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Conserved domains on  [gi|1018191487|ref|NP_001309823|]
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actin-binding LIM protein 1 isoform o [Homo sapiens]

Protein Classification

actin-binding LIM protein( domain architecture ID 10912200)

actin-binding LIM protein (abLIM) may act as a scaffold protein for signaling modules of the actin cytoskeleton

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AbLIM_anchor pfam16182
Putative adherens-junction anchoring region of AbLIM; AbLIM_anchor is a domain lying between ...
 33-365 1.64e-152

Putative adherens-junction anchoring region of AbLIM; AbLIM_anchor is a domain lying between the LIM actin-binding and the vilin-head domain of actin-binding LIM proteins. It is likely that this domain is involved in anchoring abLIMs to circumferential actin bundles in specific cell types.


:

Pssm-ID: 465046 [Multi-domain]  Cd Length: 319  Bit Score: 434.21  E-value: 1.64e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191487  33 TRTSSESIYSRPGSSIPGSPGHTIYAKVDNEILDYKDLAAIPKVKAIYDIERPDLITYEPFYTSGYDDKQERQSLGESPR 112
Cdd:pfam16182   1 TRTSSESIISPPGSSISGSPSRVIYAKLDNEILDYKDLAALPKVKAIYDIERPDLISYEPYVSYSSDDRLERQSYGESLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191487 113 TLSptPSAEGYQDVRDRMIHRSTSQGSINSPVYSRHSYTPTTSRSPQHFHRPGNEpsSGRNSPLPYRPDSRPLTPTYAQA 192
Cdd:pfam16182  81 TLS--PSSEDSYDSRELRQRRSSSPGSIGSPTYSRHGYTPTLSRSPQHFHRPGSE--SGRSSPSLSQPSDRKSPPTYVQA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191487 193 PKHFHVPDQGI--NIYRKPPIYKQHGP--------DMKRRSSGR--EEDDEELLRRRQLQEEQLMKLNSGLGQLILKEEM 260
Cdd:pfam16182 157 PKHFHVPDTGVkdNIYRKPPIYKQHGTsasasqssEDIIHSSRFpaSGGEEEGWNRRLLQEEELSKIQSGLGKLILKEEM 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191487 261 EKES-RERSSLLASRYDSPINSA-SHIPSSKTASLPGYGRNGLHRPVSTDFAQYNSYGDVSGGvrdyqtlpdghmpamrm 338
Cdd:pfam16182 237 EARSgSERRDPWSSPRSSPSGSSgSDSPYSKSASLPGYGRNGLHRPQSADFFQYGSDGDVSWG----------------- 299

                         330       340
                  ....*....|....*....|....*..
gi 1018191487 339 drgvsmpNMLEPKIFPYEMLMVTNRGR 365
Cdd:pfam16182 300 -------GMREYKIYPYEMLAVTNRGR 319
VHP smart00153
Villin headpiece domain;
380-415 1.85e-15

Villin headpiece domain;


:

Pssm-ID: 128458  Cd Length: 36  Bit Score: 69.66  E-value: 1.85e-15
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1018191487  380 HLAPEVFREIFGMSIQEFDRLPLWRRNDMKKKAKLF 415
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
LIM super family cl02475
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
 1-24 1.98e-12

LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid).


The actual alignment was detected with superfamily member cd09330:

Pssm-ID: 413332  Cd Length: 56  Bit Score: 61.61  E-value: 1.98e-12
                          10        20
                  ....*....|....*....|....
gi 1018191487   1 MFTEGEEMYLQGSTVWHPDCKQST 24
Cdd:cd09330    33 MFGEGEEMYLQGSEIWHPDCRQAA 56
 
Name Accession Description Interval E-value
AbLIM_anchor pfam16182
Putative adherens-junction anchoring region of AbLIM; AbLIM_anchor is a domain lying between ...
 33-365 1.64e-152

Putative adherens-junction anchoring region of AbLIM; AbLIM_anchor is a domain lying between the LIM actin-binding and the vilin-head domain of actin-binding LIM proteins. It is likely that this domain is involved in anchoring abLIMs to circumferential actin bundles in specific cell types.


Pssm-ID: 465046 [Multi-domain]  Cd Length: 319  Bit Score: 434.21  E-value: 1.64e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191487  33 TRTSSESIYSRPGSSIPGSPGHTIYAKVDNEILDYKDLAAIPKVKAIYDIERPDLITYEPFYTSGYDDKQERQSLGESPR 112
Cdd:pfam16182   1 TRTSSESIISPPGSSISGSPSRVIYAKLDNEILDYKDLAALPKVKAIYDIERPDLISYEPYVSYSSDDRLERQSYGESLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191487 113 TLSptPSAEGYQDVRDRMIHRSTSQGSINSPVYSRHSYTPTTSRSPQHFHRPGNEpsSGRNSPLPYRPDSRPLTPTYAQA 192
Cdd:pfam16182  81 TLS--PSSEDSYDSRELRQRRSSSPGSIGSPTYSRHGYTPTLSRSPQHFHRPGSE--SGRSSPSLSQPSDRKSPPTYVQA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191487 193 PKHFHVPDQGI--NIYRKPPIYKQHGP--------DMKRRSSGR--EEDDEELLRRRQLQEEQLMKLNSGLGQLILKEEM 260
Cdd:pfam16182 157 PKHFHVPDTGVkdNIYRKPPIYKQHGTsasasqssEDIIHSSRFpaSGGEEEGWNRRLLQEEELSKIQSGLGKLILKEEM 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191487 261 EKES-RERSSLLASRYDSPINSA-SHIPSSKTASLPGYGRNGLHRPVSTDFAQYNSYGDVSGGvrdyqtlpdghmpamrm 338
Cdd:pfam16182 237 EARSgSERRDPWSSPRSSPSGSSgSDSPYSKSASLPGYGRNGLHRPQSADFFQYGSDGDVSWG----------------- 299

                         330       340
                  ....*....|....*....|....*..
gi 1018191487 339 drgvsmpNMLEPKIFPYEMLMVTNRGR 365
Cdd:pfam16182 300 -------GMREYKIYPYEMLAVTNRGR 319
VHP smart00153
Villin headpiece domain;
380-415 1.85e-15

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 69.66  E-value: 1.85e-15
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1018191487  380 HLAPEVFREIFGMSIQEFDRLPLWRRNDMKKKAKLF 415
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
VHP pfam02209
Villin headpiece domain;
380-415 1.62e-13

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 64.32  E-value: 1.62e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1018191487 380 HLAPEVFREIFGMSIQEFDRLPLWRRNDMKKKAKLF 415
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
LIM4_abLIM cd09330
The fourth LIM domain of actin binding LIM (abLIM) proteins; The fourth LIM domain of actin ...
 1-24 1.98e-12

The fourth LIM domain of actin binding LIM (abLIM) proteins; The fourth LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188716  Cd Length: 56  Bit Score: 61.61  E-value: 1.98e-12
                          10        20
                  ....*....|....*....|....
gi 1018191487   1 MFTEGEEMYLQGSTVWHPDCKQST 24
Cdd:cd09330    33 MFGEGEEMYLQGSEIWHPDCRQAA 56
 
Name Accession Description Interval E-value
AbLIM_anchor pfam16182
Putative adherens-junction anchoring region of AbLIM; AbLIM_anchor is a domain lying between ...
 33-365 1.64e-152

Putative adherens-junction anchoring region of AbLIM; AbLIM_anchor is a domain lying between the LIM actin-binding and the vilin-head domain of actin-binding LIM proteins. It is likely that this domain is involved in anchoring abLIMs to circumferential actin bundles in specific cell types.


Pssm-ID: 465046 [Multi-domain]  Cd Length: 319  Bit Score: 434.21  E-value: 1.64e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191487  33 TRTSSESIYSRPGSSIPGSPGHTIYAKVDNEILDYKDLAAIPKVKAIYDIERPDLITYEPFYTSGYDDKQERQSLGESPR 112
Cdd:pfam16182   1 TRTSSESIISPPGSSISGSPSRVIYAKLDNEILDYKDLAALPKVKAIYDIERPDLISYEPYVSYSSDDRLERQSYGESLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191487 113 TLSptPSAEGYQDVRDRMIHRSTSQGSINSPVYSRHSYTPTTSRSPQHFHRPGNEpsSGRNSPLPYRPDSRPLTPTYAQA 192
Cdd:pfam16182  81 TLS--PSSEDSYDSRELRQRRSSSPGSIGSPTYSRHGYTPTLSRSPQHFHRPGSE--SGRSSPSLSQPSDRKSPPTYVQA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191487 193 PKHFHVPDQGI--NIYRKPPIYKQHGP--------DMKRRSSGR--EEDDEELLRRRQLQEEQLMKLNSGLGQLILKEEM 260
Cdd:pfam16182 157 PKHFHVPDTGVkdNIYRKPPIYKQHGTsasasqssEDIIHSSRFpaSGGEEEGWNRRLLQEEELSKIQSGLGKLILKEEM 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018191487 261 EKES-RERSSLLASRYDSPINSA-SHIPSSKTASLPGYGRNGLHRPVSTDFAQYNSYGDVSGGvrdyqtlpdghmpamrm 338
Cdd:pfam16182 237 EARSgSERRDPWSSPRSSPSGSSgSDSPYSKSASLPGYGRNGLHRPQSADFFQYGSDGDVSWG----------------- 299

                         330       340
                  ....*....|....*....|....*..
gi 1018191487 339 drgvsmpNMLEPKIFPYEMLMVTNRGR 365
Cdd:pfam16182 300 -------GMREYKIYPYEMLAVTNRGR 319
VHP smart00153
Villin headpiece domain;
380-415 1.85e-15

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 69.66  E-value: 1.85e-15
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1018191487  380 HLAPEVFREIFGMSIQEFDRLPLWRRNDMKKKAKLF 415
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
VHP pfam02209
Villin headpiece domain;
380-415 1.62e-13

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 64.32  E-value: 1.62e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1018191487 380 HLAPEVFREIFGMSIQEFDRLPLWRRNDMKKKAKLF 415
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
LIM4_abLIM cd09330
The fourth LIM domain of actin binding LIM (abLIM) proteins; The fourth LIM domain of actin ...
 1-24 1.98e-12

The fourth LIM domain of actin binding LIM (abLIM) proteins; The fourth LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188716  Cd Length: 56  Bit Score: 61.61  E-value: 1.98e-12
                          10        20
                  ....*....|....*....|....
gi 1018191487   1 MFTEGEEMYLQGSTVWHPDCKQST 24
Cdd:cd09330    33 MFGEGEEMYLQGSEIWHPDCRQAA 56
 
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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