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Conserved domains on  [gi|568979570|ref|XP_006515892|]
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A-kinase anchor protein 6 isoform X3 [Mus musculus]

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 ...
 715-941 8.12e-12

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: 66.70  E-value: 8.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979570  715 LLDFDSEYQELWDWLIDMESLVMD---SHDLMMSEEQQQHLyKRYSVEMSIRHLKKTELLSKVEALKKGGLSLPNDILEK 791
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSStdyGDDLESVEALLKKH-EALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979570  792 VDSINEKWELLGKTL---REKIQDTMAGHSGSgprdllspesgSLVRQLEVRIKELKRWLRDTELfifnsclrqEKEGTS 868
Cdd:cd00176    81 LEELNQRWEELRELAeerRQRLEEALDLQQFF-----------RDADDLEQWLEEKEAALASEDL---------GKDLES 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568979570  869 AEKQLQYFKSLCHEIKQRRRGVASILRLCQHLLDDRDTCNLNADHQPMQliivNLERRWEAIVMQAVQWQTRL 941
Cdd:cd00176   141 VEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLE----ELNERWEELLELAEERQKKL 209
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 537-681 4.87e-05

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: 46.67  E-value: 4.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979570  537 FVNKLDEFIQWLNEAMETTENWTPPKAETdSLRLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELiASHKAEGLKDMLK 616
Cdd:cd00176     5 FLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQERLE 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568979570  617 MIASQWKELQRQIKRQHSWILRAL---------DTIKAEILATDVSVEDEEGTGSP-KAEAQLCYLEAQRDAVEQ 681
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALdlqqffrdaDDLEQWLEEKEAALASEDLGKDLeSVEELLKKHKELEEELEA 157
 
Name Accession Description Interval E-value
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 715-941 8.12e-12

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: 66.70  E-value: 8.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979570  715 LLDFDSEYQELWDWLIDMESLVMD---SHDLMMSEEQQQHLyKRYSVEMSIRHLKKTELLSKVEALKKGGLSLPNDILEK 791
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSStdyGDDLESVEALLKKH-EALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979570  792 VDSINEKWELLGKTL---REKIQDTMAGHSGSgprdllspesgSLVRQLEVRIKELKRWLRDTELfifnsclrqEKEGTS 868
Cdd:cd00176    81 LEELNQRWEELRELAeerRQRLEEALDLQQFF-----------RDADDLEQWLEEKEAALASEDL---------GKDLES 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568979570  869 AEKQLQYFKSLCHEIKQRRRGVASILRLCQHLLDDRDTCNLNADHQPMQliivNLERRWEAIVMQAVQWQTRL 941
Cdd:cd00176   141 VEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLE----ELNERWEELLELAEERQKKL 209
SPEC smart00150
Spectrin repeats;
718-809 4.82e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 44.24  E-value: 4.82e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979570    718 FDSEYQELWDWLIDMESLVMD---SHDLMMSEEQQQHLyKRYSVEMSIRHLKKTELLSKVEALKKGGLSLPNDILEKVDS 794
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASedlGKDLESVEALLKKH-EAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEE 81

                            90
                    ....*....|....*
gi 568979570    795 INEKWELLGKTLREK 809
Cdd:smart00150   82 LNERWEELKELAEER 96
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 537-681 4.87e-05

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: 46.67  E-value: 4.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979570  537 FVNKLDEFIQWLNEAMETTENWTPPKAETdSLRLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELiASHKAEGLKDMLK 616
Cdd:cd00176     5 FLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQERLE 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568979570  617 MIASQWKELQRQIKRQHSWILRAL---------DTIKAEILATDVSVEDEEGTGSP-KAEAQLCYLEAQRDAVEQ 681
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALdlqqffrdaDDLEQWLEEKEAALASEDLGKDLeSVEELLKKHKELEEELEA 157
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 537-638 8.45e-04

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: 8.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979570   537 FVNKLDEFIQWLNEAMETTeNWTPPKAETDSLRLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELiASHKAEGLKDMLK 616
Cdd:pfam00435    6 FFRDADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQERLE 83

                           90       100
                   ....*....|....*....|..
gi 568979570   617 MIASQWKELQRQIKRQHSWILR 638
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
537-636 2.63e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 39.24  E-value: 2.63e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979570    537 FVNKLDEFIQWLNEaMETTENWTPPKAETDSLRLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELIASHKAEgLKDMLK 616
Cdd:smart00150    3 FLRDADELEAWLEE-KEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE-IEERLE 80

                            90       100
                    ....*....|....*....|
gi 568979570    617 MIASQWKELQRQIKRQHSWI 636
Cdd:smart00150   81 ELNERWEELKELAEERRQKL 100
 
Name Accession Description Interval E-value
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 715-941 8.12e-12

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: 66.70  E-value: 8.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979570  715 LLDFDSEYQELWDWLIDMESLVMD---SHDLMMSEEQQQHLyKRYSVEMSIRHLKKTELLSKVEALKKGGLSLPNDILEK 791
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSStdyGDDLESVEALLKKH-EALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979570  792 VDSINEKWELLGKTL---REKIQDTMAGHSGSgprdllspesgSLVRQLEVRIKELKRWLRDTELfifnsclrqEKEGTS 868
Cdd:cd00176    81 LEELNQRWEELRELAeerRQRLEEALDLQQFF-----------RDADDLEQWLEEKEAALASEDL---------GKDLES 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568979570  869 AEKQLQYFKSLCHEIKQRRRGVASILRLCQHLLDDRDTCNLNADHQPMQliivNLERRWEAIVMQAVQWQTRL 941
Cdd:cd00176   141 VEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLE----ELNERWEELLELAEERQKKL 209
SPEC smart00150
Spectrin repeats;
718-809 4.82e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 44.24  E-value: 4.82e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979570    718 FDSEYQELWDWLIDMESLVMD---SHDLMMSEEQQQHLyKRYSVEMSIRHLKKTELLSKVEALKKGGLSLPNDILEKVDS 794
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASedlGKDLESVEALLKKH-EAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEE 81

                            90
                    ....*....|....*
gi 568979570    795 INEKWELLGKTLREK 809
Cdd:smart00150   82 LNERWEELKELAEER 96
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 537-681 4.87e-05

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: 46.67  E-value: 4.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979570  537 FVNKLDEFIQWLNEAMETTENWTPPKAETdSLRLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELiASHKAEGLKDMLK 616
Cdd:cd00176     5 FLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQERLE 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568979570  617 MIASQWKELQRQIKRQHSWILRAL---------DTIKAEILATDVSVEDEEGTGSP-KAEAQLCYLEAQRDAVEQ 681
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALdlqqffrdaDDLEQWLEEKEAALASEDLGKDLeSVEELLKKHKELEEELEA 157
SPEC smart00150
Spectrin repeats;
835-941 4.35e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 41.55  E-value: 4.35e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979570    835 RQLEVRIKELKRWLRDTELFifnscLRQEKEG---TSAEKQLQYFKSLCHEIKQRRRGVASILRLCQHLLDDRDtcnlnA 911
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQL-----LASEDLGkdlESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH-----P 70

                            90       100       110
                    ....*....|....*....|....*....|
gi 568979570    912 DHQPMQLIIVNLERRWEAIVMQAVQWQTRL 941
Cdd:smart00150   71 DAEEIEERLEELNERWEELKELAEERRQKL 100
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 537-638 8.45e-04

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: 8.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979570   537 FVNKLDEFIQWLNEAMETTeNWTPPKAETDSLRLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELiASHKAEGLKDMLK 616
Cdd:pfam00435    6 FFRDADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQERLE 83

                           90       100
                   ....*....|....*....|..
gi 568979570   617 MIASQWKELQRQIKRQHSWILR 638
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLEE 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 833-945 2.33e-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: 41.66  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979570  833 LVRQLEVRIKELKRWLRDTELFIFNSCLRQEKEgtSAEKQLQYFKSLCHEIKQRRRGVASILRLCQHLLDDRDtcnlnAD 912
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLE--SVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-----PD 73

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568979570  913 HQPMQLIIVNLERRWEAIVMQAVQWQTRLRKKM 945
Cdd:cd00176    74 AEEIQERLEELNQRWEELRELAEERRQRLEEAL 106
SPEC smart00150
Spectrin repeats;
537-636 2.63e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 39.24  E-value: 2.63e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979570    537 FVNKLDEFIQWLNEaMETTENWTPPKAETDSLRLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELIASHKAEgLKDMLK 616
Cdd:smart00150    3 FLRDADELEAWLEE-KEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE-IEERLE 80

                            90       100
                    ....*....|....*....|
gi 568979570    617 MIASQWKELQRQIKRQHSWI 636
Cdd:smart00150   81 ELNERWEELKELAEERRQKL 100
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 537-640 3.38e-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: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568979570  537 FVNKLDEFIQWLNEAMETTENwTPPKAETDSLRLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELIASHKAEGLKDMLK 616
Cdd:cd00176   111 FFRDADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLE 189

                          90       100
                  ....*....|....*....|....
gi 568979570  617 MIASQWKELQRQIKRQHSWILRAL 640
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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