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Conserved domains on  [gi|663071131|ref|NP_001284636|]
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calmodulin-regulated spectrin-associated protein 2 isoform 1 [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 ...
 1349-1477 5.24e-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: 238.80  E-value: 5.24e-73
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663071131   1349 GPKLYKEPSAKSNKHIIQNALAHCCLAGKVNEGQKKKILEEMEKSDANNFLILFRDSGCQFRSLYTYCPETEEINKLTGI 1428
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 663071131   1429 GPKSITKKMIEGLYKYNSDRKQFSHIPAKTLSASVDAITIHSHLWQTKR 1477
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 237-315 4.47e-41

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


:

Pssm-ID: 432229  Cd Length: 85  Bit Score: 145.91  E-value: 4.47e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663071131   237 KQLPCIPLVENLLKDGTDGCALAALIHFYCPDVVRLEDICLKETMSLADSLYNLQLIQEFCQEYL-NQCCHFTLEDMLYA 315
Cdd:pfam11971    5 RSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLEDLLYA 84
CAMSAP_CC1 pfam17095
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ...
 754-804 6.30e-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: 90.44  E-value: 6.30e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 663071131   754 TQLLASEMVHLRMKLEEKRRAIEAQKKKMEAAFTKQRQKMGRTAFLTVVKK 804
Cdd:pfam17095    9 SPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 932-1141 2.54e-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: 42.62  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663071131  932 PPQPSPQKQIRDfkPSKQAGLSSAIAPFSSDSPRPTHPSPQSSNRKSASFSVKSQRTPRPNELKITPLNRTLTPPRSVDS 1011
Cdd:PHA03247 2592 PPQSARPRAPVD--DRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARR 2669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663071131 1012 LPR-------LRRFSPSQVPIQTRSFVCFGDDGEPQLKESKPKEEVKKEELESKGTLEQRGHNPeEKEIKPFESTVSEVL 1084
Cdd:PHA03247 2670 LGRaaqasspPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASP-ALPAAPAPPAVPAGP 2748

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663071131 1085 SLPVTETVCLTP----NEDQLNQPTEPPPKPVFPPTAPKNVNLIEVSLSDLKPPEKADVPV 1141
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 ...
 1349-1477 5.24e-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: 238.80  E-value: 5.24e-73
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663071131   1349 GPKLYKEPSAKSNKHIIQNALAHCCLAGKVNEGQKKKILEEMEKSDANNFLILFRDSGCQFRSLYTYCPETEEINKLTGI 1428
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 663071131   1429 GPKSITKKMIEGLYKYNSDRKQFSHIPAKTLSASVDAITIHSHLWQTKR 1477
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CKK pfam08683
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1350-1468 1.59e-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: 237.18  E-value: 1.59e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663071131  1350 PKLYKEPSAKSNKHIIQNALAHCCLAGKVNEGQKKKILEEMEKSDANNFLILFRDSGCQFRSLYTYCPETEEINKLTGIG 1429
Cdd:pfam08683    1 PKLFKKPSAKSNKKIIHNALSHCCLAGKVNEDQKNKILEELEKSESKHFLILFRDSGCQFRALYSYNPETEELVKLHGIG 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 663071131  1430 PKSITKKMIEGLYKYNSDRKQFSHIPAKTLSASVDAITI 1468
Cdd:pfam08683   81 PRVVTPKMIEKFYKYNSGRKQFTEIPTKTLSVSIDAFTI 119
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 237-315 4.47e-41

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


Pssm-ID: 432229  Cd Length: 85  Bit Score: 145.91  E-value: 4.47e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663071131   237 KQLPCIPLVENLLKDGTDGCALAALIHFYCPDVVRLEDICLKETMSLADSLYNLQLIQEFCQEYL-NQCCHFTLEDMLYA 315
Cdd:pfam11971    5 RSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLEDLLYA 84
CAMSAP_CC1 pfam17095
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ...
 754-804 6.30e-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: 90.44  E-value: 6.30e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 663071131   754 TQLLASEMVHLRMKLEEKRRAIEAQKKKMEAAFTKQRQKMGRTAFLTVVKK 804
Cdd:pfam17095    9 SPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59
PHA03247 PHA03247
large tegument protein UL36; Provisional
 932-1141 2.54e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663071131  932 PPQPSPQKQIRDfkPSKQAGLSSAIAPFSSDSPRPTHPSPQSSNRKSASFSVKSQRTPRPNELKITPLNRTLTPPRSVDS 1011
Cdd:PHA03247 2592 PPQSARPRAPVD--DRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARR 2669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663071131 1012 LPR-------LRRFSPSQVPIQTRSFVCFGDDGEPQLKESKPKEEVKKEELESKGTLEQRGHNPeEKEIKPFESTVSEVL 1084
Cdd:PHA03247 2670 LGRaaqasspPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASP-ALPAAPAPPAVPAGP 2748

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663071131 1085 SLPVTETVCLTP----NEDQLNQPTEPPPKPVFPPTAPKNVNLIEVSLSDLKPPEKADVPV 1141
Cdd:PHA03247 2749 ATPGGPARPARPpttaGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPA 2809
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 253-282 3.06e-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: 3.06e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 663071131  253 TDGCALAALIHFYCPDVVRLEDICLKETMS 282
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 ...
 1349-1477 5.24e-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: 238.80  E-value: 5.24e-73
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663071131   1349 GPKLYKEPSAKSNKHIIQNALAHCCLAGKVNEGQKKKILEEMEKSDANNFLILFRDSGCQFRSLYTYCPETEEINKLTGI 1428
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 663071131   1429 GPKSITKKMIEGLYKYNSDRKQFSHIPAKTLSASVDAITIHSHLWQTKR 1477
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CKK pfam08683
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1350-1468 1.59e-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: 237.18  E-value: 1.59e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663071131  1350 PKLYKEPSAKSNKHIIQNALAHCCLAGKVNEGQKKKILEEMEKSDANNFLILFRDSGCQFRSLYTYCPETEEINKLTGIG 1429
Cdd:pfam08683    1 PKLFKKPSAKSNKKIIHNALSHCCLAGKVNEDQKNKILEELEKSESKHFLILFRDSGCQFRALYSYNPETEELVKLHGIG 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 663071131  1430 PKSITKKMIEGLYKYNSDRKQFSHIPAKTLSASVDAITI 1468
Cdd:pfam08683   81 PRVVTPKMIEKFYKYNSGRKQFTEIPTKTLSVSIDAFTI 119
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 237-315 4.47e-41

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


Pssm-ID: 432229  Cd Length: 85  Bit Score: 145.91  E-value: 4.47e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663071131   237 KQLPCIPLVENLLKDGTDGCALAALIHFYCPDVVRLEDICLKETMSLADSLYNLQLIQEFCQEYL-NQCCHFTLEDMLYA 315
Cdd:pfam11971    5 RSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLEDLLYA 84
CAMSAP_CC1 pfam17095
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ...
 754-804 6.30e-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: 90.44  E-value: 6.30e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 663071131   754 TQLLASEMVHLRMKLEEKRRAIEAQKKKMEAAFTKQRQKMGRTAFLTVVKK 804
Cdd:pfam17095    9 SPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59
PHA03247 PHA03247
large tegument protein UL36; Provisional
 932-1141 2.54e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663071131  932 PPQPSPQKQIRDfkPSKQAGLSSAIAPFSSDSPRPTHPSPQSSNRKSASFSVKSQRTPRPNELKITPLNRTLTPPRSVDS 1011
Cdd:PHA03247 2592 PPQSARPRAPVD--DRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARR 2669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663071131 1012 LPR-------LRRFSPSQVPIQTRSFVCFGDDGEPQLKESKPKEEVKKEELESKGTLEQRGHNPeEKEIKPFESTVSEVL 1084
Cdd:PHA03247 2670 LGRaaqasspPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASP-ALPAAPAPPAVPAGP 2748

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663071131 1085 SLPVTETVCLTP----NEDQLNQPTEPPPKPVFPPTAPKNVNLIEVSLSDLKPPEKADVPV 1141
Cdd:PHA03247 2749 ATPGGPARPARPpttaGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPA 2809
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 253-282 3.06e-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: 3.06e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 663071131  253 TDGCALAALIHFYCPDVVRLEDICLKETMS 282
Cdd:cd21224    28 ADGRALCYLIHHYLPSLLPLDAIRQPTTQT 57
 
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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