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Conserved domains on  [gi|1720398604|ref|XP_030106040|]
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SEC14 domain and spectrin repeat-containing protein 1 isoform X1 [Mus musculus]

Protein Classification

CRAL_TRIO_2 and SPEC domain-containing protein( domain architecture ID 10617211)

CRAL_TRIO_2 and SPEC domain-containing protein

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 1720398604  33 LCLEQTSMDELSVTLDYLLSIPSEKCKARGFTVIVDGRKSQ------WNVVKTVVLMLQNVVPAEVSLVCVVKPDEFWDK 106
Cdd:pfam13716  12 LPSRPASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVTsenfpsLSFLKKAYDLLPRAFKKNLKAVYVVHPSTFLRT 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1720398604 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 1720398604 273 QLEEIQQKVMQVVNWLEGpgSEQLRAQWGIGDSIRASQALQQKHEEIESQHSEWFAVYVELNQQIAALLNAGDEEDLV-- 350
Cdd:cd00176     1 KLQQFLRDADELEAWLSE--KEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEiq 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398604 351 -ELKSLQQQLSDVCyrqaSQLEFRQNLLQAALE---FHGVAQDLSQQLDGLLGMLCVDVAPADGASIQ---QTLKLLEEK 423
Cdd:cd00176    79 eRLEELNQRWEELR----ELAEERRQRLEEALDlqqFFRDADDLEQWLEEKEAALASEDLGKDLESVEellKKHKELEEE 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720398604 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 1720398604 413 IQQTLKLLEEKLKSVDV-GLQGLREKGQGLLDQISNQASW-----AYGKDVTIENKENVDHIQGVMEDMQLRKQRCEDMV 486
Cdd:cd00176    16 LSEKEELLSSTDYGDDLeSVEALLKKHEALEAELAAHEERvealnELGEQLIEEGHPDAEEIQERLEELNQRWEELRELA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398604 487 DVRRLKMLQMVQLFKCEEDASQAVEWLSELLDALLKThiRLGDDAQETKVLLEKHRKFV-DVAQSTYDYGRQLLQATVVL 565
Cdd:cd00176    96 EERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASE--DLGKDLESVEELLKKHKELEeELEAHEPRLKSLNELAEELL 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720398604 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 1720398604  33 LCLEQTSMDELSVTLDYLLSIPSEKCKARGFTVIVDGRKSQ------WNVVKTVVLMLQNVVPAEVSLVCVVKPDEFWDK 106
Cdd:pfam13716  12 LPSRPASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVTsenfpsLSFLKKAYDLLPRAFKKNLKAVYVVHPSTFLRT 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1720398604 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 1720398604   10 LKKKLAFLSG--GKDRRSGLILTIPL---CLEQTSMDEL----SVTLDYLLSIPSEKCKARGFTVIVD-----GRKSQWN 75
Cdd:smart00516   2 LELLKAYIPGgrGYDKDGRPVLIERAgrfDLKSVTLEELlrylVYVLEKILQEEKKTGGIEGFTVIFDlkglsMSNPDLS 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720398604   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 1720398604 273 QLEEIQQKVMQVVNWLEGpgSEQLRAQWGIGDSIRASQALQQKHEEIESQHSEWFAVYVELNQQIAALLNAGDEEDLV-- 350
Cdd:cd00176     1 KLQQFLRDADELEAWLSE--KEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEiq 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398604 351 -ELKSLQQQLSDVCyrqaSQLEFRQNLLQAALE---FHGVAQDLSQQLDGLLGMLCVDVAPADGASIQ---QTLKLLEEK 423
Cdd:cd00176    79 eRLEELNQRWEELR----ELAEERRQRLEEALDlqqFFRDADDLEQWLEEKEAALASEDLGKDLESVEellKKHKELEEE 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720398604 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 1720398604 413 IQQTLKLLEEKLKSVDV-GLQGLREKGQGLLDQISNQASW-----AYGKDVTIENKENVDHIQGVMEDMQLRKQRCEDMV 486
Cdd:cd00176    16 LSEKEELLSSTDYGDDLeSVEALLKKHEALEAELAAHEERvealnELGEQLIEEGHPDAEEIQERLEELNQRWEELRELA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398604 487 DVRRLKMLQMVQLFKCEEDASQAVEWLSELLDALLKThiRLGDDAQETKVLLEKHRKFV-DVAQSTYDYGRQLLQATVVL 565
Cdd:cd00176    96 EERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASE--DLGKDLESVEELLKKHKELEeELEAHEPRLKSLNELAEELL 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720398604 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 1720398604   7 LPILKKKL--AFLSGGKDRRSGLILTIPLCL---EQTSMDELSVTLDYLLSIPSEKCKAR--GFTVIVDGRKSQWN---- 75
Cdd:cd00170     1 LEELLELLggIGYLGGRDKEGRPVLVFRAGWdppKLLDLEELLRYLVYLLEKALRELEEQveGFVVIIDLKGFSLSnlsd 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720398604  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 1720398604  33 LCLEQTSMDELSVTLDYLLSIPSEKCKARGFTVIVDGRKSQ------WNVVKTVVLMLQNVVPAEVSLVCVVKPDEFWDK 106
Cdd:pfam13716  12 LPSRPASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVTsenfpsLSFLKKAYDLLPRAFKKNLKAVYVVHPSTFLRT 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1720398604 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 1720398604   10 LKKKLAFLSG--GKDRRSGLILTIPL---CLEQTSMDEL----SVTLDYLLSIPSEKCKARGFTVIVD-----GRKSQWN 75
Cdd:smart00516   2 LELLKAYIPGgrGYDKDGRPVLIERAgrfDLKSVTLEELlrylVYVLEKILQEEKKTGGIEGFTVIFDlkglsMSNPDLS 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720398604   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 1720398604 273 QLEEIQQKVMQVVNWLEGpgSEQLRAQWGIGDSIRASQALQQKHEEIESQHSEWFAVYVELNQQIAALLNAGDEEDLV-- 350
Cdd:cd00176     1 KLQQFLRDADELEAWLSE--KEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEiq 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398604 351 -ELKSLQQQLSDVCyrqaSQLEFRQNLLQAALE---FHGVAQDLSQQLDGLLGMLCVDVAPADGASIQ---QTLKLLEEK 423
Cdd:cd00176    79 eRLEELNQRWEELR----ELAEERRQRLEEALDlqqFFRDADDLEQWLEEKEAALASEDLGKDLESVEellKKHKELEEE 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720398604 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 1720398604 413 IQQTLKLLEEKLKSVDV-GLQGLREKGQGLLDQISNQASW-----AYGKDVTIENKENVDHIQGVMEDMQLRKQRCEDMV 486
Cdd:cd00176    16 LSEKEELLSSTDYGDDLeSVEALLKKHEALEAELAAHEERvealnELGEQLIEEGHPDAEEIQERLEELNQRWEELRELA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398604 487 DVRRLKMLQMVQLFKCEEDASQAVEWLSELLDALLKThiRLGDDAQETKVLLEKHRKFV-DVAQSTYDYGRQLLQATVVL 565
Cdd:cd00176    96 EERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASE--DLGKDLESVEELLKKHKELEeELEAHEPRLKSLNELAEELL 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720398604 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 1720398604   7 LPILKKKL--AFLSGGKDRRSGLILTIPLCL---EQTSMDELSVTLDYLLSIPSEKCKAR--GFTVIVDGRKSQWN---- 75
Cdd:cd00170     1 LEELLELLggIGYLGGRDKEGRPVLVFRAGWdppKLLDLEELLRYLVYLLEKALRELEEQveGFVVIIDLKGFSLSnlsd 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720398604  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 1720398604 498 QLFKCEEDASQAVEWLSELLDALLKTHirLGDDAQETKVLLEKHRKFVDVAQSTYDYGRQLLQATVVLCQSLRCTSRSSG 577
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTD--YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720398604 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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