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Conserved domains on  [gi|30425210|ref|NP_780674|]
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SEC14 domain and spectrin repeat-containing protein 1 [Mus musculus]

Protein Classification

CRAL-TRIO domain-containing protein( domain architecture ID 10617211)

CRAL-TRIO domain-containing protein act as a lipid binding protein which may bind small lipophilic molecules such as retinal, inositol, and vitamin E

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 33-153 1.48e-16

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


:

Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 76.98  E-value: 1.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30425210    33 LCLEQTSMDELSVTLDYLLSIPSEKCKARGFTVIVDGRKSQ------WNVVKTVVLMLQNVVPAEVSLVCVVKPDEFWDK 106
Cdd:pfam13716  12 LPSRPASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVTsenfpsLSFLKKAYDLLPRAFKKNLKAVYVVHPSTFLRT 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 30425210   107 KV-THFCFWKEKDRLGFEVILVSANKLTRYIEPCQLTEDFGGSLTYDH 153
Cdd:pfam13716  92 FLkTLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLPTELPGVLSYDE 139
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 273-478 3.43e-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: 42.43  E-value: 3.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30425210 273 QLEEIQQKVMQVVNWLEGpgSEQLRAQWGIGDSIRASQALQQKHEEIESQHSEWFAVYVELNQQIAALLNAGDEEDLV-- 350
Cdd:cd00176   1 KLQQFLRDADELEAWLSE--KEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEiq 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30425210 351 -ELKSLQQQLSDVCyrqaSQLEFRQNLLQAALE---FHGVAQDLSQQLDGLLGMLCVDVAPADGASIQ---QTLKLLEEK 423
Cdd:cd00176  79 eRLEELNQRWEELR----ELAEERRQRLEEALDlqqFFRDADDLEQWLEEKEAALASEDLGKDLESVEellKKHKELEEE 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 30425210 424 LKSVDVGLQGLREKGQGLLDQISNQASwAYGKDVTIENKENVDHIQGVMEDMQLR 478
Cdd:cd00176 155 LEAHEPRLKSLNELAEELLEEGHPDAD-EEIEEKLEELNERWEELLELAEERQKK 208
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 413-605 1.30e-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


The actual alignment was detected with superfamily member cd00176:

Pssm-ID: 413338 [Multi-domain]  Cd Length: 213  Bit Score: 40.89  E-value: 1.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30425210 413 IQQTLKLLEEKLKSVDV-GLQGLREKGQGLLDQISNQASW-----AYGKDVTIENKENVDHIQGVMEDMQLRKQRCEDMV 486
Cdd:cd00176  16 LSEKEELLSSTDYGDDLeSVEALLKKHEALEAELAAHEERvealnELGEQLIEEGHPDAEEIQERLEELNQRWEELRELA 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30425210 487 DVRRLKMLQMVQLFKCEEDASQAVEWLSELLDALLKThiRLGDDAQETKVLLEKHRKFV-DVAQSTYDYGRQLLQATVVL 565
Cdd:cd00176  96 EERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASE--DLGKDLESVEELLKKHKELEeELEAHEPRLKSLNELAEELL 173

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 30425210 566 CQSLRCTSRSSGDTLPRLNRVWKQFTVASEERVHRLEMAI 605
Cdd:cd00176 174 EEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
 
Name Accession Description Interval E-value
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 33-153 1.48e-16

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 76.98  E-value: 1.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30425210    33 LCLEQTSMDELSVTLDYLLSIPSEKCKARGFTVIVDGRKSQ------WNVVKTVVLMLQNVVPAEVSLVCVVKPDEFWDK 106
Cdd:pfam13716  12 LPSRPASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVTsenfpsLSFLKKAYDLLPRAFKKNLKAVYVVHPSTFLRT 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 30425210   107 KV-THFCFWKEKDRLGFEVILVSANKLTRYIEPCQLTEDFGGSLTYDH 153
Cdd:pfam13716  92 FLkTLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLPTELPGVLSYDE 139
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 10-149 1.83e-07

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 51.15  E-value: 1.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30425210     10 LKKKLAFLSG--GKDRRSGLILTIPL---CLEQTSMDEL----SVTLDYLLSIPSEKCKARGFTVIVD-----GRKSQWN 75
Cdd:smart00516   2 LELLKAYIPGgrGYDKDGRPVLIERAgrfDLKSVTLEELlrylVYVLEKILQEEKKTGGIEGFTVIFDlkglsMSNPDLS 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30425210     76 VVKTVVLMLQNVVPAEVSLVCVVKPDEFWDK--KVTHFcFWKEKDRLGFEVI-LVSANKLTRYIEPCQLTEDFGGSL 149
Cdd:smart00516  82 VLRKILKILQDHYPERLGKVYIINPPWFFRVlwKIIKP-FLDEKTREKIRFVgNDSKEELLEYIDKEQLPEELGGTL 157
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 273-478 3.43e-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: 3.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30425210 273 QLEEIQQKVMQVVNWLEGpgSEQLRAQWGIGDSIRASQALQQKHEEIESQHSEWFAVYVELNQQIAALLNAGDEEDLV-- 350
Cdd:cd00176   1 KLQQFLRDADELEAWLSE--KEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEiq 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30425210 351 -ELKSLQQQLSDVCyrqaSQLEFRQNLLQAALE---FHGVAQDLSQQLDGLLGMLCVDVAPADGASIQ---QTLKLLEEK 423
Cdd:cd00176  79 eRLEELNQRWEELR----ELAEERRQRLEEALDlqqFFRDADDLEQWLEEKEAALASEDLGKDLESVEellKKHKELEEE 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 30425210 424 LKSVDVGLQGLREKGQGLLDQISNQASwAYGKDVTIENKENVDHIQGVMEDMQLR 478
Cdd:cd00176 155 LEAHEPRLKSLNELAEELLEEGHPDAD-EEIEEKLEELNERWEELLELAEERQKK 208
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 413-605 1.30e-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: 40.89  E-value: 1.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30425210 413 IQQTLKLLEEKLKSVDV-GLQGLREKGQGLLDQISNQASW-----AYGKDVTIENKENVDHIQGVMEDMQLRKQRCEDMV 486
Cdd:cd00176  16 LSEKEELLSSTDYGDDLeSVEALLKKHEALEAELAAHEERvealnELGEQLIEEGHPDAEEIQERLEELNQRWEELRELA 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30425210 487 DVRRLKMLQMVQLFKCEEDASQAVEWLSELLDALLKThiRLGDDAQETKVLLEKHRKFV-DVAQSTYDYGRQLLQATVVL 565
Cdd:cd00176  96 EERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASE--DLGKDLESVEELLKKHKELEeELEAHEPRLKSLNELAEELL 173

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 30425210 566 CQSLRCTSRSSGDTLPRLNRVWKQFTVASEERVHRLEMAI 605
Cdd:cd00176 174 EEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 7-148 1.35e-03

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 40.01  E-value: 1.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30425210   7 LPILKKKL--AFLSGGKDRRSGLILTIPLCL---EQTSMDELSVTLDYLLSIPSEKCKAR--GFTVIVDGRKSQWN---- 75
Cdd:cd00170   1 LEELLELLggIGYLGGRDKEGRPVLVFRAGWdppKLLDLEELLRYLVYLLEKALRELEEQveGFVVIIDLKGFSLSnlsd 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30425210  76 --VVKTVVLMLQNVVPAEVSLVCVVKPDEFWDKKVTHFCFW-KEKDRLGFEVILVSANKLTRYIEPCQLTEDFGGS 148
Cdd:cd00170  81 lsLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFlSEKTRKKIVFLGSDLEELLEYIDPDQLPKELGGT 156
 
Name Accession Description Interval E-value
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 33-153 1.48e-16

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 76.98  E-value: 1.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30425210    33 LCLEQTSMDELSVTLDYLLSIPSEKCKARGFTVIVDGRKSQ------WNVVKTVVLMLQNVVPAEVSLVCVVKPDEFWDK 106
Cdd:pfam13716  12 LPSRPASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVTsenfpsLSFLKKAYDLLPRAFKKNLKAVYVVHPSTFLRT 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 30425210   107 KV-THFCFWKEKDRLGFEVILVSANKLTRYIEPCQLTEDFGGSLTYDH 153
Cdd:pfam13716  92 FLkTLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLPTELPGVLSYDE 139
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 10-149 1.83e-07

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 51.15  E-value: 1.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30425210     10 LKKKLAFLSG--GKDRRSGLILTIPL---CLEQTSMDEL----SVTLDYLLSIPSEKCKARGFTVIVD-----GRKSQWN 75
Cdd:smart00516   2 LELLKAYIPGgrGYDKDGRPVLIERAgrfDLKSVTLEELlrylVYVLEKILQEEKKTGGIEGFTVIFDlkglsMSNPDLS 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30425210     76 VVKTVVLMLQNVVPAEVSLVCVVKPDEFWDK--KVTHFcFWKEKDRLGFEVI-LVSANKLTRYIEPCQLTEDFGGSL 149
Cdd:smart00516  82 VLRKILKILQDHYPERLGKVYIINPPWFFRVlwKIIKP-FLDEKTREKIRFVgNDSKEELLEYIDKEQLPEELGGTL 157
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 273-478 3.43e-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: 3.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30425210 273 QLEEIQQKVMQVVNWLEGpgSEQLRAQWGIGDSIRASQALQQKHEEIESQHSEWFAVYVELNQQIAALLNAGDEEDLV-- 350
Cdd:cd00176   1 KLQQFLRDADELEAWLSE--KEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEiq 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30425210 351 -ELKSLQQQLSDVCyrqaSQLEFRQNLLQAALE---FHGVAQDLSQQLDGLLGMLCVDVAPADGASIQ---QTLKLLEEK 423
Cdd:cd00176  79 eRLEELNQRWEELR----ELAEERRQRLEEALDlqqFFRDADDLEQWLEEKEAALASEDLGKDLESVEellKKHKELEEE 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 30425210 424 LKSVDVGLQGLREKGQGLLDQISNQASwAYGKDVTIENKENVDHIQGVMEDMQLR 478
Cdd:cd00176 155 LEAHEPRLKSLNELAEELLEEGHPDAD-EEIEEKLEELNERWEELLELAEERQKK 208
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 413-605 1.30e-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: 40.89  E-value: 1.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30425210 413 IQQTLKLLEEKLKSVDV-GLQGLREKGQGLLDQISNQASW-----AYGKDVTIENKENVDHIQGVMEDMQLRKQRCEDMV 486
Cdd:cd00176  16 LSEKEELLSSTDYGDDLeSVEALLKKHEALEAELAAHEERvealnELGEQLIEEGHPDAEEIQERLEELNQRWEELRELA 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30425210 487 DVRRLKMLQMVQLFKCEEDASQAVEWLSELLDALLKThiRLGDDAQETKVLLEKHRKFV-DVAQSTYDYGRQLLQATVVL 565
Cdd:cd00176  96 EERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASE--DLGKDLESVEELLKKHKELEeELEAHEPRLKSLNELAEELL 173

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 30425210 566 CQSLRCTSRSSGDTLPRLNRVWKQFTVASEERVHRLEMAI 605
Cdd:cd00176 174 EEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 7-148 1.35e-03

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 40.01  E-value: 1.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30425210   7 LPILKKKL--AFLSGGKDRRSGLILTIPLCL---EQTSMDELSVTLDYLLSIPSEKCKAR--GFTVIVDGRKSQWN---- 75
Cdd:cd00170   1 LEELLELLggIGYLGGRDKEGRPVLVFRAGWdppKLLDLEELLRYLVYLLEKALRELEEQveGFVVIIDLKGFSLSnlsd 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30425210  76 --VVKTVVLMLQNVVPAEVSLVCVVKPDEFWDKKVTHFCFW-KEKDRLGFEVILVSANKLTRYIEPCQLTEDFGGS 148
Cdd:cd00170  81 lsLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFlSEKTRKKIVFLGSDLEELLEYIDPDQLPKELGGT 156
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 498-645 2.39e-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: 40.12  E-value: 2.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30425210 498 QLFKCEEDASQAVEWLSELLDALLKTHirLGDDAQETKVLLEKHRKFVDVAQSTYDYGRQLLQATVVLCQSLRCTSRSSG 577
Cdd:cd00176   1 KLQQFLRDADELEAWLSEKEELLSSTD--YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30425210 578 DTLPRLNRVWKQFTVASEERVHRLEMAIA---FHSNAEKILQDCPEEPEAMNDEEQFEEIEAIgKSLLDRL 645
Cdd:cd00176  79 ERLEELNQRWEELRELAEERRQRLEEALDlqqFFRDADDLEQWLEEKEAALASEDLGKDLESV-EELLKKH 148
 
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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