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Conserved domains on  [gi|119120816|ref|NP_071310|]
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nesprin-1 isoform 2 [Mus musculus]

Protein Classification

SPEC and KASH domain-containing protein( domain architecture ID 10075249)

SPEC and KASH 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 ...
 155-365 4.14e-25

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: 104.06  E-value: 4.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816 155 LWQKFLDDYSRFEDWLEVSERTAAFPSSSGVLyTVAKEELKKFEAFQRQVHESLTQLELINKQYRRLARENRTDSAcSLR 234
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-EIQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816 235 QMVHGGNQRWDDLQKRVTSILRRLKHFISQREEFETARDsILVWLTEMDLQLTNIEHF-SECDVQAKIKQLKAFQQEISL 313
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGkDLESVEELLKKHKELEEELEA 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 119120816 314 NHNKIEQIIAQGEQLIEKSEPLDAAVIEEELDELRRYCQEVFGRVERYHKKL 365
Cdd:cd00176  158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKL 209
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 593-812 9.26e-25

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: 103.29  E-value: 9.26e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816 593 KWQQFNSDLNNIWAWLGETEEELDRLQHlalSTDIHTIESHIKKLKELQKAVDHRKAIILSINLCSSEFTQADSKESHDL 672
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDY---GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816 673 QDRLSQMNGRWDRVCSLLEDWRGLLQDALMQCQEFHEMSHalllMLENIDRRKNEIVPIDSTLDPETLQDHHKQLMQIKQ 752
Cdd:cd00176   78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD----LEQWLEEKEAALASEDLGKDLESVEELLKKHKELEE 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816 753 ELLKSQLRVASLQDMSRQLLVNAEGSDCLEAKEKVHVIGNRLKLLLKEVSHHIKDLEKLL 812
Cdd:cd00176  154 ELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
KASH pfam10541
Nuclear envelope localization domain; The KASH (for Klarsicht/ANC-1/Syne-1 homology) or KLS ...
 892-948 1.08e-16

Nuclear envelope localization domain; The KASH (for Klarsicht/ANC-1/Syne-1 homology) or KLS domain is a highly hydrophobic nuclear envelope localization domain of approximately 60 amino acids comprising a 20-amino-acid transmembrane region and a 30-35-residue C-terminal region that lies between the inner and the outer nuclear membranes. During meiotic prophase, telomeres cluster to form a bouquet arrangement of chromosomes. SUN and KASH domain proteins form complexes that span both membranes of the nuclear envelope. The KASH domain links the dynein motor complex of the microtubules, through the outer nuclear membrane to the Sad1 domain in the inner nuclear membrane which then interacts with the bouquet proteins Bqt1 and Bqt2 that are complexed with Bqt4, Rap1 and Taz1 and attached to the telomere. SUN domain-containing proteins are essential for recruiting KASH domain proteins at the outer nuclear membrane, and KASH domains provide a generic NE tethering device for functionally distinct proteins whose cytoplasmic domains mediate nuclear positioning, maintain physical connections with other cellular organelles, and possibly even influence chromosome dynamics.


:

Pssm-ID: 463142  Cd Length: 58  Bit Score: 74.94  E-value: 1.08e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 119120816  892 FLFRILRAALPFQLLLLLLIGLTCLVPMSEKDYSCALSNNFARSFHPMLRYTNGPPP 948
Cdd:pfam10541   1 FLGRVLRAALPLQLLLLLLLLLACLLPAGEEDYSCTLANNFARSFHPMLRYVNGPPP 57
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 43-251 9.35e-14

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: 71.32  E-value: 9.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816  43 QQLDKNMGSLRTWLAHMESELAKPivYDSCNSEEIQRKLNEQQELQRDIEKHSTGVASVLNLCEVLLHDCDACAtdaecD 122
Cdd:cd00176    3 QQFLRDADELEAWLSEKEELLSST--DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA-----E 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816 123 SIQQATRNLDRRWRNICAMSMERRLKIEETWRLWQkFLDDYSRFEDWLEVSERTAAFPSSSGVLYTVaKEELKKFEAFQR 202
Cdd:cd00176   76 EIQERLEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASEDLGKDLESV-EELLKKHKELEE 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 119120816 203 QVHESLTQLELINKQYRRLARENRTDSACSLRQMVHGGNQRWDDLQKRV 251
Cdd:cd00176  154 ELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELA 202
 
Name Accession Description Interval E-value
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 155-365 4.14e-25

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: 104.06  E-value: 4.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816 155 LWQKFLDDYSRFEDWLEVSERTAAFPSSSGVLyTVAKEELKKFEAFQRQVHESLTQLELINKQYRRLARENRTDSAcSLR 234
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-EIQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816 235 QMVHGGNQRWDDLQKRVTSILRRLKHFISQREEFETARDsILVWLTEMDLQLTNIEHF-SECDVQAKIKQLKAFQQEISL 313
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGkDLESVEELLKKHKELEEELEA 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 119120816 314 NHNKIEQIIAQGEQLIEKSEPLDAAVIEEELDELRRYCQEVFGRVERYHKKL 365
Cdd:cd00176  158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKL 209
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 593-812 9.26e-25

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: 103.29  E-value: 9.26e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816 593 KWQQFNSDLNNIWAWLGETEEELDRLQHlalSTDIHTIESHIKKLKELQKAVDHRKAIILSINLCSSEFTQADSKESHDL 672
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDY---GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816 673 QDRLSQMNGRWDRVCSLLEDWRGLLQDALMQCQEFHEMSHalllMLENIDRRKNEIVPIDSTLDPETLQDHHKQLMQIKQ 752
Cdd:cd00176   78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD----LEQWLEEKEAALASEDLGKDLESVEELLKKHKELEE 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816 753 ELLKSQLRVASLQDMSRQLLVNAEGSDCLEAKEKVHVIGNRLKLLLKEVSHHIKDLEKLL 812
Cdd:cd00176  154 ELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
KASH pfam10541
Nuclear envelope localization domain; The KASH (for Klarsicht/ANC-1/Syne-1 homology) or KLS ...
 892-948 1.08e-16

Nuclear envelope localization domain; The KASH (for Klarsicht/ANC-1/Syne-1 homology) or KLS domain is a highly hydrophobic nuclear envelope localization domain of approximately 60 amino acids comprising a 20-amino-acid transmembrane region and a 30-35-residue C-terminal region that lies between the inner and the outer nuclear membranes. During meiotic prophase, telomeres cluster to form a bouquet arrangement of chromosomes. SUN and KASH domain proteins form complexes that span both membranes of the nuclear envelope. The KASH domain links the dynein motor complex of the microtubules, through the outer nuclear membrane to the Sad1 domain in the inner nuclear membrane which then interacts with the bouquet proteins Bqt1 and Bqt2 that are complexed with Bqt4, Rap1 and Taz1 and attached to the telomere. SUN domain-containing proteins are essential for recruiting KASH domain proteins at the outer nuclear membrane, and KASH domains provide a generic NE tethering device for functionally distinct proteins whose cytoplasmic domains mediate nuclear positioning, maintain physical connections with other cellular organelles, and possibly even influence chromosome dynamics.


Pssm-ID: 463142  Cd Length: 58  Bit Score: 74.94  E-value: 1.08e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 119120816  892 FLFRILRAALPFQLLLLLLIGLTCLVPMSEKDYSCALSNNFARSFHPMLRYTNGPPP 948
Cdd:pfam10541   1 FLGRVLRAALPLQLLLLLLLLLACLLPAGEEDYSCTLANNFARSFHPMLRYVNGPPP 57
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 43-251 9.35e-14

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: 71.32  E-value: 9.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816  43 QQLDKNMGSLRTWLAHMESELAKPivYDSCNSEEIQRKLNEQQELQRDIEKHSTGVASVLNLCEVLLHDCDACAtdaecD 122
Cdd:cd00176    3 QQFLRDADELEAWLSEKEELLSST--DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA-----E 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816 123 SIQQATRNLDRRWRNICAMSMERRLKIEETWRLWQkFLDDYSRFEDWLEVSERTAAFPSSSGVLYTVaKEELKKFEAFQR 202
Cdd:cd00176   76 EIQERLEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASEDLGKDLESV-EELLKKHKELEE 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 119120816 203 QVHESLTQLELINKQYRRLARENRTDSACSLRQMVHGGNQRWDDLQKRV 251
Cdd:cd00176  154 ELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELA 202
SPEC smart00150
Spectrin repeats;
595-698 3.93e-13

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 66.20  E-value: 3.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816   595 QQFNSDLNNIWAWLGETEEELdrlQHLALSTDIHTIESHIKKLKELQKAVDHRKAIILSINLCSSEFTQADSKESHDLQD 674
Cdd:smart00150   1 QQFLRDADELEAWLEEKEQLL---ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEE 77

                           90       100
                   ....*....|....*....|....
gi 119120816   675 RLSQMNGRWDRVCSLLEDWRGLLQ 698
Cdd:smart00150  78 RLEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
266-365 2.28e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 61.19  E-value: 2.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816   266 EEFETARDSILVWLTEMDLQLTNIEHF-SECDVQAKIKQLKAFQQEISLNHNKIEQIIAQGEQLIEKSEPlDAAVIEEEL 344
Cdd:smart00150   1 QQFLRDADELEAWLEEKEQLLASEDLGkDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP-DAEEIEERL 79

                           90       100
                   ....*....|....*....|.
gi 119120816   345 DELRRYCQEVFGRVERYHKKL 365
Cdd:smart00150  80 EELNERWEELKELAEERRQKL 100
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 592-699 5.32e-10

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: 57.33  E-value: 5.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816  592 QKWQQFNSDLNNIWAWLGETEEELDRLQhlaLSTDIHTIESHIKKLKELQKAVDHRKAIILSINLCSSEFTQADSKESHD 671
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSED---YGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE 77

                          90       100
                  ....*....|....*....|....*...
gi 119120816  672 LQDRLSQMNGRWDRVCSLLEDWRGLLQD 699
Cdd:pfam00435  78 IQERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
43-150 4.99e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.56  E-value: 4.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816    43 QQLDKNMGSLRTWLAHMESELAKPIVYDScnSEEIQRKLNEQQELQRDIEKHSTGVASVLNLCEVLLHDCDAcatdaECD 122
Cdd:smart00150   1 QQFLRDADELEAWLEEKEQLLASEDLGKD--LESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP-----DAE 73

                           90       100
                   ....*....|....*....|....*...
gi 119120816   123 SIQQATRNLDRRWRNICAMSMERRLKIE 150
Cdd:smart00150  74 EIEERLEELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 264-365 6.93e-06

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: 45.77  E-value: 6.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816  264 QREEFETARDSILVWLTEMDLQLTNIEHF-SECDVQAKIKQLKAFQQEISLNHNKIEQIIAQGEQLIEkSEPLDAAVIEE 342
Cdd:pfam00435   2 LLQQFFRDADDLESWIEEKEALLSSEDYGkDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID-EGHYASEEIQE 80

                          90       100
                  ....*....|....*....|...
gi 119120816  343 ELDELRRYCQEVFGRVERYHKKL 365
Cdd:pfam00435  81 RLEELNERWEQLLELAAERKQKL 103
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
190-356 6.29e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 6.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816 190 AKEELKKFEAFQRQVHESLTQLELINKQYRRLARENRT----DSACSLRQMVHGGNQRWDDLQKRVTSILRRLKHFISQR 265
Cdd:COG4717   83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKleklLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816 266 EEFETARDSILVWLTEMDLQLTNIEHFSECDVQAKIKQLKAFQQEISLNHNKIEQIIAQGEQLIEKSEPL-DAAVIEEEL 344
Cdd:COG4717  163 EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLeNELEAAALE 242

                        170
                 ....*....|..
gi 119120816 345 DELRRYCQEVFG 356
Cdd:COG4717  243 ERLKEARLLLLI 254
 
Name Accession Description Interval E-value
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 155-365 4.14e-25

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: 104.06  E-value: 4.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816 155 LWQKFLDDYSRFEDWLEVSERTAAFPSSSGVLyTVAKEELKKFEAFQRQVHESLTQLELINKQYRRLARENRTDSAcSLR 234
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-EIQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816 235 QMVHGGNQRWDDLQKRVTSILRRLKHFISQREEFETARDsILVWLTEMDLQLTNIEHF-SECDVQAKIKQLKAFQQEISL 313
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGkDLESVEELLKKHKELEEELEA 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 119120816 314 NHNKIEQIIAQGEQLIEKSEPLDAAVIEEELDELRRYCQEVFGRVERYHKKL 365
Cdd:cd00176  158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKL 209
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 593-812 9.26e-25

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: 103.29  E-value: 9.26e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816 593 KWQQFNSDLNNIWAWLGETEEELDRLQHlalSTDIHTIESHIKKLKELQKAVDHRKAIILSINLCSSEFTQADSKESHDL 672
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTDY---GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816 673 QDRLSQMNGRWDRVCSLLEDWRGLLQDALMQCQEFHEMSHalllMLENIDRRKNEIVPIDSTLDPETLQDHHKQLMQIKQ 752
Cdd:cd00176   78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD----LEQWLEEKEAALASEDLGKDLESVEELLKKHKELEE 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816 753 ELLKSQLRVASLQDMSRQLLVNAEGSDCLEAKEKVHVIGNRLKLLLKEVSHHIKDLEKLL 812
Cdd:cd00176  154 ELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
KASH pfam10541
Nuclear envelope localization domain; The KASH (for Klarsicht/ANC-1/Syne-1 homology) or KLS ...
 892-948 1.08e-16

Nuclear envelope localization domain; The KASH (for Klarsicht/ANC-1/Syne-1 homology) or KLS domain is a highly hydrophobic nuclear envelope localization domain of approximately 60 amino acids comprising a 20-amino-acid transmembrane region and a 30-35-residue C-terminal region that lies between the inner and the outer nuclear membranes. During meiotic prophase, telomeres cluster to form a bouquet arrangement of chromosomes. SUN and KASH domain proteins form complexes that span both membranes of the nuclear envelope. The KASH domain links the dynein motor complex of the microtubules, through the outer nuclear membrane to the Sad1 domain in the inner nuclear membrane which then interacts with the bouquet proteins Bqt1 and Bqt2 that are complexed with Bqt4, Rap1 and Taz1 and attached to the telomere. SUN domain-containing proteins are essential for recruiting KASH domain proteins at the outer nuclear membrane, and KASH domains provide a generic NE tethering device for functionally distinct proteins whose cytoplasmic domains mediate nuclear positioning, maintain physical connections with other cellular organelles, and possibly even influence chromosome dynamics.


Pssm-ID: 463142  Cd Length: 58  Bit Score: 74.94  E-value: 1.08e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 119120816  892 FLFRILRAALPFQLLLLLLIGLTCLVPMSEKDYSCALSNNFARSFHPMLRYTNGPPP 948
Cdd:pfam10541   1 FLGRVLRAALPLQLLLLLLLLLACLLPAGEEDYSCTLANNFARSFHPMLRYVNGPPP 57
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 43-251 9.35e-14

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: 71.32  E-value: 9.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816  43 QQLDKNMGSLRTWLAHMESELAKPivYDSCNSEEIQRKLNEQQELQRDIEKHSTGVASVLNLCEVLLHDCDACAtdaecD 122
Cdd:cd00176    3 QQFLRDADELEAWLSEKEELLSST--DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA-----E 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816 123 SIQQATRNLDRRWRNICAMSMERRLKIEETWRLWQkFLDDYSRFEDWLEVSERTAAFPSSSGVLYTVaKEELKKFEAFQR 202
Cdd:cd00176   76 EIQERLEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASEDLGKDLESV-EELLKKHKELEE 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 119120816 203 QVHESLTQLELINKQYRRLARENRTDSACSLRQMVHGGNQRWDDLQKRV 251
Cdd:cd00176  154 ELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELA 202
SPEC smart00150
Spectrin repeats;
595-698 3.93e-13

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 66.20  E-value: 3.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816   595 QQFNSDLNNIWAWLGETEEELdrlQHLALSTDIHTIESHIKKLKELQKAVDHRKAIILSINLCSSEFTQADSKESHDLQD 674
Cdd:smart00150   1 QQFLRDADELEAWLEEKEQLL---ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEE 77

                           90       100
                   ....*....|....*....|....
gi 119120816   675 RLSQMNGRWDRVCSLLEDWRGLLQ 698
Cdd:smart00150  78 RLEELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 524-701 2.06e-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: 64.39  E-value: 2.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816 524 KGYMKLLGECSGSIDSVRRLEHKLAEEESFpgfvnlNSTETQT--AGVIDRWELLQAQAMSKELRMKQNLQKwQQFNSDL 601
Cdd:cd00176   43 EALEAELAAHEERVEALNELGEQLIEEGHP------DAEEIQErlEELNQRWEELRELAEERRQRLEEALDL-QQFFRDA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816 602 NNIWAWLGETEEELDRLQHlalSTDIHTIESHIKKLKELQKAVDHRKAIILSINLCSSEFTQADSKESHD-LQDRLSQMN 680
Cdd:cd00176  116 DDLEQWLEEKEAALASEDL---GKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEeIEEKLEELN 192

                        170       180
                 ....*....|....*....|.
gi 119120816 681 GRWDRVCSLLEDWRGLLQDAL 701
Cdd:cd00176  193 ERWEELLELAEERQKKLEEAL 213
SPEC smart00150
Spectrin repeats;
266-365 2.28e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 61.19  E-value: 2.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816   266 EEFETARDSILVWLTEMDLQLTNIEHF-SECDVQAKIKQLKAFQQEISLNHNKIEQIIAQGEQLIEKSEPlDAAVIEEEL 344
Cdd:smart00150   1 QQFLRDADELEAWLEEKEQLLASEDLGkDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP-DAEEIEERL 79

                           90       100
                   ....*....|....*....|.
gi 119120816   345 DELRRYCQEVFGRVERYHKKL 365
Cdd:smart00150  80 EELNERWEELKELAEERRQKL 100
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 592-699 5.32e-10

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: 57.33  E-value: 5.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816  592 QKWQQFNSDLNNIWAWLGETEEELDRLQhlaLSTDIHTIESHIKKLKELQKAVDHRKAIILSINLCSSEFTQADSKESHD 671
Cdd:pfam00435   1 LLLQQFFRDADDLESWIEEKEALLSSED---YGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE 77

                          90       100
                  ....*....|....*....|....*...
gi 119120816  672 LQDRLSQMNGRWDRVCSLLEDWRGLLQD 699
Cdd:pfam00435  78 IQERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
43-150 4.99e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.56  E-value: 4.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816    43 QQLDKNMGSLRTWLAHMESELAKPIVYDScnSEEIQRKLNEQQELQRDIEKHSTGVASVLNLCEVLLHDCDAcatdaECD 122
Cdd:smart00150   1 QQFLRDADELEAWLEEKEQLLASEDLGKD--LESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP-----DAE 73

                           90       100
                   ....*....|....*....|....*...
gi 119120816   123 SIQQATRNLDRRWRNICAMSMERRLKIE 150
Cdd:smart00150  74 EIEERLEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
157-259 3.71e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 49.25  E-value: 3.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816   157 QKFLDDYSRFEDWLEVSERTAAFPSSSGVLYTVaKEELKKFEAFQRQVHESLTQLELINKQYRRLARENRTDSAcSLRQM 236
Cdd:smart00150   1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESV-EALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAE-EIEER 78

                           90       100
                   ....*....|....*....|...
gi 119120816   237 VHGGNQRWDDLQKRVTSILRRLK 259
Cdd:smart00150  79 LEELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 30-151 1.55e-06

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: 50.14  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816  30 SRVKKLKETLVAVQQLDKnMGSLRTWLAHMESELAKPIVYDScnSEEIQRKLNEQQELQRDIEKHSTGVASVLNLCEVLL 109
Cdd:cd00176   97 ERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKD--LESVEELLKKHKELEEELEAHEPRLKSLNELAEELL 173

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 119120816 110 HDCdacaTDAECDSIQQATRNLDRRWRNICAMSMERRLKIEE 151
Cdd:cd00176  174 EEG----HPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 264-365 6.93e-06

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: 45.77  E-value: 6.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816  264 QREEFETARDSILVWLTEMDLQLTNIEHF-SECDVQAKIKQLKAFQQEISLNHNKIEQIIAQGEQLIEkSEPLDAAVIEE 342
Cdd:pfam00435   2 LLQQFFRDADDLESWIEEKEALLSSEDYGkDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID-EGHYASEEIQE 80

                          90       100
                  ....*....|....*....|...
gi 119120816  343 ELDELRRYCQEVFGRVERYHKKL 365
Cdd:pfam00435  81 RLEELNERWEQLLELAAERKQKL 103
MAP65_ASE1 pfam03999
Microtubule associated protein (MAP65/ASE1 family);
599-813 6.00e-03

Microtubule associated protein (MAP65/ASE1 family);


Pssm-ID: 427641 [Multi-domain]  Cd Length: 477  Bit Score: 40.37  E-value: 6.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816  599 SDLNNIWAWLGETEEEldRLQHLAlstdihTIESHIKKL--KELQKAVDHRKAIILSINLCSSEFTQADSK-ESHDLQDR 675
Cdd:pfam03999   5 DHLHVIWQEIGFSEDK--RLQILS------RLKDHIKEFytDALSEENDKEQRILQSIADLRAEAAILCLYmRNRLLHEE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816  676 LSQMNgrwDRVCSLLEDWRGLLQDALMQCQ-EFHEMSHALLLMLENIDRRKNEI------VPIDSTLDPETLQDHHKQLM 748
Cdd:pfam03999  77 RDPFE---PKKGMSLLQKEKKLDTQLEHLRkEKAPRLAEIKELLEQLQQLCEELgeeplpLLIDPLPSLEELESFRKHLE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816  749 QIKQELLK-----SQLRVASLQDMS-----------RQLLVNAEGSDCLEakekvHVIGNRLKLLLKEVSHHIKDLEKLL 812
Cdd:pfam03999 154 NLRNEKERrleevNELKKQIKLLMEeldlvpgtdfeEDLLCESEDNFCLS-----RENIDKLRKLIKQLEEQKAEREEKI 228


                  .
gi 119120816  813 D 813
Cdd:pfam03999 229 D 229
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
190-356 6.29e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 6.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816 190 AKEELKKFEAFQRQVHESLTQLELINKQYRRLARENRT----DSACSLRQMVHGGNQRWDDLQKRVTSILRRLKHFISQR 265
Cdd:COG4717   83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKleklLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119120816 266 EEFETARDSILVWLTEMDLQLTNIEHFSECDVQAKIKQLKAFQQEISLNHNKIEQIIAQGEQLIEKSEPL-DAAVIEEEL 344
Cdd:COG4717  163 EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLeNELEAAALE 242

                        170
                 ....*....|..
gi 119120816 345 DELRRYCQEVFG 356
Cdd:COG4717  243 ERLKEARLLLLI 254
 
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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