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Conserved domains on  [gi|1958784567|ref|XP_038968817|]
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A-kinase anchor protein 6 isoform X3 [Rattus norvegicus]

Protein Classification

spectrin repeat-containing protein( domain architecture ID 10242646)

spectrin repeat-containing protein such as plectin, a prototypical plakin that tethers intermediate filaments to membrane-associated complexes

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 ...
 961-1188 1.60e-11

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: 65.16  E-value: 1.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784567  961 LLDFDSEYQELWDWLIDMESLVMD---SHDLMMSEEQQQHLyKRYSVEMSIRHLKKSELLSKVEALKKGGLSLPDDILEK 1037
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSStdyGDDLESVEALLKKH-EALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784567 1038 VDSINEKWELLGKTL---REKIQDTIAGHSGSgprdllspesgSLVRQLEVRIKELKRWLRDTELfifnsclrqEKEGTS 1114
Cdd:cd00176     81 LEELNQRWEELRELAeerRQRLEEALDLQQFF-----------RDADDLEQWLEEKEAALASEDL---------GKDLES 140

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958784567 1115 AEKQLQYFKSLCREIKQRRRGVASILRLCQHLLDDRDTCNLNADHQPMQliivNLERRWEAIVMQAVQWQTRLQ 1188
Cdd:cd00176    141 VEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLE----ELNERWEELLELAEERQKKLE 210
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 783-887 1.89e-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: 44.36  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784567  783 FVNKLDEFIQWLNEAMETTENWTPPKAETdSLRLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELVVSHKAEgLKDTLR 862
Cdd:cd00176      5 FLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE-IQERLE 82

                           90       100
                   ....*....|....*....|....*
gi 1958784567  863 MIASQWKELQRQIKRQHSWILRALD 887
Cdd:cd00176     83 ELNQRWEELRELAEERRQRLEEALD 107
 
Name Accession Description Interval E-value
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 961-1188 1.60e-11

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: 65.16  E-value: 1.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784567  961 LLDFDSEYQELWDWLIDMESLVMD---SHDLMMSEEQQQHLyKRYSVEMSIRHLKKSELLSKVEALKKGGLSLPDDILEK 1037
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSStdyGDDLESVEALLKKH-EALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784567 1038 VDSINEKWELLGKTL---REKIQDTIAGHSGSgprdllspesgSLVRQLEVRIKELKRWLRDTELfifnsclrqEKEGTS 1114
Cdd:cd00176     81 LEELNQRWEELRELAeerRQRLEEALDLQQFF-----------RDADDLEQWLEEKEAALASEDL---------GKDLES 140

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958784567 1115 AEKQLQYFKSLCREIKQRRRGVASILRLCQHLLDDRDTCNLNADHQPMQliivNLERRWEAIVMQAVQWQTRLQ 1188
Cdd:cd00176    141 VEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLE----ELNERWEELLELAEERQKKLE 210
SPEC smart00150
Spectrin repeats;
964-1055 1.50e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.01  E-value: 1.50e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784567   964 FDSEYQELWDWLIDMESLVMD---SHDLMMSEEQQQHLyKRYSVEMSIRHLKKSELLSKVEALKKGGLSLPDDILEKVDS 1040
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASedlGKDLESVEALLKKH-EAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEE 81

                            90
                    ....*....|....*
gi 1958784567  1041 INEKWELLGKTLREK 1055
Cdd:smart00150   82 LNERWEELKELAEER 96
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 783-887 1.89e-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: 44.36  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784567  783 FVNKLDEFIQWLNEAMETTENWTPPKAETdSLRLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELVVSHKAEgLKDTLR 862
Cdd:cd00176      5 FLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE-IQERLE 82

                           90       100
                   ....*....|....*....|....*
gi 1958784567  863 MIASQWKELQRQIKRQHSWILRALD 887
Cdd:cd00176     83 ELNQRWEELRELAEERRQRLEEALD 107
SPEC smart00150
Spectrin repeats;
783-882 2.87e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 38.46  E-value: 2.87e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784567   783 FVNKLDEFIQWLNEaMETTENWTPPKAETDSLRLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELVVSHKAEgLKDTLR 862
Cdd:smart00150    3 FLRDADELEAWLEE-KEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE-IEERLE 80

                            90       100
                    ....*....|....*....|
gi 1958784567   863 MIASQWKELQRQIKRQHSWI 882
Cdd:smart00150   81 ELNERWEELKELAEERRQKL 100
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 783-884 3.32e-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: 38.45  E-value: 3.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784567  783 FVNKLDEFIQWLNEAMETTeNWTPPKAETDSLRLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELVVsHKAEGLKDTLR 862
Cdd:pfam00435    6 FFRDADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGH-YASEEIQERLE 83

                           90       100
                   ....*....|....*....|..
gi 1958784567  863 MIASQWKELQRQIKRQHSWILR 884
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLEE 105
 
Name Accession Description Interval E-value
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 961-1188 1.60e-11

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: 65.16  E-value: 1.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784567  961 LLDFDSEYQELWDWLIDMESLVMD---SHDLMMSEEQQQHLyKRYSVEMSIRHLKKSELLSKVEALKKGGLSLPDDILEK 1037
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSStdyGDDLESVEALLKKH-EALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784567 1038 VDSINEKWELLGKTL---REKIQDTIAGHSGSgprdllspesgSLVRQLEVRIKELKRWLRDTELfifnsclrqEKEGTS 1114
Cdd:cd00176     81 LEELNQRWEELRELAeerRQRLEEALDLQQFF-----------RDADDLEQWLEEKEAALASEDL---------GKDLES 140

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958784567 1115 AEKQLQYFKSLCREIKQRRRGVASILRLCQHLLDDRDTCNLNADHQPMQliivNLERRWEAIVMQAVQWQTRLQ 1188
Cdd:cd00176    141 VEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLE----ELNERWEELLELAEERQKKLE 210
SPEC smart00150
Spectrin repeats;
964-1055 1.50e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.01  E-value: 1.50e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784567   964 FDSEYQELWDWLIDMESLVMD---SHDLMMSEEQQQHLyKRYSVEMSIRHLKKSELLSKVEALKKGGLSLPDDILEKVDS 1040
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASedlGKDLESVEALLKKH-EAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEE 81

                            90
                    ....*....|....*
gi 1958784567  1041 INEKWELLGKTLREK 1055
Cdd:smart00150   82 LNERWEELKELAEER 96
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 783-887 1.89e-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: 44.36  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784567  783 FVNKLDEFIQWLNEAMETTENWTPPKAETdSLRLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELVVSHKAEgLKDTLR 862
Cdd:cd00176      5 FLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE-IQERLE 82

                           90       100
                   ....*....|....*....|....*
gi 1958784567  863 MIASQWKELQRQIKRQHSWILRALD 887
Cdd:cd00176     83 ELNQRWEELRELAEERRQRLEEALD 107
SPEC smart00150
Spectrin repeats;
1081-1188 3.91e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 40.78  E-value: 3.91e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784567  1081 RQLEVRIKELKRWLRDTELFifnscLRQEKEG---TSAEKQLQYFKSLCREIKQRRRGVASILRLCQHLLDDRDtcnlnA 1157
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQL-----LASEDLGkdlESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH-----P 70

                            90       100       110
                    ....*....|....*....|....*....|.
gi 1958784567  1158 DHQPMQLIIVNLERRWEAIVMQAVQWQTRLQ 1188
Cdd:smart00150   71 DAEEIEERLEELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 1079-1198 6.64e-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: 42.43  E-value: 6.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784567 1079 LVRQLEVRIKELKRWLRDTELFIFNSCLRQEKEgtSAEKQLQYFKSLCREIKQRRRGVASILRLCQHLLDDRDtcnlnAD 1158
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLE--SVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-----PD 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958784567 1159 HQPMQLIIVNLERRWEAIVMQAVQWQTRLQKKMGKESFYS 1198
Cdd:cd00176     74 AEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR 113
SPEC smart00150
Spectrin repeats;
783-882 2.87e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 38.46  E-value: 2.87e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784567   783 FVNKLDEFIQWLNEaMETTENWTPPKAETDSLRLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELVVSHKAEgLKDTLR 862
Cdd:smart00150    3 FLRDADELEAWLEE-KEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE-IEERLE 80

                            90       100
                    ....*....|....*....|
gi 1958784567   863 MIASQWKELQRQIKRQHSWI 882
Cdd:smart00150   81 ELNERWEELKELAEERRQKL 100
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 783-884 3.32e-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: 38.45  E-value: 3.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784567  783 FVNKLDEFIQWLNEAMETTeNWTPPKAETDSLRLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELVVsHKAEGLKDTLR 862
Cdd:pfam00435    6 FFRDADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGH-YASEEIQERLE 83

                           90       100
                   ....*....|....*....|..
gi 1958784567  863 MIASQWKELQRQIKRQHSWILR 884
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLEE 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 783-886 6.34e-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: 39.74  E-value: 6.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784567  783 FVNKLDEFIQWLNEAMETTENwTPPKAETDSLRLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELVVSHKAEGLKDTLR 862
Cdd:cd00176    111 FFRDADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLE 189

                           90       100
                   ....*....|....*....|....
gi 1958784567  863 MIASQWKELQRQIKRQHSWILRAL 886
Cdd:cd00176    190 ELNERWEELLELAEERQKKLEEAL 213
 
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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