PREDICTED: abnormal spindle-like microcephaly-associated protein homolog [Sinocyclocheilus rhinocerous]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| CH_ASPM_rpt2 | cd21224 | second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
1110-1258 | 2.91e-62 | ||||
second 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 CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. : Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 209.85 E-value: 2.91e-62
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| CH_ASPM_rpt1 | cd21223 | first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
941-1054 | 7.98e-59 | ||||
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: 198.97 E-value: 7.98e-59
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| ASH | pfam15780 | Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ... |
35-132 | 9.68e-33 | ||||
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal domain of abnormal spindle-like microcephaly-associated protein are found in proteins associated with cilia, flagella, the centrosome and the Golgi complex. The domain is also found in Hydin and OCRL whose deficiencies are associated with hydrocephalus and Lowe oculocerebrorenal syndrome (OCRL), respectively. The fact that Human ASPM protein carries an ASH domain indicates possible roles for ASPM in sperm flagellar or in ependymal cells' cilia. The presence of ASH in centrosomal and ciliary proteins indicates that ASPM may possess roles not only in mitotic spindle regulation, but also in ciliary and flagellar function. : Pssm-ID: 464865 [Multi-domain] Cd Length: 98 Bit Score: 123.93 E-value: 9.68e-33
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| COG5022 super family | cl34868 | Myosin heavy chain [General function prediction only]; |
2490-2647 | 3.27e-08 | ||||
Myosin heavy chain [General function prediction only]; The actual alignment was detected with superfamily member COG5022: Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 60.09 E-value: 3.27e-08
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| COG5022 super family | cl34868 | Myosin heavy chain [General function prediction only]; |
1836-1990 | 2.20e-07 | ||||
Myosin heavy chain [General function prediction only]; The actual alignment was detected with superfamily member COG5022: Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 57.40 E-value: 2.20e-07
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| COG5022 super family | cl34868 | Myosin heavy chain [General function prediction only]; |
3248-3401 | 2.36e-07 | ||||
Myosin heavy chain [General function prediction only]; The actual alignment was detected with superfamily member COG5022: Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 57.40 E-value: 2.36e-07
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| COG5022 super family | cl34868 | Myosin heavy chain [General function prediction only]; |
1544-1687 | 2.55e-05 | ||||
Myosin heavy chain [General function prediction only]; The actual alignment was detected with superfamily member COG5022: Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.46 E-value: 2.55e-05
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| COG5022 super family | cl34868 | Myosin heavy chain [General function prediction only]; |
2822-2971 | 4.15e-05 | ||||
Myosin heavy chain [General function prediction only]; The actual alignment was detected with superfamily member COG5022: Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.08 E-value: 4.15e-05
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| COG5022 super family | cl34868 | Myosin heavy chain [General function prediction only]; |
2165-2320 | 4.59e-05 | ||||
Myosin heavy chain [General function prediction only]; The actual alignment was detected with superfamily member COG5022: Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 49.69 E-value: 4.59e-05
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| COG5022 super family | cl34868 | Myosin heavy chain [General function prediction only]; |
1439-1610 | 1.34e-04 | ||||
Myosin heavy chain [General function prediction only]; The actual alignment was detected with superfamily member COG5022: Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.15 E-value: 1.34e-04
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| COG5022 super family | cl34868 | Myosin heavy chain [General function prediction only]; |
2287-2418 | 1.59e-04 | ||||
Myosin heavy chain [General function prediction only]; The actual alignment was detected with superfamily member COG5022: Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.15 E-value: 1.59e-04
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| COG5022 super family | cl34868 | Myosin heavy chain [General function prediction only]; |
2944-3124 | 2.33e-04 | ||||
Myosin heavy chain [General function prediction only]; The actual alignment was detected with superfamily member COG5022: Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.38 E-value: 2.33e-04
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| COG5022 super family | cl34868 | Myosin heavy chain [General function prediction only]; |
2610-2791 | 9.16e-04 | ||||
Myosin heavy chain [General function prediction only]; The actual alignment was detected with superfamily member COG5022: Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.45 E-value: 9.16e-04
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| IQCD | cd23767 | IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ... |
1306-1339 | 1.17e-03 | ||||
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor. : Pssm-ID: 467745 [Multi-domain] Cd Length: 37 Bit Score: 39.06 E-value: 1.17e-03
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| COG5022 super family | cl34868 | Myosin heavy chain [General function prediction only]; |
1953-2134 | 1.82e-03 | ||||
Myosin heavy chain [General function prediction only]; The actual alignment was detected with superfamily member COG5022: Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.30 E-value: 1.82e-03
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| COG5022 super family | cl34868 | Myosin heavy chain [General function prediction only]; |
1634-1764 | 2.92e-03 | ||||
Myosin heavy chain [General function prediction only]; The actual alignment was detected with superfamily member COG5022: Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.91 E-value: 2.92e-03
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| Name | Accession | Description | Interval | E-value | ||||||
| CH_ASPM_rpt2 | cd21224 | second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
1110-1258 | 2.91e-62 | ||||||
second 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 CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 209.85 E-value: 2.91e-62
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| CH_ASPM_rpt1 | cd21223 | first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
941-1054 | 7.98e-59 | ||||||
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: 198.97 E-value: 7.98e-59
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| ASH | pfam15780 | Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ... |
35-132 | 9.68e-33 | ||||||
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal domain of abnormal spindle-like microcephaly-associated protein are found in proteins associated with cilia, flagella, the centrosome and the Golgi complex. The domain is also found in Hydin and OCRL whose deficiencies are associated with hydrocephalus and Lowe oculocerebrorenal syndrome (OCRL), respectively. The fact that Human ASPM protein carries an ASH domain indicates possible roles for ASPM in sperm flagellar or in ependymal cells' cilia. The presence of ASH in centrosomal and ciliary proteins indicates that ASPM may possess roles not only in mitotic spindle regulation, but also in ciliary and flagellar function. Pssm-ID: 464865 [Multi-domain] Cd Length: 98 Bit Score: 123.93 E-value: 9.68e-33
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
2490-2647 | 3.27e-08 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 60.09 E-value: 3.27e-08
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
1836-1990 | 2.20e-07 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 57.40 E-value: 2.20e-07
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
3248-3401 | 2.36e-07 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 57.40 E-value: 2.36e-07
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| CH | pfam00307 | Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
1107-1168 | 1.26e-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: 49.59 E-value: 1.26e-06
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
1544-1687 | 2.55e-05 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.46 E-value: 2.55e-05
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| CH | smart00033 | Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
966-1054 | 2.66e-05 | ||||||
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: 45.77 E-value: 2.66e-05
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| SAC6 | COG5069 | Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
959-1299 | 2.80e-05 | ||||||
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 49.94 E-value: 2.80e-05
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
2822-2971 | 4.15e-05 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.08 E-value: 4.15e-05
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
2165-2320 | 4.59e-05 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 49.69 E-value: 4.59e-05
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| CH | pfam00307 | Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
946-1057 | 6.07e-05 | ||||||
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: 44.97 E-value: 6.07e-05
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
1439-1610 | 1.34e-04 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.15 E-value: 1.34e-04
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
2287-2418 | 1.59e-04 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.15 E-value: 1.59e-04
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
2944-3124 | 2.33e-04 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.38 E-value: 2.33e-04
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
2610-2791 | 9.16e-04 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.45 E-value: 9.16e-04
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| IQCD | cd23767 | IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ... |
1306-1339 | 1.17e-03 | ||||||
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor. Pssm-ID: 467745 [Multi-domain] Cd Length: 37 Bit Score: 39.06 E-value: 1.17e-03
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| CH | smart00033 | Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
1114-1152 | 1.54e-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: 40.76 E-value: 1.54e-03
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
1953-2134 | 1.82e-03 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.30 E-value: 1.82e-03
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
1634-1764 | 2.92e-03 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.91 E-value: 2.92e-03
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| Name | Accession | Description | Interval | E-value | ||||||
| CH_ASPM_rpt2 | cd21224 | second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
1110-1258 | 2.91e-62 | ||||||
second 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 CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 209.85 E-value: 2.91e-62
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| CH_ASPM_rpt1 | cd21223 | first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
941-1054 | 7.98e-59 | ||||||
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: 198.97 E-value: 7.98e-59
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| ASH | pfam15780 | Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ... |
35-132 | 9.68e-33 | ||||||
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal domain of abnormal spindle-like microcephaly-associated protein are found in proteins associated with cilia, flagella, the centrosome and the Golgi complex. The domain is also found in Hydin and OCRL whose deficiencies are associated with hydrocephalus and Lowe oculocerebrorenal syndrome (OCRL), respectively. The fact that Human ASPM protein carries an ASH domain indicates possible roles for ASPM in sperm flagellar or in ependymal cells' cilia. The presence of ASH in centrosomal and ciliary proteins indicates that ASPM may possess roles not only in mitotic spindle regulation, but also in ciliary and flagellar function. Pssm-ID: 464865 [Multi-domain] Cd Length: 98 Bit Score: 123.93 E-value: 9.68e-33
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| CH_DMD-like_rpt1 | cd21186 | first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
966-1058 | 1.60e-12 | ||||||
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. 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: 409035 Cd Length: 107 Bit Score: 66.25 E-value: 1.60e-12
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| CH_SpAIN1-like_rpt1 | cd21215 | first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
955-1056 | 2.83e-12 | ||||||
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: 65.88 E-value: 2.83e-12
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| CH_beta_spectrin_rpt1 | cd21193 | first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
959-1053 | 4.54e-10 | ||||||
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: 59.62 E-value: 4.54e-10
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| CH_jitterbug-like_rpt1 | cd21227 | first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
959-1058 | 5.82e-10 | ||||||
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: 59.22 E-value: 5.82e-10
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| CH_SYNE1_rpt1 | cd21241 | first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
966-1059 | 6.91e-10 | ||||||
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 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: 409090 Cd Length: 113 Bit Score: 58.93 E-value: 6.91e-10
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| CH_PLEC-like_rpt1 | cd21188 | first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
966-1057 | 7.86e-10 | ||||||
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: 58.57 E-value: 7.86e-10
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| CH_DMD_rpt1 | cd21231 | first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
966-1059 | 9.56e-10 | ||||||
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain. Pssm-ID: 409080 Cd Length: 111 Bit Score: 58.78 E-value: 9.56e-10
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| CH_SPTB-like_rpt1 | cd21246 | first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
966-1053 | 1.23e-09 | ||||||
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: 58.53 E-value: 1.23e-09
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| CH_SPTBN4_rpt1 | cd21318 | first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
955-1054 | 3.78e-09 | ||||||
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) 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. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 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: 409167 Cd Length: 139 Bit Score: 57.73 E-value: 3.78e-09
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| CH_SPTBN2_rpt1 | cd21317 | first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
966-1054 | 2.08e-08 | ||||||
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: 55.45 E-value: 2.08e-08
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
2490-2647 | 3.27e-08 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 60.09 E-value: 3.27e-08
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| CH_DYST_rpt1 | cd21236 | first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
966-1058 | 3.99e-08 | ||||||
first calponin homology (CH) domain found in dystonin and similar proteins; 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. Dystonin 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: 409085 Cd Length: 128 Bit Score: 54.61 E-value: 3.99e-08
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| CH_FLN-like_rpt2 | cd21184 | second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
1113-1251 | 4.34e-08 | ||||||
second 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 second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409033 Cd Length: 103 Bit Score: 53.78 E-value: 4.34e-08
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| CH_UTRN_rpt1 | cd21232 | first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
966-1059 | 4.86e-08 | ||||||
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain. Pssm-ID: 409081 Cd Length: 107 Bit Score: 53.86 E-value: 4.86e-08
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| CH_ACTN_rpt1 | cd21214 | first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
965-1053 | 5.96e-08 | ||||||
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: 53.16 E-value: 5.96e-08
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| CH_CLMN_rpt1 | cd21191 | first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
965-1059 | 8.62e-08 | ||||||
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin 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: 409040 Cd Length: 114 Bit Score: 53.35 E-value: 8.62e-08
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| CH_PLEC_rpt1 | cd21235 | first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
966-1066 | 1.09e-07 | ||||||
first calponin homology (CH) domain found in plectin and similar proteins; 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 can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin 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: 409084 Cd Length: 119 Bit Score: 53.10 E-value: 1.09e-07
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| CH_dFLNA-like_rpt1 | cd21311 | first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
959-1058 | 1.41e-07 | ||||||
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: 52.84 E-value: 1.41e-07
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| CH_SYNE-like_rpt1 | cd21190 | first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
966-1059 | 1.51e-07 | ||||||
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. 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: 409039 Cd Length: 113 Bit Score: 52.57 E-value: 1.51e-07
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
1836-1990 | 2.20e-07 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 57.40 E-value: 2.20e-07
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
3248-3401 | 2.36e-07 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 57.40 E-value: 2.36e-07
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| CH_CYTSB | cd21257 | calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
1103-1222 | 3.22e-07 | ||||||
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409106 Cd Length: 112 Bit Score: 51.57 E-value: 3.22e-07
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| CH | pfam00307 | Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
1107-1168 | 1.26e-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: 49.59 E-value: 1.26e-06
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| CH_NAV2-like | cd21212 | calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
966-1049 | 1.40e-06 | ||||||
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: 49.50 E-value: 1.40e-06
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| CH_PLS_FIM_rpt3 | cd21219 | third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
966-1053 | 2.80e-06 | ||||||
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409068 Cd Length: 113 Bit Score: 48.82 E-value: 2.80e-06
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| CH_FLN-like_rpt1 | cd21183 | first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
959-1056 | 4.19e-06 | ||||||
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: 48.25 E-value: 4.19e-06
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| CH_FLN_rpt1 | cd21228 | first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
963-1056 | 6.77e-06 | ||||||
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: 47.48 E-value: 6.77e-06
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| CH_FLNB_rpt1 | cd21309 | first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
959-1066 | 7.42e-06 | ||||||
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: 48.15 E-value: 7.42e-06
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
1544-1687 | 2.55e-05 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.46 E-value: 2.55e-05
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| CH | smart00033 | Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
966-1054 | 2.66e-05 | ||||||
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: 45.77 E-value: 2.66e-05
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| SAC6 | COG5069 | Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
959-1299 | 2.80e-05 | ||||||
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 49.94 E-value: 2.80e-05
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| CH_CYTSA | cd21256 | calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
1103-1222 | 2.84e-05 | ||||||
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409105 Cd Length: 119 Bit Score: 46.22 E-value: 2.84e-05
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| CH_FLNA_rpt1 | cd21308 | first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
963-1060 | 3.09e-05 | ||||||
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (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 anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A 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: 409157 Cd Length: 129 Bit Score: 46.23 E-value: 3.09e-05
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| CH_SPTBN1_rpt1 | cd21316 | first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
955-1054 | 3.12e-05 | ||||||
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) 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. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also 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. SPTBN1 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: 409165 Cd Length: 154 Bit Score: 46.96 E-value: 3.12e-05
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| CH_MACF1_rpt1 | cd21237 | first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
966-1058 | 3.89e-05 | ||||||
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; 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. MACF1 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: 409086 Cd Length: 118 Bit Score: 45.79 E-value: 3.89e-05
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
2822-2971 | 4.15e-05 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.08 E-value: 4.15e-05
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
1410-1665 | 4.19e-05 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.08 E-value: 4.19e-05
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| CH_SF | cd00014 | calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
960-1053 | 4.47e-05 | ||||||
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: 45.02 E-value: 4.47e-05
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
2165-2320 | 4.59e-05 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 49.69 E-value: 4.59e-05
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| CH_SYNE2_rpt1 | cd21242 | first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
965-1059 | 5.84e-05 | ||||||
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 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: 409091 Cd Length: 111 Bit Score: 44.82 E-value: 5.84e-05
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| CH | pfam00307 | Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
946-1057 | 6.07e-05 | ||||||
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: 44.97 E-value: 6.07e-05
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| CH_SF | cd00014 | calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
1114-1163 | 1.01e-04 | ||||||
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: 44.25 E-value: 1.01e-04
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
1439-1610 | 1.34e-04 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.15 E-value: 1.34e-04
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
2287-2418 | 1.59e-04 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.15 E-value: 1.59e-04
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| CH_FLNC_rpt1 | cd21310 | first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
966-1060 | 1.74e-04 | ||||||
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (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. FLN-C 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: 409159 Cd Length: 125 Bit Score: 44.25 E-value: 1.74e-04
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| CH_SPTBN5_rpt1 | cd21247 | first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
963-1058 | 2.31e-04 | ||||||
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) 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. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 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: 409096 Cd Length: 125 Bit Score: 43.59 E-value: 2.31e-04
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
2944-3124 | 2.33e-04 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.38 E-value: 2.33e-04
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| CH_MICALL2 | cd21253 | calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
1114-1251 | 2.75e-04 | ||||||
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409102 Cd Length: 106 Bit Score: 43.10 E-value: 2.75e-04
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| CH_MICAL_EHBP-like | cd22198 | calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
1114-1152 | 4.06e-04 | ||||||
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409188 Cd Length: 105 Bit Score: 42.27 E-value: 4.06e-04
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
2054-2319 | 4.16e-04 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.61 E-value: 4.16e-04
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| CH_CTX_rpt1 | cd21225 | first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
966-1050 | 4.68e-04 | ||||||
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: 42.52 E-value: 4.68e-04
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| CH_SMTN-like | cd21200 | calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
1112-1257 | 6.90e-04 | ||||||
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409049 Cd Length: 107 Bit Score: 41.94 E-value: 6.90e-04
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| CH_FIMB_rpt3 | cd21300 | third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
965-1052 | 8.34e-04 | ||||||
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409149 Cd Length: 119 Bit Score: 42.03 E-value: 8.34e-04
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
2610-2791 | 9.16e-04 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.45 E-value: 9.16e-04
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| IQCD | cd23767 | IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ... |
1306-1339 | 1.17e-03 | ||||||
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor. Pssm-ID: 467745 [Multi-domain] Cd Length: 37 Bit Score: 39.06 E-value: 1.17e-03
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| CH | smart00033 | Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
1114-1152 | 1.54e-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: 40.76 E-value: 1.54e-03
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
1953-2134 | 1.82e-03 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.30 E-value: 1.82e-03
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| CH_EHBP | cd21198 | calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
1114-1151 | 1.94e-03 | ||||||
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409047 Cd Length: 105 Bit Score: 40.49 E-value: 1.94e-03
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| CH_MICALL | cd21197 | calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
1114-1251 | 1.98e-03 | ||||||
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409046 Cd Length: 105 Bit Score: 40.60 E-value: 1.98e-03
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| CH_PLS_FIM_rpt2 | cd21218 | second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
1113-1160 | 2.37e-03 | ||||||
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409067 Cd Length: 114 Bit Score: 40.36 E-value: 2.37e-03
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| CH_SMTNB | cd21259 | calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
1113-1151 | 2.64e-03 | ||||||
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409108 Cd Length: 112 Bit Score: 40.36 E-value: 2.64e-03
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| CH_PARV_rpt2 | cd21222 | second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
955-1052 | 2.74e-03 | ||||||
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: 40.26 E-value: 2.74e-03
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
1634-1764 | 2.92e-03 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.91 E-value: 2.92e-03
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
2434-2600 | 3.07e-03 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.91 E-value: 3.07e-03
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
1780-1943 | 4.92e-03 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.14 E-value: 4.92e-03
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| COG5022 | COG5022 | Myosin heavy chain [General function prediction only]; |
1471-1666 | 5.92e-03 | ||||||
Myosin heavy chain [General function prediction only]; Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 5.92e-03
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| CH_EHBP1L1 | cd21255 | calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
1114-1151 | 7.72e-03 | ||||||
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs. Pssm-ID: 409104 Cd Length: 105 Bit Score: 38.62 E-value: 7.72e-03
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