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Conserved domains on  [gi|7708363|emb|CAB90188|]
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hypothetical protein [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_PARVG_rpt1 cd21305
first calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
 45-150 3.96e-56

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: 172.59  E-value: 3.96e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7708363   45 ELQKVLMEWINATLLPEHIVVRSLEEDMFDGLILHHLFQRLAALKLEAEDIALTATSQKHKLTVVLEAVNRSLQLEEWQA 124
Cdd:cd21305   1 ELKEVLIDWINTTLKQEHIVVKSLEEDLYDGLVLHHLLVKLAGVKLEVEEIALTENAQKRKLTVILEAVNQSLQLEESQL 80

                        90       100
                ....*....|....*....|....*.
gi 7708363  125 KWSVESIFNKDLLSTLHLLVALAKRF 150
Cdd:cd21305  81 KWSVELIHNKDLLATLHLLVAIAKHF 106
 
Name Accession Description Interval E-value
CH_PARVG_rpt1 cd21305
first calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
 45-150 3.96e-56

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: 172.59  E-value: 3.96e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7708363   45 ELQKVLMEWINATLLPEHIVVRSLEEDMFDGLILHHLFQRLAALKLEAEDIALTATSQKHKLTVVLEAVNRSLQLEEWQA 124
Cdd:cd21305   1 ELKEVLIDWINTTLKQEHIVVKSLEEDLYDGLVLHHLLVKLAGVKLEVEEIALTENAQKRKLTVILEAVNQSLQLEESQL 80

                        90       100
                ....*....|....*....|....*.
gi 7708363  125 KWSVESIFNKDLLSTLHLLVALAKRF 150
Cdd:cd21305  81 KWSVELIHNKDLLATLHLLVAIAKHF 106
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 44-151 2.15e-14

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 65.77  E-value: 2.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7708363     44 EELQKVLMEWINATL--LPEHIVVRSLEEDMFDGLILHHLFQRLAALKLEAEDIALTATSQKHKLTVVLEAVNRSLQLEE 121
Cdd:pfam00307   1 LELEKELLRWINSHLaeYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKKLGVPK 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 7708363    122 WQAKwsVESIFNKDLLSTLHLLVALAKRFQ 151
Cdd:pfam00307  81 VLIE--PEDLVEGDNKSVLTYLASLFRRFQ 108
 
Name Accession Description Interval E-value
CH_PARVG_rpt1 cd21305
first calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
 45-150 3.96e-56

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: 172.59  E-value: 3.96e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7708363   45 ELQKVLMEWINATLLPEHIVVRSLEEDMFDGLILHHLFQRLAALKLEAEDIALTATSQKHKLTVVLEAVNRSLQLEEWQA 124
Cdd:cd21305   1 ELKEVLIDWINTTLKQEHIVVKSLEEDLYDGLVLHHLLVKLAGVKLEVEEIALTENAQKRKLTVILEAVNQSLQLEESQL 80

                        90       100
                ....*....|....*....|....*.
gi 7708363  125 KWSVESIFNKDLLSTLHLLVALAKRF 150
Cdd:cd21305  81 KWSVELIHNKDLLATLHLLVAIAKHF 106
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 45-150 4.38e-47

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: 149.35  E-value: 4.38e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7708363   45 ELQKVLMEWINATLLPEHIVVRSLEEDMFDGLILHHLFQRLAALKLEAEDIALTATSQKHKLTVVLEAVNRSLQLEEWQA 124
Cdd:cd21221   1 ELVRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEVAQSEEGQKQKLAVVLACVNFLLGLEEDEA 80

                        90       100
                ....*....|....*....|....*.
gi 7708363  125 KWSVESIFNKDLLSTLHLLVALAKRF 150
Cdd:cd21221  81 RWTVDGIYNKDLVSILHLLVALAHHY 106
CH_PARVA_B_rpt1 cd21304
first calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
 45-150 5.20e-36

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: 121.26  E-value: 5.20e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7708363   45 ELQKVLMEWINATLLPEHIVVRSLEEDMFDGLILHHLFQRLAALKLEAEDIALTATSQKHKLTVVLEAVNRSLQLEEW-Q 123
Cdd:cd21304   1 ELIKVLIEWINDELAEQRIIVKDIEEDLYDGQVLQKLLEKLTGVKLEVAEVTQSEVGQKQKLRTVLDKINRILNLPRWsQ 80

                        90       100
                ....*....|....*....|....*..
gi 7708363  124 AKWSVESIFNKDLLSTLHLLVALAKRF 150
Cdd:cd21304  81 QKWSVDSIHSKNLVAILHLLVALARHF 107
CH_PARVB_rpt1 cd21336
first calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is ...
 45-150 1.31e-28

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: 102.66  E-value: 1.31e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7708363   45 ELQKVLMEWINATLLPEHIVVRSLEEDMFDGLILHHLFQRLAALKLEAEDIALTATSQKHKLTVVLEAVNRSLQLEEWQA 124
Cdd:cd21336   1 ELVKVLIDWINDVLVEERIIVKDLEEDLYDGQVLQKLLEKLAGRKLNVAEVTQSEIGQKQKLQTVLEAVNDLLRPQGWAI 80

                        90       100
                ....*....|....*....|....*.
gi 7708363  125 KWSVESIFNKDLLSTLHLLVALAKRF 150
Cdd:cd21336  81 KWSVDSIHGKNLVAILHLLVALAMHF 106
CH_PARVA_rpt1 cd21335
first calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, ...
 40-151 6.34e-27

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: 98.56  E-value: 6.34e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7708363   40 DPKFEELQKVLMEWINATLLPEHIVVRSLEEDMFDGLILHHLFQRLAALKLEAEDIALTATSQKHKLTVVLEAVNRSLQL 119
Cdd:cd21335   1 DPKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFEKLEGEKLNVAEVTQSEIAQKQKLQTVLEKINETLKL 80

                        90       100       110
                ....*....|....*....|....*....|..
gi 7708363  120 EEWQAKWSVESIFNKDLLSTLHLLVALAKRFQ 151
Cdd:cd21335  81 PPRSIKWNVDSVHAKSLVAILHLLVALSQYFR 112
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 44-151 2.15e-14

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 65.77  E-value: 2.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7708363     44 EELQKVLMEWINATL--LPEHIVVRSLEEDMFDGLILHHLFQRLAALKLEAEDIALTATSQKHKLTVVLEAVNRSLQLEE 121
Cdd:pfam00307   1 LELEKELLRWINSHLaeYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKKLGVPK 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 7708363    122 WQAKwsVESIFNKDLLSTLHLLVALAKRFQ 151
Cdd:pfam00307  81 VLIE--PEDLVEGDNKSVLTYLASLFRRFQ 108
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 41-150 5.12e-04

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: 38.34  E-value: 5.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7708363   41 PKFEELQKVLMEWINATLLPEHIVVRSLEEDMFDGLILHHLFQRLAALKLEAEDIALTATSQKHKltvvLEAVNRSLQL- 119
Cdd:cd21222  12 EKLAEVKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPLHEYHLTPSTDDEK----LHNVKLALELm 87

                        90       100       110
                ....*....|....*....|....*....|....
gi 7708363  120 ---EEWQAKWSVESIFNKDLLSTLHLLVALAKRF 150
Cdd:cd21222  88 edaGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
 
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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