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Conserved domains on  [gi|219282782|ref|NP_001136440|]
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uncharacterized protein LOC271278 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GAS2 super family cl02524
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ...
 675-703 1.33e-09

Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members and Gas2 family members. The GAR domain comprises around 57 amino acids and has been shown to bind to microtubules.


The actual alignment was detected with superfamily member smart00243:

Pssm-ID: 470602  Cd Length: 73  Bit Score: 55.15  E-value: 1.33e-09
                           10        20
                   ....*....|....*....|....*....
gi 219282782   675 RGAMMVRVGGGWAALDEFLVKNDPVRAKG 703
Cdd:smart00243  45 RSTVMVRVGGGWETLDEYLLKHDPCRAKG 73
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 157-267 4.26e-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: 4.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219282782 157 ELCTQWHRLVQQAETRWRLLEQLVPAAQSFETACKALLvRLSSSEQLLAELWLG--PKGLEESLPYLQEVCEGVVASTRD 234
Cdd:cd00176   83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQ-WLEEKEAALASEDLGkdLESVEELLKKHKELEEELEAHEPR 161

                         90       100       110
                 ....*....|....*....|....*....|...
gi 219282782 235 LERVLQTGQRLAELLSSDQARLVRQQLNQFQER 267
Cdd:cd00176  162 LKSLNELAEELLEEGHPDADEEIEEKLEELNER 194
 
Name Accession Description Interval E-value
GAS2 smart00243
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
 675-703 1.33e-09

Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain


Pssm-ID: 128539  Cd Length: 73  Bit Score: 55.15  E-value: 1.33e-09
                           10        20
                   ....*....|....*....|....*....
gi 219282782   675 RGAMMVRVGGGWAALDEFLVKNDPVRAKG 703
Cdd:smart00243  45 RSTVMVRVGGGWETLDEYLLKHDPCRAKG 73
GAS2 pfam02187
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ...
 675-701 4.34e-09

Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members and Gas2 family members. The GAR domain comprises around 57 amino acids and has been shown to bind to microtubules.


Pssm-ID: 460480  Cd Length: 69  Bit Score: 53.37  E-value: 4.34e-09
                          10        20
                  ....*....|....*....|....*..
gi 219282782  675 RGAMMVRVGGGWAALDEFLVKNDPVRA 701
Cdd:pfam02187  43 RSHVMVRVGGGWDTLEEYLLKHDPCRA 69
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 157-267 4.26e-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: 4.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219282782 157 ELCTQWHRLVQQAETRWRLLEQLVPAAQSFETACKALLvRLSSSEQLLAELWLG--PKGLEESLPYLQEVCEGVVASTRD 234
Cdd:cd00176   83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQ-WLEEKEAALASEDLGkdLESVEELLKKHKELEEELEAHEPR 161

                         90       100       110
                 ....*....|....*....|....*....|...
gi 219282782 235 LERVLQTGQRLAELLSSDQARLVRQQLNQFQER 267
Cdd:cd00176  162 LKSLNELAEELLEEGHPDADEEIEEKLEELNER 194
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 156-349 6.78e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 6.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219282782 156 SELCTQWHRLVQQAETRWRLLEQLVPAAQSFETAcKALLVRLSSSEqllaelwlgPKGLEESLPYLQEVCEGVVASTRDL 235
Cdd:COG4942   86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQ-PPLALLLSPED---------FLDAVRRLQYLKYLAPARREQAEEL 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219282782 236 ERVLQTGQRLAELLSSDQARLVRQQLNQFQERVKLTESQAtcARQKLLfaqrtesskplppAGLEAQLelegsASTPPQL 315
Cdd:COG4942  156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKA--ERQKLL-------------ARLEKEL-----AELAAEL 215

                        170       180       190
                 ....*....|....*....|....*....|....
gi 219282782 316 KDLKQLSVQLVQLAERLEQLAQWAETSSQVAAPA 349
Cdd:COG4942  216 AELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
 
Name Accession Description Interval E-value
GAS2 smart00243
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
 675-703 1.33e-09

Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain


Pssm-ID: 128539  Cd Length: 73  Bit Score: 55.15  E-value: 1.33e-09
                           10        20
                   ....*....|....*....|....*....
gi 219282782   675 RGAMMVRVGGGWAALDEFLVKNDPVRAKG 703
Cdd:smart00243  45 RSTVMVRVGGGWETLDEYLLKHDPCRAKG 73
GAS2 pfam02187
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ...
 675-701 4.34e-09

Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members and Gas2 family members. The GAR domain comprises around 57 amino acids and has been shown to bind to microtubules.


Pssm-ID: 460480  Cd Length: 69  Bit Score: 53.37  E-value: 4.34e-09
                          10        20
                  ....*....|....*....|....*..
gi 219282782  675 RGAMMVRVGGGWAALDEFLVKNDPVRA 701
Cdd:pfam02187  43 RSHVMVRVGGGWDTLEEYLLKHDPCRA 69
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 157-267 4.26e-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: 4.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219282782 157 ELCTQWHRLVQQAETRWRLLEQLVPAAQSFETACKALLvRLSSSEQLLAELWLG--PKGLEESLPYLQEVCEGVVASTRD 234
Cdd:cd00176   83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQ-WLEEKEAALASEDLGkdLESVEELLKKHKELEEELEAHEPR 161

                         90       100       110
                 ....*....|....*....|....*....|...
gi 219282782 235 LERVLQTGQRLAELLSSDQARLVRQQLNQFQER 267
Cdd:cd00176  162 LKSLNELAEELLEEGHPDADEEIEEKLEELNER 194
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 156-349 6.78e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 6.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219282782 156 SELCTQWHRLVQQAETRWRLLEQLVPAAQSFETAcKALLVRLSSSEqllaelwlgPKGLEESLPYLQEVCEGVVASTRDL 235
Cdd:COG4942   86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQ-PPLALLLSPED---------FLDAVRRLQYLKYLAPARREQAEEL 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219282782 236 ERVLQTGQRLAELLSSDQARLVRQQLNQFQERVKLTESQAtcARQKLLfaqrtesskplppAGLEAQLelegsASTPPQL 315
Cdd:COG4942  156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKA--ERQKLL-------------ARLEKEL-----AELAAEL 215

                        170       180       190
                 ....*....|....*....|....*....|....
gi 219282782 316 KDLKQLSVQLVQLAERLEQLAQWAETSSQVAAPA 349
Cdd:COG4942  216 AELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
 
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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