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Conserved domains on  [gi|568991926|ref|XP_006520780|]
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protein MTSS 1 isoform X29 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAR super family cl12013
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 1-160 4.00e-104

The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.


The actual alignment was detected with superfamily member cd07643:

Pssm-ID: 472257  Cd Length: 231  Bit Score: 316.31  E-value: 4.00e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926   1 MCMRHRSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKvdaqGRGD 80
Cdd:cd07643   76 MCMRHKSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIRLQKKARK----GKGD 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926  81 IQPQLDSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTISEDLKSLTMDPHKLP 160
Cdd:cd07643  152 LQPQLDSAMQDVNDKYLLLEETEKKAVRNALIEERGRFCTFVSFLKPVLDEEISMLGEVTHLQTIMEDLASLTADPHKLP 231
WH2_MTSS1 cd22060
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein ...
 647-677 9.15e-14

Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein 1 (MTSS-1); This family contains the first tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) found in metastasis suppressor protein 1 (MTSS1, also called also known as missing in metastasis or MIM). MTSS1 may be related to cancer progression or tumor metastasis in a variety of organ sites, most likely through an interaction with the actin cytoskeleton. It interacts with actin via its WH2 domain. MTSS1 is a novel potential metastasis suppressor gene in several types of human cancers; its expression is down-regulated in ovarian cancer, colorectal cancer, oesophageal cancer, prostate cancer and breast cancer, whereas it has also been observed to be up-regulated in hepato-cellular carcinoma and breast cancer.


:

Pssm-ID: 409203  Cd Length: 31  Bit Score: 65.50  E-value: 9.15e-14
                         10        20        30
                 ....*....|....*....|....*....|.
gi 568991926 647 ESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 677
Cdd:cd22060    1 DEPQGEDMLSAIRRGVKLRKTVTNDRSAPRI 31
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 487-677 5.34e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 5.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926  487 AKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKT---PTVPDLPGVLPSPPDGPEER 563
Cdd:PHA03247 2766 PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAspaGPLPPPTSAQPTAPPPPPGP 2845

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926  564 GEHS----------------PESPSAGEGPQGVSNIPSSLWSGQAPVNP--PLPGPKPSIPeehRQAIPESEAEDQERDP 625
Cdd:PHA03247 2846 PPPSlplggsvapggdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSteSFALPPDQPE---RPPQPQAPPPPQPQPQ 2922

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568991926  626 PSATVSPGPIPESDP---ADLSPRESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 677
Cdd:PHA03247 2923 PPPPPQPQPPPPPPPrpqPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRF 2977
 
Name Accession Description Interval E-value
I-BAR_IMD_MIM cd07643
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; ...
 1-160 4.00e-104

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. Members of this subfamily include missing in metastasis (MIM) or metastasis suppressor 1 (MTSS1), metastasis suppressor 1-like (MTSSL) or ABBA (Actin-Bundling protein with BAIAP2 homology), and similar proteins. They contain an N-terminal IMD and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. MIM was originally identified as a missing transcript from metastatic bladder and prostate cancer cells. It is a scaffold protein that functions in a signaling pathway between the PDGF receptor, Src kinases, and actin assembly. It may also function as a cofactor of the Sonic hedgehog (Shh) transcriptional pathway and may participate in tumor development and progression via this pathway. ABBA regulates actin and plasma membrane dynamics to promote the extension of radial glia, which is important in neuronal migration, axon guidance and neurogenesis. The IMD domain of MIM binds and bundles actin filaments, binds membranes, and interacts with the small GTPase Rac.


Pssm-ID: 153327  Cd Length: 231  Bit Score: 316.31  E-value: 4.00e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926   1 MCMRHRSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKvdaqGRGD 80
Cdd:cd07643   76 MCMRHKSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIRLQKKARK----GKGD 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926  81 IQPQLDSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTISEDLKSLTMDPHKLP 160
Cdd:cd07643  152 LQPQLDSAMQDVNDKYLLLEETEKKAVRNALIEERGRFCTFVSFLKPVLDEEISMLGEVTHLQTIMEDLASLTADPHKLP 231
IMD pfam08397
IRSp53/MIM homology domain; The N-terminal predicted helical stretch of the insulin receptor ...
 1-159 2.09e-79

IRSp53/MIM homology domain; The N-terminal predicted helical stretch of the insulin receptor tyrosine kinase substrate p53 (IRSp53) is an evolutionary conserved F-actin bundling domain involved in filopodium formation. The domain has been named IMD after the IRSp53 and missing in metastasis (MIM) proteins in which it occurs. Filopodium-inducing IMD activity is regulated by Cdc42 and Rac1 and is SH3-independent.


Pssm-ID: 429972  Cd Length: 218  Bit Score: 251.72  E-value: 2.09e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926    1 MCMRHRSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKvdaqGRGD 80
Cdd:pfam08397  63 MCMRHRSIESKLEQFVQAFHGGLLNPLEENTELDKKFANQLDKDYAKEYRHARAELKKCSSELLKLQKKADK----GKGD 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926   81 IQPQLDSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGE-ITHLQTISEDLKSLTMDPHKL 159
Cdd:pfam08397 139 QQPQLDEALQDVNDKYLLLEETVSQAVRAALIEERRRFCFLIEKLLPVSNTELQMLGEaITHLQNIVLLWKELTSEPHRL 218
WH2_MTSS1 cd22060
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein ...
 647-677 9.15e-14

Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein 1 (MTSS-1); This family contains the first tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) found in metastasis suppressor protein 1 (MTSS1, also called also known as missing in metastasis or MIM). MTSS1 may be related to cancer progression or tumor metastasis in a variety of organ sites, most likely through an interaction with the actin cytoskeleton. It interacts with actin via its WH2 domain. MTSS1 is a novel potential metastasis suppressor gene in several types of human cancers; its expression is down-regulated in ovarian cancer, colorectal cancer, oesophageal cancer, prostate cancer and breast cancer, whereas it has also been observed to be up-regulated in hepato-cellular carcinoma and breast cancer.


Pssm-ID: 409203  Cd Length: 31  Bit Score: 65.50  E-value: 9.15e-14
                         10        20        30
                 ....*....|....*....|....*....|.
gi 568991926 647 ESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 677
Cdd:cd22060    1 DEPQGEDMLSAIRRGVKLRKTVTNDRSAPRI 31
PHA03247 PHA03247
large tegument protein UL36; Provisional
 487-677 5.34e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 5.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926  487 AKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKT---PTVPDLPGVLPSPPDGPEER 563
Cdd:PHA03247 2766 PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAspaGPLPPPTSAQPTAPPPPPGP 2845

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926  564 GEHS----------------PESPSAGEGPQGVSNIPSSLWSGQAPVNP--PLPGPKPSIPeehRQAIPESEAEDQERDP 625
Cdd:PHA03247 2846 PPPSlplggsvapggdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSteSFALPPDQPE---RPPQPQAPPPPQPQPQ 2922

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568991926  626 PSATVSPGPIPESDP---ADLSPRESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 677
Cdd:PHA03247 2923 PPPPPQPQPPPPPPPrpqPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRF 2977
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 29-114 2.92e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 41.42  E-value: 2.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926    29 EQMEEWKKVANQLD---KDHAKEYKKARQEIKKKSSdtlKLQKKAKKVDAQGRGDIQPQLDSALQDVNDKYLLLEE---T 102
Cdd:smart00935  11 QESPAGKAAQKQLEkefKKRQAELEKLEKELQKLKE---KLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQdlqK 87

                           90
                   ....*....|..
gi 568991926   103 EKQAVRKALIEE 114
Cdd:smart00935  88 RQQEELQKILDK 99
WH2 pfam02205
WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in ...
 648-673 5.69e-03

WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in WASP and Scar1 (mammalian homolog) to be the region that interacts with actin.


Pssm-ID: 460490  Cd Length: 28  Bit Score: 34.78  E-value: 5.69e-03
                          10        20
                  ....*....|....*....|....*..
gi 568991926  648 SPQGEDMLNAIRRGVKLKKT-TTNDRS 673
Cdd:pfam02205   2 GGGRGALLADIRAGKKLKKVeETNDRS 28
 
Name Accession Description Interval E-value
I-BAR_IMD_MIM cd07643
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; ...
 1-160 4.00e-104

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. Members of this subfamily include missing in metastasis (MIM) or metastasis suppressor 1 (MTSS1), metastasis suppressor 1-like (MTSSL) or ABBA (Actin-Bundling protein with BAIAP2 homology), and similar proteins. They contain an N-terminal IMD and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. MIM was originally identified as a missing transcript from metastatic bladder and prostate cancer cells. It is a scaffold protein that functions in a signaling pathway between the PDGF receptor, Src kinases, and actin assembly. It may also function as a cofactor of the Sonic hedgehog (Shh) transcriptional pathway and may participate in tumor development and progression via this pathway. ABBA regulates actin and plasma membrane dynamics to promote the extension of radial glia, which is important in neuronal migration, axon guidance and neurogenesis. The IMD domain of MIM binds and bundles actin filaments, binds membranes, and interacts with the small GTPase Rac.


Pssm-ID: 153327  Cd Length: 231  Bit Score: 316.31  E-value: 4.00e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926   1 MCMRHRSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKvdaqGRGD 80
Cdd:cd07643   76 MCMRHKSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIRLQKKARK----GKGD 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926  81 IQPQLDSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTISEDLKSLTMDPHKLP 160
Cdd:cd07643  152 LQPQLDSAMQDVNDKYLLLEETEKKAVRNALIEERGRFCTFVSFLKPVLDEEISMLGEVTHLQTIMEDLASLTADPHKLP 231
IMD pfam08397
IRSp53/MIM homology domain; The N-terminal predicted helical stretch of the insulin receptor ...
 1-159 2.09e-79

IRSp53/MIM homology domain; The N-terminal predicted helical stretch of the insulin receptor tyrosine kinase substrate p53 (IRSp53) is an evolutionary conserved F-actin bundling domain involved in filopodium formation. The domain has been named IMD after the IRSp53 and missing in metastasis (MIM) proteins in which it occurs. Filopodium-inducing IMD activity is regulated by Cdc42 and Rac1 and is SH3-independent.


Pssm-ID: 429972  Cd Length: 218  Bit Score: 251.72  E-value: 2.09e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926    1 MCMRHRSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKvdaqGRGD 80
Cdd:pfam08397  63 MCMRHRSIESKLEQFVQAFHGGLLNPLEENTELDKKFANQLDKDYAKEYRHARAELKKCSSELLKLQKKADK----GKGD 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926   81 IQPQLDSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGE-ITHLQTISEDLKSLTMDPHKL 159
Cdd:pfam08397 139 QQPQLDEALQDVNDKYLLLEETVSQAVRAALIEERRRFCFLIEKLLPVSNTELQMLGEaITHLQNIVLLWKELTSEPHRL 218
I-BAR_IMD cd07605
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module ...
 1-153 1.55e-53

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module that binds and bends membranes; Inverse (I)-BAR (or IMD) is a member of the Bin/Amphiphysin/Rvs (BAR) domain family. It is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. IMD domains are found in Insulin Receptor tyrosine kinase Substrate p53 (IRSp53), Missing in Metastasis (MIM), and Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-like (BAIAP2L) proteins. These are multi-domain proteins that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. Most members contain an N-terminal IMD, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus, exccept for MIM which does not carry an SH3 domain. Some members contain additional domains and motifs. The IMD domain binds and bundles actin filaments, binds membranes and produces membrane protrusions, and interacts with the small GTPase Rac.


Pssm-ID: 153289 [Multi-domain]  Cd Length: 223  Bit Score: 183.34  E-value: 1.55e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926   1 MCMRHRSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKVdaqGRGD 80
Cdd:cd07605   73 IVDTHKSIEASLEQVAKAFHGELILPLEKKLELDQKVINKFEKDYKKEYKQKREDLDKARSELKKLQKKSQKS---GTGK 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568991926  81 IQPQLDSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISM-LGEITHLQTISEDLKSLT 153
Cdd:cd07605  150 YQEKLDQALEELNDKQKELEAFVSQGLRDALLEERRRYCFLVDKHCSVAKHEIAYhAKAMTLLSTRLPLWQELC 223
WH2_MTSS1 cd22060
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein ...
 647-677 9.15e-14

Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein 1 (MTSS-1); This family contains the first tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) found in metastasis suppressor protein 1 (MTSS1, also called also known as missing in metastasis or MIM). MTSS1 may be related to cancer progression or tumor metastasis in a variety of organ sites, most likely through an interaction with the actin cytoskeleton. It interacts with actin via its WH2 domain. MTSS1 is a novel potential metastasis suppressor gene in several types of human cancers; its expression is down-regulated in ovarian cancer, colorectal cancer, oesophageal cancer, prostate cancer and breast cancer, whereas it has also been observed to be up-regulated in hepato-cellular carcinoma and breast cancer.


Pssm-ID: 409203  Cd Length: 31  Bit Score: 65.50  E-value: 9.15e-14
                         10        20        30
                 ....*....|....*....|....*....|.
gi 568991926 647 ESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 677
Cdd:cd22060    1 DEPQGEDMLSAIRRGVKLRKTVTNDRSAPRI 31
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 1-139 2.19e-13

The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.


Pssm-ID: 153271 [Multi-domain]  Cd Length: 194  Bit Score: 69.40  E-value: 2.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926   1 MCMRHRSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKvdaqgrGD 80
Cdd:cd07307   55 ALEKFGKIQKELEEFRDQLEQKLENKVIEPLKEYLKKDLKEIKKRRKKLDKARLDYDAAREKLKKLRKKKKD------SS 128

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568991926  81 IQPQLDSALQDVNDKYLLLEETEKQAVRKaLIEERGR-----FCTFISMLRPVIEEEISMLGEI 139
Cdd:cd07307  129 KLAEAEEELQEAKEKYEELREELIEDLNK-LEEKRKElflslLLSFIEAQSEFFKEVLKILEQL 191
PHA03247 PHA03247
large tegument protein UL36; Provisional
 487-677 5.34e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 5.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926  487 AKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKT---PTVPDLPGVLPSPPDGPEER 563
Cdd:PHA03247 2766 PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAspaGPLPPPTSAQPTAPPPPPGP 2845

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926  564 GEHS----------------PESPSAGEGPQGVSNIPSSLWSGQAPVNP--PLPGPKPSIPeehRQAIPESEAEDQERDP 625
Cdd:PHA03247 2846 PPPSlplggsvapggdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSteSFALPPDQPE---RPPQPQAPPPPQPQPQ 2922

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568991926  626 PSATVSPGPIPESDP---ADLSPRESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 677
Cdd:PHA03247 2923 PPPPPQPQPPPPPPPrpqPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRF 2977
WH2_WAS_WASL cd22064
Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein (WIP); ...
 648-675 1.08e-04

Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein (WIP); This family contains the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) found in WAS/WASL-interacting protein family (WIPF, also known as WASP-interacting protein or WIP). Human WIP protein is proline rich and has high sequence similarity to yeast protein verprolin (included in this model). WIP forms complexes with WASP/N-WASP and modulates their function in vivo. It is involved in the regulation of endocytosis and participates in several cellular processes, some of which are relevant in cancer and may be dependent on different oncogenic stimuli. WIP interacts directly with mammalian actin-binding protein-1 (mABP1) via the SH3 domain during platelet-derived growth factor (PDGF)-mediated dorsal ruffle formation. WIP family includes members 1 (WAS/WASL-interacting protein family member 1) or WIPF1), 2 (WIPF2) and 3 (WIPF3). Aberrant expression of WIPF1 contributes to the invasion and metastasis of several malignancies such breast cancer, glioma and colorectal cancer; it has been identified as an oncoprotein in human pancreatic ductal adenocarcinoma (PDAC) and is associated with poor survival. WIPF2 may be an important regulator of the actin cytoskeleton. WIPF2 binds to N-WASP, regulating actin dynamics close to the plasma membrane; N-WASP in turn controls the second phase insulin secretion through the regulation of the Arp2/3 complex. WIPF3, along with LIPA (lysosomal acid lipase A), are expressed in microphages and are involved in pathological abdominal aortic aneurysm (AAA), a serious condition of the aorta. In yeast, verprolin is involved in cytoskeletal organization and cellular growth. It may exert its effects on the cytoskeleton directly, or indirectly via proline-binding proteins, such as profilin, or via proteins possessing SH3 domains.


Pssm-ID: 409207 [Multi-domain]  Cd Length: 29  Bit Score: 39.76  E-value: 1.08e-04
                         10        20
                 ....*....|....*....|....*....
gi 568991926 648 SPQGED-MLNAIRRGVKLKKTTTNDRSAP 675
Cdd:cd22064    1 EQKGRGaLLGDIRKGMKLKKTVTNDRSAP 29
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 528-676 1.39e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 44.95  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926 528 GAGPIPIKTPVIPVKTPTVPDLPGVLPSPPDGP------EERGEHSPESPSAGEGPQGVSNIPSslwsgqaPVNPPLPGP 601
Cdd:PTZ00441 336 GKDGNPNEENLFPPGDDEVPDESNVPPNPPNVPggsnseFSSDVENPPNPPNPDIPEQEPNIPE-------DSNKEVPED 408

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568991926 602 KPSIPEEHR-QAIPESEAEDQERDPPSATVSPGPIP-ESDPADLSPRESPQGEDmlNAIRRGVKLKKTTTNDRSAPR 676
Cdd:PTZ00441 409 VPMEPEDDRdNNFNEPKKPENKGDGQNEPVIPKPLDnERDQSNKNKQVNPGNRH--NSEDRYTRPHGRNNENRNYNN 483
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 487-660 2.71e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.39  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926  487 AKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSvrrgtiGAGPIPIKTPVIPVKTPtVPDLPGVLPSPPdGPEERGEH 566
Cdd:PHA03307   79 APANESRSTPTWSLSTLAPASPAREGSPTPPGPSS------PDPPPPTPPPASPPPSP-APDLSEMLRPVG-SPGPPPAA 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926  567 SPESPSAGEGPqgvsnipsslwSGQAPVNPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPGPIPESDPADLSPR 646
Cdd:PHA03307  151 SPPAAGASPAA-----------VASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASS 219

                         170
                  ....*....|....
gi 568991926  647 ESPQGEDMLNAIRR 660
Cdd:PHA03307  220 PAPAPGRSAADDAG 233
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 29-114 2.92e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 41.42  E-value: 2.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926    29 EQMEEWKKVANQLD---KDHAKEYKKARQEIKKKSSdtlKLQKKAKKVDAQGRGDIQPQLDSALQDVNDKYLLLEE---T 102
Cdd:smart00935  11 QESPAGKAAQKQLEkefKKRQAELEKLEKELQKLKE---KLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQdlqK 87

                           90
                   ....*....|..
gi 568991926   103 EKQAVRKALIEE 114
Cdd:smart00935  88 RQQEELQKILDK 99
PHA03247 PHA03247
large tegument protein UL36; Provisional
 249-649 3.57e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926  249 SQDAFQSKSPSPMPPEAANQLSNGFSHCSLSSESHAGPVGAGPFPhclPASRLLPRVTSVHLPDYAHYYTIGPGmfPSSQ 328
Cdd:PHA03247 2605 RGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPP---ERPRDDPAPGRVSRPRRARRLGRAAQ--ASSP 2679

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926  329 IPSWKDWAKPGPYdQPLVNTLQRRKEKREPdsngggptttggppagaEEAQRPRSMTVSAATRPGEEMAACEELTLAlsr 408
Cdd:PHA03247 2680 PQRPRRRAARPTV-GSLTSLADPPPPPPTP-----------------EPAPHALVSATPLPPGPAAARQASPALPAA--- 2738

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926  409 glqlDVQRSSRDSLQCSSGYSTQTTTPCCSEDTIPSQVSDydyfSVSGDQEAEQQEFDKSSTIPRNSDISQSYRRMFQAK 488
Cdd:PHA03247 2739 ----PAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAA----PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAA 2810

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926  489 RPASTAGLPTTLGPAMVTPGVATIRRTPSTKPS-------------------VRRGTIGAGPIPIKTPVIP----VKTPT 545
Cdd:PHA03247 2811 VLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPgppppslplggsvapggdvRRRPPSRSPAAKPAAPARPpvrrLARPA 2890

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926  546 VPDLPGVLPSPPDGPEErgehsPESPSAGEGPQGVSNIPSSlwsGQAPVNPPLPGPKPSIPEEHRQAIPESEAEDQERDP 625
Cdd:PHA03247 2891 VSRSTESFALPPDQPER-----PPQPQAPPPPQPQPQPPPP---PQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQP 2962

                         410       420
                  ....*....|....*....|....*..
gi 568991926  626 PSATVSPGPIP---ESDPADLSPRESP 649
Cdd:PHA03247 2963 WLGALVPGRVAvprFRVPQPAPSREAP 2989
PHA03247 PHA03247
large tegument protein UL36; Provisional
 507-651 6.80e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 6.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926  507 PGVATIRRTPSTK-PSVRRGTIGAGPIPIKTPVIPvKTPTVPdLPGVLPSPPDGPEE--------RGEHSPESPSAGEGP 577
Cdd:PHA03247 2475 PGAPVYRRPAEARfPFAAGAAPDPGGGGPPDPDAP-PAPSRL-APAILPDEPVGEPVhprmltwiRGLEELASDDAGDPP 2552

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926  578 QGVSNIPSSLWSGQApVNPPLPGPKPSIP----EEHRQAIPESEAEDQ----ERDPPSATVSPGPIPesdPADLSPRESP 649
Cdd:PHA03247 2553 PPLPPAAPPAAPDRS-VPPPRPAPRPSEPavtsRARRPDAPPQSARPRapvdDRGDPRGPAPPSPLP---PDTHAPDPPP 2628


                  ..
gi 568991926  650 QG 651
Cdd:PHA03247 2629 PS 2630
WH2_WAS_WASL-1 cd22076
Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein family ...
 654-675 1.23e-03

Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein family member 1; This family contains the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) in WAS/WASL-interacting protein family (WIPF, also known as WASP-interacting protein or WIP) member 1 (WIPF1). WIPF1 is a ubiquitously expressed proline-rich multidomain protein and is a binding partner and chaperone of WASP. It stabilizes actin filaments and regulates actin organization and polymerization which are associated with cell migration and invasion. Mutations in the WIPF1 binding site of WASP or in WIPF1 itself cause Wiskott-Aldrich syndrome (WAS), a rare X-linked recessive disease characterized by eczema, thrombocytopenia, immune deficiency, and bloody diarrhea. Aberrant expression of WIPF1 contributes to the invasion and metastasis of several malignancies such breast cancer, glioma and colorectal cancer; it has been identified as an oncoprotein in human pancreatic ductal adenocarcinoma (PDAC) and is associated with poor survival.


Pssm-ID: 409219 [Multi-domain]  Cd Length: 32  Bit Score: 36.87  E-value: 1.23e-03
                         10        20
                 ....*....|....*....|..
gi 568991926 654 MLNAIRRGVKLKKTTTNDRSAP 675
Cdd:cd22076    8 LLSDINKGKKLKKTVTNDRSAP 29
PHA03247 PHA03247
large tegument protein UL36; Provisional
 502-643 1.40e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926  502 PAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPV-IPVKTPTVPDLPGVLPSPPDGPEERGEhspesPSAGEGPqgv 580
Cdd:PHA03247  375 PKRASLPTRKRRSARHAATPFARGPGGDDQTRPAAPVpASVPTPAPTPVPASAPPPPATPLPSAE-----PGSDDGP--- 446

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568991926  581 snipsslwsgqapvnPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPGPiPESDPADL 643
Cdd:PHA03247  447 ---------------APPPERQPPAPATEPAPDDPDDATRKALDALRERRPPEP-PGADLAEL 493
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
 20-105 2.89e-03

calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).


Pssm-ID: 409646 [Multi-domain]  Cd Length: 149  Bit Score: 38.64  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926  20 IDCL--INPLQEQMEEWKKVANQLDKDhaKEykKARQEIKKKSSDTLKLQKKAKKVDAQGRGDIQPQLDSALQDVNDkyl 97
Cdd:cd21759   68 IKGLrkIRALEKQLKEMEEIASQLKKD--KD--KWTKQVKELKKEIDALIKKIKTNDMITRKEIDKLYNALVKKVDK--- 140


                 ....*...
gi 568991926  98 LLEETEKQ 105
Cdd:cd21759  141 QLAELQKK 148
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 540-634 4.13e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 39.99  E-value: 4.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926 540 PVKTPTVPDLPGVLPSPPDGPEERGEHSPESPSA-GEGPQGVSNIPSSLWSGQAPVNPPLPGP-KPSIPEEHRQAIPESE 617
Cdd:PHA03264 263 GYEPPPAPSGGSPAPPGDDRPEAKPEPGPVEDGApGRETGGEGEGPEPAGRDGAAGGEPKPGPpRPAPDADRPEGWPSLE 342

                         90
                 ....*....|....*..
gi 568991926 618 AEDQerdPPSATVSPGP 634
Cdd:PHA03264 343 AITF---PPPTPATPAV 356
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 486-664 4.86e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 4.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926 486 QAKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRrGTIGAGPIPIKTPVIPvkTPTVPDLPGVLPSPPDGPEERGE 565
Cdd:PRK07764 632 AAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW-PAKAGGAAPAAPPPAP--APAAPAAPAGAAPAQPAPAPAAT 708

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926 566 HSPE-SPSAGEGPQGVSNIPSSLWSGQAPVNPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPGPIPESDPADLS 644
Cdd:PRK07764 709 PPAGqADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAED 788

                        170       180
                 ....*....|....*....|
gi 568991926 645 PRESPQGEDMLNAIRRGVKL 664
Cdd:PRK07764 789 DAPSMDDEDRRDAEEVAMEL 808
WH2 pfam02205
WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in ...
 648-673 5.69e-03

WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in WASP and Scar1 (mammalian homolog) to be the region that interacts with actin.


Pssm-ID: 460490  Cd Length: 28  Bit Score: 34.78  E-value: 5.69e-03
                          10        20
                  ....*....|....*....|....*..
gi 568991926  648 SPQGEDMLNAIRRGVKLKKT-TTNDRS 673
Cdd:pfam02205   2 GGGRGALLADIRAGKKLKKVeETNDRS 28
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 487-668 6.58e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 39.79  E-value: 6.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926 487 AKRPASTAGLPTTLGPAMVTPGVAtirrtPSTKPSvrrgTIGAGPIPIKTPVIPVKTPTvpdlpgvlPSPPDgpeergeh 566
Cdd:PRK14950 361 VPVPAPQPAKPTAAAPSPVRPTPA-----PSTRPK----AAAAANIPPKEPVRETATPP--------PVPPR-------- 415

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926 567 spespsagegpqgvsnipsslwsgqaPVNPPLPGPKPSIPEEHRQAIPESEAEDQERDPP-----SATVSPGPIPE---- 637
Cdd:PRK14950 416 --------------------------PVAPPVPHTPESAPKLTRAAIPVDEKPKYTPPAPpkeeeKALIADGDVLEqlea 469

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568991926 638 --SDPADLSPRESPQGEDMLNAIRRGVKLKKTT 668
Cdd:PRK14950 470 iwKQILRDVPPRSPAVQALLSSGVRPVSVEKNT 502
I-BAR_IMD_IRSp53 cd07646
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Insulin Receptor ...
 1-119 6.87e-03

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Insulin Receptor tyrosine kinase Substrate p53; The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. IRSp53 (Insulin Receptor tyrosine kinase Substrate p53) is also known as BAIAP2 (Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2). It is a scaffolding protein that takes part in many signaling pathways including Cdc42-induced filopodia formation, Rac-mediated lamellipodia extension, and spine morphogenesis. IRSp53 exists as multiple splicing variants that differ mainly at the C-termini. One variant (T-form) is expressed exclusively in human breast cancer cells. The gene encoding IRSp53 is a putative susceptibility gene for Gilles de la Tourette syndrome. IRSp53 contains an N-terminal IMD, a CRIB (Cdc42 and Rac interactive binding motif), an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. Its IMD domain binds and bundles actin filaments, binds membranes, and interacts with the small GTPase Rac.


Pssm-ID: 153330  Cd Length: 232  Bit Score: 38.76  E-value: 6.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568991926   1 MCMRHRSIEAKLRQfssaLIDCLINPLQEQMEewKKVanQLDKDH-AKEYKKARQEIKKKSSDTLKLQKKAKKVDAQGRG 79
Cdd:cd07646   75 MAEVHRQIQNQLEE----MLKSFHNELLTQLE--QKV--ELDSRYlTAALKKYQTEHRSKGESLEKCQAELKKLRKKSQG 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568991926  80 DIQPQL--DSALQDV---NDKYLLLEETEKQAVRKALIEERGRFC 119
Cdd:cd07646  147 SKNPQKysDKELQYIeaiSNKQGELENYVSDGYKTALTEERRRYC 191
 
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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