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Conserved domains on  [gi|755499248|ref|XP_011237749|]
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SEC14 domain and spectrin repeat-containing protein 1 isoform X2 [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 ...
 1-71 5.52e-06

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: 46.17  E-value: 5.52e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755499248    1 MLQNVVPAEVSLVCVVKPDEFWDKKV-THFCFWKEKDRLGFEVILVSANKLTRYIEPCQLTEDFGGSLTYDH 71
Cdd:pfam13716  68 LLPRAFKKNLKAVYVVHPSTFLRTFLkTLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLPTELPGVLSYDE 139
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 191-396 1.56e-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: 40.51  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755499248 191 QLEEIQQKVMQVVNWLEGpgSEQLRAQWGIGDSIRASQALQQKHEEIESQHSEWFAVYVELNQQIAALLNAGDEEDLV-- 268
Cdd:cd00176    1 KLQQFLRDADELEAWLSE--KEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEiq 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755499248 269 -ELKSLQQQLSDVCyrqaSQLEFRQNLLQAALE---FHGVAQDLSQQLDGLLGMLCVDVAPADGASIQ---QTLKLLEEK 341
Cdd:cd00176   79 eRLEELNQRWEELR----ELAEERRQRLEEALDlqqFFRDADDLEQWLEEKEAALASEDLGKDLESVEellKKHKELEEE 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755499248 342 LKSVDVGLQGLREKGQGLLDQISNQASwAYGKDVTIENKENVDHIQGVMEDMQLR 396
Cdd:cd00176  155 LEAHEPRLKSLNELAEELLEEGHPDAD-EEIEEKLEELNERWEELLELAEERQKK 208
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 331-523 4.15e-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: 38.97  E-value: 4.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755499248 331 IQQTLKLLEEKLKSVDV-GLQGLREKGQGLLDQISNQASW-----AYGKDVTIENKENVDHIQGVMEDMQLRKQRCEDMV 404
Cdd:cd00176   16 LSEKEELLSSTDYGDDLeSVEALLKKHEALEAELAAHEERvealnELGEQLIEEGHPDAEEIQERLEELNQRWEELRELA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755499248 405 DVRRLKMLQMVQLFKCEEDASQAVEWLSELLDALLKThiRLGDDAQETKVLLEKHRKFV-DVAQSTYDYGRQLLQATVVL 483
Cdd:cd00176   96 EERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASE--DLGKDLESVEELLKKHKELEeELEAHEPRLKSLNELAEELL 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 755499248 484 CQSLRCTSRSSGDTLPRLNRVWKQFTVASEERVHRLEMAI 523
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 ...
 1-71 5.52e-06

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: 46.17  E-value: 5.52e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755499248    1 MLQNVVPAEVSLVCVVKPDEFWDKKV-THFCFWKEKDRLGFEVILVSANKLTRYIEPCQLTEDFGGSLTYDH 71
Cdd:pfam13716  68 LLPRAFKKNLKAVYVVHPSTFLRTFLkTLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLPTELPGVLSYDE 139
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 191-396 1.56e-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: 40.51  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755499248 191 QLEEIQQKVMQVVNWLEGpgSEQLRAQWGIGDSIRASQALQQKHEEIESQHSEWFAVYVELNQQIAALLNAGDEEDLV-- 268
Cdd:cd00176    1 KLQQFLRDADELEAWLSE--KEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEiq 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755499248 269 -ELKSLQQQLSDVCyrqaSQLEFRQNLLQAALE---FHGVAQDLSQQLDGLLGMLCVDVAPADGASIQ---QTLKLLEEK 341
Cdd:cd00176   79 eRLEELNQRWEELR----ELAEERRQRLEEALDlqqFFRDADDLEQWLEEKEAALASEDLGKDLESVEellKKHKELEEE 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755499248 342 LKSVDVGLQGLREKGQGLLDQISNQASwAYGKDVTIENKENVDHIQGVMEDMQLR 396
Cdd:cd00176  155 LEAHEPRLKSLNELAEELLEEGHPDAD-EEIEEKLEELNERWEELLELAEERQKK 208
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 331-523 4.15e-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: 38.97  E-value: 4.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755499248 331 IQQTLKLLEEKLKSVDV-GLQGLREKGQGLLDQISNQASW-----AYGKDVTIENKENVDHIQGVMEDMQLRKQRCEDMV 404
Cdd:cd00176   16 LSEKEELLSSTDYGDDLeSVEALLKKHEALEAELAAHEERvealnELGEQLIEEGHPDAEEIQERLEELNQRWEELRELA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755499248 405 DVRRLKMLQMVQLFKCEEDASQAVEWLSELLDALLKThiRLGDDAQETKVLLEKHRKFV-DVAQSTYDYGRQLLQATVVL 483
Cdd:cd00176   96 EERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASE--DLGKDLESVEELLKKHKELEeELEAHEPRLKSLNELAEELL 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 755499248 484 CQSLRCTSRSSGDTLPRLNRVWKQFTVASEERVHRLEMAI 523
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 ...
 1-71 5.52e-06

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: 46.17  E-value: 5.52e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755499248    1 MLQNVVPAEVSLVCVVKPDEFWDKKV-THFCFWKEKDRLGFEVILVSANKLTRYIEPCQLTEDFGGSLTYDH 71
Cdd:pfam13716  68 LLPRAFKKNLKAVYVVHPSTFLRTFLkTLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLPTELPGVLSYDE 139
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 191-396 1.56e-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: 40.51  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755499248 191 QLEEIQQKVMQVVNWLEGpgSEQLRAQWGIGDSIRASQALQQKHEEIESQHSEWFAVYVELNQQIAALLNAGDEEDLV-- 268
Cdd:cd00176    1 KLQQFLRDADELEAWLSE--KEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEiq 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755499248 269 -ELKSLQQQLSDVCyrqaSQLEFRQNLLQAALE---FHGVAQDLSQQLDGLLGMLCVDVAPADGASIQ---QTLKLLEEK 341
Cdd:cd00176   79 eRLEELNQRWEELR----ELAEERRQRLEEALDlqqFFRDADDLEQWLEEKEAALASEDLGKDLESVEellKKHKELEEE 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755499248 342 LKSVDVGLQGLREKGQGLLDQISNQASwAYGKDVTIENKENVDHIQGVMEDMQLR 396
Cdd:cd00176  155 LEAHEPRLKSLNELAEELLEEGHPDAD-EEIEEKLEELNERWEELLELAEERQKK 208
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 331-523 4.15e-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: 38.97  E-value: 4.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755499248 331 IQQTLKLLEEKLKSVDV-GLQGLREKGQGLLDQISNQASW-----AYGKDVTIENKENVDHIQGVMEDMQLRKQRCEDMV 404
Cdd:cd00176   16 LSEKEELLSSTDYGDDLeSVEALLKKHEALEAELAAHEERvealnELGEQLIEEGHPDAEEIQERLEELNQRWEELRELA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755499248 405 DVRRLKMLQMVQLFKCEEDASQAVEWLSELLDALLKThiRLGDDAQETKVLLEKHRKFV-DVAQSTYDYGRQLLQATVVL 483
Cdd:cd00176   96 EERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASE--DLGKDLESVEELLKKHKELEeELEAHEPRLKSLNELAEELL 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 755499248 484 CQSLRCTSRSSGDTLPRLNRVWKQFTVASEERVHRLEMAI 523
Cdd:cd00176  174 EEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 416-563 6.92e-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: 38.20  E-value: 6.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755499248 416 QLFKCEEDASQAVEWLSELLDALLKTHirLGDDAQETKVLLEKHRKFVDVAQSTYDYGRQLLQATVVLCQSLRCTSRSSG 495
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTD--YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755499248 496 DTLPRLNRVWKQFTVASEERVHRLEMAIA---FHSNAEKILQDCPEEPEAMNDEEQFEEIEAIgKSLLDRL 563
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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