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Conserved domains on  [gi|51477696|ref|NP_001003828|]
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beta-parvin isoform a [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_PARVB_rpt2 cd21338
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ...
 268-397 9.25e-85

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: 254.13  E-value: 9.25e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 268 GRFERDAFDTLFDHAPDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHHFYLTPESFDQ 347
Cdd:cd21338   1 GRFERDAFDTLFDHAPDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHNFYLTPESFDQ 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 51477696 348 KVHNVSFAFELMLDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE 397
Cdd:cd21338  81 KVHNVSFAFELMQDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE 130
CH_PARVB_rpt1 cd21336
first calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is ...
 121-226 3.76e-69

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: 213.21  E-value: 3.76e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 121 ELVKVLLDWINDVLVEERIIVKQLEEDLYDGQVLQKLLEKLAGCKLNVAEVTQSEIGQKQKLQTVLEAVHDLLRPRGWAL 200
Cdd:cd21336   1 ELVKVLIDWINDVLVEERIIVKDLEEDLYDGQVLQKLLEKLAGRKLNVAEVTQSEIGQKQKLQTVLEAVNDLLRPQGWAI 80

                        90       100
                ....*....|....*....|....*.
gi 51477696 201 RWSVDSIHGKNLVAILHLLVSLAMHF 226
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, ...
 268-397 9.25e-85

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: 254.13  E-value: 9.25e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 268 GRFERDAFDTLFDHAPDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHHFYLTPESFDQ 347
Cdd:cd21338   1 GRFERDAFDTLFDHAPDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHNFYLTPESFDQ 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 51477696 348 KVHNVSFAFELMLDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE 397
Cdd:cd21338  81 KVHNVSFAFELMQDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE 130
CH_PARVB_rpt1 cd21336
first calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is ...
 121-226 3.76e-69

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: 213.21  E-value: 3.76e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 121 ELVKVLLDWINDVLVEERIIVKQLEEDLYDGQVLQKLLEKLAGCKLNVAEVTQSEIGQKQKLQTVLEAVHDLLRPRGWAL 200
Cdd:cd21336   1 ELVKVLIDWINDVLVEERIIVKDLEEDLYDGQVLQKLLEKLAGRKLNVAEVTQSEIGQKQKLQTVLEAVNDLLRPQGWAI 80

                        90       100
                ....*....|....*....|....*.
gi 51477696 201 RWSVDSIHGKNLVAILHLLVSLAMHF 226
Cdd:cd21336  81 KWSVDSIHGKNLVAILHLLVALAMHF 106
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 120-228 2.07e-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: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 82.72  E-value: 2.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696   120 KELVKVLLDWINDVLVE--ERIIVKQLEEDLYDGQVLQKLLEKLAGCKLNVAEVTQSEIGQKQKLQTVLEAVHDLLRPRG 197
Cdd:pfam00307   1 LELEKELLRWINSHLAEygPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKKLGVPK 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 51477696   198 WaLRWSVDSIHGKNLvAILHLLVSLAMHFRA 228
Cdd:pfam00307  81 V-LIEPEDLVEGDNK-SVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 288-394 5.32e-11

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 59.22  E-value: 5.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696   288 VVKKSLITFVNKHLNKL--NLEVTELETQFADGVYLVLLMGLLEDYFVPLHHFYLTPEsfdQKVHNVSFAFEL-MLDGGL 364
Cdd:pfam00307   2 ELEKELLRWINSHLAEYgpGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEF---DKLENINLALDVaEKKLGV 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 51477696   365 KKPKARPEDVVNLDLKSTLRVLYNLFTKYK 394
Cdd:pfam00307  79 PKVLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 124-193 9.59e-04

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: 38.45  E-value: 9.59e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51477696    124 KVLLDWINDVLVEE-RIIVKQLEEDLYDGQVLQKLLEKLAGCKLNVAEVTQ--SEIGQKQKLQTVLEAVHDLL 193
Cdd:smart00033   1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAslSRFKKIENINLALSFAEKLG 73
 
Name Accession Description Interval E-value
CH_PARVB_rpt2 cd21338
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ...
 268-397 9.25e-85

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: 254.13  E-value: 9.25e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 268 GRFERDAFDTLFDHAPDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHHFYLTPESFDQ 347
Cdd:cd21338   1 GRFERDAFDTLFDHAPDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHNFYLTPESFDQ 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 51477696 348 KVHNVSFAFELMLDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE 397
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 ...
 273-393 1.12e-82

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: 248.49  E-value: 1.12e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 273 DAFDTLFDHAPDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHHFYLTPESFDQKVHNV 352
Cdd:cd21306   1 DAFDTLFDHAPDKLNVVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPTSFEQKVHNV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 51477696 353 SFAFELMLDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKY 393
Cdd:cd21306  81 QFAFELMQDAGLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
CH_PARVA_rpt2 cd21337
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ...
 269-397 4.79e-78

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: 236.81  E-value: 4.79e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 269 RFERDAFDTLFDHAPDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHHFYLTPESFDQK 348
Cdd:cd21337   1 RHERDAFDTLFDHAPDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTPDSFEQK 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 51477696 349 VHNVSFAFELMLDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE 397
Cdd:cd21337  81 VLNVSFAFELMQDGGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYRNVE 129
CH_PARVB_rpt1 cd21336
first calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is ...
 121-226 3.76e-69

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: 213.21  E-value: 3.76e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 121 ELVKVLLDWINDVLVEERIIVKQLEEDLYDGQVLQKLLEKLAGCKLNVAEVTQSEIGQKQKLQTVLEAVHDLLRPRGWAL 200
Cdd:cd21336   1 ELVKVLIDWINDVLVEERIIVKDLEEDLYDGQVLQKLLEKLAGRKLNVAEVTQSEIGQKQKLQTVLEAVNDLLRPQGWAI 80

                        90       100
                ....*....|....*....|....*.
gi 51477696 201 RWSVDSIHGKNLVAILHLLVSLAMHF 226
Cdd:cd21336  81 KWSVDSIHGKNLVAILHLLVALAMHF 106
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 273-393 1.10e-62

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: 197.04  E-value: 1.10e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 273 DAFDTLFDHAPDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHHFYLTPESFDQKVHNV 352
Cdd:cd21222   1 DAFDDLFDEAPEKLAEVKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPLHEYHLTPSTDDEKLHNV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 51477696 353 SFAFELMLDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKY 393
Cdd:cd21222  81 KLALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
CH_PARVA_B_rpt1 cd21304
first calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
 121-226 2.99e-62

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: 195.61  E-value: 2.99e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 121 ELVKVLLDWINDVLVEERIIVKQLEEDLYDGQVLQKLLEKLAGCKLNVAEVTQSEIGQKQKLQTVLEAVHDLLR-PRGWA 199
Cdd:cd21304   1 ELIKVLIEWINDELAEQRIIVKDIEEDLYDGQVLQKLLEKLTGVKLEVAEVTQSEVGQKQKLRTVLDKINRILNlPRWSQ 80

                        90       100
                ....*....|....*....|....*..
gi 51477696 200 LRWSVDSIHGKNLVAILHLLVSLAMHF 226
Cdd:cd21304  81 QKWSVDSIHSKNLVAILHLLVALARHF 107
CH_PARVA_rpt1 cd21335
first calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, ...
 116-230 7.11e-54

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: 174.45  E-value: 7.11e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 116 DPKFKELVKVLLDWINDVLVEERIIVKQLEEDLYDGQVLQKLLEKLAGCKLNVAEVTQSEIGQKQKLQTVLEAVHDLLRP 195
Cdd:cd21335   1 DPKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFEKLEGEKLNVAEVTQSEIAQKQKLQTVLEKINETLKL 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 51477696 196 RGWALRWSVDSIHGKNLVAILHLLVSLAMHFRAPI 230
Cdd:cd21335  81 PPRSIKWNVDSVHAKSLVAILHLLVALSQYFRAPI 115
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 121-226 2.08e-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: 167.45  E-value: 2.08e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 121 ELVKVLLDWINDVLVEERIIVKQLEEDLYDGQVLQKLLEKLAGCKLNVAEVTQSEIGQKQKLQTVLEAVHDLLRPRGWAL 200
Cdd:cd21221   1 ELVRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEVAQSEEGQKQKLAVVLACVNFLLGLEEDEA 80

                        90       100
                ....*....|....*....|....*.
gi 51477696 201 RWSVDSIHGKNLVAILHLLVSLAMHF 226
Cdd:cd21221  81 RWTVDGIYNKDLVSILHLLVALAHHY 106
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
 273-394 9.32e-48

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: 158.67  E-value: 9.32e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 273 DAFDTLFDHAPDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHHFYLTPESFDQKVHNV 352
Cdd:cd21307   1 DAIDELFKLGPDKVNTVKKAILHFVNKHLGNLGLNVKDLDSQFADGVILLLLIGQLEGFFIHLSEFFLTPSSTSEMLHNV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 51477696 353 SFAFELMLDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYK 394
Cdd:cd21307  81 TLALELLKEGGLLNFPVNPEDIVNGDSKATIRVLYCLFSKYK 122
CH_PARVG_rpt1 cd21305
first calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
 121-226 1.02e-32

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: 118.67  E-value: 1.02e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 121 ELVKVLLDWINDVLVEERIIVKQLEEDLYDGQVLQKLLEKLAGCKLNVAEVTQSEIGQKQKLQTVLEAVHDLLRPRGWAL 200
Cdd:cd21305   1 ELKEVLIDWINTTLKQEHIVVKSLEEDLYDGLVLHHLLVKLAGVKLEVEEIALTENAQKRKLTVILEAVNQSLQLEESQL 80

                        90       100
                ....*....|....*....|....*.
gi 51477696 201 RWSVDSIHGKNLVAILHLLVSLAMHF 226
Cdd:cd21305  81 KWSVELIHNKDLLATLHLLVAIAKHF 106
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 120-228 2.07e-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: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 82.72  E-value: 2.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696   120 KELVKVLLDWINDVLVE--ERIIVKQLEEDLYDGQVLQKLLEKLAGCKLNVAEVTQSEIGQKQKLQTVLEAVHDLLRPRG 197
Cdd:pfam00307   1 LELEKELLRWINSHLAEygPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKKLGVPK 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 51477696   198 WaLRWSVDSIHGKNLvAILHLLVSLAMHFRA 228
Cdd:pfam00307  81 V-LIEPEDLVEGDNK-SVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 288-394 5.32e-11

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 59.22  E-value: 5.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696   288 VVKKSLITFVNKHLNKL--NLEVTELETQFADGVYLVLLMGLLEDYFVPLHHFYLTPEsfdQKVHNVSFAFEL-MLDGGL 364
Cdd:pfam00307   2 ELEKELLRWINSHLAEYgpGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEF---DKLENINLALDVaEKKLGV 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 51477696   365 KKPKARPEDVVNLDLKSTLRVLYNLFTKYK 394
Cdd:pfam00307  79 PKVLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 123-223 2.43e-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: 51.57  E-value: 2.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 123 VKVLLDWINDVLVEERII-VKQLEEDLYDGQVLQKLLEKLAGCKLNVAEVTQ-SEIGQKQKLQTVLEAVHDLLRPRgwAL 200
Cdd:cd00014   1 EEELLKWINEVLGEELPVsITDLFESLRDGVLLCKLINKLSPGSIPKINKKPkSPFKKRENINLFLNACKKLGLPE--LD 78

                        90       100
                ....*....|....*....|....
gi 51477696 201 RWSVDSIH-GKNLVAILHLLVSLA 223
Cdd:cd00014  79 LFEPEDLYeKGNLKKVLGTLWALA 102
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 287-393 7.23e-08

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: 50.09  E-value: 7.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 287 SVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDyfVPLHHFYLTPESFDQKVHNVSFAFELMLDGGLKK 366
Cdd:cd21215   3 DVQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGD--ESLGRYNKNPKMRVQKLENVNKALEFIKSRGVKL 80

                        90       100
                ....*....|....*....|....*..
gi 51477696 367 PKARPEDVVNLDLKSTLRVLYNLFTKY 393
Cdd:cd21215  81 TNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 290-383 2.91e-07

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: 48.54  E-value: 2.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 290 KKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLhhfyltPESFDQKVH---NVSFAFELMLDGGLKK 366
Cdd:cd21214   7 RKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPK------PERGKMRFHkiaNVNKALDFIASKGVKL 80

                        90
                ....*....|....*..
gi 51477696 367 PKARPEDVVNLDLKSTL 383
Cdd:cd21214  81 VSIGAEEIVDGNLKMTL 97
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 290-393 1.12e-06

first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409076  Cd Length: 109  Bit Score: 46.90  E-value: 1.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 290 KKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYfvPLHHFYLTPESFDQKVHNVSFAFELMLDGGLKKPKA 369
Cdd:cd21227   6 KNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGR--KLGRVIKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83

                        90       100
                ....*....|....*....|....
gi 51477696 370 RPEDVVNLDLKSTLRVLYNLFTKY 393
Cdd:cd21227  84 GNEDIVNGNLKLILGLIWHLILRY 107
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 290-389 1.94e-06

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: 46.18  E-value: 1.94e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 290 KKSLITFVNKHLNK-LNLEVTELETQFADGVYLVLLMGLLEDYFVPLHHfyLTPESFDQKVHNVSFAFELMLDGGLKKPK 368
Cdd:cd00014   1 EEELLKWINEVLGEeLPVSITDLFESLRDGVLLCKLINKLSPGSIPKIN--KKPKSPFKKRENINLFLNACKKLGLPELD 78

                        90       100
                ....*....|....*....|...
gi 51477696 369 -ARPEDVVNL-DLKSTLRVLYNL 389
Cdd:cd00014  79 lFEPEDLYEKgNLKKVLGTLWAL 101
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 271-393 2.75e-06

first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA 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: 409160  Cd Length: 124  Bit Score: 46.29  E-value: 2.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 271 ERDafdtLFDHAPDKLsVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPlhHFYLTPESFDQKVH 350
Cdd:cd21311   3 ERD----LAEDAQWKR-IQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFP--KFNKRPTFRSQKLE 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 51477696 351 NVSFAFELM-LDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKY 393
Cdd:cd21311  76 NVSVALKFLeEDEGIKIVNIDSSDIVDGKLKLILGLIWTLILHY 119
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 297-389 6.16e-06

first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409072  Cd Length: 113  Bit Score: 44.89  E-value: 6.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 297 VNKHLNKL--------------NLEVTELETQFADGVYLVLLMGLLEDYFVPLHHFYLTPESFDQKVHNVSFAFELMLDG 362
Cdd:cd21223   1 LTRHLGYLgyvlshvqtpldefDFAVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVPAISRLQKLHNVEVALKALKEA 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 51477696 363 GLKKP----KARPEDVVNLDLKSTLRVLYNL 389
Cdd:cd21223  81 GVLRGgdggGITAKDIVDGHREKTLALLWRI 111
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 297-394 3.28e-05

calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.


Pssm-ID: 409061  Cd Length: 105  Bit Score: 42.57  E-value: 3.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 297 VNKHLNKLNLE--VTELETQFADGVYLVLLMGLLEDYFVPLHHfyLTPESFDQKVHNVSFAFELMLDGGLKKPKARPEDV 374
Cdd:cd21212   9 ANHYLEKGGHKriITDLQKDLGDGLTLVNLIEAVAGEKVPGIH--SRPKTRAQKLENIQACLQFLAALGVDVQGITAEDI 86

                        90       100
                ....*....|....*....|
gi 51477696 375 VNLDLKSTLRVLYNLfTKYK 394
Cdd:cd21212  87 VDGNLKAILGLFFSL-SRYK 105
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 296-393 1.34e-04

first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409077  Cd Length: 108  Bit Score: 40.93  E-value: 1.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 296 FVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPlHHFYLTPESFDQKVHNVSFAFELMLDGGLKKPKARPEDVV 375
Cdd:cd21228  12 WCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMY-KKYNKRPTFRQMKLENVSVALEFLERESIKLVSIDSSAIV 90

                        90
                ....*....|....*...
gi 51477696 376 NLDLKSTLRVLYNLFTKY 393
Cdd:cd21228  91 DGNLKLILGLIWTLILHY 108
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 287-383 1.56e-04

first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. 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: 409037  Cd Length: 105  Bit Score: 40.85  E-value: 1.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 287 SVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHHFYLtpeSFdQKVHNVSFAFELMLDGGLKK 366
Cdd:cd21188   2 AVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRM---RF-HRLQNVQTALDFLKYRKIKL 77

                        90
                ....*....|....*..
gi 51477696 367 PKARPEDVVNLDLKSTL 383
Cdd:cd21188  78 VNIRAEDIVDGNPKLTL 94
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 129-227 2.50e-04

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: 39.97  E-value: 2.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 129 WINDVLVEERII--VKQLEEDLYDGQVLQKLLEKLAGCKLN-VAEVTQSEIGQKQKLQTVLeavhDLLRPRGWALR-WSV 204
Cdd:cd21213   8 WVNSQLKKRPGIrpVQDLRRDLRDGVALAQLIEILAGEKLPgIDWNPTTDAERKENVEKVL----QFMASKRIRMHqTSA 83

                        90       100
                ....*....|....*....|...
gi 51477696 205 DSIHGKNLVAILHLLVSLAMHFR 227
Cdd:cd21213  84 KDIVDGNLKAIMRLILALAAHFK 106
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 290-393 4.71e-04

first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other 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: 409032  Cd Length: 108  Bit Score: 39.39  E-value: 4.71e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 290 KKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYfvPLHHFYLTPESFDQ-KVHNVSFAFELMLDGGLKKPK 368
Cdd:cd21183   6 ANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTR--PLKRSYNRRPAFQQhYLENVSTALKFIEADHIKLVN 83

                        90       100
                ....*....|....*....|....*
gi 51477696 369 ARPEDVVNLDLKSTLRVLYNLFTKY 393
Cdd:cd21183  84 IGSGDIVNGNIKLILGLIWTLILHY 108
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 124-227 8.22e-04

first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. 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: 409037  Cd Length: 105  Bit Score: 38.54  E-value: 8.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 124 KVLLDWINDVLVEERIIVKQLEEDLYDGQVLQKLLEKLAGCKLnvaevtQSEIGQKQ--KLQTVLEAVhDLLRPRGWAL- 200
Cdd:cd21188   6 KTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESL------PRERGRMRfhRLQNVQTAL-DFLKYRKIKLv 78

                        90       100
                ....*....|....*....|....*..
gi 51477696 201 RWSVDSIHGKNLVAILHLLVSLAMHFR 227
Cdd:cd21188  79 NIRAEDIVDGNPKLTLGLIWTIILHFQ 105
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 124-193 9.59e-04

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: 38.45  E-value: 9.59e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51477696    124 KVLLDWINDVLVEE-RIIVKQLEEDLYDGQVLQKLLEKLAGCKLNVAEVTQ--SEIGQKQKLQTVLEAVHDLL 193
Cdd:smart00033   1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAslSRFKKIENINLALSFAEKLG 73
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 270-330 1.52e-03

first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. 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: 409042  Cd Length: 116  Bit Score: 38.05  E-value: 1.52e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51477696 270 FERDAFDTLFDhapDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGvylVLLMGLLED 330
Cdd:cd21193   1 FEKGRIRALQE---ERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDG---KLLLKLLEI 55
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 288-394 1.65e-03

first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and 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: 409074  Cd Length: 111  Bit Score: 37.90  E-value: 1.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 288 VVKKSLITFVNKHLNKLNLE-VTELETQFADGVYLVLLMGLLEDYFVPlHHFYLTPESFDQKVHNVSFAFELML-DGGLK 365
Cdd:cd21225   4 VQIKAFTAWVNSVLEKRGIPkISDLATDLSDGVRLIFFLELVSGKKFP-KKFDLEPKNRIQMIQNLHLAMLFIEeDLKIR 82

                        90       100
                ....*....|....*....|....*....
gi 51477696 366 KPKARPEDVVNLDLKSTLRVLYNLFTKYK 394
Cdd:cd21225  83 VQGIGAEDFVDNNKKLILGLLWTLYRKYR 111
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 270-392 2.23e-03

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 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: 409166  Cd Length: 132  Bit Score: 38.11  E-value: 2.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 270 FERDAFDTLFDhapDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPlhhfylTPESFDQKV 349
Cdd:cd21317  16 FERSRIKALAD---EREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLP------KPTKGRMRI 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 51477696 350 H---NVSFAFELMLDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTK 392
Cdd:cd21317  87 HcleNVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIILR 132
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 128-226 2.32e-03

calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.


Pssm-ID: 409061  Cd Length: 105  Bit Score: 37.18  E-value: 2.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 128 DWINDVLVEE--RIIVKQLEEDLYDGQVLQKLLEKLAGCKlnVAEVTQSEIGQKQKLQ------TVLEA----VHDLlrp 195
Cdd:cd21212   7 DWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEK--VPGIHSRPKTRAQKLEniqaclQFLAAlgvdVQGI--- 81

                        90       100       110
                ....*....|....*....|....*....|.
gi 51477696 196 rgwalrwSVDSIHGKNLVAILHLLVSLAMHF 226
Cdd:cd21212  82 -------TAEDIVDGNLKAILGLFFSLSRYK 105
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 294-394 3.65e-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: 36.89  E-value: 3.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 294 ITFVNKHLNKL--NLEVTELETQFADGVYLVLLMGLLEDYFVPLHHFYltPESFDQKVHNVSFAFELMLDGGLKKPKARP 371
Cdd:cd21213   6 VAWVNSQLKKRpgIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWN--PTTDAERKENVEKVLQFMASKRIRMHQTSA 83

                        90       100
                ....*....|....*....|...
gi 51477696 372 EDVVNLDLKSTLRVLYNLFTKYK 394
Cdd:cd21213  84 KDIVDGNLKAIMRLILALAAHFK 106
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 120-166 5.01e-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: 36.21  E-value: 5.01e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 51477696 120 KELVKVLLDWINDVLVEERIIVKQLEEDLYDGQVLQKLLEKLAGCKL 166
Cdd:cd21214   4 KQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERL 50
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
 278-393 5.26e-03

first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B 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: 409158  Cd Length: 131  Bit Score: 36.98  E-value: 5.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51477696 278 LFDHAPDKlSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVpLHHFYLTPESFDQKVHNVSFAFE 357
Cdd:cd21309   8 LAEDAPWK-KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRM-YRKYHQRPTFRQMQLENVSVALE 85

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 51477696 358 LMLDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKY 393
Cdd:cd21309  86 FLDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHY 121
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 129-166 6.60e-03

first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. 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: 409042  Cd Length: 116  Bit Score: 36.12  E-value: 6.60e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 51477696 129 WINDVLVEERIIVKQLEEDLYDGQVLQKLLEKLAGCKL 166
Cdd:cd21193  24 WINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKL 61
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 124-166 9.97e-03

first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. 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: 409095  Cd Length: 117  Bit Score: 35.81  E-value: 9.97e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 51477696 124 KVLLDWINDVLVEERIIVKQLEEDLYDGQVLQKLLEKLAGCKL 166
Cdd:cd21246  19 KTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERL 61
 
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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