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Conserved domains on  [gi|20521756|dbj|BAA83030|]
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KIAA1078 protein, partial [Homo sapiens]

Protein Classification

CAMSAP_CH and CAMSAP_CKK domain-containing protein( domain architecture ID 11191686)

protein containing domains CAMSAP_CH, CAMSAP_CC1, and CAMSAP_CKK

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 ...
 1225-1353 9.94e-73

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: 238.03  E-value: 9.94e-73
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20521756    1225 GPKLYKEPSAKSNKHIIQNALAHCCLAGKVNEGQKKKILEEMEKSDANNFLILFRDSGCQFRSLYTYCPETEEINKLTGI 1304
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 20521756    1305 GPKSITKKMIEGLYKYNSDRKQFSHIPAKTLSASVDAITIHSHLWQTKR 1353
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 113-191 3.41e-41

CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.


:

Pssm-ID: 432229  Cd Length: 85  Bit Score: 146.29  E-value: 3.41e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20521756    113 KQLPCIPLVENLLKDGTDGCALAALIHFYCPDVVRLEDICLKETMSLADSLYNLQLIQEFCQEYL-NQCCHFTLEDMLYA 191
Cdd:pfam11971    5 RSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLEDLLYA 84
CAMSAP_CC1 pfam17095
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ...
 630-680 8.28e-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: 90.06  E-value: 8.28e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 20521756    630 TQLLASEMVHLRMKLEEKRRAIEAQKKKMEAAFTKQRQKMGRTAFLTVVKK 680
Cdd:pfam17095    9 SPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 808-1017 1.75e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20521756   808 PPQPSPQKQIRDfkPSKQAGLSSAIAPFSSDSPRPTHPSPQSSNRKSASFSVKSQRTPRPNELKITPLNRTLTPPRSVDS 887
Cdd:PHA03247 2592 PPQSARPRAPVD--DRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARR 2669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20521756   888 LPR-------LRRFSPSQVPIQTRSFVCFGDDGEPQLKESKPKEEVKKEELESKGTLEQRGHNPeEKEIKPFESTVSEVL 960
Cdd:PHA03247 2670 LGRaaqasspPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASP-ALPAAPAPPAVPAGP 2748

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20521756   961 SLPVTETVCLTP----NEDQLNQPTEPPPKPVFPPTAPKNVNLIEVSLSDLKPPEKADVPV 1017
Cdd:PHA03247 2749 ATPGGPARPARPpttaGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPA 2809
 
Name Accession Description Interval E-value
CAMSAP_CKK smart01051
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1225-1353 9.94e-73

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: 238.03  E-value: 9.94e-73
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20521756    1225 GPKLYKEPSAKSNKHIIQNALAHCCLAGKVNEGQKKKILEEMEKSDANNFLILFRDSGCQFRSLYTYCPETEEINKLTGI 1304
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 20521756    1305 GPKSITKKMIEGLYKYNSDRKQFSHIPAKTLSASVDAITIHSHLWQTKR 1353
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CKK pfam08683
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1226-1344 2.11e-72

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: 236.41  E-value: 2.11e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20521756   1226 PKLYKEPSAKSNKHIIQNALAHCCLAGKVNEGQKKKILEEMEKSDANNFLILFRDSGCQFRSLYTYCPETEEINKLTGIG 1305
Cdd:pfam08683    1 PKLFKKPSAKSNKKIIHNALSHCCLAGKVNEDQKNKILEELEKSESKHFLILFRDSGCQFRALYSYNPETEELVKLHGIG 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 20521756   1306 PKSITKKMIEGLYKYNSDRKQFSHIPAKTLSASVDAITI 1344
Cdd:pfam08683   81 PRVVTPKMIEKFYKYNSGRKQFTEIPTKTLSVSIDAFTI 119
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 113-191 3.41e-41

CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.


Pssm-ID: 432229  Cd Length: 85  Bit Score: 146.29  E-value: 3.41e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20521756    113 KQLPCIPLVENLLKDGTDGCALAALIHFYCPDVVRLEDICLKETMSLADSLYNLQLIQEFCQEYL-NQCCHFTLEDMLYA 191
Cdd:pfam11971    5 RSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLEDLLYA 84
CAMSAP_CC1 pfam17095
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ...
 630-680 8.28e-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: 90.06  E-value: 8.28e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 20521756    630 TQLLASEMVHLRMKLEEKRRAIEAQKKKMEAAFTKQRQKMGRTAFLTVVKK 680
Cdd:pfam17095    9 SPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59
PHA03247 PHA03247
large tegument protein UL36; Provisional
 808-1017 1.75e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20521756   808 PPQPSPQKQIRDfkPSKQAGLSSAIAPFSSDSPRPTHPSPQSSNRKSASFSVKSQRTPRPNELKITPLNRTLTPPRSVDS 887
Cdd:PHA03247 2592 PPQSARPRAPVD--DRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARR 2669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20521756   888 LPR-------LRRFSPSQVPIQTRSFVCFGDDGEPQLKESKPKEEVKKEELESKGTLEQRGHNPeEKEIKPFESTVSEVL 960
Cdd:PHA03247 2670 LGRaaqasspPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASP-ALPAAPAPPAVPAGP 2748

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20521756   961 SLPVTETVCLTP----NEDQLNQPTEPPPKPVFPPTAPKNVNLIEVSLSDLKPPEKADVPV 1017
Cdd:PHA03247 2749 ATPGGPARPARPpttaGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPA 2809
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 129-158 2.79e-03

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: 39.59  E-value: 2.79e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 20521756  129 TDGCALAALIHFYCPDVVRLEDICLKETMS 158
Cdd:cd21224   28 ADGRALCYLIHHYLPSLLPLDAIRQPTTQT 57
 
Name Accession Description Interval E-value
CAMSAP_CKK smart01051
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1225-1353 9.94e-73

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: 238.03  E-value: 9.94e-73
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20521756    1225 GPKLYKEPSAKSNKHIIQNALAHCCLAGKVNEGQKKKILEEMEKSDANNFLILFRDSGCQFRSLYTYCPETEEINKLTGI 1304
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 20521756    1305 GPKSITKKMIEGLYKYNSDRKQFSHIPAKTLSASVDAITIHSHLWQTKR 1353
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CKK pfam08683
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1226-1344 2.11e-72

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: 236.41  E-value: 2.11e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20521756   1226 PKLYKEPSAKSNKHIIQNALAHCCLAGKVNEGQKKKILEEMEKSDANNFLILFRDSGCQFRSLYTYCPETEEINKLTGIG 1305
Cdd:pfam08683    1 PKLFKKPSAKSNKKIIHNALSHCCLAGKVNEDQKNKILEELEKSESKHFLILFRDSGCQFRALYSYNPETEELVKLHGIG 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 20521756   1306 PKSITKKMIEGLYKYNSDRKQFSHIPAKTLSASVDAITI 1344
Cdd:pfam08683   81 PRVVTPKMIEKFYKYNSGRKQFTEIPTKTLSVSIDAFTI 119
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 113-191 3.41e-41

CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.


Pssm-ID: 432229  Cd Length: 85  Bit Score: 146.29  E-value: 3.41e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20521756    113 KQLPCIPLVENLLKDGTDGCALAALIHFYCPDVVRLEDICLKETMSLADSLYNLQLIQEFCQEYL-NQCCHFTLEDMLYA 191
Cdd:pfam11971    5 RSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLEDLLYA 84
CAMSAP_CC1 pfam17095
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ...
 630-680 8.28e-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: 90.06  E-value: 8.28e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 20521756    630 TQLLASEMVHLRMKLEEKRRAIEAQKKKMEAAFTKQRQKMGRTAFLTVVKK 680
Cdd:pfam17095    9 SPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59
PHA03247 PHA03247
large tegument protein UL36; Provisional
 808-1017 1.75e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20521756   808 PPQPSPQKQIRDfkPSKQAGLSSAIAPFSSDSPRPTHPSPQSSNRKSASFSVKSQRTPRPNELKITPLNRTLTPPRSVDS 887
Cdd:PHA03247 2592 PPQSARPRAPVD--DRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARR 2669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20521756   888 LPR-------LRRFSPSQVPIQTRSFVCFGDDGEPQLKESKPKEEVKKEELESKGTLEQRGHNPeEKEIKPFESTVSEVL 960
Cdd:PHA03247 2670 LGRaaqasspPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASP-ALPAAPAPPAVPAGP 2748

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20521756   961 SLPVTETVCLTP----NEDQLNQPTEPPPKPVFPPTAPKNVNLIEVSLSDLKPPEKADVPV 1017
Cdd:PHA03247 2749 ATPGGPARPARPpttaGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPA 2809
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 129-158 2.79e-03

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: 39.59  E-value: 2.79e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 20521756  129 TDGCALAALIHFYCPDVVRLEDICLKETMS 158
Cdd:cd21224   28 ADGRALCYLIHHYLPSLLPLDAIRQPTTQT 57
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 111-207 9.18e-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: 37.66  E-value: 9.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20521756  111 LLKQLPCIPLVENLLKDGTDGCALAALIHFYCPDVVRLEDIclKETMSLADSLYNLQLIQEFCQEyLNQCCHFTLEDMLy 190
Cdd:cd21218   23 LKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKELV--LEVLSEEDLEKRAEKVLQAAEK-LGCKYFLTPEDIV- 98

                         90
                 ....*....|....*..
gi 20521756  191 aASSIKSNyLVFMAELF 207
Cdd:cd21218   99 -SGNPRLN-LAFVATLF 113
 
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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