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Conserved domains on  [gi|755551323|ref|XP_011243850|]
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protein MTSS 1 isoform X23 [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; ...
 7-241 1.98e-163

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: 470.01  E-value: 1.98e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323   7 KECSALGGLFQTIISDMKGSYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGGTREIGSALTRMCMRH 86
Cdd:cd07643    1 KECSALGGLFQAIINDMKGSYPLWEDFVSKATKLHSQLRATIVATSAFLDAFQKIADAATNTRGATKEIGSALTRMCMRH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  87 RSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKvdaqGRGDIQPQL 166
Cdd:cd07643   81 KSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIRLQKKARK----GKGDLQPQL 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755551323 167 DSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTISEDLKSLTMDPHKLP 241
Cdd:cd07643  157 DSAMQDVNDKYLLLEETEKKAVRNALIEERGRFCTFVSFLKPVLDEEISMLGEVTHLQTIMEDLASLTADPHKLP 231
WH2_MTSS1 cd22060
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein ...
 698-728 1.87e-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: 1.87e-13
                         10        20        30
                 ....*....|....*....|....*....|.
gi 755551323 698 ESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 728
Cdd:cd22060    1 DEPQGEDMLSAIRRGVKLRKTVTNDRSAPRI 31
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 330-728 4.62e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.79  E-value: 4.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  330 SQDAFQSKSPSP--MPPEAANQDWAKPGPYDQPLVNTLQRRKEK----------REPDSNGGGPTTTGGPPAGAEEAQRP 397
Cdd:PHA03247 2545 SDDAGDPPPPLPpaAPPAAPDRSVPPPRPAPRPSEPAVTSRARRpdappqsarpRAPVDDRGDPRGPAPPSPLPPDTHAP 2624

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  398 RSMTVSAATRPGEEMAACEELTLALSRGLQLD-VQRSSRDSLQCSSGYSTQTTTpccsedtiPSQGTRRPACRPAFRAGP 476
Cdd:PHA03247 2625 DPPPPSPSPAANEPDPHPPPTVPPPERPRDDPaPGRVSRPRRARRLGRAAQASS--------PPQRPRRRAARPTVGSLT 2696

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  477 AWEK-KSCGPGPGPSNRILSSVSDYDYFSVSGDQEAEQQEFDKSSTIPRNSDISQSYRRMFQAK-------RPASTAGLP 548
Cdd:PHA03247 2697 SLADpPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPpttagppAPAPPAAPA 2776

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  549 TTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKT---PTVPDLPGVLPSPPDGPEERGEHS------- 618
Cdd:PHA03247 2777 AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAspaGPLPPPTSAQPTAPPPPPGPPPPSlplggsv 2856

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  619 ---------PESPSAGEGPQGVSNIPSSLWSGQAPVNPPLPGPKPSIPEEhRQAIPESEAEDQERDPPSATVSPGPIPES 689
Cdd:PHA03247 2857 apggdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPE-RPPQPQAPPPPQPQPQPPPPPQPQPPPPP 2935

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 755551323  690 DP---ADLSPRESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 728
Cdd:PHA03247 2936 PPrpqPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRF 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; ...
 7-241 1.98e-163

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: 470.01  E-value: 1.98e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323   7 KECSALGGLFQTIISDMKGSYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGGTREIGSALTRMCMRH 86
Cdd:cd07643    1 KECSALGGLFQAIINDMKGSYPLWEDFVSKATKLHSQLRATIVATSAFLDAFQKIADAATNTRGATKEIGSALTRMCMRH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  87 RSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKvdaqGRGDIQPQL 166
Cdd:cd07643   81 KSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIRLQKKARK----GKGDLQPQL 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755551323 167 DSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTISEDLKSLTMDPHKLP 241
Cdd:cd07643  157 DSAMQDVNDKYLLLEETEKKAVRNALIEERGRFCTFVSFLKPVLDEEISMLGEVTHLQTIMEDLASLTADPHKLP 231
IMD pfam08397
IRSp53/MIM homology domain; The N-terminal predicted helical stretch of the insulin receptor ...
 16-240 7.54e-115

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: 344.94  E-value: 7.54e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323   16 FQTIISDMKgsyPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHRSIEAKLRQ 95
Cdd:pfam08397   1 YKTIMEQFN---PALENFIYKGNNYLSALRTTVEAAEAYFDAFQKVGEMATNSRG-SRELGSALTQMCMRHRSIESKLEQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323   96 FSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKvdaqGRGDIQPQLDSALQDVND 175
Cdd:pfam08397  77 FVQAFHGGLLNPLEENTELDKKFANQLDKDYAKEYRHARAELKKCSSELLKLQKKADK----GKGDQQPQLDEALQDVND 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551323  176 KYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGE-ITHLQTISEDLKSLTMDPHKL 240
Cdd:pfam08397 153 KYLLLEETVSQAVRAALIEERRRFCFLIEKLLPVSNTELQMLGEaITHLQNIVLLWKELTSEPHRL 218
WH2_MTSS1 cd22060
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein ...
 698-728 1.87e-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: 1.87e-13
                         10        20        30
                 ....*....|....*....|....*....|.
gi 755551323 698 ESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 728
Cdd:cd22060    1 DEPQGEDMLSAIRRGVKLRKTVTNDRSAPRI 31
PHA03247 PHA03247
large tegument protein UL36; Provisional
 330-728 4.62e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.79  E-value: 4.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  330 SQDAFQSKSPSP--MPPEAANQDWAKPGPYDQPLVNTLQRRKEK----------REPDSNGGGPTTTGGPPAGAEEAQRP 397
Cdd:PHA03247 2545 SDDAGDPPPPLPpaAPPAAPDRSVPPPRPAPRPSEPAVTSRARRpdappqsarpRAPVDDRGDPRGPAPPSPLPPDTHAP 2624

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  398 RSMTVSAATRPGEEMAACEELTLALSRGLQLD-VQRSSRDSLQCSSGYSTQTTTpccsedtiPSQGTRRPACRPAFRAGP 476
Cdd:PHA03247 2625 DPPPPSPSPAANEPDPHPPPTVPPPERPRDDPaPGRVSRPRRARRLGRAAQASS--------PPQRPRRRAARPTVGSLT 2696

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  477 AWEK-KSCGPGPGPSNRILSSVSDYDYFSVSGDQEAEQQEFDKSSTIPRNSDISQSYRRMFQAK-------RPASTAGLP 548
Cdd:PHA03247 2697 SLADpPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPpttagppAPAPPAAPA 2776

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  549 TTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKT---PTVPDLPGVLPSPPDGPEERGEHS------- 618
Cdd:PHA03247 2777 AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAspaGPLPPPTSAQPTAPPPPPGPPPPSlplggsv 2856

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  619 ---------PESPSAGEGPQGVSNIPSSLWSGQAPVNPPLPGPKPSIPEEhRQAIPESEAEDQERDPPSATVSPGPIPES 689
Cdd:PHA03247 2857 apggdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPE-RPPQPQAPPPPQPQPQPPPPPQPQPPPPP 2935

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 755551323  690 DP---ADLSPRESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 728
Cdd:PHA03247 2936 PPrpqPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRF 2977
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 110-195 5.11e-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: 41.03  E-value: 5.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323   110 EQMEEWKKVANQLD---KDHAKEYKKARQEIKKKSSdtlKLQKKAKKVDAQGRGDIQPQLDSALQDVNDKYLLLEE---T 183
Cdd:smart00935  11 QESPAGKAAQKQLEkefKKRQAELEKLEKELQKLKE---KLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQdlqK 87

                           90
                   ....*....|..
gi 755551323   184 EKQAVRKALIEE 195
Cdd:smart00935  88 RQQEELQKILDK 99
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 541-700 2.95e-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: 40.91  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  541 PASTAGLPTTLGPAMVTPGVATIrrTPSTKPSVRRGTIGAGPIPIKTPVIPVKTPTVPDLPGVLPSPP------DGPEER 614
Cdd:pfam03154 200 TPSAPSVPPQGSPATSQPPNQTQ--STAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPlpqpslHGQMPP 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  615 GEHSPES-PSAGEGPQGVSNIPSSLWSGQAPVnPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPgPIPESDPAD 693
Cdd:pfam03154 278 MPHSLQTgPSHMQHPVPPQPFPLTPQSSQSQV-PPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLP-PAPLSMPHI 355


                  ....*..
gi 755551323  694 LSPRESP 700
Cdd:pfam03154 356 KPPPTTP 362
 
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; ...
 7-241 1.98e-163

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: 470.01  E-value: 1.98e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323   7 KECSALGGLFQTIISDMKGSYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGGTREIGSALTRMCMRH 86
Cdd:cd07643    1 KECSALGGLFQAIINDMKGSYPLWEDFVSKATKLHSQLRATIVATSAFLDAFQKIADAATNTRGATKEIGSALTRMCMRH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  87 RSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKvdaqGRGDIQPQL 166
Cdd:cd07643   81 KSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIRLQKKARK----GKGDLQPQL 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755551323 167 DSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTISEDLKSLTMDPHKLP 241
Cdd:cd07643  157 DSAMQDVNDKYLLLEETEKKAVRNALIEERGRFCTFVSFLKPVLDEEISMLGEVTHLQTIMEDLASLTADPHKLP 231
IMD pfam08397
IRSp53/MIM homology domain; The N-terminal predicted helical stretch of the insulin receptor ...
 16-240 7.54e-115

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: 344.94  E-value: 7.54e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323   16 FQTIISDMKgsyPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHRSIEAKLRQ 95
Cdd:pfam08397   1 YKTIMEQFN---PALENFIYKGNNYLSALRTTVEAAEAYFDAFQKVGEMATNSRG-SRELGSALTQMCMRHRSIESKLEQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323   96 FSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKvdaqGRGDIQPQLDSALQDVND 175
Cdd:pfam08397  77 FVQAFHGGLLNPLEENTELDKKFANQLDKDYAKEYRHARAELKKCSSELLKLQKKADK----GKGDQQPQLDEALQDVND 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551323  176 KYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGE-ITHLQTISEDLKSLTMDPHKL 240
Cdd:pfam08397 153 KYLLLEETVSQAVRAALIEERRRFCFLIEKLLPVSNTELQMLGEaITHLQNIVLLWKELTSEPHRL 218
I-BAR_IMD cd07605
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module ...
 10-234 3.71e-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: 3.71e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  10 SALGGLFQTIISDMKG-SYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHRS 88
Cdd:cd07605    1 EELNRLTENIYKNIKEqFNPVLRNLIKAGKKYQKALQALSQAAKVFFDALAKIGELASQSRG-SQELGEALKQIVDTHKS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  89 IEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKVdaqGRGDIQPQLDS 168
Cdd:cd07605   80 IEASLEQVAKAFHGELILPLEKKLELDQKVINKFEKDYKKEYKQKREDLDKARSELKKLQKKSQKS---GTGKYQEKLDQ 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755551323 169 ALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISM-LGEITHLQTISEDLKSLT 234
Cdd:cd07605  157 ALEELNDKQKELEAFVSQGLRDALLEERRRYCFLVDKHCSVAKHEIAYhAKAMTLLSTRLPLWQELC 223
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 19-220 1.96e-16

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: 78.26  E-value: 1.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  19 IISDMKGSYPVWEDFINKAGKLQSQLRTtvvaAAAFLDAFQKVADMATNtrggtrEIGSALTRMCMRHRSIEAKLRQFSS 98
Cdd:cd07307    2 LDELEKLLKKLIKDTKKLLDSLKELPAA----AEKLSEALQELGKELPD------LSNTDLGEALEKFGKIQKELEEFRD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  99 ALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKvdaqgrGDIQPQLDSALQDVNDKYL 178
Cdd:cd07307   72 QLEQKLENKVIEPLKEYLKKDLKEIKKRRKKLDKARLDYDAAREKLKKLRKKKKD------SSKLAEAEEELQEAKEKYE 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 755551323 179 LLEETEKQAVRKaLIEERGR-----FCTFISMLRPVIEEEISMLGEI 220
Cdd:cd07307  146 ELREELIEDLNK-LEEKRKElflslLLSFIEAQSEFFKEVLKILEQL 191
WH2_MTSS1 cd22060
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein ...
 698-728 1.87e-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: 1.87e-13
                         10        20        30
                 ....*....|....*....|....*....|.
gi 755551323 698 ESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 728
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 ...
 15-200 1.18e-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: 62.25  E-value: 1.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  15 LFQTIISDMKgsyPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHRSIEAKLR 94
Cdd:cd07646   12 VYKTIMEQFN---PSLRNFIAMGKNYEKALASVTFAAKGYFDALVKMGELASESQG-SKELGDVLFQMAEVHRQIQNQLE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  95 QfssaLIDCLINPLQEQMEewKKVanQLDKDH-AKEYKKARQEIKKKSSDTLKLQKKAKKVDAQGRGDIQPQL--DSALQ 171
Cdd:cd07646   88 E----MLKSFHNELLTQLE--QKV--ELDSRYlTAALKKYQTEHRSKGESLEKCQAELKKLRKKSQGSKNPQKysDKELQ 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 755551323 172 DV---NDKYLLLEETEKQAVRKALIEERGRFC 200
Cdd:cd07646  160 YIeaiSNKQGELENYVSDGYKTALTEERRRYC 191
PHA03247 PHA03247
large tegument protein UL36; Provisional
 330-728 4.62e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.79  E-value: 4.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  330 SQDAFQSKSPSP--MPPEAANQDWAKPGPYDQPLVNTLQRRKEK----------REPDSNGGGPTTTGGPPAGAEEAQRP 397
Cdd:PHA03247 2545 SDDAGDPPPPLPpaAPPAAPDRSVPPPRPAPRPSEPAVTSRARRpdappqsarpRAPVDDRGDPRGPAPPSPLPPDTHAP 2624

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  398 RSMTVSAATRPGEEMAACEELTLALSRGLQLD-VQRSSRDSLQCSSGYSTQTTTpccsedtiPSQGTRRPACRPAFRAGP 476
Cdd:PHA03247 2625 DPPPPSPSPAANEPDPHPPPTVPPPERPRDDPaPGRVSRPRRARRLGRAAQASS--------PPQRPRRRAARPTVGSLT 2696

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  477 AWEK-KSCGPGPGPSNRILSSVSDYDYFSVSGDQEAEQQEFDKSSTIPRNSDISQSYRRMFQAK-------RPASTAGLP 548
Cdd:PHA03247 2697 SLADpPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPpttagppAPAPPAAPA 2776

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  549 TTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKT---PTVPDLPGVLPSPPDGPEERGEHS------- 618
Cdd:PHA03247 2777 AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAspaGPLPPPTSAQPTAPPPPPGPPPPSlplggsv 2856

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  619 ---------PESPSAGEGPQGVSNIPSSLWSGQAPVNPPLPGPKPSIPEEhRQAIPESEAEDQERDPPSATVSPGPIPES 689
Cdd:PHA03247 2857 apggdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPE-RPPQPQAPPPPQPQPQPPPPPQPQPPPPP 2935

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 755551323  690 DP---ADLSPRESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 728
Cdd:PHA03247 2936 PPrpqPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRF 2977
PHA03247 PHA03247
large tegument protein UL36; Provisional
 338-700 6.43e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 6.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  338 SPSPMPPEAANQDWAKPGPYDQPLVNTLQRR-KEKREPDSNGGGPTTTGGPPAGAEEAQRPRSMTVSAATRPGEEMAACE 416
Cdd:PHA03247 2630 SPSPAANEPDPHPPPTVPPPERPRDDPAPGRvSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPE 2709

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  417 ELTLALSRGLQLDVQRSSrdSLQCSSGYSTQTTTPCCSEDTIPSQGTRRPAcRPAFRAGPAWEKKSCGPGPGPSNRILSS 496
Cdd:PHA03247 2710 PAPHALVSATPLPPGPAA--ARQASPALPAAPAPPAVPAGPATPGGPARPA-RPPTTAGPPAPAPPAAPAAGPPRRLTRP 2786

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  497 vsdydyfSVSGDQEAEQQEFDKSSTIPRNSDISQSYRRMFQAKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSV--- 573
Cdd:PHA03247 2787 -------AVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVapg 2859

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  574 ----RRGTIGAGP----IPIKTPVIPVKTPTVPDLPGVLPSPPDGPEErgehsPESPSAGEGPQGVSNIPSSlwsGQAPV 645
Cdd:PHA03247 2860 gdvrRRPPSRSPAakpaAPARPPVRRLARPAVSRSTESFALPPDQPER-----PPQPQAPPPPQPQPQPPPP---PQPQP 2931

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 755551323  646 NPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPGPIP---ESDPADLSPRESP 700
Cdd:PHA03247 2932 PPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAvprFRVPQPAPSREAP 2989
I-BAR_IMD_BAIAP2L1 cd07645
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Brain-specific ...
 28-200 2.16e-05

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: 46.45  E-value: 2.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  28 PVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHR----SIEAKLRQFSSALIdc 103
Cdd:cd07645   20 PGLRNLINLGKNYEKAVNAMVLAGKAYYDGVAKIGEIAAVSPV-SKELGHVLMEISDVHKklndSLEENFKKFHREII-- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323 104 liNPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAkkvdaQGRGDI---QPQLDSALQDVNDKYLLL 180
Cdd:cd07645   97 --AELERKTDLDVKYMTATLKRYQTEHKNKLDSLEKSQADLKKIRRKS-----QGRRNAskyEHKENEYLETVTSRQSDI 169

                        170       180
                 ....*....|....*....|
gi 755551323 181 EETEKQAVRKALIEERGRFC 200
Cdd:cd07645  170 QKFIADGCREALLEEKRRFC 189
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 579-727 8.02e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 46.11  E-value: 8.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323 579 GAGPIPIKTPVIPVKTPTVPDLPGVLPSPPDGP------EERGEHSPESPSAGEGPQGVSNIPSslwsgqaPVNPPLPGP 652
Cdd:PTZ00441 336 GKDGNPNEENLFPPGDDEVPDESNVPPNPPNVPggsnseFSSDVENPPNPPNPDIPEQEPNIPE-------DSNKEVPED 408

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755551323 653 KPSIPEEHR-QAIPESEAEDQERDPPSATVSPGPIP-ESDPADLSPRESPQGEDmlNAIRRGVKLKKTTTNDRSAPR 727
Cdd:PTZ00441 409 VPMEPEDDRdNNFNEPKKPENKGDGQNEPVIPKPLDnERDQSNKNKQVNPGNRH--NSEDRYTRPHGRNNENRNYNN 483
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 538-711 1.88e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  538 AKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSvrrgtiGAGPIPIKTPVIPVKTPtVPDLPGVLPSPPdGPEERGEH 617
Cdd:PHA03307   79 APANESRSTPTWSLSTLAPASPAREGSPTPPGPSS------PDPPPPTPPPASPPPSP-APDLSEMLRPVG-SPGPPPAA 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  618 SPESPSAGEGPqgvsnipsslwSGQAPVNPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPGPIPESDPADLSPR 697
Cdd:PHA03307  151 SPPAAGASPAA-----------VASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASS 219

                         170
                  ....*....|....
gi 755551323  698 ESPQGEDMLNAIRR 711
Cdd:PHA03307  220 PAPAPGRSAADDAG 233
WH2_WAS_WASL cd22064
Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein (WIP); ...
 699-726 2.01e-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: 2.01e-04
                         10        20
                 ....*....|....*....|....*....
gi 755551323 699 SPQGED-MLNAIRRGVKLKKTTTNDRSAP 726
Cdd:cd22064    1 EQKGRGaLLGDIRKGMKLKKTVTNDRSAP 29
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 110-195 5.11e-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: 41.03  E-value: 5.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323   110 EQMEEWKKVANQLD---KDHAKEYKKARQEIKKKSSdtlKLQKKAKKVDAQGRGDIQPQLDSALQDVNDKYLLLEE---T 183
Cdd:smart00935  11 QESPAGKAAQKQLEkefKKRQAELEKLEKELQKLKE---KLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQdlqK 87

                           90
                   ....*....|..
gi 755551323   184 EKQAVRKALIEE 195
Cdd:smart00935  88 RQQEELQKILDK 99
PHA03247 PHA03247
large tegument protein UL36; Provisional
 558-702 5.47e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 5.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  558 PGVATIRRTPSTK-PSVRRGTIGAGPIPIKTPVIPvKTPTVPdLPGVLPSPPDGPEE--------RGEHSPESPSAGEGP 628
Cdd:PHA03247 2475 PGAPVYRRPAEARfPFAAGAAPDPGGGGPPDPDAP-PAPSRL-APAILPDEPVGEPVhprmltwiRGLEELASDDAGDPP 2552

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  629 QGVSNIPSSLWSGQApVNPPLPGPKPSIP----EEHRQAIPESEAEDQ----ERDPPSATVSPGPIPesdPADLSPRESP 700
Cdd:PHA03247 2553 PPLPPAAPPAAPDRS-VPPPRPAPRPSEPavtsRARRPDAPPQSARPRapvdDRGDPRGPAPPSPLP---PDTHAPDPPP 2628


                  ..
gi 755551323  701 QG 702
Cdd:PHA03247 2629 PS 2630
PHA03247 PHA03247
large tegument protein UL36; Provisional
 553-694 1.19e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  553 PAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPV-IPVKTPTVPDLPGVLPSPPDGPEERGEhspesPSAGEGPqgv 631
Cdd:PHA03247  375 PKRASLPTRKRRSARHAATPFARGPGGDDQTRPAAPVpASVPTPAPTPVPASAPPPPATPLPSAE-----PGSDDGP--- 446

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755551323  632 snipsslwsgqapvnPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPGPiPESDPADL 694
Cdd:PHA03247  447 ---------------APPPERQPPAPATEPAPDDPDDATRKALDALRERRPPEP-PGADLAEL 493
WH2_WAS_WASL-1 cd22076
Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein family ...
 705-726 2.14e-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: 36.10  E-value: 2.14e-03
                         10        20
                 ....*....|....*....|..
gi 755551323 705 MLNAIRRGVKLKKTTTNDRSAP 726
Cdd:cd22076    8 LLSDINKGKKLKKTVTNDRSAP 29
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 591-685 2.53e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 40.76  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323 591 PVKTPTVPDLPGVLPSPPDGPEERGEHSPESPSA-GEGPQGVSNIPSSLWSGQAPVNPPLPGP-KPSIPEEHRQAIPESE 668
Cdd:PHA03264 263 GYEPPPAPSGGSPAPPGDDRPEAKPEPGPVEDGApGRETGGEGEGPEPAGRDGAAGGEPKPGPpRPAPDADRPEGWPSLE 342

                         90
                 ....*....|....*..
gi 755551323 669 AEDQerdPPSATVSPGP 685
Cdd:PHA03264 343 AITF---PPPTPATPAV 356
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 541-700 2.95e-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: 40.91  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  541 PASTAGLPTTLGPAMVTPGVATIrrTPSTKPSVRRGTIGAGPIPIKTPVIPVKTPTVPDLPGVLPSPP------DGPEER 614
Cdd:pfam03154 200 TPSAPSVPPQGSPATSQPPNQTQ--STAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPlpqpslHGQMPP 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  615 GEHSPES-PSAGEGPQGVSNIPSSLWSGQAPVnPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPgPIPESDPAD 693
Cdd:pfam03154 278 MPHSLQTgPSHMQHPVPPQPFPLTPQSSQSQV-PPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLP-PAPLSMPHI 355


                  ....*..
gi 755551323  694 LSPRESP 700
Cdd:pfam03154 356 KPPPTTP 362
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
 101-186 3.14e-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: 3.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323 101 IDCL--INPLQEQMEEWKKVANQLDKDhaKEykKARQEIKKKSSDTLKLQKKAKKVDAQGRGDIQPQLDSALQDVNDkyl 178
Cdd:cd21759   68 IKGLrkIRALEKQLKEMEEIASQLKKD--KD--KWTKQVKELKKEIDALIKKIKTNDMITRKEIDKLYNALVKKVDK--- 140


                 ....*...
gi 755551323 179 LLEETEKQ 186
Cdd:cd21759  141 QLAELQKK 148
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 537-715 5.38e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 5.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323 537 QAKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRrGTIGAGPIPIKTPVIPvkTPTVPDLPGVLPSPPDGPEERGE 616
Cdd:PRK07764 632 AAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW-PAKAGGAAPAAPPPAP--APAAPAAPAGAAPAQPAPAPAAT 708

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323 617 HSPE-SPSAGEGPQGVSNIPSSLWSGQAPVNPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPGPIPESDPADLS 695
Cdd:PRK07764 709 PPAGqADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAED 788

                        170       180
                 ....*....|....*....|
gi 755551323 696 PRESPQGEDMLNAIRRGVKL 715
Cdd:PRK07764 789 DAPSMDDEDRRDAEEVAMEL 808
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 456-711 8.76e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 39.77  E-value: 8.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  456 DTIPSQGTRRPACRPAFRAGPAWEKKSCGPGPGPSNRILSSVSDYDYFSVSGDQEAEQQEFDKSSTIPR----------- 524
Cdd:PHA03307   51 AAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPtpppaspppsp 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  525 NSDISQSYRRMFQAKRPASTAGLPTTLGPAMVTPGVATIRR----TPSTKPSVRRGTIGAGPIPIKTPVIPVK-TPTVPD 599
Cdd:PHA03307  131 APDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQaalpLSSPEETARAPSSPPAEPPPSTPPAAASpRPPRRS 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323  600 LPGVLPSPPDGPEeRGEHSPESPSAGEGPQGVSNIPSSLWSGQ--APVNPPLPGPKPSIPEEHRQAIPE--------SEA 669
Cdd:PHA03307  211 SPISASASSPAPA-PGRSAADDAGASSSDSSSSESSGCGWGPEneCPLPRPAPITLPTRIWEASGWNGPssrpgpasSSS 289

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 755551323  670 EDQERDPPSATVSPGPIPESDPADLSPRESPQGEDMLNAIRR 711
Cdd:PHA03307  290 SPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSS 331
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 538-719 8.86e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 39.41  E-value: 8.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323 538 AKRPASTAGLPTTLGPAMVTPGVAtirrtPSTKPSvrrgTIGAGPIPIKTPVIPVKTPTvpdlpgvlPSPPDgpeergeh 617
Cdd:PRK14950 361 VPVPAPQPAKPTAAAPSPVRPTPA-----PSTRPK----AAAAANIPPKEPVRETATPP--------PVPPR-------- 415

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551323 618 spespsagegpqgvsnipsslwsgqaPVNPPLPGPKPSIPEEHRQAIPESEAEDQERDPP-----SATVSPGPIPE---- 688
Cdd:PRK14950 416 --------------------------PVAPPVPHTPESAPKLTRAAIPVDEKPKYTPPAPpkeeeKALIADGDVLEqlea 469

                        170       180       190
                 ....*....|....*....|....*....|...
gi 755551323 689 --SDPADLSPRESPQGEDMLNAIRRGVKLKKTT 719
Cdd:PRK14950 470 iwKQILRDVPPRSPAVQALLSSGVRPVSVEKNT 502
 
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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