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Conserved domains on  [gi|398365759|ref|NP_010414|]
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fimbrin [Saccharomyces cerevisiae S288C]

Protein Classification

SAC6 family protein (domain architecture ID 11473718)

SAC6 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
1-640 0e+00

Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];


:

Pssm-ID: 227401  Cd Length: 612  Bit Score: 809.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759   1 MNIVKLQ----RKFPILTQEDLFS-TIEKFRAIDLDDKGWVEKQQALEAVSKDGDATYDEARETLKHVGVDASGRVELDD 75
Cdd:COG5069    1 MEAKKWQkvqkKTFTKWTNEKLISgGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759  76 YVGlvaklresktgaapQTTFNVAPNStpivstAATGLQHKGKGtqakIIVAGSQTGTTHTINEEErrEFTKHINSVLAG 155
Cdd:COG5069   81 GKG--------------VKLFNIGPQD------IVDGNPKLILG----LIWSLISRLTIATINEEG--ELTKHINLLLWC 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 156 DQDIGDLLPfPTDTFQLFDECRDGLVLSKLINDSVPDTIDTRVLNWPKKGKELNNFQASENANIVINSAKAIG-CVVVNV 234
Cdd:COG5069  135 DEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKALNNFQAFENANKVIGIARLIGvEDIVNV 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 235 HSEDiieGREHLILgLIWQIIRRGLLSKIDIKLHpELYRLLEDDETLEQfLRLPPEQILLRWFN-YHLKQANWNrrVTNF 313
Cdd:COG5069  214 SIPD---ERSIMTY-VSWYIIRFGLLEKIDIALH-RVYRLLEADETLIQ-LRLPYEIILLRLLNlIHLKQANWK--VVNF 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 314 SKDVSDGENYTILLNQLDpALCSKAPLQTTDLMERAEQVLQNAEKLDCRKYLTPsslvAGNPKLNLAFVAHLFNTHPGLE 393
Cdd:COG5069  286 SKDVSDGENYTDLLNQLN-ALCSRAPLETTDLHSLAGQILQNAEKYDCRKYLPP----AGNPKLDLAFVAHLFNTHPGQE 360
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 394 PIQEEEKPEIEEFDAEGEREARVFTLWLNSLDVDPPVISLFDDLKDGLILLQAYEKV-MPGAVDFKHVNKRPASGAEISR 472
Cdd:COG5069  361 PLEEEEKPEIEEFDAEGEFEARVFTFWLNSLDVSPEITNLFGDLRDQLILLQALSKKlMPMTVTHKLVKKQPASGIEENR 440
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 473 FKALENTNYAVDLGRAKGFSLVGIEGSDIVDGNKlLTLGLVWQLMRRNISITMKTLSSSGRDMSDSQILKWAQDQVTKGG 552
Cdd:COG5069  441 FKAFENENYAVDLGITEGFSLVGIKGLEILDGIR-LKLTLVWQVLRSNTALFNHVLKKDGCGLSDSDLCAWLGSLGLKGD 519
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 553 KNSTIRSFKDQALSN-AHFLLDVLNGIAPGYVDYDLVTPGNTEEERYANAR-LAIS--IARKLGALIWLVPEDINEVRAR 628
Cdd:COG5069  520 KEEGIRSFGDPAGSVsGVFYLDVLKGIHSELVDYDLVTRGFTEFDDIADARsLAISskILRSLGAIIKFLPEDINGVRPR 599
                        650
                 ....*....|...
gi 398365759 629 L-IITFIASLMTL 640
Cdd:COG5069  600 LdVLTFIESLMAD 612
 
Name Accession Description Interval E-value
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
1-640 0e+00

Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];


Pssm-ID: 227401  Cd Length: 612  Bit Score: 809.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759   1 MNIVKLQ----RKFPILTQEDLFS-TIEKFRAIDLDDKGWVEKQQALEAVSKDGDATYDEARETLKHVGVDASGRVELDD 75
Cdd:COG5069    1 MEAKKWQkvqkKTFTKWTNEKLISgGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759  76 YVGlvaklresktgaapQTTFNVAPNStpivstAATGLQHKGKGtqakIIVAGSQTGTTHTINEEErrEFTKHINSVLAG 155
Cdd:COG5069   81 GKG--------------VKLFNIGPQD------IVDGNPKLILG----LIWSLISRLTIATINEEG--ELTKHINLLLWC 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 156 DQDIGDLLPfPTDTFQLFDECRDGLVLSKLINDSVPDTIDTRVLNWPKKGKELNNFQASENANIVINSAKAIG-CVVVNV 234
Cdd:COG5069  135 DEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKALNNFQAFENANKVIGIARLIGvEDIVNV 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 235 HSEDiieGREHLILgLIWQIIRRGLLSKIDIKLHpELYRLLEDDETLEQfLRLPPEQILLRWFN-YHLKQANWNrrVTNF 313
Cdd:COG5069  214 SIPD---ERSIMTY-VSWYIIRFGLLEKIDIALH-RVYRLLEADETLIQ-LRLPYEIILLRLLNlIHLKQANWK--VVNF 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 314 SKDVSDGENYTILLNQLDpALCSKAPLQTTDLMERAEQVLQNAEKLDCRKYLTPsslvAGNPKLNLAFVAHLFNTHPGLE 393
Cdd:COG5069  286 SKDVSDGENYTDLLNQLN-ALCSRAPLETTDLHSLAGQILQNAEKYDCRKYLPP----AGNPKLDLAFVAHLFNTHPGQE 360
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 394 PIQEEEKPEIEEFDAEGEREARVFTLWLNSLDVDPPVISLFDDLKDGLILLQAYEKV-MPGAVDFKHVNKRPASGAEISR 472
Cdd:COG5069  361 PLEEEEKPEIEEFDAEGEFEARVFTFWLNSLDVSPEITNLFGDLRDQLILLQALSKKlMPMTVTHKLVKKQPASGIEENR 440
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 473 FKALENTNYAVDLGRAKGFSLVGIEGSDIVDGNKlLTLGLVWQLMRRNISITMKTLSSSGRDMSDSQILKWAQDQVTKGG 552
Cdd:COG5069  441 FKAFENENYAVDLGITEGFSLVGIKGLEILDGIR-LKLTLVWQVLRSNTALFNHVLKKDGCGLSDSDLCAWLGSLGLKGD 519
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 553 KNSTIRSFKDQALSN-AHFLLDVLNGIAPGYVDYDLVTPGNTEEERYANAR-LAIS--IARKLGALIWLVPEDINEVRAR 628
Cdd:COG5069  520 KEEGIRSFGDPAGSVsGVFYLDVLKGIHSELVDYDLVTRGFTEFDDIADARsLAISskILRSLGAIIKFLPEDINGVRPR 599
                        650
                 ....*....|...
gi 398365759 629 L-IITFIASLMTL 640
Cdd:COG5069  600 LdVLTFIESLMAD 612
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
287-391 6.13e-23

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: 306753  Cd Length: 109  Bit Score: 95.82  E-value: 6.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759  287 LPPEQILLRWFNYHLKQANWNRRVTNFSKDVSDGENYTILLNQLDPALCSKA--PLQTTDLMERAEQVLQNAE-KLDCRK 363
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDYKklNKSEFDKLENINLALDVAEkKLGVPK 80
                          90       100
                  ....*....|....*....|....*....
gi 398365759  364 YL-TPSSLVAGNPKLNLAFVAHLFNTHPG 391
Cdd:pfam00307  81 VLiEPEDLVEGDNKSVLTYLASLFRRFPK 109
CH cd00014
Calponin homology domain; actin-binding domain which may be present as a single copy or in ...
140-259 1.09e-22

Calponin homology domain; actin-binding domain which may be present as a single copy or in tandem repeats (which increases binding affinity). The CH domain is found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 237981  Cd Length: 107  Bit Score: 95.07  E-value: 1.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 140 EERREFTKHINSVLAGDqdigdllpFPTDTFQLFDECRDGLVLSKLINDSVPDTIDTRVLNwpkkgkELNNFQASENANI 219
Cdd:cd00014    1 SQKEELLRWINKVLGEY--------GPVTINNFSTDLKDGIALCKLLNSLSPDLIDKKKIN------PLSRFKRLENINL 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 398365759 220 VINSAKAIGCVVVNVHSEDIIE-GREHLILGLIWQIIRRGL 259
Cdd:cd00014   67 ALNFAEKLGVPVVNFDAEDLVEdGDEKLVLGLLWSLIRKFL 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
415-519 4.15e-22

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  Cd Length: 101  Bit Score: 93.15  E-value: 4.15e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759   415 RVFTLWLNSL---DVDPPVISLFDDLKDGLILLQAYEKVMPGAVDFKHVNkrpasgAEISRFKALENTNYAVDLGRAKGF 491
Cdd:smart00033   1 KTLLRWVNSLlaeYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVA------ASLSRFKKIENINLALSFAEKLGG 74
                           90       100
                   ....*....|....*....|....*...
gi 398365759   492 SLVGIEGSDIVDGNKlLTLGLVWQLMRR 519
Cdd:smart00033  75 KVVLFEPEDLVEGPK-LILGVIWTLISL 101
 
Name Accession Description Interval E-value
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
1-640 0e+00

Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];


Pssm-ID: 227401  Cd Length: 612  Bit Score: 809.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759   1 MNIVKLQ----RKFPILTQEDLFS-TIEKFRAIDLDDKGWVEKQQALEAVSKDGDATYDEARETLKHVGVDASGRVELDD 75
Cdd:COG5069    1 MEAKKWQkvqkKTFTKWTNEKLISgGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759  76 YVGlvaklresktgaapQTTFNVAPNStpivstAATGLQHKGKGtqakIIVAGSQTGTTHTINEEErrEFTKHINSVLAG 155
Cdd:COG5069   81 GKG--------------VKLFNIGPQD------IVDGNPKLILG----LIWSLISRLTIATINEEG--ELTKHINLLLWC 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 156 DQDIGDLLPfPTDTFQLFDECRDGLVLSKLINDSVPDTIDTRVLNWPKKGKELNNFQASENANIVINSAKAIG-CVVVNV 234
Cdd:COG5069  135 DEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKALNNFQAFENANKVIGIARLIGvEDIVNV 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 235 HSEDiieGREHLILgLIWQIIRRGLLSKIDIKLHpELYRLLEDDETLEQfLRLPPEQILLRWFN-YHLKQANWNrrVTNF 313
Cdd:COG5069  214 SIPD---ERSIMTY-VSWYIIRFGLLEKIDIALH-RVYRLLEADETLIQ-LRLPYEIILLRLLNlIHLKQANWK--VVNF 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 314 SKDVSDGENYTILLNQLDpALCSKAPLQTTDLMERAEQVLQNAEKLDCRKYLTPsslvAGNPKLNLAFVAHLFNTHPGLE 393
Cdd:COG5069  286 SKDVSDGENYTDLLNQLN-ALCSRAPLETTDLHSLAGQILQNAEKYDCRKYLPP----AGNPKLDLAFVAHLFNTHPGQE 360
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 394 PIQEEEKPEIEEFDAEGEREARVFTLWLNSLDVDPPVISLFDDLKDGLILLQAYEKV-MPGAVDFKHVNKRPASGAEISR 472
Cdd:COG5069  361 PLEEEEKPEIEEFDAEGEFEARVFTFWLNSLDVSPEITNLFGDLRDQLILLQALSKKlMPMTVTHKLVKKQPASGIEENR 440
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 473 FKALENTNYAVDLGRAKGFSLVGIEGSDIVDGNKlLTLGLVWQLMRRNISITMKTLSSSGRDMSDSQILKWAQDQVTKGG 552
Cdd:COG5069  441 FKAFENENYAVDLGITEGFSLVGIKGLEILDGIR-LKLTLVWQVLRSNTALFNHVLKKDGCGLSDSDLCAWLGSLGLKGD 519
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 553 KNSTIRSFKDQALSN-AHFLLDVLNGIAPGYVDYDLVTPGNTEEERYANAR-LAIS--IARKLGALIWLVPEDINEVRAR 628
Cdd:COG5069  520 KEEGIRSFGDPAGSVsGVFYLDVLKGIHSELVDYDLVTRGFTEFDDIADARsLAISskILRSLGAIIKFLPEDINGVRPR 599
                        650
                 ....*....|...
gi 398365759 629 L-IITFIASLMTL 640
Cdd:COG5069  600 LdVLTFIESLMAD 612
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
287-391 6.13e-23

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: 306753  Cd Length: 109  Bit Score: 95.82  E-value: 6.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759  287 LPPEQILLRWFNYHLKQANWNRRVTNFSKDVSDGENYTILLNQLDPALCSKA--PLQTTDLMERAEQVLQNAE-KLDCRK 363
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDYKklNKSEFDKLENINLALDVAEkKLGVPK 80
                          90       100
                  ....*....|....*....|....*....
gi 398365759  364 YL-TPSSLVAGNPKLNLAFVAHLFNTHPG 391
Cdd:pfam00307  81 VLiEPEDLVEGDNKSVLTYLASLFRRFPK 109
CH cd00014
Calponin homology domain; actin-binding domain which may be present as a single copy or in ...
140-259 1.09e-22

Calponin homology domain; actin-binding domain which may be present as a single copy or in tandem repeats (which increases binding affinity). The CH domain is found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 237981  Cd Length: 107  Bit Score: 95.07  E-value: 1.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 140 EERREFTKHINSVLAGDqdigdllpFPTDTFQLFDECRDGLVLSKLINDSVPDTIDTRVLNwpkkgkELNNFQASENANI 219
Cdd:cd00014    1 SQKEELLRWINKVLGEY--------GPVTINNFSTDLKDGIALCKLLNSLSPDLIDKKKIN------PLSRFKRLENINL 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 398365759 220 VINSAKAIGCVVVNVHSEDIIE-GREHLILGLIWQIIRRGL 259
Cdd:cd00014   67 ALNFAEKLGVPVVNFDAEDLVEdGDEKLVLGLLWSLIRKFL 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
415-519 4.15e-22

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  Cd Length: 101  Bit Score: 93.15  E-value: 4.15e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759   415 RVFTLWLNSL---DVDPPVISLFDDLKDGLILLQAYEKVMPGAVDFKHVNkrpasgAEISRFKALENTNYAVDLGRAKGF 491
Cdd:smart00033   1 KTLLRWVNSLlaeYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVA------ASLSRFKKIENINLALSFAEKLGG 74
                           90       100
                   ....*....|....*....|....*...
gi 398365759   492 SLVGIEGSDIVDGNKlLTLGLVWQLMRR 519
Cdd:smart00033  75 KVVLFEPEDLVEGPK-LILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
411-520 1.09e-21

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: 306753  Cd Length: 109  Bit Score: 91.97  E-value: 1.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759  411 EREARVFTLWLNS---LDVDPPVI-SLFDDLKDGLILLQAYEKVMPGAVDFKHVNKRPasgaeisrFKALENTNYAVDLG 486
Cdd:pfam00307   1 LELEKELLRWINShlaEYGPGVRVtNFTTDLRDGLALCALLNKLAPGLVDYKKLNKSE--------FDKLENINLALDVA 72
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 398365759  487 RAK-GFSLVGIEGSDIVDGNKLLTLGLVWQLMRRN 520
Cdd:pfam00307  73 EKKlGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
143-257 4.04e-21

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  Cd Length: 101  Bit Score: 90.45  E-value: 4.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759   143 REFTKHINSVLAGDQdigdllpfPTDTFQLFDECRDGLVLSKLINDSVPDTIDTRVLNwpkkgKELNNFQASENANIVIN 222
Cdd:smart00033   1 KTLLRWVNSLLAEYD--------KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVA-----ASLSRFKKIENINLALS 67
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 398365759   223 SAKAIGCVVVNVHSEDIIEGReHLILGLIWQIIRR 257
Cdd:smart00033  68 FAEKLGGKVVLFEPEDLVEGP-KLILGVIWTLISL 101
CH cd00014
Calponin homology domain; actin-binding domain which may be present as a single copy or in ...
288-390 2.02e-19

Calponin homology domain; actin-binding domain which may be present as a single copy or in tandem repeats (which increases binding affinity). The CH domain is found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 237981  Cd Length: 107  Bit Score: 85.83  E-value: 2.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 288 PPEQILLRWFNYHLKQANWnRRVTNFSKDVSDGENYTILLNQLDPALCSKA---PLQTTDLMERAEQVLQNAEKLDCRK- 363
Cdd:cd00014    1 SQKEELLRWINKVLGEYGP-VTINNFSTDLKDGIALCKLLNSLSPDLIDKKkinPLSRFKRLENINLALNFAEKLGVPVv 79
                         90       100
                 ....*....|....*....|....*...
gi 398365759 364 YLTPSSLV-AGNPKLNLAFVAHLFNTHP 390
Cdd:cd00014   80 NFDAEDLVeDGDEKLVLGLLWSLIRKFL 107
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
139-258 3.26e-17

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: 306753  Cd Length: 109  Bit Score: 79.26  E-value: 3.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759  139 EEERREFTKHINSVLAGDQDigdllpfPTDTFQLFDECRDGLVLSKLINDSVPDTIDTRVLNWpkkgkelNNFQASENAN 218
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGP-------GVRVTNFTTDLRDGLALCALLNKLAPGLVDYKKLNK-------SEFDKLENIN 66
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 398365759  219 IVINSA-KAIGCVVVNVHSEDIIEGREHLILGLIWQIIRRG 258
Cdd:pfam00307  67 LALDVAeKKLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRF 107
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
292-386 3.40e-15

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  Cd Length: 101  Bit Score: 73.50  E-value: 3.40e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759   292 ILLRWFNYHLKQANwNRRVTNFSKDVSDGENYTILLNQLDPALCSK----APLQTTDLMERAEQVLQNAEKL-DCRKYLT 366
Cdd:smart00033   2 TLLRWVNSLLAEYD-KPPVTNFSSDLKDGVALCALLNSLSPGLVDKkkvaASLSRFKKIENINLALSFAEKLgGKVVLFE 80
                           90       100
                   ....*....|....*....|
gi 398365759   367 PSSLVAGnPKLNLAFVAHLF 386
Cdd:smart00033  81 PEDLVEG-PKLILGVIWTLI 99
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
534-638 1.69e-14

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: 306753  Cd Length: 109  Bit Score: 71.55  E-value: 1.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759  534 DMSDSQILKWAQDQVTKGGKNSTIRSFKDQaLSNAHFLLDVLNGIAPGYVDYDLVTPgnTEEERYANARLAISIAR-KLG 612
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFTTD-LRDGLALCALLNKLAPGLVDYKKLNK--SEFDKLENINLALDVAEkKLG 77
                          90       100
                  ....*....|....*....|....*..
gi 398365759  613 ALIWLV-PEDINEVRARLIITFIASLM 638
Cdd:pfam00307  78 VPKVLIePEDLVEGDNKSVLTYLASLF 104
CH cd00014
Calponin homology domain; actin-binding domain which may be present as a single copy or in ...
417-519 3.34e-14

Calponin homology domain; actin-binding domain which may be present as a single copy or in tandem repeats (which increases binding affinity). The CH domain is found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 237981  Cd Length: 107  Bit Score: 70.80  E-value: 3.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 417 FTLWLNSL---DVDPPVISLFDDLKDGLILLQAYEKVMPGAVDFKHVNKrpasgaeISRFKALENTNYAVDLGRAKGFSL 493
Cdd:cd00014    6 LLRWINKVlgeYGPVTINNFSTDLKDGIALCKLLNSLSPDLIDKKKINP-------LSRFKRLENINLALNFAEKLGVPV 78
                         90       100
                 ....*....|....*....|....*..
gi 398365759 494 VGIEGSDIV-DGNKLLTLGLVWQLMRR 519
Cdd:cd00014   79 VNFDAEDLVeDGDEKLVLGLLWSLIRK 105
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
539-640 8.80e-14

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  Cd Length: 101  Bit Score: 69.27  E-value: 8.80e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759   539 QILKWAQDQVTKGGKnsTIRSFKDQALSNAHFLLDVLNGIAPGYVDYDLVTPGNTEEERYANARLAISIARKLG-ALIWL 617
Cdd:smart00033   2 TLLRWVNSLLAEYDK--PPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGgKVVLF 79
                           90       100
                   ....*....|....*....|...
gi 398365759   618 VPEDINEVRaRLIITFIASLMTL 640
Cdd:smart00033  80 EPEDLVEGP-KLILGVIWTLISL 101
CH cd00014
Calponin homology domain; actin-binding domain which may be present as a single copy or in ...
536-638 1.48e-06

Calponin homology domain; actin-binding domain which may be present as a single copy or in tandem repeats (which increases binding affinity). The CH domain is found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 237981  Cd Length: 107  Bit Score: 48.08  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365759 536 SDSQILKWAQdQVTKGGKNSTIRSFkDQALSNAHFLLDVLNGIAPGYVDYDLVTPGNTEEERYaNARLAISIARKLGA-L 614
Cdd:cd00014    2 QKEELLRWIN-KVLGEYGPVTINNF-STDLKDGIALCKLLNSLSPDLIDKKKINPLSRFKRLE-NINLALNFAEKLGVpV 78
                         90       100
                 ....*....|....*....|....*
gi 398365759 615 IWLVPEDI-NEVRARLIITFIASLM 638
Cdd:cd00014   79 VNFDAEDLvEDGDEKLVLGLLWSLI 103
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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