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Conserved domains on  [gi|18860551|ref|NP_573395|]
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beta-parvin [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_SF super family cl00030
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 236-365 2.65e-70

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).


The actual alignment was detected with superfamily member cd21338:

Pssm-ID: 469584  Cd Length: 130  Bit Score: 215.99  E-value: 2.65e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860551 236 GRFERDAFDTLFDHAPDKLNLVKKSLITFVNKHLNKLNLEVTDLETQFADGVYLVLLLGLLEDYFVPLHNFYLTPDSFDQ 315
Cdd:cd21338   1 GRFERDAFDTLFDHAPDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHNFYLTPESFDQ 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 18860551 316 KVHNVAFAFELMLDGGLKKPKARPEDVVNLDLKSTLRVLYTLFTKYKDVE 365
Cdd:cd21338  81 KVHNVSFAFELMQDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE 130
CH_PARVB_rpt1 cd21336
first calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is ...
 89-194 3.85e-67

first calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-parvin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


:

Pssm-ID: 409185  Cd Length: 106  Bit Score: 207.05  E-value: 3.85e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860551  89 ELVKVLLDWINDVLAEERIIVKQLEEDLYDGQVLQKLLEKLAHCKLNVAEVTQSEIGQKQKLQTVLEAVQDLLRPHGWPL 168
Cdd:cd21336   1 ELVKVLIDWINDVLVEERIIVKDLEEDLYDGQVLQKLLEKLAGRKLNVAEVTQSEIGQKQKLQTVLEAVNDLLRPQGWAI 80

                        90       100
                ....*....|....*....|....*.
gi 18860551 169 RWNVDSIHGKNLVAILHLLVSLAMHF 194
Cdd:cd21336  81 KWSVDSIHGKNLVAILHLLVALAMHF 106
 
Name Accession Description Interval E-value
CH_PARVB_rpt2 cd21338
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ...
 236-365 2.65e-70

second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409187  Cd Length: 130  Bit Score: 215.99  E-value: 2.65e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860551 236 GRFERDAFDTLFDHAPDKLNLVKKSLITFVNKHLNKLNLEVTDLETQFADGVYLVLLLGLLEDYFVPLHNFYLTPDSFDQ 315
Cdd:cd21338   1 GRFERDAFDTLFDHAPDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHNFYLTPESFDQ 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 18860551 316 KVHNVAFAFELMLDGGLKKPKARPEDVVNLDLKSTLRVLYTLFTKYKDVE 365
Cdd:cd21338  81 KVHNVSFAFELMQDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE 130
CH_PARVB_rpt1 cd21336
first calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is ...
 89-194 3.85e-67

first calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-parvin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409185  Cd Length: 106  Bit Score: 207.05  E-value: 3.85e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860551  89 ELVKVLLDWINDVLAEERIIVKQLEEDLYDGQVLQKLLEKLAHCKLNVAEVTQSEIGQKQKLQTVLEAVQDLLRPHGWPL 168
Cdd:cd21336   1 ELVKVLIDWINDVLVEERIIVKDLEEDLYDGQVLQKLLEKLAGRKLNVAEVTQSEIGQKQKLQTVLEAVNDLLRPQGWAI 80

                        90       100
                ....*....|....*....|....*.
gi 18860551 169 RWNVDSIHGKNLVAILHLLVSLAMHF 194
Cdd:cd21336  81 KWSVDSIHGKNLVAILHLLVALAMHF 106
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 88-196 1.11e-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: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 80.41  E-value: 1.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860551    88 KELVKVLLDWINDVLAE--ERIIVKQLEEDLYDGQVLQKLLEKLAHCKLNVAEVTQSEIGQKQKLQTVLEAVQDLLRPHG 165
Cdd:pfam00307   1 LELEKELLRWINSHLAEygPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKKLGVPK 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 18860551   166 WpLRWNVDSIHGKNLvAILHLLVSLAMHFRA 196
Cdd:pfam00307  81 V-LIEPEDLVEGDNK-SVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 257-362 2.06e-06

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: 46.13  E-value: 2.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860551   257 VKKSLITFVNKHLNKL--NLEVTDLETQFADGvylvlllglledyfVPLHNFY--LTPDSFD---------QKVHNVAFA 323
Cdd:pfam00307   3 LEKELLRWINSHLAEYgpGVRVTNFTTDLRDG--------------LALCALLnkLAPGLVDkkklnksefDKLENINLA 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 18860551   324 FEL-MLDGGLKKPKARPEDVVNLDLKSTLRVLYTLFTKYK 362
Cdd:pfam00307  69 LDVaEKKLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 92-130 3.57e-03

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: 36.52  E-value: 3.57e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 18860551     92 KVLLDWINDVLAEE-RIIVKQLEEDLYDGQVLQKLLEKLA 130
Cdd:smart00033   1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLS 40
 
Name Accession Description Interval E-value
CH_PARVB_rpt2 cd21338
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ...
 236-365 2.65e-70

second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409187  Cd Length: 130  Bit Score: 215.99  E-value: 2.65e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860551 236 GRFERDAFDTLFDHAPDKLNLVKKSLITFVNKHLNKLNLEVTDLETQFADGVYLVLLLGLLEDYFVPLHNFYLTPDSFDQ 315
Cdd:cd21338   1 GRFERDAFDTLFDHAPDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHNFYLTPESFDQ 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 18860551 316 KVHNVAFAFELMLDGGLKKPKARPEDVVNLDLKSTLRVLYTLFTKYKDVE 365
Cdd:cd21338  81 KVHNVSFAFELMQDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE 130
CH_PARVA_B_rpt2 cd21306
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
 241-361 1.92e-68

second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409155  Cd Length: 121  Bit Score: 210.74  E-value: 1.92e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860551 241 DAFDTLFDHAPDKLNLVKKSLITFVNKHLNKLNLEVTDLETQFADGVYLVLLLGLLEDYFVPLHNFYLTPDSFDQKVHNV 320
Cdd:cd21306   1 DAFDTLFDHAPDKLNVVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPTSFEQKVHNV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 18860551 321 AFAFELMLDGGLKKPKARPEDVVNLDLKSTLRVLYTLFTKY 361
Cdd:cd21306  81 QFAFELMQDAGLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
CH_PARVB_rpt1 cd21336
first calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is ...
 89-194 3.85e-67

first calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-parvin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409185  Cd Length: 106  Bit Score: 207.05  E-value: 3.85e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860551  89 ELVKVLLDWINDVLAEERIIVKQLEEDLYDGQVLQKLLEKLAHCKLNVAEVTQSEIGQKQKLQTVLEAVQDLLRPHGWPL 168
Cdd:cd21336   1 ELVKVLIDWINDVLVEERIIVKDLEEDLYDGQVLQKLLEKLAGRKLNVAEVTQSEIGQKQKLQTVLEAVNDLLRPQGWAI 80

                        90       100
                ....*....|....*....|....*.
gi 18860551 169 RWNVDSIHGKNLVAILHLLVSLAMHF 194
Cdd:cd21336  81 KWSVDSIHGKNLVAILHLLVALAMHF 106
CH_PARVA_rpt2 cd21337
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ...
 237-365 8.48e-65

second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409186  Cd Length: 129  Bit Score: 201.76  E-value: 8.48e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860551 237 RFERDAFDTLFDHAPDKLNLVKKSLITFVNKHLNKLNLEVTDLETQFADGVYLVLLLGLLEDYFVPLHNFYLTPDSFDQK 316
Cdd:cd21337   1 RHERDAFDTLFDHAPDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTPDSFEQK 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 18860551 317 VHNVAFAFELMLDGGLKKPKARPEDVVNLDLKSTLRVLYTLFTKYKDVE 365
Cdd:cd21337  81 VLNVSFAFELMQDGGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYRNVE 129
CH_PARVA_B_rpt1 cd21304
first calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
 89-194 2.48e-60

first calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409153  Cd Length: 107  Bit Score: 189.44  E-value: 2.48e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860551  89 ELVKVLLDWINDVLAEERIIVKQLEEDLYDGQVLQKLLEKLAHCKLNVAEVTQSEIGQKQKLQTVLEAVQDLLR-PHGWP 167
Cdd:cd21304   1 ELIKVLIEWINDELAEQRIIVKDIEEDLYDGQVLQKLLEKLTGVKLEVAEVTQSEVGQKQKLRTVLDKINRILNlPRWSQ 80

                        90       100
                ....*....|....*....|....*..
gi 18860551 168 LRWNVDSIHGKNLVAILHLLVSLAMHF 194
Cdd:cd21304  81 QKWSVDSIHSKNLVAILHLLVALARHF 107
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 241-361 1.10e-51

second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409071  Cd Length: 121  Bit Score: 167.76  E-value: 1.10e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860551 241 DAFDTLFDHAPDKLNLVKKSLITFVNKHLNKLNLEVTDLETQFADGVYLVLLLGLLEDYFVPLHNFYLTPDSFDQKVHNV 320
Cdd:cd21222   1 DAFDDLFDEAPEKLAEVKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPLHEYHLTPSTDDEKLHNV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 18860551 321 AFAFELMLDGGLKKPKARPEDVVNLDLKSTLRVLYTLFTKY 361
Cdd:cd21222  81 KLALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
CH_PARVA_rpt1 cd21335
first calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, ...
 84-198 3.19e-51

first calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409184  Cd Length: 115  Bit Score: 166.36  E-value: 3.19e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860551  84 DPKFKELVKVLLDWINDVLAEERIIVKQLEEDLYDGQVLQKLLEKLAHCKLNVAEVTQSEIGQKQKLQTVLEAVQDLLRP 163
Cdd:cd21335   1 DPKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFEKLEGEKLNVAEVTQSEIAQKQKLQTVLEKINETLKL 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 18860551 164 HGWPLRWNVDSIHGKNLVAILHLLVSLAMHFRAPI 198
Cdd:cd21335  81 PPRSIKWNVDSVHAKSLVAILHLLVALSQYFRAPI 115
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 89-194 5.10e-51

first calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409070  Cd Length: 106  Bit Score: 165.52  E-value: 5.10e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860551  89 ELVKVLLDWINDVLAEERIIVKQLEEDLYDGQVLQKLLEKLAHCKLNVAEVTQSEIGQKQKLQTVLEAVQDLLRPHGWPL 168
Cdd:cd21221   1 ELVRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEVAQSEEGQKQKLAVVLACVNFLLGLEEDEA 80

                        90       100
                ....*....|....*....|....*.
gi 18860551 169 RWNVDSIHGKNLVAILHLLVSLAMHF 194
Cdd:cd21221  81 RWTVDGIYNKDLVSILHLLVALAHHY 106
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
 241-362 3.74e-41

second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409156 [Multi-domain]  Cd Length: 122  Bit Score: 140.56  E-value: 3.74e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860551 241 DAFDTLFDHAPDKLNLVKKSLITFVNKHLNKLNLEVTDLETQFADGVYLVLLLGLLEDYFVPLHNFYLTPDSFDQKVHNV 320
Cdd:cd21307   1 DAIDELFKLGPDKVNTVKKAILHFVNKHLGNLGLNVKDLDSQFADGVILLLLIGQLEGFFIHLSEFFLTPSSTSEMLHNV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 18860551 321 AFAFELMLDGGLKKPKARPEDVVNLDLKSTLRVLYTLFTKYK 362
Cdd:cd21307  81 TLALELLKEGGLLNFPVNPEDIVNGDSKATIRVLYCLFSKYK 122
CH_PARVG_rpt1 cd21305
first calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
 89-194 2.84e-31

first calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. It contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409154  Cd Length: 106  Bit Score: 114.04  E-value: 2.84e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860551  89 ELVKVLLDWINDVLAEERIIVKQLEEDLYDGQVLQKLLEKLAHCKLNVAEVTQSEIGQKQKLQTVLEAVQDLLRPHGWPL 168
Cdd:cd21305   1 ELKEVLIDWINTTLKQEHIVVKSLEEDLYDGLVLHHLLVKLAGVKLEVEEIALTENAQKRKLTVILEAVNQSLQLEESQL 80

                        90       100
                ....*....|....*....|....*.
gi 18860551 169 RWNVDSIHGKNLVAILHLLVSLAMHF 194
Cdd:cd21305  81 KWSVELIHNKDLLATLHLLVAIAKHF 106
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 88-196 1.11e-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: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 80.41  E-value: 1.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860551    88 KELVKVLLDWINDVLAE--ERIIVKQLEEDLYDGQVLQKLLEKLAHCKLNVAEVTQSEIGQKQKLQTVLEAVQDLLRPHG 165
Cdd:pfam00307   1 LELEKELLRWINSHLAEygPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKKLGVPK 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 18860551   166 WpLRWNVDSIHGKNLvAILHLLVSLAMHFRA 196
Cdd:pfam00307  81 V-LIEPEDLVEGDNK-SVLTYLASLFRRFQA 109
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 91-191 3.24e-08

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: 50.80  E-value: 3.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860551  91 VKVLLDWINDVLAEERII-VKQLEEDLYDGQVLQKLLEKLAHCKLNVAEVTQ-SEIGQKQKLQTVLEAVQDLLRPHgwPL 168
Cdd:cd00014   1 EEELLKWINEVLGEELPVsITDLFESLRDGVLLCKLINKLSPGSIPKINKKPkSPFKKRENINLFLNACKKLGLPE--LD 78

                        90       100
                ....*....|....*....|....
gi 18860551 169 RWNVDSIH-GKNLVAILHLLVSLA 191
Cdd:cd00014  79 LFEPEDLYeKGNLKKVLGTLWALA 102
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 257-362 2.06e-06

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: 46.13  E-value: 2.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860551   257 VKKSLITFVNKHLNKL--NLEVTDLETQFADGvylvlllglledyfVPLHNFY--LTPDSFD---------QKVHNVAFA 323
Cdd:pfam00307   3 LEKELLRWINSHLAEYgpGVRVTNFTTDLRDG--------------LALCALLnkLAPGLVDkkklnksefDKLENINLA 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 18860551   324 FEL-MLDGGLKKPKARPEDVVNLDLKSTLRVLYTLFTKYK 362
Cdd:pfam00307  69 LDVaEKKLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 258-361 2.33e-04

first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409064  Cd Length: 107  Bit Score: 40.08  E-value: 2.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860551 258 KKSLITFVNKHLNKLNLEVTDLETQFADGVYLVLLLGLLEDYFVPLHNfyLTPDSFDQKVHNVAFAFELMLDGGLKKPKA 337
Cdd:cd21215   6 KKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRYN--KNPKMRVQKLENVNKALEFIKSRGVKLTNI 83

                        90       100
                ....*....|....*....|....
gi 18860551 338 RPEDVVNLDLKSTLRVLYTLFTKY 361
Cdd:cd21215  84 GAEDIVDGNLKLILGLLWTLILRF 107
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 258-357 1.14e-03

first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409063  Cd Length: 105  Bit Score: 38.14  E-value: 1.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860551 258 KKSLITFVNKHLNKLNLEVTDLETQFADGVYLVLLLGLLEDYFVPLhnfyltPDSFDQKVH---NVAFAFELMLDGGLKK 334
Cdd:cd21214   7 RKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPK------PERGKMRFHkiaNVNKALDFIASKGVKL 80

                        90       100
                ....*....|....*....|...
gi 18860551 335 PKARPEDVVNLDLKSTLRVLYTL 357
Cdd:cd21214  81 VSIGAEEIVDGNLKMTLGMIWTI 103
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 97-195 1.48e-03

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. 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: 409062  Cd Length: 107  Bit Score: 37.66  E-value: 1.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860551  97 WINDVLAEERII--VKQLEEDLYDGQVLQKLLEKLAHCKLN-VAEVTQSEIGQKQKLQTVLEAVQDL-LRPHgwplRWNV 172
Cdd:cd21213   8 WVNSQLKKRPGIrpVQDLRRDLRDGVALAQLIEILAGEKLPgIDWNPTTDAERKENVEKVLQFMASKrIRMH----QTSA 83

                        90       100
                ....*....|....*....|...
gi 18860551 173 DSIHGKNLVAILHLLVSLAMHFR 195
Cdd:cd21213  84 KDIVDGNLKAIMRLILALAAHFK 106
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 92-130 3.57e-03

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: 36.52  E-value: 3.57e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 18860551     92 KVLLDWINDVLAEE-RIIVKQLEEDLYDGQVLQKLLEKLA 130
Cdd:smart00033   1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLS 40
 
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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