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Conserved domains on  [gi|557878671|ref|NP_001273617|]
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actin-binding LIM protein 2 isoform 8 [Homo sapiens]

Protein Classification

LIM domain-containing protein( domain architecture ID 10912199)

LIM domain-containing protein; LIM is a small protein-protein interaction domain containing two zinc fingers; similar to Homo sapiens leupaxin, a transcriptional coactivator for androgen receptor (AR) and serum response factor (SRF)

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 ...
 33-296 1.47e-95

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: 286.68  E-value: 1.47e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878671   33 TRTSSESIISVPASSTSGSPSRVIYAKLGGEILDYRDLAALPKSKAIYDIDRPDMISYSPYISHS---AGDRQSYGESPQ 109
Cdd:pfam16182   1 TRTSSESIISPPGSSISGSPSRVIYAKLDNEILDYKDLAALPKVKAIYDIERPDLISYEPYVSYSsddRLERQSYGESLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878671  110 LLSPtPTEGDQDDRSYKQCRTSSPSSTGSVSLGR--YTPT-SRSPQHYSR------------------------------ 156
Cdd:pfam16182  81 TLSP-SSEDSYDSRELRQRRSSSPGSIGSPTYSRhgYTPTlSRSPQHFHRpgsesgrsspslsqpsdrkspptyvqapkh 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878671  157 ---PDTGVKDNIYRKPPIYRQHAARRS------------------DGEDGSLDQDNRKQKSSW-------LMLKGDADTR 208
Cdd:pfam16182 160 fhvPDTGVKDNIYRKPPIYKQHGTSASasqssediihssrfpasgGEEEGWNRRLLQEEELSKiqsglgkLILKEEMEAR 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878671  209 TNSPDLDTQSLSHSSGTDRDPlqrmagdsfhSRFPYSKSDPLPGHGKNGLDQ-RNANLAPCGADPDASWG-MREYKIYPY 286
Cdd:pfam16182 240 SGSERRDPWSSPRSSPSGSSG----------SDSPYSKSASLPGYGRNGLHRpQSADFFQYGSDGDVSWGgMREYKIYPY 309

                         330
                  ....*....|
gi 557878671  287 DSLIVTNRIR 296
Cdd:pfam16182 310 EMLAVTNRGR 319
VHP pfam02209
Villin headpiece domain;
311-346 9.38e-17

Villin headpiece domain;


:

Pssm-ID: 460493  Cd Length: 36  Bit Score: 72.80  E-value: 9.38e-17
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 557878671  311 HLSPEEFQEVFGMSIEEFDRLALWKRNDLKKKALLF 346
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
LIM super family cl02475
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
 1-24 4.96e-13

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: 63.15  E-value: 4.96e-13
                         10        20
                 ....*....|....*....|....
gi 557878671   1 MFAEGEEMYLQGSSIWHPACRQAA 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 ...
 33-296 1.47e-95

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: 286.68  E-value: 1.47e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878671   33 TRTSSESIISVPASSTSGSPSRVIYAKLGGEILDYRDLAALPKSKAIYDIDRPDMISYSPYISHS---AGDRQSYGESPQ 109
Cdd:pfam16182   1 TRTSSESIISPPGSSISGSPSRVIYAKLDNEILDYKDLAALPKVKAIYDIERPDLISYEPYVSYSsddRLERQSYGESLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878671  110 LLSPtPTEGDQDDRSYKQCRTSSPSSTGSVSLGR--YTPT-SRSPQHYSR------------------------------ 156
Cdd:pfam16182  81 TLSP-SSEDSYDSRELRQRRSSSPGSIGSPTYSRhgYTPTlSRSPQHFHRpgsesgrsspslsqpsdrkspptyvqapkh 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878671  157 ---PDTGVKDNIYRKPPIYRQHAARRS------------------DGEDGSLDQDNRKQKSSW-------LMLKGDADTR 208
Cdd:pfam16182 160 fhvPDTGVKDNIYRKPPIYKQHGTSASasqssediihssrfpasgGEEEGWNRRLLQEEELSKiqsglgkLILKEEMEAR 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878671  209 TNSPDLDTQSLSHSSGTDRDPlqrmagdsfhSRFPYSKSDPLPGHGKNGLDQ-RNANLAPCGADPDASWG-MREYKIYPY 286
Cdd:pfam16182 240 SGSERRDPWSSPRSSPSGSSG----------SDSPYSKSASLPGYGRNGLHRpQSADFFQYGSDGDVSWGgMREYKIYPY 309

                         330
                  ....*....|
gi 557878671  287 DSLIVTNRIR 296
Cdd:pfam16182 310 EMLAVTNRGR 319
VHP pfam02209
Villin headpiece domain;
311-346 9.38e-17

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 72.80  E-value: 9.38e-17
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 557878671  311 HLSPEEFQEVFGMSIEEFDRLALWKRNDLKKKALLF 346
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
VHP smart00153
Villin headpiece domain;
311-346 2.43e-16

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 71.58  E-value: 2.43e-16
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 557878671   311 HLSPEEFQEVFGMSIEEFDRLALWKRNDLKKKALLF 346
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
LIM4_abLIM cd09330
The fourth LIM domain of actin binding LIM (abLIM) proteins; The fourth LIM domain of actin ...
 1-24 4.96e-13

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: 63.15  E-value: 4.96e-13
                         10        20
                 ....*....|....*....|....
gi 557878671   1 MFAEGEEMYLQGSSIWHPACRQAA 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 ...
 33-296 1.47e-95

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: 286.68  E-value: 1.47e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878671   33 TRTSSESIISVPASSTSGSPSRVIYAKLGGEILDYRDLAALPKSKAIYDIDRPDMISYSPYISHS---AGDRQSYGESPQ 109
Cdd:pfam16182   1 TRTSSESIISPPGSSISGSPSRVIYAKLDNEILDYKDLAALPKVKAIYDIERPDLISYEPYVSYSsddRLERQSYGESLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878671  110 LLSPtPTEGDQDDRSYKQCRTSSPSSTGSVSLGR--YTPT-SRSPQHYSR------------------------------ 156
Cdd:pfam16182  81 TLSP-SSEDSYDSRELRQRRSSSPGSIGSPTYSRhgYTPTlSRSPQHFHRpgsesgrsspslsqpsdrkspptyvqapkh 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878671  157 ---PDTGVKDNIYRKPPIYRQHAARRS------------------DGEDGSLDQDNRKQKSSW-------LMLKGDADTR 208
Cdd:pfam16182 160 fhvPDTGVKDNIYRKPPIYKQHGTSASasqssediihssrfpasgGEEEGWNRRLLQEEELSKiqsglgkLILKEEMEAR 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878671  209 TNSPDLDTQSLSHSSGTDRDPlqrmagdsfhSRFPYSKSDPLPGHGKNGLDQ-RNANLAPCGADPDASWG-MREYKIYPY 286
Cdd:pfam16182 240 SGSERRDPWSSPRSSPSGSSG----------SDSPYSKSASLPGYGRNGLHRpQSADFFQYGSDGDVSWGgMREYKIYPY 309

                         330
                  ....*....|
gi 557878671  287 DSLIVTNRIR 296
Cdd:pfam16182 310 EMLAVTNRGR 319
VHP pfam02209
Villin headpiece domain;
311-346 9.38e-17

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 72.80  E-value: 9.38e-17
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 557878671  311 HLSPEEFQEVFGMSIEEFDRLALWKRNDLKKKALLF 346
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
VHP smart00153
Villin headpiece domain;
311-346 2.43e-16

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 71.58  E-value: 2.43e-16
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 557878671   311 HLSPEEFQEVFGMSIEEFDRLALWKRNDLKKKALLF 346
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
LIM4_abLIM cd09330
The fourth LIM domain of actin binding LIM (abLIM) proteins; The fourth LIM domain of actin ...
 1-24 4.96e-13

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: 63.15  E-value: 4.96e-13
                         10        20
                 ....*....|....*....|....
gi 557878671   1 MFAEGEEMYLQGSSIWHPACRQAA 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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