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Conserved domains on  [gi|258597953|ref|XP_001348875|]
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CKK domain-containing protein, putative [Plasmodium falciparum 3D7]

Protein Classification

CAMSAP_CKK domain-containing protein( domain architecture ID 10660423)

CAMSAP_CKK domain-containing protein

Graphical summary

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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 ...
 823-945 3.71e-29

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: 112.84  E-value: 3.71e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597953   823 LNKELSAISNRDSVIHALKYTLLNKPQNFTTLQNFLFkiDVEFVEYKNFVLLITksVRKLQLEALYGLNDFSI-FEKVYG 901
Cdd:smart01051   4 LYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILE--EMEKSEANHFLILFR--DAKCQFRALYTLNPETEeLVKLYG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 258597953   902 kkVAPRFLISKKVKMFYKYDKFYQKFRElVNVREFSGITDAVEL 945
Cdd:smart01051  80 --NGPRVITSKMVESLYKYDSSRKQFTQ-IPSKTLSVSVDAFTI 120
 
Name Accession Description Interval E-value
CAMSAP_CKK smart01051
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 823-945 3.71e-29

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: 112.84  E-value: 3.71e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597953   823 LNKELSAISNRDSVIHALKYTLLNKPQNFTTLQNFLFkiDVEFVEYKNFVLLITksVRKLQLEALYGLNDFSI-FEKVYG 901
Cdd:smart01051   4 LYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILE--EMEKSEANHFLILFR--DAKCQFRALYTLNPETEeLVKLYG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 258597953   902 kkVAPRFLISKKVKMFYKYDKFYQKFRElVNVREFSGITDAVEL 945
Cdd:smart01051  80 --NGPRVITSKMVESLYKYDSSRKQFTQ-IPSKTLSVSVDAFTI 120
 
Name Accession Description Interval E-value
CAMSAP_CKK smart01051
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 823-945 3.71e-29

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: 112.84  E-value: 3.71e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597953   823 LNKELSAISNRDSVIHALKYTLLNKPQNFTTLQNFLFkiDVEFVEYKNFVLLITksVRKLQLEALYGLNDFSI-FEKVYG 901
Cdd:smart01051   4 LYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILE--EMEKSEANHFLILFR--DAKCQFRALYTLNPETEeLVKLYG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 258597953   902 kkVAPRFLISKKVKMFYKYDKFYQKFRElVNVREFSGITDAVEL 945
Cdd:smart01051  80 --NGPRVITSKMVESLYKYDSSRKQFTQ-IPSKTLSVSVDAFTI 120
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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