressed predominantly in the ...
 43-107 1.50e-04

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: 43.01  E-value: 1.50e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   43 DFRTGLENGILLCELLNAIKPGLV--KKINRLP--TPIAGLDNTILFLRGCKE-LGLKESQLFDPSDLQD 107
Cdd:cd21262     31 DLAQALRDGVLLCQLLNNLLPHAVnlREINLRPqmSQFLCLKNIRTFLSTCCEkFGLRKSELFEAFDLFD 100
LIM3_Zyxin_like cd09357
The third LIM domain of Zyxin-like family; The third LIM domain of Zyxin like family: This ...
 1462-1519 3.26e-04

The third LIM domain of Zyxin-like family; The third LIM domain of Zyxin like family: This family includes Ajuba, Limd1, WTIP, Zyxin, LPP, and Trip6 LIM proteins. Members of Zyxin family contain three tandem C-terminal LIM domains, and a proline-rich N-terminal region. Zyxin proteins are detected primarily in focal adhesion plaques. They function as scaffolds, participating in the assembly of multiple interactions and signal transduction networks, which regulate cell adhesion, spreading, and motility. They can also shuffle into nucleus. In nucleus, zyxin proteins affect gene transcription by interaction with a variety of nuclear proteins, including several transcription factors, playing regulating roles in cell proliferation, differentiation and apoptosis. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188743  Cd Length: 63  Bit Score: 40.10  E-value: 3.26e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2195004491 1462 CSSCGLAL----GKGAAMIIETLNLYFHIQCFRCGICKGQLGDAVSGTDVRIRNGLLNCTDC 1519
Cdd:cd09357      1 CSVCGEPImpepGQDETVRIVALDRSFHVNCYKCEDCGMLLSSEDEGQGCYPLDGHLLCKSC 62
CH_betaPIX cd21266
calponin homology (CH) domain found in beta-Pak Interactive eXchange factor; Beta-Pak ...
 44-110 3.58e-04

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: 41.83  E-value: 3.58e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2195004491   44 FRTGLENGILLCELLNAIKPGLVKKINRLP-TPIAGLDNTILFLRGCKELGLkesQLFDPSDLQDTSN 110
Cdd:cd21266     29 LQASLKDGVVLCRLLERLLPGSIDKVYPEPrTESECLSNIREFLRGCGALRL---ETFDANDLYQGQN 93
CH_LRCH cd21205
calponin homology (CH) domain found in the leucine-rich repeat and calponin homology ...
 48-105 5.21e-04

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 [Multi-domain]  Cd Length: 107  Bit Score: 41.13  E-value: 5.21e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2195004491   48 LENGILLCELLNAIKPGLVKKINRLP------TPIAGLDNTILFLRGCKELGLKESQLFDPSDL 105
Cdd:cd21205     26 LMDGVVLCHLANHVRPRSVPSIHVPSpavpklSMAKCRRNVENFLEACRKLGVPEERLCSPGDI 89
CH_TAGLN-like cd21209
calponin homology (CH) domain found in the transgelin family; The transgelin (TAGLN) family ...
 40-116 1.40e-03

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 [Multi-domain]  Cd Length: 119  Bit Score: 40.19  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   40 GDKDFRTGLENGILLCELLNAIKP---GLVKKINRLPTPIAGLDNTILFLRGCKELGLKESQLFDPSDLQDTSNRVTVKN 116
Cdd:cd21209     26 GRLGFQKWLKDGTVLCKLINSLYPegsKPVKKIQSSKMAFKQMEQISQFLKAAEDYGVRTTDIFQTVDLWEGKDMAAVQR 105
LIM2_LMO4 cd09387
The second LIM domain of LMO4 (LIM domain only protein 4); The second LIM domain of LMO4 (LIM ...
 1462-1519 2.07e-03

The second LIM domain of LMO4 (LIM domain only protein 4); The second LIM domain of LMO4 (LIM domain only protein 4): LMO4 is a nuclear protein that plays important roles in transcriptional regulation and development. LMO4 is involved in various functions in tumorigenesis and cellular differentiation. LMO4 proteins regulate gene expression by interacting with a wide variety of transcription factors and cofactors to form large transcription complexes. It can interact with Smad proteins, and associate with the promoter of the PAI-1 (plasminogen activator inhibitor-1) gene in a TGFbeta (transforming growth factor beta)-dependent manner. LMO4 can also form a complex with transcription regulator CREB (cAMP response element-binding protein) and interact with CLIM1 and CLIM2. In breast tissue, LMO4 interacts with multiple proteins, including the cofactor CtIP [CtBP (C-terminal binding protein)-interacting protein], the breast and ovarian tumor suppressor BRCA1 (breast-cancer susceptibility gene 1) and the LIM-domain-binding protein LDB1. Functionally, LMO4 is shown to repress BRCA1-mediated transcription activation, thus invoking a potential role for LMO4 as a negative regulator of BRCA1 in sporadic breast cancer. LMO4 also forms complex to both ERa (oestrogen receptor alpha), MTA1 (metastasis tumor antigen 1), and HDACs (histone deacetylases), implying that LMO4 is also a component of the MTA1 corepressor complex. Over-expressed LMO4 represses ERa transactivation functions in an HDAC-dependent manner, and contributes to the process of breast cancer progression by allowing the development of Era-negative phenotypes. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188773  Cd Length: 55  Bit Score: 37.85  E-value: 2.07e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2195004491 1462 CSSCGLALgKGAAMIIETLNLYFHIQCFRCGICKGQLgdaVSGTDVRIRNGLLNC-TDC 1519
Cdd:cd09387      1 CSACGQSI-PASELVMRAQGNVYHLKCFTCSTCHNQL---VPGDRFHYVNGSLFCeHDR 55
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 276-412 3.81e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 3.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491  276 QTAYVPAPLRKKKAEREEYRKSWSTATSPLGGERPFSYPETIEEEGSEAGSPTEDDPSSQMDPDGKPEcgleAPPSNGKA 355
Cdd:PRK07764   428 APQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPA----APAAPAAP 503

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2195004491  356 QSPEDAAAVPAAIPEDREAVERQKRRRLE----------------QAGIKVMPAAQRFASQKQSSEEKEAIRD 412
Cdd:PRK07764   504 AGADDAATLRERWPEILAAVPKRSRKTWAillpeatvlgvrgdtlVLGFSTGGLARRFASPGNAEVLVTALAE 576
CH_LRCH4 cd21273
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 25-105 5.28e-03

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: 38.34  E-value: 5.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   25 AEAQKWIEQVTGRSFGDkDFRTGLENGILLCELLNAIKPGLVKKINrLPTP-------IAGLDNTILFLRGCKELGLKES 97
Cdd:cd21273      7 AQLRKTLESRLKVTLPE-DLAEALSNGAVLCQLANQLRPRSVSIIH-VPSPavpklskAKCRKNVENFIEACRKMGVPEV 84


                   ....*...
gi 2195004491   98 QLFDPSDL 105
Cdd:cd21273     85 DLCSPSDV 92
LIM2_PINCH cd09332
The second LIM domain of protein PINCH; The second LIM domain of protein PINCH: PINCH plays a ...
 1462-1500 7.14e-03

The second LIM domain of protein PINCH; The second LIM domain of protein PINCH: PINCH plays a pivotal role in the assembly of focal adhesions (FAs), regulating diverse functions in cell adhesion, growth, and differentiation through LIM-mediated protein-protein interactions. PINCH comprises an array of five LIM domains that interact with integrin-linked kinase (ILK), Nck2 (also called Nckbeta or Grb4) and other interaction partners. These interactions are essential for triggering the FA assembly and for relaying diverse mechanical and biochemical signals between Cell-extracellular matrix and the actin cytoskeleton. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188718 [Multi-domain]  Cd Length: 52  Bit Score: 36.16  E-value: 7.14e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2195004491 1462 CSSCG-LALGKgaamIIETLNLYFHIQCFRCGICKGQLGD 1500
Cdd:cd09332      1 CGKCGeFVIGR----VIKAMNNNWHPDCFRCEICNKELAD 36
CH_TAGLN2 cd21280
calponin homology (CH) domain found in transgelin-2; Transgelin-2, also called epididymis ...
 40-115 8.40e-03

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 [Multi-domain]  Cd Length: 137  Bit Score: 38.32  E-value: 8.40e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2195004491   40 GDKDFRTGLENGILLCELLNAIKP---GLVKKINRLPTPIAGLDNTILFLRGCKELGLKESQLFDPSDLQDTSNRVTVK 115
Cdd:cd21280     31 GRENFQNWLKDGTVLCHLINSLYPkgqAPVKKIQASTMAFKQMEQISQFLQAAERYGINTTDIFQTVDLWEGKNMASVQ 109
CH_GAS2 cd21267
calponin homology (CH) domain found in growth arrest-specific protein 2; Growth ...
 30-105 8.46e-03

calponin homology (CH) domain found in growth arrest-specific protein 2; Growth arrest-specific protein 2 (GAS-2) may play a role in apoptosis by acting as a cell death substrate for caspases. It contains a single copy of the CH domain at the N-terminal region. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409116  Cd Length: 136  Bit Score: 38.38  E-value: 8.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2195004491   30 WIEQVTGRSFGDKDFRTGLENGILLCELLNAI------------KPGL---VKKINRLPTPIAG----LDNTILFLRGCK 90
Cdd:cd21267     15 WLTNLLGKEITAESFMEKLDNGALLCQLAETLqekfkensadanKPGKslpVRKIPCRANAPSGsffaRDNTANFLSWCR 94

                           90
                   ....*....|....*
gi 2195004491   91 ELGLKESQLFDPSDL 105
Cdd:cd21267     95 DVGVGDTCLFESEGL 109
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 1245-1282 8.94e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.87  E-value: 8.94e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2195004491 1245 EEERRRQEKWQQEQERLLQERYQKEQDKLKEEWEKAQK 1282
Cdd:cd16269    218 EEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLK 255
 
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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