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Conserved domains on  [gi|15224051|ref|NP_178552|]
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actin binding calponin homology domain-containing protein [Arabidopsis thaliana]

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List of domain hits

Name Accession Description Interval E-value
CH cd00014
Calponin homology domain; actin-binding domain which may be present as a single copy or in ...
117-231 1.37e-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: 85.06  E-value: 1.37e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 117 SEKASYVSHINSYLKdepnlksyLPINPTTNALFDLVKDGVLLCKLINIAVPGTIDERAINTkkeLNPWERTENLSLCLN 196
Cdd:cd00014   1 SQKEELLRWINKVLG--------EYGPVTINNFSTDLKDGIALCKLLNSLSPDLIDKKKINP---LSRFKRLENINLALN 69
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15224051 197 SAKAIGCTVVNIGTQDIAE-GTPHLVLGLIFQIIKI 231
Cdd:cd00014  70 FAEKLGVPVVNFDAEDLVEdGDEKLVLGLLWSLIRK 105
CH cd00014
Calponin homology domain; actin-binding domain which may be present as a single copy or in ...
263-362 1.20e-16

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: 76.58  E-value: 1.20e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 263 PEKLLLKWMNFHLKKAGYEKqVTNFSSDVKDGEAYAYLLNALAPEHSTNVTLEIKDPS---ERATKVLEQAEKLDCKRF- 338
Cdd:cd00014   2 QKEELLRWINKVLGEYGPVT-INNFSTDLKDGIALCKLLNSLSPDLIDKKKINPLSRFkrlENINLALNFAEKLGVPVVn 80
                        90       100
                ....*....|....*....|....*
gi 15224051 339 LSPKDIVE-GSANLNLAFVAQLFHH 362
Cdd:cd00014  81 FDAEDLVEdGDEKLVLGLLWSLIRK 105
CH cd00014
Calponin homology domain; actin-binding domain which may be present as a single copy or in ...
397-492 6.05e-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: 68.88  E-value: 6.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 397 WMNS-LGAVTY--VDNVFEDVRNGWVLLEVLDKVSPGSVNWKHANKppiKMPFKKVENCNQVIKIGKELNFSLVNVAGHD 473
Cdd:cd00014   9 WINKvLGEYGPvtINNFSTDLKDGIALCKLLNSLSPDLIDKKKINP---LSRFKRLENINLALNFAEKLGVPVVNFDAED 85
                        90       100
                ....*....|....*....|
gi 15224051 474 IMQ-GNKKLLLAFLWQLMRY 492
Cdd:cd00014  86 LVEdGDEKLVLGLLWSLIRK 105
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
514-615 2.80e-13

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


:

Pssm-ID: 214479  Cd Length: 101  Bit Score: 66.57  E-value: 2.80e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051    514 DILNWANRKVKKSGrtSQAVSFKDKNLANGIFFLELLSAVEPRVVNWSLVSKGETQEEKNLNATYIISVARKLGCSIFLL 593
Cdd:smart00033   2 TLLRWVNSLLAEYD--KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLF 79
                           90       100
                   ....*....|....*....|...
gi 15224051    594 -PEDILEVNqRMMLILAASIMNW 615
Cdd:smart00033  80 ePEDLVEGP-KLILGVIWTLISL 101
 
Name Accession Description Interval E-value
CH cd00014
Calponin homology domain; actin-binding domain which may be present as a single copy or in ...
117-231 1.37e-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: 85.06  E-value: 1.37e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 117 SEKASYVSHINSYLKdepnlksyLPINPTTNALFDLVKDGVLLCKLINIAVPGTIDERAINTkkeLNPWERTENLSLCLN 196
Cdd:cd00014   1 SQKEELLRWINKVLG--------EYGPVTINNFSTDLKDGIALCKLLNSLSPDLIDKKKINP---LSRFKRLENINLALN 69
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15224051 197 SAKAIGCTVVNIGTQDIAE-GTPHLVLGLIFQIIKI 231
Cdd:cd00014  70 FAEKLGVPVVNFDAEDLVEdGDEKLVLGLLWSLIRK 105
CH cd00014
Calponin homology domain; actin-binding domain which may be present as a single copy or in ...
263-362 1.20e-16

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: 76.58  E-value: 1.20e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 263 PEKLLLKWMNFHLKKAGYEKqVTNFSSDVKDGEAYAYLLNALAPEHSTNVTLEIKDPS---ERATKVLEQAEKLDCKRF- 338
Cdd:cd00014   2 QKEELLRWINKVLGEYGPVT-INNFSTDLKDGIALCKLLNSLSPDLIDKKKINPLSRFkrlENINLALNFAEKLGVPVVn 80
                        90       100
                ....*....|....*....|....*
gi 15224051 339 LSPKDIVE-GSANLNLAFVAQLFHH 362
Cdd:cd00014  81 FDAEDLVEdGDEKLVLGLLWSLIRK 105
CH cd00014
Calponin homology domain; actin-binding domain which may be present as a single copy or in ...
397-492 6.05e-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: 68.88  E-value: 6.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 397 WMNS-LGAVTY--VDNVFEDVRNGWVLLEVLDKVSPGSVNWKHANKppiKMPFKKVENCNQVIKIGKELNFSLVNVAGHD 473
Cdd:cd00014   9 WINKvLGEYGPvtINNFSTDLKDGIALCKLLNSLSPDLIDKKKINP---LSRFKRLENINLALNFAEKLGVPVVNFDAED 85
                        90       100
                ....*....|....*....|
gi 15224051 474 IMQ-GNKKLLLAFLWQLMRY 492
Cdd:cd00014  86 LVEdGDEKLVLGLLWSLIRK 105
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
264-362 4.06e-19

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: 249759  Cd Length: 104  Bit Score: 83.49  E-value: 4.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051   264 EKLLLKWMNFHLKKaGYEKQVTNFSSDVKDGEAYAYLLNALAPEHS--TNVTLEIKDPSERATKVLEQAEK-LDCKRFLS 340
Cdd:pfam00307   1 EKALLRWINEVLEK-YQGLPITNFFEDLRDGVALCALLNKLRPGLIdlKKVNKNRFDKLENLNLALEFAEKkLGVPKVLE 79
                          90       100
                  ....*....|....*....|...
gi 15224051   341 PKDIVE-GSANLNLAFVAQLFHH 362
Cdd:pfam00307  80 PEDLVEdGNKKLVLTLLAQLFRR 102
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
394-492 6.25e-19

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: 83.13  E-value: 6.25e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051    394 FRHWMNSLGAV---TYVDNVFEDVRNGWVLLEVLDKVSPGSVNWKHANKPpiKMPFKKVENCNQVIKIGKELNFSLVNVA 470
Cdd:smart00033   3 LLRWVNSLLAEydkPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAS--LSRFKKIENINLALSFAEKLGGKVVLFE 80
                           90       100
                   ....*....|....*....|..
gi 15224051    471 GHDIMQGnKKLLLAFLWQLMRY 492
Cdd:smart00033  81 PEDLVEG-PKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
391-494 2.79e-18

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: 249759  Cd Length: 104  Bit Score: 81.18  E-value: 2.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051   391 ERCFRHWMNSLGAVTY---VDNVFEDVRNGWVLLEVLDKVSPGSVNWKHANkppiKMPFKKVENCNQVIKIGKE-LNFSL 466
Cdd:pfam00307   1 EKALLRWINEVLEKYQglpITNFFEDLRDGVALCALLNKLRPGLIDLKKVN----KNRFDKLENLNLALEFAEKkLGVPK 76
                          90       100
                  ....*....|....*....|....*....
gi 15224051   467 VNvAGHDIM-QGNKKLLLAFLWQLMRYTM 494
Cdd:pfam00307  77 VL-EPEDLVeDGNKKLVLTLLAQLFRRFE 104
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
142-231 3.64e-17

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: 78.13  E-value: 3.64e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051    142 INPTTNALFDLVKDGVLLCKLINIAVPGTIDERAINTKKelNPWERTENLSLCLNSAKAIGCTVVNIGTQDIAEGtPHLV 221
Cdd:smart00033  15 DKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASL--SRFKKIENINLALSFAEKLGGKVVLFEPEDLVEG-PKLI 91
                           90
                   ....*....|
gi 15224051    222 LGLIFQIIKI 231
Cdd:smart00033  92 LGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
119-230 1.32e-13

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: 249759  Cd Length: 104  Bit Score: 67.70  E-value: 1.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051   119 KASYVSHINSYLKDEPNLksylpinPTTNaLFDLVKDGVLLCKLINIAVPGTIDERAINTkkelNPWERTENLSLCLNSA 198
Cdd:pfam00307   1 EKALLRWINEVLEKYQGL-------PITN-FFEDLRDGVALCALLNKLRPGLIDLKKVNK----NRFDKLENLNLALEFA 68
                          90       100       110
                  ....*....|....*....|....*....|....
gi 15224051   199 KA-IGCTVVNiGTQDIAE-GTPHLVLGLIFQIIK 230
Cdd:pfam00307  69 EKkLGVPKVL-EPEDLVEdGNKKLVLTLLAQLFR 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
265-360 2.47e-13

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


Pssm-ID: 214479  Cd Length: 101  Bit Score: 66.96  E-value: 2.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051    265 KLLLKWMNFHLKKAGYEKqVTNFSSDVKDGEAYAYLLNALAP----EHSTNVTLEIKDPSERATKVLEQAEKLDCKRFL- 339
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPP-VTNFSSDLKDGVALCALLNSLSPglvdKKKVAASLSRFKKIENINLALSFAEKLGGKVVLf 79
                           90       100
                   ....*....|....*....|.
gi 15224051    340 SPKDIVEGSaNLNLAFVAQLF 360
Cdd:smart00033  80 EPEDLVEGP-KLILGVIWTLI 99
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
514-615 2.80e-13

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


Pssm-ID: 214479  Cd Length: 101  Bit Score: 66.57  E-value: 2.80e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051    514 DILNWANRKVKKSGrtSQAVSFKDKNLANGIFFLELLSAVEPRVVNWSLVSKGETQEEKNLNATYIISVARKLGCSIFLL 593
Cdd:smart00033   2 TLLRWVNSLLAEYD--KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLF 79
                           90       100
                   ....*....|....*....|...
gi 15224051    594 -PEDILEVNqRMMLILAASIMNW 615
Cdd:smart00033  80 ePEDLVEGP-KLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
512-615 1.82e-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: 249759  Cd Length: 104  Bit Score: 61.53  E-value: 1.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051   512 EADILNWANRKVKKsGRTSQAVSFKdKNLANGIFFLELLSAVEPRVVNWSLVSKgeTQEEKNLNATYIISVA-RKLGCSI 590
Cdd:pfam00307   1 EKALLRWINEVLEK-YQGLPITNFF-EDLRDGVALCALLNKLRPGLIDLKKVNK--NRFDKLENLNLALEFAeKKLGVPK 76
                          90       100
                  ....*....|....*....|....*.
gi 15224051   591 FLLPEDILE-VNQRMMLILAASIMNW 615
Cdd:pfam00307  77 VLEPEDLVEdGNKKLVLTLLAQLFRR 102
CH cd00014
Calponin homology domain; actin-binding domain which may be present as a single copy or in ...
510-617 3.68e-09

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: 54.62  E-value: 3.68e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 510 ITEADILNWANRKVKKSGrtSQAVSFKDKNLANGIFFLELLSAVEPRVVNWSlVSKGETQEEKNLNATYIISVARKLGCS 589
Cdd:cd00014   1 SQKEELLRWINKVLGEYG--PVTINNFSTDLKDGIALCKLLNSLSPDLIDKK-KINPLSRFKRLENINLALNFAEKLGVP 77
                        90       100       110
                ....*....|....*....|....*....|
gi 15224051 590 IFLL-PEDI-LEVNQRMMLILAASIMNWSL 617
Cdd:cd00014  78 VVNFdAEDLvEDGDEKLVLGLLWSLIRKFL 107
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]
112-607 8.71e-73

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 247.93  E-value: 8.71e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 112 HSINESEKasYVSHINSYLKDEPNLKSYLPiNPTTNALFDLVKDGVLLCKLINIAVPGTIDERAINTK---KELNPWERT 188
Cdd:COG5069 116 ATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQkknKALNNFQAF 192
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 189 ENLSLCLNSAKAIG-CTVVNIGTQDIAEgtpHLVLgLIFQIIKIQLLA--DLNLKKTPQLVELVEENQDveelMGLAPEK 265
Cdd:COG5069 193 ENANKVIGIARLIGvEDIVNVSIPDERS---IMTY-VSWYIIRFGLLEkiDIALHRVYRLLEADETLIQ----LRLPYEI 264
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 266 LLLKWMNFHLKKAGYEKqVTNFSSDVKDGEAYAYLLNALAPEHSTNVtLEIKDPSERATKVLEQAEKLDCKRFLSPKdiv 345
Cdd:COG5069 265 ILLRLLNLIHLKQANWK-VVNFSKDVSDGENYTDLLNQLNALCSRAP-LETTDLHSLAGQILQNAEKYDCRKYLPPA--- 339
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 346 eGSANLNLAFVAQLFhhrNGLSDESPKVPISVAEMVTEDEETSREERCFRHWMNSLGAVTYVDNVFEDVRNGWVLLEVLD 425
Cdd:COG5069 340 -GNPKLDLAFVAHLF---NTHPGQEPLEEEEKPEIEEFDAEGEFEARVFTFWLNSLDVSPEITNLFGDLRDQLILLQALS 415
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 426 KV-SPGSVNWKHANKPPIK----MPFKKVENCNQVIKIGKELNFSLVNVAGHDIMQGNkKLLLAFLWQLMRYTMLQILNN 500
Cdd:COG5069 416 KKlMPMTVTHKLVKKQPASgieeNRFKAFENENYAVDLGITEGFSLVGIKGLEILDGI-RLKLTLVWQVLRSNTALFNHV 494
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 501 LRShcQGKDITEADILNWANRKVKKSGRTSQAVSFKDKNLAN-GIFFLELLSAVEPRVVNWSLVSKGETQEEKNLNA-TY 578
Cdd:COG5069 495 LKK--DGCGLSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSVsGVFYLDVLKGIHSELVDYDLVTRGFTEFDDIADArSL 572
                       490       500       510
                ....*....|....*....|....*....|.
gi 15224051 579 IIS--VARKLGCSIFLLPEDILEVNQRMMLI 607
Cdd:COG5069 573 AISskILRSLGAIIKFLPEDINGVRPRLDVL 603
 
Name Accession Description Interval E-value
CH cd00014
Calponin homology domain; actin-binding domain which may be present as a single copy or in ...
117-231 1.37e-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: 85.06  E-value: 1.37e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 117 SEKASYVSHINSYLKdepnlksyLPINPTTNALFDLVKDGVLLCKLINIAVPGTIDERAINTkkeLNPWERTENLSLCLN 196
Cdd:cd00014   1 SQKEELLRWINKVLG--------EYGPVTINNFSTDLKDGIALCKLLNSLSPDLIDKKKINP---LSRFKRLENINLALN 69
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15224051 197 SAKAIGCTVVNIGTQDIAE-GTPHLVLGLIFQIIKI 231
Cdd:cd00014  70 FAEKLGVPVVNFDAEDLVEdGDEKLVLGLLWSLIRK 105
CH cd00014
Calponin homology domain; actin-binding domain which may be present as a single copy or in ...
263-362 1.20e-16

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: 76.58  E-value: 1.20e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 263 PEKLLLKWMNFHLKKAGYEKqVTNFSSDVKDGEAYAYLLNALAPEHSTNVTLEIKDPS---ERATKVLEQAEKLDCKRF- 338
Cdd:cd00014   2 QKEELLRWINKVLGEYGPVT-INNFSTDLKDGIALCKLLNSLSPDLIDKKKINPLSRFkrlENINLALNFAEKLGVPVVn 80
                        90       100
                ....*....|....*....|....*
gi 15224051 339 LSPKDIVE-GSANLNLAFVAQLFHH 362
Cdd:cd00014  81 FDAEDLVEdGDEKLVLGLLWSLIRK 105
CH cd00014
Calponin homology domain; actin-binding domain which may be present as a single copy or in ...
397-492 6.05e-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: 68.88  E-value: 6.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 397 WMNS-LGAVTY--VDNVFEDVRNGWVLLEVLDKVSPGSVNWKHANKppiKMPFKKVENCNQVIKIGKELNFSLVNVAGHD 473
Cdd:cd00014   9 WINKvLGEYGPvtINNFSTDLKDGIALCKLLNSLSPDLIDKKKINP---LSRFKRLENINLALNFAEKLGVPVVNFDAED 85
                        90       100
                ....*....|....*....|
gi 15224051 474 IMQ-GNKKLLLAFLWQLMRY 492
Cdd:cd00014  86 LVEdGDEKLVLGLLWSLIRK 105
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
264-362 4.06e-19

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: 249759  Cd Length: 104  Bit Score: 83.49  E-value: 4.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051   264 EKLLLKWMNFHLKKaGYEKQVTNFSSDVKDGEAYAYLLNALAPEHS--TNVTLEIKDPSERATKVLEQAEK-LDCKRFLS 340
Cdd:pfam00307   1 EKALLRWINEVLEK-YQGLPITNFFEDLRDGVALCALLNKLRPGLIdlKKVNKNRFDKLENLNLALEFAEKkLGVPKVLE 79
                          90       100
                  ....*....|....*....|...
gi 15224051   341 PKDIVE-GSANLNLAFVAQLFHH 362
Cdd:pfam00307  80 PEDLVEdGNKKLVLTLLAQLFRR 102
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
394-492 6.25e-19

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: 83.13  E-value: 6.25e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051    394 FRHWMNSLGAV---TYVDNVFEDVRNGWVLLEVLDKVSPGSVNWKHANKPpiKMPFKKVENCNQVIKIGKELNFSLVNVA 470
Cdd:smart00033   3 LLRWVNSLLAEydkPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAS--LSRFKKIENINLALSFAEKLGGKVVLFE 80
                           90       100
                   ....*....|....*....|..
gi 15224051    471 GHDIMQGnKKLLLAFLWQLMRY 492
Cdd:smart00033  81 PEDLVEG-PKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
391-494 2.79e-18

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: 249759  Cd Length: 104  Bit Score: 81.18  E-value: 2.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051   391 ERCFRHWMNSLGAVTY---VDNVFEDVRNGWVLLEVLDKVSPGSVNWKHANkppiKMPFKKVENCNQVIKIGKE-LNFSL 466
Cdd:pfam00307   1 EKALLRWINEVLEKYQglpITNFFEDLRDGVALCALLNKLRPGLIDLKKVN----KNRFDKLENLNLALEFAEKkLGVPK 76
                          90       100
                  ....*....|....*....|....*....
gi 15224051   467 VNvAGHDIM-QGNKKLLLAFLWQLMRYTM 494
Cdd:pfam00307  77 VL-EPEDLVeDGNKKLVLTLLAQLFRRFE 104
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
142-231 3.64e-17

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: 78.13  E-value: 3.64e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051    142 INPTTNALFDLVKDGVLLCKLINIAVPGTIDERAINTKKelNPWERTENLSLCLNSAKAIGCTVVNIGTQDIAEGtPHLV 221
Cdd:smart00033  15 DKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASL--SRFKKIENINLALSFAEKLGGKVVLFEPEDLVEG-PKLI 91
                           90
                   ....*....|
gi 15224051    222 LGLIFQIIKI 231
Cdd:smart00033  92 LGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
119-230 1.32e-13

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: 249759  Cd Length: 104  Bit Score: 67.70  E-value: 1.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051   119 KASYVSHINSYLKDEPNLksylpinPTTNaLFDLVKDGVLLCKLINIAVPGTIDERAINTkkelNPWERTENLSLCLNSA 198
Cdd:pfam00307   1 EKALLRWINEVLEKYQGL-------PITN-FFEDLRDGVALCALLNKLRPGLIDLKKVNK----NRFDKLENLNLALEFA 68
                          90       100       110
                  ....*....|....*....|....*....|....
gi 15224051   199 KA-IGCTVVNiGTQDIAE-GTPHLVLGLIFQIIK 230
Cdd:pfam00307  69 EKkLGVPKVL-EPEDLVEdGNKKLVLTLLAQLFR 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
265-360 2.47e-13

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


Pssm-ID: 214479  Cd Length: 101  Bit Score: 66.96  E-value: 2.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051    265 KLLLKWMNFHLKKAGYEKqVTNFSSDVKDGEAYAYLLNALAP----EHSTNVTLEIKDPSERATKVLEQAEKLDCKRFL- 339
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPP-VTNFSSDLKDGVALCALLNSLSPglvdKKKVAASLSRFKKIENINLALSFAEKLGGKVVLf 79
                           90       100
                   ....*....|....*....|.
gi 15224051    340 SPKDIVEGSaNLNLAFVAQLF 360
Cdd:smart00033  80 EPEDLVEGP-KLILGVIWTLI 99
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
514-615 2.80e-13

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


Pssm-ID: 214479  Cd Length: 101  Bit Score: 66.57  E-value: 2.80e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051    514 DILNWANRKVKKSGrtSQAVSFKDKNLANGIFFLELLSAVEPRVVNWSLVSKGETQEEKNLNATYIISVARKLGCSIFLL 593
Cdd:smart00033   2 TLLRWVNSLLAEYD--KPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLF 79
                           90       100
                   ....*....|....*....|...
gi 15224051    594 -PEDILEVNqRMMLILAASIMNW 615
Cdd:smart00033  80 ePEDLVEGP-KLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
512-615 1.82e-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: 249759  Cd Length: 104  Bit Score: 61.53  E-value: 1.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051   512 EADILNWANRKVKKsGRTSQAVSFKdKNLANGIFFLELLSAVEPRVVNWSLVSKgeTQEEKNLNATYIISVA-RKLGCSI 590
Cdd:pfam00307   1 EKALLRWINEVLEK-YQGLPITNFF-EDLRDGVALCALLNKLRPGLIDLKKVNK--NRFDKLENLNLALEFAeKKLGVPK 76
                          90       100
                  ....*....|....*....|....*.
gi 15224051   591 FLLPEDILE-VNQRMMLILAASIMNW 615
Cdd:pfam00307  77 VLEPEDLVEdGNKKLVLTLLAQLFRR 102
CH cd00014
Calponin homology domain; actin-binding domain which may be present as a single copy or in ...
510-617 3.68e-09

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: 54.62  E-value: 3.68e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 510 ITEADILNWANRKVKKSGrtSQAVSFKDKNLANGIFFLELLSAVEPRVVNWSlVSKGETQEEKNLNATYIISVARKLGCS 589
Cdd:cd00014   1 SQKEELLRWINKVLGEYG--PVTINNFSTDLKDGIALCKLLNSLSPDLIDKK-KINPLSRFKRLENINLALNFAEKLGVP 77
                        90       100       110
                ....*....|....*....|....*....|
gi 15224051 590 IFLL-PEDI-LEVNQRMMLILAASIMNWSL 617
Cdd:cd00014  78 VVNFdAEDLvEDGDEKLVLGLLWSLIRKFL 107
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]
112-607 8.71e-73

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 247.93  E-value: 8.71e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 112 HSINESEKasYVSHINSYLKDEPNLKSYLPiNPTTNALFDLVKDGVLLCKLINIAVPGTIDERAINTK---KELNPWERT 188
Cdd:COG5069 116 ATINEEGE--LTKHINLLLWCDEDTGGYKP-EVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQkknKALNNFQAF 192
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 189 ENLSLCLNSAKAIG-CTVVNIGTQDIAEgtpHLVLgLIFQIIKIQLLA--DLNLKKTPQLVELVEENQDveelMGLAPEK 265
Cdd:COG5069 193 ENANKVIGIARLIGvEDIVNVSIPDERS---IMTY-VSWYIIRFGLLEkiDIALHRVYRLLEADETLIQ----LRLPYEI 264
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 266 LLLKWMNFHLKKAGYEKqVTNFSSDVKDGEAYAYLLNALAPEHSTNVtLEIKDPSERATKVLEQAEKLDCKRFLSPKdiv 345
Cdd:COG5069 265 ILLRLLNLIHLKQANWK-VVNFSKDVSDGENYTDLLNQLNALCSRAP-LETTDLHSLAGQILQNAEKYDCRKYLPPA--- 339
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 346 eGSANLNLAFVAQLFhhrNGLSDESPKVPISVAEMVTEDEETSREERCFRHWMNSLGAVTYVDNVFEDVRNGWVLLEVLD 425
Cdd:COG5069 340 -GNPKLDLAFVAHLF---NTHPGQEPLEEEEKPEIEEFDAEGEFEARVFTFWLNSLDVSPEITNLFGDLRDQLILLQALS 415
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 426 KV-SPGSVNWKHANKPPIK----MPFKKVENCNQVIKIGKELNFSLVNVAGHDIMQGNkKLLLAFLWQLMRYTMLQILNN 500
Cdd:COG5069 416 KKlMPMTVTHKLVKKQPASgieeNRFKAFENENYAVDLGITEGFSLVGIKGLEILDGI-RLKLTLVWQVLRSNTALFNHV 494
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 501 LRShcQGKDITEADILNWANRKVKKSGRTSQAVSFKDKNLAN-GIFFLELLSAVEPRVVNWSLVSKGETQEEKNLNA-TY 578
Cdd:COG5069 495 LKK--DGCGLSDSDLCAWLGSLGLKGDKEEGIRSFGDPAGSVsGVFYLDVLKGIHSELVDYDLVTRGFTEFDDIADArSL 572
                       490       500       510
                ....*....|....*....|....*....|.
gi 15224051 579 IIS--VARKLGCSIFLLPEDILEVNQRMMLI 607
Cdd:COG5069 573 AISskILRSLGAIIKFLPEDINGVRPRLDVL 603
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]
388-610 9.97e-03

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 37.61  E-value: 9.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 388 SREERCFRHWMN---SLGAVTYVDNVFEDVRnGWV----LLEVLDKVSPGSVNwkhankPPIKMPFKKVENCNQVIKIGK 460
Cdd:COG5069   8 KVQKKTFTKWTNeklISGGQKEFGDLDTDLK-DGVklaqLLEALQKDNAGEYN------ETPETRIHVMENVSGRLEFIK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224051 461 ELNFSLVNVAGHDIMQGNKKLLLAFLWQLMRYTMLQILNNlrshcQGKDITEADILNWANRKVKKSGRTSQAVSFKDKnL 540
Cdd:COG5069  81 GKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINE-----EGELTKHINLLLWCDEDTGGYKPEVDTFDFFRS-W 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15224051 541 ANGIFFLELLS-----AVEPRVVNWSLVSKGETQEEKNLNATYIISVARKLGCsifllpEDILEV---NQRMMLILAA 610
Cdd:COG5069 155 RDGLAFSALIHdsrpdTLDPNVLDLQKKNKALNNFQAFENANKVIGIARLIGV------EDIVNVsipDERSIMTYVS 226
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • 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 et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • 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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