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Conserved domains on  [gi|755551312|ref|XP_011243846|]
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protein MTSS 1 isoform X10 [Mus musculus]

Protein Classification

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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 ...
 9-182 5.15e-114

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: 344.82  E-value: 5.15e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312   9 SKGGTREIGSALTRMCMRHRSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKL 88
Cdd:cd07643   62 TRGATKEIGSALTRMCMRHKSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIRL 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  89 QKKAKKvdaqGRGDIQPQLDSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTIS 168
Cdd:cd07643  142 QKKARK----GKGDLQPQLDSAMQDVNDKYLLLEETEKKAVRNALIEERGRFCTFVSFLKPVLDEEISMLGEVTHLQTIM 217

                        170
                 ....*....|....
gi 755551312 169 EDLKSLTMDPHKLP 182
Cdd:cd07643  218 EDLASLTADPHKLP 231
WH2_MTSS1 cd22060
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein ...
 744-774 1.44e-13

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: 65.12  E-value: 1.44e-13
                         10        20        30
                 ....*....|....*....|....*....|.
gi 755551312 744 ESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 774
Cdd:cd22060    1 DEPQGEDMLSAIRRGVKLRKTVTNDRSAPRI 31
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 505-774 1.95e-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: 48.40  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  505 PSQGTRRPACRPAFRAGPAWEK-KSCGPGPGPSNRILSSVSDYDYFSVSGDQEAEQQEFDKSSTIPRNSDISQSYRRMFQ 583
Cdd:PHA03247 2679 PPQRPRRRAARPTVGSLTSLADpPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPA 2758

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  584 AK-------RPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKT---PTVPDLPGVLPSP 653
Cdd:PHA03247 2759 RPpttagppAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAspaGPLPPPTSAQPTA 2838

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  654 PDGPEERGEHS----------------PESPSAGEGPQGVSNIPSSLWSGQAPVNP--PLPGPKPSIPeehRQAIPESEA 715
Cdd:PHA03247 2839 PPPPPGPPPPSlplggsvapggdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSteSFALPPDQPE---RPPQPQAPP 2915

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755551312  716 EDQERDPPSATVSPGPIPESDP---ADLSPRESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 774
Cdd:PHA03247 2916 PPQPQPQPPPPPQPQPPPPPPPrpqPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRF 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; ...
 9-182 5.15e-114

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: 344.82  E-value: 5.15e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312   9 SKGGTREIGSALTRMCMRHRSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKL 88
Cdd:cd07643   62 TRGATKEIGSALTRMCMRHKSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIRL 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  89 QKKAKKvdaqGRGDIQPQLDSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTIS 168
Cdd:cd07643  142 QKKARK----GKGDLQPQLDSAMQDVNDKYLLLEETEKKAVRNALIEERGRFCTFVSFLKPVLDEEISMLGEVTHLQTIM 217

                        170
                 ....*....|....
gi 755551312 169 EDLKSLTMDPHKLP 182
Cdd:cd07643  218 EDLASLTADPHKLP 231
IMD pfam08397
IRSp53/MIM homology domain; The N-terminal predicted helical stretch of the insulin receptor ...
 12-181 1.11e-86

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: 273.29  E-value: 1.11e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312   12 GTREIGSALTRMCMRHRSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKK 91
Cdd:pfam08397  52 GSRELGSALTQMCMRHRSIESKLEQFVQAFHGGLLNPLEENTELDKKFANQLDKDYAKEYRHARAELKKCSSELLKLQKK 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312   92 AKKvdaqGRGDIQPQLDSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGE-ITHLQTISED 170
Cdd:pfam08397 132 ADK----GKGDQQPQLDEALQDVNDKYLLLEETVSQAVRAALIEERRRFCFLIEKLLPVSNTELQMLGEaITHLQNIVLL 207

                         170
                  ....*....|.
gi 755551312  171 LKSLTMDPHKL 181
Cdd:pfam08397 208 WKELTSEPHRL 218
WH2_MTSS1 cd22060
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein ...
 744-774 1.44e-13

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: 65.12  E-value: 1.44e-13
                         10        20        30
                 ....*....|....*....|....*....|.
gi 755551312 744 ESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 774
Cdd:cd22060    1 DEPQGEDMLSAIRRGVKLRKTVTNDRSAPRI 31
PHA03247 PHA03247
large tegument protein UL36; Provisional
 505-774 1.95e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  505 PSQGTRRPACRPAFRAGPAWEK-KSCGPGPGPSNRILSSVSDYDYFSVSGDQEAEQQEFDKSSTIPRNSDISQSYRRMFQ 583
Cdd:PHA03247 2679 PPQRPRRRAARPTVGSLTSLADpPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPA 2758

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  584 AK-------RPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKT---PTVPDLPGVLPSP 653
Cdd:PHA03247 2759 RPpttagppAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAspaGPLPPPTSAQPTA 2838

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  654 PDGPEERGEHS----------------PESPSAGEGPQGVSNIPSSLWSGQAPVNP--PLPGPKPSIPeehRQAIPESEA 715
Cdd:PHA03247 2839 PPPPPGPPPPSlplggsvapggdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSteSFALPPDQPE---RPPQPQAPP 2915

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755551312  716 EDQERDPPSATVSPGPIPESDP---ADLSPRESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 774
Cdd:PHA03247 2916 PPQPQPQPPPPPQPQPPPPPPPrpqPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRF 2977
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 51-136 3.39e-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: 3.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312    51 EQMEEWKKVANQLD---KDHAKEYKKARQEIKKKSSdtlKLQKKAKKVDAQGRGDIQPQLDSALQDVNDKYLLLEE---T 124
Cdd:smart00935  11 QESPAGKAAQKQLEkefKKRQAELEKLEKELQKLKE---KLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQdlqK 87

                           90
                   ....*....|..
gi 755551312   125 EKQAVRKALIEE 136
Cdd:smart00935  88 RQQEELQKILDK 99
WH2 pfam02205
WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in ...
 745-770 6.37e-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: 6.37e-03
                          10        20
                  ....*....|....*....|....*..
gi 755551312  745 SPQGEDMLNAIRRGVKLKKT-TTNDRS 770
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; ...
 9-182 5.15e-114

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: 344.82  E-value: 5.15e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312   9 SKGGTREIGSALTRMCMRHRSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKL 88
Cdd:cd07643   62 TRGATKEIGSALTRMCMRHKSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIRL 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  89 QKKAKKvdaqGRGDIQPQLDSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTIS 168
Cdd:cd07643  142 QKKARK----GKGDLQPQLDSAMQDVNDKYLLLEETEKKAVRNALIEERGRFCTFVSFLKPVLDEEISMLGEVTHLQTIM 217

                        170
                 ....*....|....
gi 755551312 169 EDLKSLTMDPHKLP 182
Cdd:cd07643  218 EDLASLTADPHKLP 231
IMD pfam08397
IRSp53/MIM homology domain; The N-terminal predicted helical stretch of the insulin receptor ...
 12-181 1.11e-86

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: 273.29  E-value: 1.11e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312   12 GTREIGSALTRMCMRHRSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKK 91
Cdd:pfam08397  52 GSRELGSALTQMCMRHRSIESKLEQFVQAFHGGLLNPLEENTELDKKFANQLDKDYAKEYRHARAELKKCSSELLKLQKK 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312   92 AKKvdaqGRGDIQPQLDSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGE-ITHLQTISED 170
Cdd:pfam08397 132 ADK----GKGDQQPQLDEALQDVNDKYLLLEETVSQAVRAALIEERRRFCFLIEKLLPVSNTELQMLGEaITHLQNIVLL 207

                         170
                  ....*....|.
gi 755551312  171 LKSLTMDPHKL 181
Cdd:pfam08397 208 WKELTSEPHRL 218
I-BAR_IMD cd07605
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module ...
 11-175 2.21e-59

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: 200.67  E-value: 2.21e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  11 GGTREIGSALTRMCMRHRSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQK 90
Cdd:cd07605   61 RGSQELGEALKQIVDTHKSIEASLEQVAKAFHGELILPLEKKLELDQKVINKFEKDYKKEYKQKREDLDKARSELKKLQK 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  91 KAKKVdaqGRGDIQPQLDSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISM-LGEITHLQTISE 169
Cdd:cd07605  141 KSQKS---GTGKYQEKLDQALEELNDKQKELEAFVSQGLRDALLEERRRYCFLVDKHCSVAKHEIAYhAKAMTLLSTRLP 217


                 ....*.
gi 755551312 170 DLKSLT 175
Cdd:cd07605  218 LWQELC 223
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 19-161 3.75e-14

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: 71.71  E-value: 3.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  19 ALTRMCMRHRSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKvdaq 98
Cdd:cd07307   51 DLGEALEKFGKIQKELEEFRDQLEQKLENKVIEPLKEYLKKDLKEIKKRRKKLDKARLDYDAAREKLKKLRKKKKD---- 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755551312  99 grGDIQPQLDSALQDVNDKYLLLEETEKQAVRKaLIEERGR-----FCTFISMLRPVIEEEISMLGEI 161
Cdd:cd07307  127 --SSKLAEAEEELQEAKEKYEELREELIEDLNK-LEEKRKElflslLLSFIEAQSEFFKEVLKILEQL 191
WH2_MTSS1 cd22060
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein ...
 744-774 1.44e-13

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: 65.12  E-value: 1.44e-13
                         10        20        30
                 ....*....|....*....|....*....|.
gi 755551312 744 ESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 774
Cdd:cd22060    1 DEPQGEDMLSAIRRGVKLRKTVTNDRSAPRI 31
I-BAR_IMD_IRSp53 cd07646
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Insulin Receptor ...
 12-141 5.84e-06

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: 48.39  E-value: 5.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  12 GTREIGSALTRMCMRHRSIEAKLRQfssaLIDCLINPLQEQMEewKKVanQLDKDH-AKEYKKARQEIKKKSSDTLKLQK 90
Cdd:cd07646   64 GSKELGDVLFQMAEVHRQIQNQLEE----MLKSFHNELLTQLE--QKV--ELDSRYlTAALKKYQTEHRSKGESLEKCQA 135

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755551312  91 KAKKVDAQGRGDIQPQL--DSALQDV---NDKYLLLEETEKQAVRKALIEERGRFC 141
Cdd:cd07646  136 ELKKLRKKSQGSKNPQKysDKELQYIeaiSNKQGELENYVSDGYKTALTEERRRYC 191
PHA03247 PHA03247
large tegument protein UL36; Provisional
 505-774 1.95e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  505 PSQGTRRPACRPAFRAGPAWEK-KSCGPGPGPSNRILSSVSDYDYFSVSGDQEAEQQEFDKSSTIPRNSDISQSYRRMFQ 583
Cdd:PHA03247 2679 PPQRPRRRAARPTVGSLTSLADpPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPA 2758

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  584 AK-------RPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKT---PTVPDLPGVLPSP 653
Cdd:PHA03247 2759 RPpttagppAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAspaGPLPPPTSAQPTA 2838

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  654 PDGPEERGEHS----------------PESPSAGEGPQGVSNIPSSLWSGQAPVNP--PLPGPKPSIPeehRQAIPESEA 715
Cdd:PHA03247 2839 PPPPPGPPPPSlplggsvapggdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSteSFALPPDQPE---RPPQPQAPP 2915

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755551312  716 EDQERDPPSATVSPGPIPESDP---ADLSPRESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 774
Cdd:PHA03247 2916 PPQPQPQPPPPPQPQPPPPPPPrpqPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRF 2977
PHA03247 PHA03247
large tegument protein UL36; Provisional
 496-746 2.67e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 2.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  496 TPCCSEDTIPSQGTRRPAcRPAFRAGPAWEKKSCGPGPGPSNRILSSvsdydyfSVSGDQEAEQQEFDKSSTIPRNSDIS 575
Cdd:PHA03247 2741 PPAVPAGPATPGGPARPA-RPPTTAGPPAPAPPAAPAAGPPRRLTRP-------AVASLSESRESLPSPWDPADPPAAVL 2812

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  576 QSYRRMFQAKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSV-------RRGTIGAGPIPIKTPVIP----VKTPTVP 644
Cdd:PHA03247 2813 APAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVapggdvrRRPPSRSPAAKPAAPARPpvrrLARPAVS 2892

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  645 DLPGVLPSPPDGPEErgehsPESPSAGEGPQGVSNIPSSlwsGQAPVNPPLPGPKPSIPEEHRQAIPESEAEDQERDPPS 724
Cdd:PHA03247 2893 RSTESFALPPDQPER-----PPQPQAPPPPQPQPQPPPP---PQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWL 2964

                         250       260
                  ....*....|....*....|....*
gi 755551312  725 ATVSPGPIP---ESDPADLSPRESP 746
Cdd:PHA03247 2965 GALVPGRVAvprFRVPQPAPSREAP 2989
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 625-773 9.88e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 45.73  E-value: 9.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312 625 GAGPIPIKTPVIPVKTPTVPDLPGVLPSPPDGP------EERGEHSPESPSAGEGPQGVSNIPSslwsgqaPVNPPLPGP 698
Cdd:PTZ00441 336 GKDGNPNEENLFPPGDDEVPDESNVPPNPPNVPggsnseFSSDVENPPNPPNPDIPEQEPNIPE-------DSNKEVPED 408

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755551312 699 KPSIPEEHR-QAIPESEAEDQERDPPSATVSPGPIP-ESDPADLSPRESPQGEDmlNAIRRGVKLKKTTTNDRSAPR 773
Cdd:PTZ00441 409 VPMEPEDDRdNNFNEPKKPENKGDGQNEPVIPKPLDnERDQSNKNKQVNPGNRH--NSEDRYTRPHGRNNENRNYNN 483
WH2_WAS_WASL cd22064
Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein (WIP); ...
 745-772 1.32e-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: 1.32e-04
                         10        20
                 ....*....|....*....|....*....
gi 755551312 745 SPQGED-MLNAIRRGVKLKKTTTNDRSAP 772
Cdd:cd22064    1 EQKGRGaLLGDIRKGMKLKKTVTNDRSAP 29
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 51-136 3.39e-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: 3.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312    51 EQMEEWKKVANQLD---KDHAKEYKKARQEIKKKSSdtlKLQKKAKKVDAQGRGDIQPQLDSALQDVNDKYLLLEE---T 124
Cdd:smart00935  11 QESPAGKAAQKQLEkefKKRQAELEKLEKELQKLKE---KLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQdlqK 87

                           90
                   ....*....|..
gi 755551312   125 EKQAVRKALIEE 136
Cdd:smart00935  88 RQQEELQKILDK 99
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 584-757 4.06e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 4.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  584 AKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSvrrgtiGAGPIPIKTPVIPVKTPtVPDLPGVLPSPPdGPEERGEH 663
Cdd:PHA03307   79 APANESRSTPTWSLSTLAPASPAREGSPTPPGPSS------PDPPPPTPPPASPPPSP-APDLSEMLRPVG-SPGPPPAA 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  664 SPESPSAGEGPqgvsnipsslwSGQAPVNPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPGPIPESDPADLSPR 743
Cdd:PHA03307  151 SPPAAGASPAA-----------VASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASS 219

                         170
                  ....*....|....
gi 755551312  744 ESPQGEDMLNAIRR 757
Cdd:PHA03307  220 PAPAPGRSAADDAG 233
PHA03247 PHA03247
large tegument protein UL36; Provisional
 604-748 7.43e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 7.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  604 PGVATIRRTPSTK-PSVRRGTIGAGPIPIKTPVIPvKTPTVPdLPGVLPSPPDGPEE--------RGEHSPESPSAGEGP 674
Cdd:PHA03247 2475 PGAPVYRRPAEARfPFAAGAAPDPGGGGPPDPDAP-PAPSRL-APAILPDEPVGEPVhprmltwiRGLEELASDDAGDPP 2552

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  675 QGVSNIPSSLWSGQApVNPPLPGPKPSIP----EEHRQAIPESEAEDQ----ERDPPSATVSPGPIPesdPADLSPRESP 746
Cdd:PHA03247 2553 PPLPPAAPPAAPDRS-VPPPRPAPRPSEPavtsRARRPDAPPQSARPRapvdDRGDPRGPAPPSPLP---PDTHAPDPPP 2628


                  ..
gi 755551312  747 QG 748
Cdd:PHA03247 2629 PS 2630
WH2_WAS_WASL-1 cd22076
Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein family ...
 751-772 1.21e-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: 1.21e-03
                         10        20
                 ....*....|....*....|..
gi 755551312 751 MLNAIRRGVKLKKTTTNDRSAP 772
Cdd:cd22076    8 LLSDINKGKKLKKTVTNDRSAP 29
PHA03247 PHA03247
large tegument protein UL36; Provisional
 599-740 1.47e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  599 PAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPV-IPVKTPTVPDLPGVLPSPPDGPEERGEhspesPSAGEGPqgv 677
Cdd:PHA03247  375 PKRASLPTRKRRSARHAATPFARGPGGDDQTRPAAPVpASVPTPAPTPVPASAPPPPATPLPSAE-----PGSDDGP--- 446

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755551312  678 snipsslwsgqapvnPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPGPiPESDPADL 740
Cdd:PHA03247  447 ---------------APPPERQPPAPATEPAPDDPDDATRKALDALRERRPPEP-PGADLAEL 493
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
 42-127 3.36e-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: 3.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312  42 IDCL--INPLQEQMEEWKKVANQLDKDhaKEykKARQEIKKKSSDTLKLQKKAKKVDAQGRGDIQPQLDSALQDVNDkyl 119
Cdd:cd21759   68 IKGLrkIRALEKQLKEMEEIASQLKKD--KD--KWTKQVKELKKEIDALIKKIKTNDMITRKEIDKLYNALVKKVDK--- 140


                 ....*...
gi 755551312 120 LLEETEKQ 127
Cdd:cd21759  141 QLAELQKK 148
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 637-731 4.87e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 39.99  E-value: 4.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312 637 PVKTPTVPDLPGVLPSPPDGPEERGEHSPESPSA-GEGPQGVSNIPSSLWSGQAPVNPPLPGP-KPSIPEEHRQAIPESE 714
Cdd:PHA03264 263 GYEPPPAPSGGSPAPPGDDRPEAKPEPGPVEDGApGRETGGEGEGPEPAGRDGAAGGEPKPGPpRPAPDADRPEGWPSLE 342

                         90
                 ....*....|....*..
gi 755551312 715 AEDQerdPPSATVSPGP 731
Cdd:PHA03264 343 AITF---PPPTPATPAV 356
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 583-761 5.75e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 5.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312 583 QAKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRrGTIGAGPIPIKTPVIPVKTPTVPDLPGVLPSPPDGPEERgE 662
Cdd:PRK07764 632 AAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW-PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAAT-P 709

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312 663 HSPESPSAGEGPQGVSNIPSSLWSGQAPVNPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPGPIPESDPADLSP 742
Cdd:PRK07764 710 PAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDD 789

                        170
                 ....*....|....*....
gi 755551312 743 RESPQGEDMLNAIRRGVKL 761
Cdd:PRK07764 790 APSMDDEDRRDAEEVAMEL 808
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 584-765 6.07e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 40.18  E-value: 6.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312 584 AKRPASTAGLPTTLGPAMVTPGVAtirrtPSTKPSvrrgTIGAGPIPIKTPVIPVKTPTvpdlpgvlPSPPDgpeergeh 663
Cdd:PRK14950 361 VPVPAPQPAKPTAAAPSPVRPTPA-----PSTRPK----AAAAANIPPKEPVRETATPP--------PVPPR-------- 415

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551312 664 spespsagegpqgvsnipsslwsgqaPVNPPLPGPKPSIPEEHRQAIPESEAEDQERDPP-----SATVSPGPIPE---- 734
Cdd:PRK14950 416 --------------------------PVAPPVPHTPESAPKLTRAAIPVDEKPKYTPPAPpkeeeKALIADGDVLEqlea 469

                        170       180       190
                 ....*....|....*....|....*....|...
gi 755551312 735 --SDPADLSPRESPQGEDMLNAIRRGVKLKKTT 765
Cdd:PRK14950 470 iwKQILRDVPPRSPAVQALLSSGVRPVSVEKNT 502
WH2 pfam02205
WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in ...
 745-770 6.37e-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: 6.37e-03
                          10        20
                  ....*....|....*....|....*..
gi 755551312  745 SPQGEDMLNAIRRGVKLKKT-TTNDRS 770
Cdd:pfam02205   2 GGGRGALLADIRAGKKLKKVeETNDRS 28
 
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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