calmodulin-regulated spectrin-associated protein 3 isoform 6 [Mus musculus]
CAMSAP_CH and CAMSAP_CKK domain-containing protein( domain architecture ID 11191686)
protein containing domains CAMSAP_CH, CAMSAP_CC1, and CAMSAP_CKK
List of domain hits
Name | Accession | Description | Interval | E-value | |||
CAMSAP_CKK | smart01051 | Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ... |
1140-1268 | 3.50e-75 | |||
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of a family of eumetazoan proteins collectively defined as calmodulin-regulated spectrin-associated, or CAMSAP, proteins. CAMSAP proteins carry an N-terminal region that includes the CH domain, a central region including a predicted coiled-coil and this C-terminal, or CKK, domain - defined as being present in CAMSAP, KIAA1078 and KIAA1543, The C-terminal domain is the part of the CAMSAP proteins that binds to microtubules. The domain appears to act by producing inhibition of neurite extension, probably by blocking microtubule function. CKK represents a domain that has evolved with the metazoa. The structure of a murine hypothetical protein from RIKEN cDNA has shown the domain to adopt a mainly beta barrel structure with an associated alpha-helical hairpin. : Pssm-ID: 198119 Cd Length: 129 Bit Score: 244.57 E-value: 3.50e-75
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CAMSAP_CH | pfam11971 | CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins. |
241-323 | 6.41e-33 | |||
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins. : Pssm-ID: 432229 Cd Length: 85 Bit Score: 122.41 E-value: 6.41e-33
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CAMSAP_CC1 | pfam17095 | Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ... |
615-672 | 2.05e-22 | |||
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on calmodulin-regulated spectrin-associated proteins in eukaryotes that binds spectrin. CAMSAPs are vertebrate microtubule-binding proteins, representatives of a family of cytoskeletal proteins that arose in animals. This conserved CC1 region binds to both spectrin and Ca2+/calmodulin in vitro, although the binding of Ca2+/calmodulin inhibited the binding of spectrin. CC1 appears to be a functional region of CAMSAP1 that links spectrin-binding to neurite outgrowth. : Pssm-ID: 465344 [Multi-domain] Cd Length: 59 Bit Score: 91.60 E-value: 2.05e-22
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PRK02224 super family | cl32023 | DNA double-strand break repair Rad50 ATPase; |
922-1020 | 3.64e-03 | |||
DNA double-strand break repair Rad50 ATPase; The actual alignment was detected with superfamily member PRK02224: Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 3.64e-03
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Name | Accession | Description | Interval | E-value | |||
CAMSAP_CKK | smart01051 | Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ... |
1140-1268 | 3.50e-75 | |||
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of a family of eumetazoan proteins collectively defined as calmodulin-regulated spectrin-associated, or CAMSAP, proteins. CAMSAP proteins carry an N-terminal region that includes the CH domain, a central region including a predicted coiled-coil and this C-terminal, or CKK, domain - defined as being present in CAMSAP, KIAA1078 and KIAA1543, The C-terminal domain is the part of the CAMSAP proteins that binds to microtubules. The domain appears to act by producing inhibition of neurite extension, probably by blocking microtubule function. CKK represents a domain that has evolved with the metazoa. The structure of a murine hypothetical protein from RIKEN cDNA has shown the domain to adopt a mainly beta barrel structure with an associated alpha-helical hairpin. Pssm-ID: 198119 Cd Length: 129 Bit Score: 244.57 E-value: 3.50e-75
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CAMSAP_CKK | pfam08683 | Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ... |
1141-1259 | 3.92e-75 | |||
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of a family of eumetazoan proteins collectively defined as calmodulin-regulated spectrin-associated, or CAMSAP, proteins. CAMSAP proteins carry an N-terminal region that includes the CH domain, a central region including a predicted coiled-coil and this C-terminal, or CKK, domain - defined as being present in CAMSAP, KIAA1078 and KIAA1543, The C-terminal domain is the part of the CAMSAP proteins that binds to microtubules. The domain appears to act by producing inhibition of neurite extension, probably by blocking microtubule function. CKK represents a domain that has evolved with the metazoa. The structure of a murine hypothetical protein from RIKEN cDNA has shown the domain to adopt a mainly beta barrel structure with an associated alpha-helical hairpin. Pssm-ID: 462558 Cd Length: 119 Bit Score: 244.11 E-value: 3.92e-75
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CAMSAP_CH | pfam11971 | CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins. |
241-323 | 6.41e-33 | |||
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins. Pssm-ID: 432229 Cd Length: 85 Bit Score: 122.41 E-value: 6.41e-33
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CAMSAP_CC1 | pfam17095 | Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ... |
615-672 | 2.05e-22 | |||
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on calmodulin-regulated spectrin-associated proteins in eukaryotes that binds spectrin. CAMSAPs are vertebrate microtubule-binding proteins, representatives of a family of cytoskeletal proteins that arose in animals. This conserved CC1 region binds to both spectrin and Ca2+/calmodulin in vitro, although the binding of Ca2+/calmodulin inhibited the binding of spectrin. CC1 appears to be a functional region of CAMSAP1 that links spectrin-binding to neurite outgrowth. Pssm-ID: 465344 [Multi-domain] Cd Length: 59 Bit Score: 91.60 E-value: 2.05e-22
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PRK02224 | PRK02224 | DNA double-strand break repair Rad50 ATPase; |
922-1020 | 3.64e-03 | |||
DNA double-strand break repair Rad50 ATPase; Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 3.64e-03
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PIN_FEN1 | cd09867 | FEN-like PIN domains of Flap endonuclease-1, a structure-specific, divalent-metal-ion ... |
928-966 | 3.65e-03 | |||
FEN-like PIN domains of Flap endonuclease-1, a structure-specific, divalent-metal-ion dependent, 5' nuclease and homologs; Flap endonuclease-1 (FEN1) is involved in multiple DNA metabolic pathways, including DNA replication processes (5' flap DNA endonuclease activity and double stranded DNA 5'-exonuclease activity) and DNA repair processes (long-patch base excision repair) in eukaryotes and archaea. Interaction between FEN1 and PCNA (Proliferating cell nuclear antigen) is an essential prerequisite to FEN1's DNA replication functionality and stimulates FEN1 nuclease activity by 10-50 fold. FEN1 belongs to the FEN1-EXO1-like subfamily of structure-specific, 5' nucleases (FEN-like family). Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), and at the C-terminus of the PIN domain a H3TH (helix-3-turn-helix) domain, an atypical helix-hairpin-helix-2-like region. Both the H3TH domain (not included in this model) and the helical arch/clamp region are involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. FEN1 has a C-terminal extension containing residues forming the consensus PIP-box - Qxx(M/L/I)xxF(Y/F) which serves to anchor FEN1 to PCNA. Pssm-ID: 350215 [Multi-domain] Cd Length: 251 Bit Score: 40.46 E-value: 3.65e-03
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DUF4670 | pfam15709 | Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
899-967 | 7.86e-03 | |||
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length. Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 40.32 E-value: 7.86e-03
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Name | Accession | Description | Interval | E-value | |||
CAMSAP_CKK | smart01051 | Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ... |
1140-1268 | 3.50e-75 | |||
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of a family of eumetazoan proteins collectively defined as calmodulin-regulated spectrin-associated, or CAMSAP, proteins. CAMSAP proteins carry an N-terminal region that includes the CH domain, a central region including a predicted coiled-coil and this C-terminal, or CKK, domain - defined as being present in CAMSAP, KIAA1078 and KIAA1543, The C-terminal domain is the part of the CAMSAP proteins that binds to microtubules. The domain appears to act by producing inhibition of neurite extension, probably by blocking microtubule function. CKK represents a domain that has evolved with the metazoa. The structure of a murine hypothetical protein from RIKEN cDNA has shown the domain to adopt a mainly beta barrel structure with an associated alpha-helical hairpin. Pssm-ID: 198119 Cd Length: 129 Bit Score: 244.57 E-value: 3.50e-75
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CAMSAP_CKK | pfam08683 | Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ... |
1141-1259 | 3.92e-75 | |||
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of a family of eumetazoan proteins collectively defined as calmodulin-regulated spectrin-associated, or CAMSAP, proteins. CAMSAP proteins carry an N-terminal region that includes the CH domain, a central region including a predicted coiled-coil and this C-terminal, or CKK, domain - defined as being present in CAMSAP, KIAA1078 and KIAA1543, The C-terminal domain is the part of the CAMSAP proteins that binds to microtubules. The domain appears to act by producing inhibition of neurite extension, probably by blocking microtubule function. CKK represents a domain that has evolved with the metazoa. The structure of a murine hypothetical protein from RIKEN cDNA has shown the domain to adopt a mainly beta barrel structure with an associated alpha-helical hairpin. Pssm-ID: 462558 Cd Length: 119 Bit Score: 244.11 E-value: 3.92e-75
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CAMSAP_CH | pfam11971 | CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins. |
241-323 | 6.41e-33 | |||
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins. Pssm-ID: 432229 Cd Length: 85 Bit Score: 122.41 E-value: 6.41e-33
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CAMSAP_CC1 | pfam17095 | Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ... |
615-672 | 2.05e-22 | |||
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on calmodulin-regulated spectrin-associated proteins in eukaryotes that binds spectrin. CAMSAPs are vertebrate microtubule-binding proteins, representatives of a family of cytoskeletal proteins that arose in animals. This conserved CC1 region binds to both spectrin and Ca2+/calmodulin in vitro, although the binding of Ca2+/calmodulin inhibited the binding of spectrin. CC1 appears to be a functional region of CAMSAP1 that links spectrin-binding to neurite outgrowth. Pssm-ID: 465344 [Multi-domain] Cd Length: 59 Bit Score: 91.60 E-value: 2.05e-22
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PRK02224 | PRK02224 | DNA double-strand break repair Rad50 ATPase; |
922-1020 | 3.64e-03 | |||
DNA double-strand break repair Rad50 ATPase; Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 3.64e-03
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PIN_FEN1 | cd09867 | FEN-like PIN domains of Flap endonuclease-1, a structure-specific, divalent-metal-ion ... |
928-966 | 3.65e-03 | |||
FEN-like PIN domains of Flap endonuclease-1, a structure-specific, divalent-metal-ion dependent, 5' nuclease and homologs; Flap endonuclease-1 (FEN1) is involved in multiple DNA metabolic pathways, including DNA replication processes (5' flap DNA endonuclease activity and double stranded DNA 5'-exonuclease activity) and DNA repair processes (long-patch base excision repair) in eukaryotes and archaea. Interaction between FEN1 and PCNA (Proliferating cell nuclear antigen) is an essential prerequisite to FEN1's DNA replication functionality and stimulates FEN1 nuclease activity by 10-50 fold. FEN1 belongs to the FEN1-EXO1-like subfamily of structure-specific, 5' nucleases (FEN-like family). Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), and at the C-terminus of the PIN domain a H3TH (helix-3-turn-helix) domain, an atypical helix-hairpin-helix-2-like region. Both the H3TH domain (not included in this model) and the helical arch/clamp region are involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. FEN1 has a C-terminal extension containing residues forming the consensus PIP-box - Qxx(M/L/I)xxF(Y/F) which serves to anchor FEN1 to PCNA. Pssm-ID: 350215 [Multi-domain] Cd Length: 251 Bit Score: 40.46 E-value: 3.65e-03
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tolA | PRK09510 | cell envelope integrity inner membrane protein TolA; Provisional |
916-999 | 4.81e-03 | |||
cell envelope integrity inner membrane protein TolA; Provisional Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.95 E-value: 4.81e-03
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DUF4670 | pfam15709 | Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
899-967 | 7.86e-03 | |||
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length. Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 40.32 E-value: 7.86e-03
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Blast search parameters | ||||
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