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Conserved domains on  [gi|226052052|ref|NP_001139652|]
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protein MTSS 1 isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 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; ...
 7-237 5.84e-165

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: 474.63  E-value: 5.84e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052   7 KECSALGGLFQTIISDMKGSYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGGTREIGSALTRMCMRH 86
Cdd:cd07643    1 KECSALGGLFQAIINDMKGSYPLWEDFVSKATKLHSQLRATIVATSAFLDAFQKIADAATNTRGATKEIGSALTRMCMRH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  87 RSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKGRGDIQPQLDSAL 166
Cdd:cd07643   81 KSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIRLQKKARKGKGDLQPQLDSAM 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226052052 167 QDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTISEDLKSLTMDPHKLP 237
Cdd:cd07643  161 QDVNDKYLLLEETEKKAVRNALIEERGRFCTFVSFLKPVLDEEISMLGEVTHLQTIMEDLASLTADPHKLP 231
WH2_MTSS1 cd22060
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein ...
 714-744 1.57e-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: 64.73  E-value: 1.57e-13
                         10        20        30
                 ....*....|....*....|....*....|.
gi 226052052 714 ESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 744
Cdd:cd22060    1 DEPQGEDMLSAIRRGVKLRKTVTNDRSAPRI 31
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 554-744 3.80e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 3.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  554 AKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKT---PTVPDLPGVLPSPPDGPEER 630
Cdd:PHA03247 2766 PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAspaGPLPPPTSAQPTAPPPPPGP 2845

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  631 GEhSPESPSAGEGPQG-VSNIPSSLWSGQAPVNPP------LPGPKPSIPEE---------HRQAIPESEAEDQERDPPS 694
Cdd:PHA03247 2846 PP-PSLPLGGSVAPGGdVRRRPPSRSPAAKPAAPArppvrrLARPAVSRSTEsfalppdqpERPPQPQAPPPPQPQPQPP 2924

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 226052052  695 ATVSPGPIPESDP---ADLSPRESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 744
Cdd:PHA03247 2925 PPPQPQPPPPPPPrpqPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRF 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; ...
 7-237 5.84e-165

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: 474.63  E-value: 5.84e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052   7 KECSALGGLFQTIISDMKGSYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGGTREIGSALTRMCMRH 86
Cdd:cd07643    1 KECSALGGLFQAIINDMKGSYPLWEDFVSKATKLHSQLRATIVATSAFLDAFQKIADAATNTRGATKEIGSALTRMCMRH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  87 RSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKGRGDIQPQLDSAL 166
Cdd:cd07643   81 KSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIRLQKKARKGKGDLQPQLDSAM 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226052052 167 QDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTISEDLKSLTMDPHKLP 237
Cdd:cd07643  161 QDVNDKYLLLEETEKKAVRNALIEERGRFCTFVSFLKPVLDEEISMLGEVTHLQTIMEDLASLTADPHKLP 231
IMD pfam08397
IRSp53/MIM homology domain; The N-terminal predicted helical stretch of the insulin receptor ...
 16-236 1.62e-116

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: 349.95  E-value: 1.62e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052   16 FQTIISDMKgsyPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHRSIEAKLRQ 95
Cdd:pfam08397   1 YKTIMEQFN---PALENFIYKGNNYLSALRTTVEAAEAYFDAFQKVGEMATNSRG-SRELGSALTQMCMRHRSIESKLEQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052   96 FSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKGRGDIQPQLDSALQDVNDKYLL 175
Cdd:pfam08397  77 FVQAFHGGLLNPLEENTELDKKFANQLDKDYAKEYRHARAELKKCSSELLKLQKKADKGKGDQQPQLDEALQDVNDKYLL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226052052  176 LEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGE-ITHLQTISEDLKSLTMDPHKL 236
Cdd:pfam08397 157 LEETVSQAVRAALIEERRRFCFLIEKLLPVSNTELQMLGEaITHLQNIVLLWKELTSEPHRL 218
WH2_MTSS1 cd22060
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein ...
 714-744 1.57e-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: 64.73  E-value: 1.57e-13
                         10        20        30
                 ....*....|....*....|....*....|.
gi 226052052 714 ESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 744
Cdd:cd22060    1 DEPQGEDMLSAIRRGVKLRKTVTNDRSAPRI 31
PHA03247 PHA03247
large tegument protein UL36; Provisional
 554-744 3.80e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 3.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  554 AKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKT---PTVPDLPGVLPSPPDGPEER 630
Cdd:PHA03247 2766 PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAspaGPLPPPTSAQPTAPPPPPGP 2845

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  631 GEhSPESPSAGEGPQG-VSNIPSSLWSGQAPVNPP------LPGPKPSIPEE---------HRQAIPESEAEDQERDPPS 694
Cdd:PHA03247 2846 PP-PSLPLGGSVAPGGdVRRRPPSRSPAAKPAAPArppvrrLARPAVSRSTEsfalppdqpERPPQPQAPPPPQPQPQPP 2924

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 226052052  695 ATVSPGPIPESDP---ADLSPRESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 744
Cdd:PHA03247 2925 PPPQPQPPPPPPPrpqPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRF 2977
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 557-716 2.06e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.68  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  557 PASTAGLPTTLGPAMVTPGVATIrrTPSTKPSVRRGTIGAGPIPIKTPVIPVKTPTVPDLPGVLPSPP------DGPEER 630
Cdd:pfam03154 200 TPSAPSVPPQGSPATSQPPNQTQ--STAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPlpqpslHGQMPP 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  631 GEHSPES-PSAGEGPQGVSNIPSSLWSGQAPVnPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPgPIPESDPAD 709
Cdd:pfam03154 278 MPHSLQTgPSHMQHPVPPQPFPLTPQSSQSQV-PPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLP-PAPLSMPHI 355


                  ....*..
gi 226052052  710 LSPRESP 716
Cdd:pfam03154 356 KPPPTTP 362
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 108-193 5.32e-03

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: 37.95  E-value: 5.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052   108 LQEQMEEWKKVANQLDKDHAK----EYKKARQEIKKKSSDtlkLQKKAKKGRGDIQPQLDSALQDVNDKYllleeteKQA 183
Cdd:smart00935  34 LEKLEKELQKLKEKLQKDAATlseaAREKKEKELQKKVQE---FQRKQQKLQQDLQKRQQEELQKILDKI-------NKA 103

                           90
                   ....*....|
gi 226052052   184 VrKALIEERG 193
Cdd:smart00935 104 I-KEVAKKKG 112
WH2 pfam02205
WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in ...
 715-740 8.90e-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: 34.40  E-value: 8.90e-03
                          10        20
                  ....*....|....*....|....*..
gi 226052052  715 SPQGEDMLNAIRRGVKLKKT-TTNDRS 740
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; ...
 7-237 5.84e-165

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: 474.63  E-value: 5.84e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052   7 KECSALGGLFQTIISDMKGSYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGGTREIGSALTRMCMRH 86
Cdd:cd07643    1 KECSALGGLFQAIINDMKGSYPLWEDFVSKATKLHSQLRATIVATSAFLDAFQKIADAATNTRGATKEIGSALTRMCMRH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  87 RSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKGRGDIQPQLDSAL 166
Cdd:cd07643   81 KSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIRLQKKARKGKGDLQPQLDSAM 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226052052 167 QDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTISEDLKSLTMDPHKLP 237
Cdd:cd07643  161 QDVNDKYLLLEETEKKAVRNALIEERGRFCTFVSFLKPVLDEEISMLGEVTHLQTIMEDLASLTADPHKLP 231
IMD pfam08397
IRSp53/MIM homology domain; The N-terminal predicted helical stretch of the insulin receptor ...
 16-236 1.62e-116

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: 349.95  E-value: 1.62e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052   16 FQTIISDMKgsyPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHRSIEAKLRQ 95
Cdd:pfam08397   1 YKTIMEQFN---PALENFIYKGNNYLSALRTTVEAAEAYFDAFQKVGEMATNSRG-SRELGSALTQMCMRHRSIESKLEQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052   96 FSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKGRGDIQPQLDSALQDVNDKYLL 175
Cdd:pfam08397  77 FVQAFHGGLLNPLEENTELDKKFANQLDKDYAKEYRHARAELKKCSSELLKLQKKADKGKGDQQPQLDEALQDVNDKYLL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226052052  176 LEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGE-ITHLQTISEDLKSLTMDPHKL 236
Cdd:pfam08397 157 LEETVSQAVRAALIEERRRFCFLIEKLLPVSNTELQMLGEaITHLQNIVLLWKELTSEPHRL 218
I-BAR_IMD cd07605
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module ...
 10-230 4.22e-84

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: 265.77  E-value: 4.22e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  10 SALGGLFQTIISDMKG-SYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHRS 88
Cdd:cd07605    1 EELNRLTENIYKNIKEqFNPVLRNLIKAGKKYQKALQALSQAAKVFFDALAKIGELASQSRG-SQELGEALKQIVDTHKS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  89 IEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKK-GRGDIQPQLDSALQ 167
Cdd:cd07605   80 IEASLEQVAKAFHGELILPLEKKLELDQKVINKFEKDYKKEYKQKREDLDKARSELKKLQKKSQKsGTGKYQEKLDQALE 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226052052 168 DVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISM-LGEITHLQTISEDLKSLT 230
Cdd:cd07605  160 ELNDKQKELEAFVSQGLRDALLEERRRYCFLVDKHCSVAKHEIAYhAKAMTLLSTRLPLWQELC 223
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 19-216 5.16e-17

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: 79.80  E-value: 5.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  19 IISDMKGSYPVWEDFINKAGKLQSQLRTtvvaAAAFLDAFQKVADMATNtrggtrEIGSALTRMCMRHRSIEAKLRQFSS 98
Cdd:cd07307    2 LDELEKLLKKLIKDTKKLLDSLKELPAA----AEKLSEALQELGKELPD------LSNTDLGEALEKFGKIQKELEEFRD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  99 ALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKGRGDiqPQLDSALQDVNDKYLLLEE 178
Cdd:cd07307   72 QLEQKLENKVIEPLKEYLKKDLKEIKKRRKKLDKARLDYDAAREKLKKLRKKKKDSSKL--AEAEEELQEAKEKYEELRE 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 226052052 179 TEKQAVRKaLIEERGR-----FCTFISMLRPVIEEEISMLGEI 216
Cdd:cd07307  150 ELIEDLNK-LEEKRKElflslLLSFIEAQSEFFKEVLKILEQL 191
WH2_MTSS1 cd22060
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein ...
 714-744 1.57e-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: 64.73  E-value: 1.57e-13
                         10        20        30
                 ....*....|....*....|....*....|.
gi 226052052 714 ESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 744
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 ...
 15-196 3.89e-10

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: 60.71  E-value: 3.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  15 LFQTIISDMKgsyPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHRSIEAKLR 94
Cdd:cd07646   12 VYKTIMEQFN---PSLRNFIAMGKNYEKALASVTFAAKGYFDALVKMGELASESQG-SKELGDVLFQMAEVHRQIQNQLE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  95 QFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAkKGRGDIQPQLDSALQDV---ND 171
Cdd:cd07646   88 EMLKSFHNELLTQLEQKVELDSRYLTAALKKYQTEHRSKGESLEKCQAELKKLRKKS-QGSKNPQKYSDKELQYIeaiSN 166

                        170       180
                 ....*....|....*....|....*
gi 226052052 172 KYLLLEETEKQAVRKALIEERGRFC 196
Cdd:cd07646  167 KQGELENYVSDGYKTALTEERRRYC 191
I-BAR_IMD_BAIAP2L1 cd07645
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Brain-specific ...
 28-196 3.56e-06

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 1; 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. BAIAP2L1 (Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 1) is also known as IRTKS (Insulin Receptor Tyrosine Kinase Substrate). It is widely expressed, serves as a substrate for the insulin receptor, and binds the small GTPase Rac. It plays a role in regulating the actin cytoskeleton and colocalizes with F-actin, cortactin, VASP, and vinculin. BAIAP2L1 expression leads to the formation of short actin bundles, distinct from filopodia-like protrusions induced by the expression of the related protein IRSp53. It contains an N-terminal IMD, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. The IMD domain of BAIAP2L1 binds and bundles actin filaments, and binds the small GTPase Rac.


Pssm-ID: 153329  Cd Length: 226  Bit Score: 48.76  E-value: 3.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  28 PVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHR----SIEAKLRQFSSALIdc 103
Cdd:cd07645   20 PGLRNLINLGKNYEKAVNAMVLAGKAYYDGVAKIGEIAAVSPV-SKELGHVLMEISDVHKklndSLEENFKKFHREII-- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052 104 liNPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKGRGDIQPQLDSA--LQDVNDKYLLLEETEK 181
Cdd:cd07645   97 --AELERKTDLDVKYMTATLKRYQTEHKNKLDSLEKSQADLKKIRRKSQGRRNASKYEHKENeyLETVTSRQSDIQKFIA 174

                        170
                 ....*....|....*
gi 226052052 182 QAVRKALIEERGRFC 196
Cdd:cd07645  175 DGCREALLEEKRRFC 189
PHA03247 PHA03247
large tegument protein UL36; Provisional
 554-744 3.80e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 3.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  554 AKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKT---PTVPDLPGVLPSPPDGPEER 630
Cdd:PHA03247 2766 PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAspaGPLPPPTSAQPTAPPPPPGP 2845

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  631 GEhSPESPSAGEGPQG-VSNIPSSLWSGQAPVNPP------LPGPKPSIPEE---------HRQAIPESEAEDQERDPPS 694
Cdd:PHA03247 2846 PP-PSLPLGGSVAPGGdVRRRPPSRSPAAKPAAPArppvrrLARPAVSRSTEsfalppdqpERPPQPQAPPPPQPQPQPP 2924

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 226052052  695 ATVSPGPIPESDP---ADLSPRESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 744
Cdd:PHA03247 2925 PPPQPQPPPPPPPrpqPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRF 2977
PHA03247 PHA03247
large tegument protein UL36; Provisional
 486-712 3.30e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 3.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  486 TPCCSEDTIPSQGTRRPACRPAFRAGPVSDYDYFSVSGDQEAEQQEFDKSSTIPRNSDISQSYRRMFQAKRPASTAGLPT 565
Cdd:PHA03247 2741 PPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPP 2820

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  566 TLGPAMVTPGVATIRRTPSTKPS-------------------VRRGTIGAGP----IPIKTPVIPVKTPTVPDLPGVLPS 622
Cdd:PHA03247 2821 AASPAGPLPPPTSAQPTAPPPPPgppppslplggsvapggdvRRRPPSRSPAakpaAPARPPVRRLARPAVSRSTESFAL 2900

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  623 PPDGPEErgehspespsagegpqgvsnipsslwsgqaPVNPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPGPI 702
Cdd:PHA03247 2901 PPDQPER------------------------------PPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPA 2950

                         250
                  ....*....|
gi 226052052  703 PESDPADLSP 712
Cdd:PHA03247 2951 GAGEPSGAVP 2960
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 595-743 6.43e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 46.11  E-value: 6.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052 595 GAGPIPIKTPVIPVKTPTVPDLPGVLPSPPDGP------EERGEHSPESPSAGEGPQGVSNIPSslwsgqaPVNPPLPGP 668
Cdd:PTZ00441 336 GKDGNPNEENLFPPGDDEVPDESNVPPNPPNVPggsnseFSSDVENPPNPPNPDIPEQEPNIPE-------DSNKEVPED 408

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226052052 669 KPSIPEEHR-QAIPESEAEDQERDPPSATVSPGPIP-ESDPADLSPRESPQGEDmlNAIRRGVKLKKTTTNDRSAPR 743
Cdd:PTZ00441 409 VPMEPEDDRdNNFNEPKKPENKGDGQNEPVIPKPLDnERDQSNKNKQVNPGNRH--NSEDRYTRPHGRNNENRNYNN 483
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 554-727 1.10e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.93  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  554 AKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSvrrgtiGAGPIPIKTPVIPVKTPtVPDLPGVLPSPPdGPEERGEH 633
Cdd:PHA03307   79 APANESRSTPTWSLSTLAPASPAREGSPTPPGPSS------PDPPPPTPPPASPPPSP-APDLSEMLRPVG-SPGPPPAA 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  634 SPESPSAGEGPqgvsnipsslwSGQAPVNPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPGPIPESDPADLSPR 713
Cdd:PHA03307  151 SPPAAGASPAA-----------VASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASS 219

                         170
                  ....*....|....
gi 226052052  714 ESPQGEDMLNAIRR 727
Cdd:PHA03307  220 PAPAPGRSAADDAG 233
WH2_WAS_WASL cd22064
Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein (WIP); ...
 715-742 1.83e-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: 38.99  E-value: 1.83e-04
                         10        20
                 ....*....|....*....|....*....
gi 226052052 715 SPQGED-MLNAIRRGVKLKKTTTNDRSAP 742
Cdd:cd22064    1 EQKGRGaLLGDIRKGMKLKKTVTNDRSAP 29
PHA03247 PHA03247
large tegument protein UL36; Provisional
 574-718 3.56e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  574 PGVATIRRTPSTK-PSVRRGTIGAGPIPIKTPVIPvKTPTVPdLPGVLPSPPDGPEE--------RGEHSPESPSAGEGP 644
Cdd:PHA03247 2475 PGAPVYRRPAEARfPFAAGAAPDPGGGGPPDPDAP-PAPSRL-APAILPDEPVGEPVhprmltwiRGLEELASDDAGDPP 2552

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  645 QGVSNIPSSLWSGQApVNPPLPGPKPSIP----EEHRQAIPESEAEDQ----ERDPPSATVSPGPIPesdPADLSPRESP 716
Cdd:PHA03247 2553 PPLPPAAPPAAPDRS-VPPPRPAPRPSEPavtsRARRPDAPPQSARPRapvdDRGDPRGPAPPSPLP---PDTHAPDPPP 2628


                  ..
gi 226052052  717 QG 718
Cdd:PHA03247 2629 PS 2630
PHA03247 PHA03247
large tegument protein UL36; Provisional
 569-710 8.30e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 8.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  569 PAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPV-IPVKTPTVPDLPGVLPSPPDGPEERGEhspesPSAGEGPqgv 647
Cdd:PHA03247  375 PKRASLPTRKRRSARHAATPFARGPGGDDQTRPAAPVpASVPTPAPTPVPASAPPPPATPLPSAE-----PGSDDGP--- 446

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226052052  648 snipsslwsgqapvnPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPGPiPESDPADL 710
Cdd:PHA03247  447 ---------------APPPERQPPAPATEPAPDDPDDATRKALDALRERRPPEP-PGADLAEL 493
PHA03247 PHA03247
large tegument protein UL36; Provisional
 527-743 8.58e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 8.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  527 AEQQEFDKSSTIPRNSDISQSYRRMFQAKRPASTA------GLPTTLGPAMVTPGVATIRRTPSTKPsvrRGTIGAGPIP 600
Cdd:PHA03247 2646 VPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPqrprrrAARPTVGSLTSLADPPPPPPTPEPAP---HALVSATPLP 2722

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  601 IKTPVIPVKTPTVPDLPgVLPSPPDGPE-ERGEHSPESPSAGEGPQGvSNIPSSLWSGQAPVNPPLPG----------PK 669
Cdd:PHA03247 2723 PGPAAARQASPALPAAP-APPAVPAGPAtPGGPARPARPPTTAGPPA-PAPPAAPAAGPPRRLTRPAVaslsesreslPS 2800

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226052052  670 PSIPEEHRQAIPESEAEDQERDPPSATVSPGPIPESDPADLSPRESPQGEDMLNAIRRGVKLKKTTTNDRSAPR 743
Cdd:PHA03247 2801 PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAK 2874
WH2_WAS_WASL-1 cd22076
Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein family ...
 721-742 1.91e-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: 36.49  E-value: 1.91e-03
                         10        20
                 ....*....|....*....|..
gi 226052052 721 MLNAIRRGVKLKKTTTNDRSAP 742
Cdd:cd22076    8 LLSDINKGKKLKKTVTNDRSAP 29
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 607-701 1.95e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 41.14  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052 607 PVKTPTVPDLPGVLPSPPDGPEERGEHSPESPSA-GEGPQGVSNIPSSLWSGQAPVNPPLPGP-KPSIPEEHRQAIPESE 684
Cdd:PHA03264 263 GYEPPPAPSGGSPAPPGDDRPEAKPEPGPVEDGApGRETGGEGEGPEPAGRDGAAGGEPKPGPpRPAPDADRPEGWPSLE 342

                         90
                 ....*....|....*..
gi 226052052 685 AEDQerdPPSATVSPGP 701
Cdd:PHA03264 343 AITF---PPPTPATPAV 356
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 557-716 2.06e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.68  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  557 PASTAGLPTTLGPAMVTPGVATIrrTPSTKPSVRRGTIGAGPIPIKTPVIPVKTPTVPDLPGVLPSPP------DGPEER 630
Cdd:pfam03154 200 TPSAPSVPPQGSPATSQPPNQTQ--STAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPlpqpslHGQMPP 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  631 GEHSPES-PSAGEGPQGVSNIPSSLWSGQAPVnPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPgPIPESDPAD 709
Cdd:pfam03154 278 MPHSLQTgPSHMQHPVPPQPFPLTPQSSQSQV-PPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLP-PAPLSMPHI 355


                  ....*..
gi 226052052  710 LSPRESP 716
Cdd:pfam03154 356 KPPPTTP 362
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 553-731 4.31e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 4.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052 553 QAKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRrGTIGAGPIPIKTPVIPvkTPTVPDLPGVLPSPPDGPEERGE 632
Cdd:PRK07764 632 AAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW-PAKAGGAAPAAPPPAP--APAAPAAPAGAAPAQPAPAPAAT 708

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052 633 HSPE-SPSAGEGPQGVSNIPSSLWSGQAPVNPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPGPIPESDPADLS 711
Cdd:PRK07764 709 PPAGqADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAED 788

                        170       180
                 ....*....|....*....|
gi 226052052 712 PRESPQGEDMLNAIRRGVKL 731
Cdd:PRK07764 789 DAPSMDDEDRRDAEEVAMEL 808
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 108-193 5.32e-03

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: 37.95  E-value: 5.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052   108 LQEQMEEWKKVANQLDKDHAK----EYKKARQEIKKKSSDtlkLQKKAKKGRGDIQPQLDSALQDVNDKYllleeteKQA 183
Cdd:smart00935  34 LEKLEKELQKLKEKLQKDAATlseaAREKKEKELQKKVQE---FQRKQQKLQQDLQKRQQEELQKILDKI-------NKA 103

                           90
                   ....*....|
gi 226052052   184 VrKALIEERG 193
Cdd:smart00935 104 I-KEVAKKKG 112
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 569-719 5.84e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.15  E-value: 5.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  569 PAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKTPTV-PDLPGVLPSPPDGPEERGEHSPESPsAGEGPQGV 647
Cdd:PHA03307   53 VTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPaSPAREGSPTPPGPSSPDPPPPTPPP-ASPPPSPA 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  648 SNIPSSLWSGQAPVNPPL---------PGPKPSIPEEHRQ-AIPESEAEDQERDPPSATVSPGPIPesDPADLSPRESPQ 717
Cdd:PHA03307  132 PDLSEMLRPVGSPGPPPAasppaagasPAAVASDAASSRQaALPLSSPEETARAPSSPPAEPPPST--PPAAASPRPPRR 209


                  ..
gi 226052052  718 GE 719
Cdd:PHA03307  210 SS 211
PHA03418 PHA03418
hypothetical E4 protein; Provisional
 586-670 6.76e-03

hypothetical E4 protein; Provisional


Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 38.95  E-value: 6.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052 586 KPSVRRGTIGAGPIPIKTPVIPVKTPTVPDLPGVLPSPPDG--------PEERGEHSPESPSAGEGPQgvsnipsslwSG 657
Cdd:PHA03418 102 RPGKRSKADEHGPAPGRAALAPFKLDLDQDPLHGDPDPPPGatggqgeePPEGGEESQPPLGEGEGAV----------EG 171

                         90
                 ....*....|...
gi 226052052 658 QAPVNPPLPGPKP 670
Cdd:PHA03418 172 HPPPLPPAPEPKP 184
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 554-727 6.92e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.15  E-value: 6.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  554 AKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRG----TIGAGPIPIKTPVIPVKTPTVPDLPGVLPSPPDGPEE 629
Cdd:PHA03307  157 ASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPstppAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASS 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052  630 RGEHSPESPSAGEGPQGvsnipsslwsgQAPVNPPLPGPKPSIPEEHRQAIPE--------SEAEDQERDPPSATVSPGP 701
Cdd:PHA03307  237 SDSSSSESSGCGWGPEN-----------ECPLPRPAPITLPTRIWEASGWNGPssrpgpasSSSSPRERSPSPSPSSPGS 305

                         170       180
                  ....*....|....*....|....*.
gi 226052052  702 IPESDPADLSPRESPQGEDMLNAIRR 727
Cdd:PHA03307  306 GPAPSSPRASSSSSSSRESSSSSTSS 331
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 554-735 8.42e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 39.41  E-value: 8.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052 554 AKRPASTAGLPTTLGPAMVTPGVAtirrtPSTKPSvrrgTIGAGPIPIKTPVIPVKTPTvpdlpgvlPSPPDgpeergeh 633
Cdd:PRK14950 361 VPVPAPQPAKPTAAAPSPVRPTPA-----PSTRPK----AAAAANIPPKEPVRETATPP--------PVPPR-------- 415

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052052 634 spespsagegpqgvsnipsslwsgqaPVNPPLPGPKPSIPEEHRQAIPESEAEDQERDPP-----SATVSPGPIPE---- 704
Cdd:PRK14950 416 --------------------------PVAPPVPHTPESAPKLTRAAIPVDEKPKYTPPAPpkeeeKALIADGDVLEqlea 469

                        170       180       190
                 ....*....|....*....|....*....|...
gi 226052052 705 --SDPADLSPRESPQGEDMLNAIRRGVKLKKTT 735
Cdd:PRK14950 470 iwKQILRDVPPRSPAVQALLSSGVRPVSVEKNT 502
WH2 pfam02205
WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in ...
 715-740 8.90e-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: 34.40  E-value: 8.90e-03
                          10        20
                  ....*....|....*....|....*..
gi 226052052  715 SPQGEDMLNAIRRGVKLKKT-TTNDRS 740
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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