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Conserved domains on  [gi|21493045|ref|NP_004265|]
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A-kinase anchor protein 6 [Homo sapiens]

Protein Classification

SPEC domain-containing protein( domain architecture ID 10242646)

SPEC domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 961-1189 7.04e-09

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 58.23  E-value: 7.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21493045  961 LLDFDSEYQELWDWLIDMESLVMD---SHDLMMSEEQQQHLyKRYSVEMSIRHLKKTELLSKVEALKKGGVLLPNDLLEK 1037
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELLSStdyGDDLESVEALLKKH-EALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21493045 1038 VDSINEKWELLGKTL---GEKIQDTMAGHSGSspRDLLspesgslvrqlevrikELKGWLRDTELFIfnscLRQEKEGTM 1114
Cdd:cd00176   81 LEELNQRWEELRELAeerRQRLEEALDLQQFF--RDAD----------------DLEQWLEEKEAAL----ASEDLGKDL 138

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21493045 1115 NT-EKQLQYFKSLCREIKQRRRGVASILRLCQHLLDDRETCNLNADHQPMQliivNLERRWEAIVMQAVQWQTRLQ 1189
Cdd:cd00176  139 ESvEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLE----ELNERWEELLELAEERQKKLE 210
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 784-887 1.35e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


The actual alignment was detected with superfamily member cd00176:

Pssm-ID: 413338 [Multi-domain]  Cd Length: 213  Bit Score: 45.51  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21493045  784 FVNKLDEFIQWLNEAMETTENWTPPKaEMDDLKLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELIASHKAGLKDMLRM 863
Cdd:cd00176    5 FLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEE 83

                         90       100
                 ....*....|....*....|....
gi 21493045  864 IASQWKELQRQIKRQHSWILRALD 887
Cdd:cd00176   84 LNQRWEELRELAEERRQRLEEALD 107
 
Name Accession Description Interval E-value
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 961-1189 7.04e-09

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 58.23  E-value: 7.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21493045  961 LLDFDSEYQELWDWLIDMESLVMD---SHDLMMSEEQQQHLyKRYSVEMSIRHLKKTELLSKVEALKKGGVLLPNDLLEK 1037
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELLSStdyGDDLESVEALLKKH-EALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21493045 1038 VDSINEKWELLGKTL---GEKIQDTMAGHSGSspRDLLspesgslvrqlevrikELKGWLRDTELFIfnscLRQEKEGTM 1114
Cdd:cd00176   81 LEELNQRWEELRELAeerRQRLEEALDLQQFF--RDAD----------------DLEQWLEEKEAAL----ASEDLGKDL 138

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21493045 1115 NT-EKQLQYFKSLCREIKQRRRGVASILRLCQHLLDDRETCNLNADHQPMQliivNLERRWEAIVMQAVQWQTRLQ 1189
Cdd:cd00176  139 ESvEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLE----ELNERWEELLELAEERQKKLE 210
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 784-887 1.35e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 45.51  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21493045  784 FVNKLDEFIQWLNEAMETTENWTPPKaEMDDLKLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELIASHKAGLKDMLRM 863
Cdd:cd00176    5 FLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEE 83

                         90       100
                 ....*....|....*....|....
gi 21493045  864 IASQWKELQRQIKRQHSWILRALD 887
Cdd:cd00176   84 LNQRWEELRELAEERRQRLEEALD 107
SPEC smart00150
Spectrin repeats;
784-882 8.13e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 40.78  E-value: 8.13e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21493045     784 FVNKLDEFIQWLNEaMETTENWTPPKAEMDDLKLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELIASHKAGLKDMLRM 863
Cdd:smart00150    3 FLRDADELEAWLEE-KEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEE 81

                            90
                    ....*....|....*....
gi 21493045     864 IASQWKELQRQIKRQHSWI 882
Cdd:smart00150   82 LNERWEELKELAEERRQKL 100
SPEC smart00150
Spectrin repeats;
964-1055 8.79e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 40.78  E-value: 8.79e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21493045     964 FDSEYQELWDWLIDMESLVMD---SHDLMMSEEQQQHLyKRYSVEMSIRHLKKTELLSKVEALKKGGVLLPNDLLEKVDS 1040
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASedlGKDLESVEALLKKH-EAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEE 81

                            90
                    ....*....|....*
gi 21493045    1041 INEKWELLGKTLGEK 1055
Cdd:smart00150   82 LNERWEELKELAEER 96
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 784-884 1.07e-03

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 40.76  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21493045    784 FVNKLDEFIQWLNEAMETTeNWTPPKAEMDDLKLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELIASHKAGLKDMLRM 863
Cdd:pfam00435    6 FFRDADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEE 84

                           90       100
                   ....*....|....*....|.
gi 21493045    864 IASQWKELQRQIKRQHSWILR 884
Cdd:pfam00435   85 LNERWEQLLELAAERKQKLEE 105
 
Name Accession Description Interval E-value
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 961-1189 7.04e-09

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 58.23  E-value: 7.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21493045  961 LLDFDSEYQELWDWLIDMESLVMD---SHDLMMSEEQQQHLyKRYSVEMSIRHLKKTELLSKVEALKKGGVLLPNDLLEK 1037
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELLSStdyGDDLESVEALLKKH-EALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21493045 1038 VDSINEKWELLGKTL---GEKIQDTMAGHSGSspRDLLspesgslvrqlevrikELKGWLRDTELFIfnscLRQEKEGTM 1114
Cdd:cd00176   81 LEELNQRWEELRELAeerRQRLEEALDLQQFF--RDAD----------------DLEQWLEEKEAAL----ASEDLGKDL 138

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21493045 1115 NT-EKQLQYFKSLCREIKQRRRGVASILRLCQHLLDDRETCNLNADHQPMQliivNLERRWEAIVMQAVQWQTRLQ 1189
Cdd:cd00176  139 ESvEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLE----ELNERWEELLELAEERQKKLE 210
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 784-887 1.35e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 45.51  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21493045  784 FVNKLDEFIQWLNEAMETTENWTPPKaEMDDLKLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELIASHKAGLKDMLRM 863
Cdd:cd00176    5 FLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEE 83

                         90       100
                 ....*....|....*....|....
gi 21493045  864 IASQWKELQRQIKRQHSWILRALD 887
Cdd:cd00176   84 LNQRWEELRELAEERRQRLEEALD 107
SPEC smart00150
Spectrin repeats;
784-882 8.13e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 40.78  E-value: 8.13e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21493045     784 FVNKLDEFIQWLNEaMETTENWTPPKAEMDDLKLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELIASHKAGLKDMLRM 863
Cdd:smart00150    3 FLRDADELEAWLEE-KEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEE 81

                            90
                    ....*....|....*....
gi 21493045     864 IASQWKELQRQIKRQHSWI 882
Cdd:smart00150   82 LNERWEELKELAEERRQKL 100
SPEC smart00150
Spectrin repeats;
964-1055 8.79e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 40.78  E-value: 8.79e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21493045     964 FDSEYQELWDWLIDMESLVMD---SHDLMMSEEQQQHLyKRYSVEMSIRHLKKTELLSKVEALKKGGVLLPNDLLEKVDS 1040
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASedlGKDLESVEALLKKH-EAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEE 81

                            90
                    ....*....|....*
gi 21493045    1041 INEKWELLGKTLGEK 1055
Cdd:smart00150   82 LNERWEELKELAEER 96
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 784-884 1.07e-03

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 40.76  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21493045    784 FVNKLDEFIQWLNEAMETTeNWTPPKAEMDDLKLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELIASHKAGLKDMLRM 863
Cdd:pfam00435    6 FFRDADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEE 84

                           90       100
                   ....*....|....*....|.
gi 21493045    864 IASQWKELQRQIKRQHSWILR 884
Cdd:pfam00435   85 LNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
1081-1189 1.34e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 40.39  E-value: 1.34e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21493045    1081 RQLEVRIKELKGWLRDTELFifnscLRQEKEGT--MNTEKQLQYFKSLCREIKQRRRGVASILRLCQHLLDDREtcnlnA 1158
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQL-----LASEDLGKdlESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH-----P 70

                            90       100       110
                    ....*....|....*....|....*....|.
gi 21493045    1159 DHQPMQLIIVNLERRWEAIVMQAVQWQTRLQ 1189
Cdd:smart00150   71 DAEEIEERLEELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 1079-1203 3.19e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 41.28  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21493045 1079 LVRQLEVRIKELKGWLRDTELFIFNSCLRQEKEGTmntEKQLQYFKSLCREIKQRRRGVASILRLCQHLLDDREtcnlnA 1158
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESV---EALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-----P 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 21493045 1159 DHQPMQLIIVNLERRWEAIVMQAVQWQTRLQKKMGKESETLNVID 1203
Cdd:cd00176   73 DAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD 117
 
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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