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Conserved domains on  [gi|578816288|ref|XP_006716767|]
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protein MTSS 1 isoform X16 [Homo sapiens]

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 9.00e-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: 9.00e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288   7 KECSALGGLFQTIISDMKGSYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGGTREIGSALTRMCMRH 86
Cdd:cd07643    1 KECSALGGLFQAIINDMKGSYPLWEDFVSKATKLHSQLRATIVATSAFLDAFQKIADAATNTRGATKEIGSALTRMCMRH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  87 RSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKvdtlGRGDIQPQL 166
Cdd:cd07643   81 KSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIRLQKKARK----GKGDLQPQL 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578816288 167 DSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTISEDLKSLTMDPHKLP 241
Cdd:cd07643  157 DSAMQDVNDKYLLLEETEKKAVRNALIEERGRFCTFVSFLKPVLDEEISMLGEVTHLQTIMEDLASLTADPHKLP 231
WH2_MTSS1 cd22060
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein ...
 727-757 8.08e-14

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


:

Pssm-ID: 409203  Cd Length: 31  Bit Score: 65.89  E-value: 8.08e-14
                         10        20        30
                 ....*....|....*....|....*....|.
gi 578816288 727 DTPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 757
Cdd:cd22060    1 DEPQGEDMLSAIRRGVKLRKTVTNDRSAPRI 31
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 329-728 1.60e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  329 SQDAFQSKSPSPMPPEAPNQLSNGFSHYSLSSESHVGPTGAGLFPhclPASRLLPRVTSVHLPDYAHYYTIGPGmfPSSQ 408
Cdd:PHA03247 2605 RGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPP---ERPRDDPAPGRVSRPRRARRLGRAAQ--ASSP 2679

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  409 IPSWKDWAKPGPYdQPLVNTlqrrkeKREPDPnggGPTTASGPPAAAEEAQRPrsmTVSAATRPGEEMEACEELALALSR 488
Cdd:PHA03247 2680 PQRPRRRAARPTV-GSLTSL------ADPPPP---PPTPEPAPHALVSATPLP---PGPAAARQASPALPAAPAPPAVPA 2746

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  489 GLQLDTQRSSRDSLQCSSGySTQTTTPCCSEDTIPSQVSDYDYFSVSGDQEADQQEFDKSstiPRNSDISQSYRRMFQAK 568
Cdd:PHA03247 2747 GPATPGGPARPARPPTTAG-PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPA---DPPAAVLAPAAALPPAA 2822

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  569 RPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSV-------RRGTIGAGPIPIKTPVIP----VKTPTVPDLPGVLPAPP 637
Cdd:PHA03247 2823 SPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVapggdvrRRPPSRSPAAKPAAPARPpvrrLARPAVSRSTESFALPP 2902

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  638 DGPEErgehsPESPsvgEGPQGVTSMPSSMWSGQASVNPPLPGPKPSIPEEHRQAIPESEAEDQEREPPSATVSPGQIPE 717
Cdd:PHA03247 2903 DQPER-----PPQP---QAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAV 2974

                         410
                  ....*....|.
gi 578816288  718 SDPADLSPRDT 728
Cdd:PHA03247 2975 PRFRVPQPAPS 2985
 
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 9.00e-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: 9.00e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288   7 KECSALGGLFQTIISDMKGSYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGGTREIGSALTRMCMRH 86
Cdd:cd07643    1 KECSALGGLFQAIINDMKGSYPLWEDFVSKATKLHSQLRATIVATSAFLDAFQKIADAATNTRGATKEIGSALTRMCMRH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  87 RSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKvdtlGRGDIQPQL 166
Cdd:cd07643   81 KSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIRLQKKARK----GKGDLQPQL 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578816288 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 2.61e-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: 349.56  E-value: 2.61e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288   16 FQTIISDMKgsyPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHRSIEAKLRQ 95
Cdd:pfam08397   1 YKTIMEQFN---PALENFIYKGNNYLSALRTTVEAAEAYFDAFQKVGEMATNSRG-SRELGSALTQMCMRHRSIESKLEQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288   96 FSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKvdtlGRGDIQPQLDSALQDVND 175
Cdd:pfam08397  77 FVQAFHGGLLNPLEENTELDKKFANQLDKDYAKEYRHARAELKKCSSELLKLQKKADK----GKGDQQPQLDEALQDVND 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578816288  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 ...
 727-757 8.08e-14

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


Pssm-ID: 409203  Cd Length: 31  Bit Score: 65.89  E-value: 8.08e-14
                         10        20        30
                 ....*....|....*....|....*....|.
gi 578816288 727 DTPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 757
Cdd:cd22060    1 DEPQGEDMLSAIRRGVKLRKTVTNDRSAPRI 31
PHA03247 PHA03247
large tegument protein UL36; Provisional
 329-728 1.60e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  329 SQDAFQSKSPSPMPPEAPNQLSNGFSHYSLSSESHVGPTGAGLFPhclPASRLLPRVTSVHLPDYAHYYTIGPGmfPSSQ 408
Cdd:PHA03247 2605 RGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPP---ERPRDDPAPGRVSRPRRARRLGRAAQ--ASSP 2679

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  409 IPSWKDWAKPGPYdQPLVNTlqrrkeKREPDPnggGPTTASGPPAAAEEAQRPrsmTVSAATRPGEEMEACEELALALSR 488
Cdd:PHA03247 2680 PQRPRRRAARPTV-GSLTSL------ADPPPP---PPTPEPAPHALVSATPLP---PGPAAARQASPALPAAPAPPAVPA 2746

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  489 GLQLDTQRSSRDSLQCSSGySTQTTTPCCSEDTIPSQVSDYDYFSVSGDQEADQQEFDKSstiPRNSDISQSYRRMFQAK 568
Cdd:PHA03247 2747 GPATPGGPARPARPPTTAG-PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPA---DPPAAVLAPAAALPPAA 2822

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  569 RPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSV-------RRGTIGAGPIPIKTPVIP----VKTPTVPDLPGVLPAPP 637
Cdd:PHA03247 2823 SPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVapggdvrRRPPSRSPAAKPAAPARPpvrrLARPAVSRSTESFALPP 2902

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  638 DGPEErgehsPESPsvgEGPQGVTSMPSSMWSGQASVNPPLPGPKPSIPEEHRQAIPESEAEDQEREPPSATVSPGQIPE 717
Cdd:PHA03247 2903 DQPER-----PPQP---QAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAV 2974

                         410
                  ....*....|.
gi 578816288  718 SDPADLSPRDT 728
Cdd:PHA03247 2975 PRFRVPQPAPS 2985
WH2 pfam02205
WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in ...
 727-753 2.29e-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: 35.94  E-value: 2.29e-03
                          10        20
                  ....*....|....*....|....*...
gi 578816288  727 DTPQGEDMLNAIRRGVKLKKT-TTNDRS 753
Cdd:pfam02205   1 GGGGRGALLADIRAGKKLKKVeETNDRS 28
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 570-729 2.36e-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: 41.29  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  570 PASTAGLPTTLGPAMVTPGVATIrrTPSTKPSVRRGTIGAGPIPIKTPVIPVKTPTVPDLPGVLPAPP------DGPEER 643
Cdd:pfam03154 200 TPSAPSVPPQGSPATSQPPNQTQ--STAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPlpqpslHGQMPP 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  644 GEHSPES-PSVGEGPQGVTSMPSSMWSGQASVnPPLPGPKPSIPEEHRQAIPESEAEDQEREPPSATVSPgQIPESDPAD 722
Cdd:pfam03154 278 MPHSLQTgPSHMQHPVPPQPFPLTPQSSQSQV-PPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLP-PAPLSMPHI 355


                  ....*..
gi 578816288  723 LSPRDTP 729
Cdd:pfam03154 356 KPPPTTP 362
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 110-195 9.87e-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: 37.18  E-value: 9.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288   110 EQMEEWKKVANQLD---KDHAKEYKKARQEIKKKSSdtlKLQKKAKKVDTLGRGDIQPQLDSALQDVNDKYLLLEE---T 183
Cdd:smart00935  11 QESPAGKAAQKQLEkefKKRQAELEKLEKELQKLKE---KLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQdlqK 87

                           90
                   ....*....|..
gi 578816288   184 EKQAVRKALIEE 195
Cdd:smart00935  88 RQQEELQKILDK 99
 
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 9.00e-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: 9.00e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288   7 KECSALGGLFQTIISDMKGSYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGGTREIGSALTRMCMRH 86
Cdd:cd07643    1 KECSALGGLFQAIINDMKGSYPLWEDFVSKATKLHSQLRATIVATSAFLDAFQKIADAATNTRGATKEIGSALTRMCMRH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  87 RSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKvdtlGRGDIQPQL 166
Cdd:cd07643   81 KSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIRLQKKARK----GKGDLQPQL 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578816288 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 2.61e-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: 349.56  E-value: 2.61e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288   16 FQTIISDMKgsyPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHRSIEAKLRQ 95
Cdd:pfam08397   1 YKTIMEQFN---PALENFIYKGNNYLSALRTTVEAAEAYFDAFQKVGEMATNSRG-SRELGSALTQMCMRHRSIESKLEQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288   96 FSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKvdtlGRGDIQPQLDSALQDVND 175
Cdd:pfam08397  77 FVQAFHGGLLNPLEENTELDKKFANQLDKDYAKEYRHARAELKKCSSELLKLQKKADK----GKGDQQPQLDEALQDVND 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578816288  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 6.69e-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: 6.69e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  10 SALGGLFQTIISDMKG-SYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHRS 88
Cdd:cd07605    1 EELNRLTENIYKNIKEqFNPVLRNLIKAGKKYQKALQALSQAAKVFFDALAKIGELASQSRG-SQELGEALKQIVDTHKS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  89 IEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKVdtlGRGDIQPQLDS 168
Cdd:cd07605   80 IEASLEQVAKAFHGELILPLEKKLELDQKVINKFEKDYKKEYKQKREDLDKARSELKKLQKKSQKS---GTGKYQEKLDQ 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578816288 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 1.17e-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: 79.03  E-value: 1.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  19 IISDMKGSYPVWEDFINKAGKLQSQLRTtvvaAAAFLDAFQKVADMATNtrggtrEIGSALTRMCMRHRSIEAKLRQFSS 98
Cdd:cd07307    2 LDELEKLLKKLIKDTKKLLDSLKELPAA----AEKLSEALQELGKELPD------LSNTDLGEALEKFGKIQKELEEFRD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  99 ALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKVDTLgrgdiqPQLDSALQDVNDKYL 178
Cdd:cd07307   72 QLEQKLENKVIEPLKEYLKKDLKEIKKRRKKLDKARLDYDAAREKLKKLRKKKKDSSKL------AEAEEELQEAKEKYE 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 578816288 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 ...
 727-757 8.08e-14

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


Pssm-ID: 409203  Cd Length: 31  Bit Score: 65.89  E-value: 8.08e-14
                         10        20        30
                 ....*....|....*....|....*....|.
gi 578816288 727 DTPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 757
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 1.80e-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: 61.87  E-value: 1.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  15 LFQTIISDMKgsyPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHRSIEAKLR 94
Cdd:cd07646   12 VYKTIMEQFN---PSLRNFIAMGKNYEKALASVTFAAKGYFDALVKMGELASESQG-SKELGDVLFQMAEVHRQIQNQLE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  95 QfssaLIDCLINPLQEQMEewKKVanQLDKDH-AKEYKKARQEIKKKSSDTLKLQKKAKKVDTLGRGDIQPQL--DSALQ 171
Cdd:cd07646   88 E----MLKSFHNELLTQLE--QKV--ELDSRYlTAALKKYQTEHRSKGESLEKCQAELKKLRKKSQGSKNPQKysDKELQ 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 578816288 172 DV---NDKYLLLEETEKQAVRKALIEERGRFC 200
Cdd:cd07646  160 YIeaiSNKQGELENYVSDGYKTALTEERRRYC 191
PHA03247 PHA03247
large tegument protein UL36; Provisional
 329-728 1.60e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  329 SQDAFQSKSPSPMPPEAPNQLSNGFSHYSLSSESHVGPTGAGLFPhclPASRLLPRVTSVHLPDYAHYYTIGPGmfPSSQ 408
Cdd:PHA03247 2605 RGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPP---ERPRDDPAPGRVSRPRRARRLGRAAQ--ASSP 2679

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  409 IPSWKDWAKPGPYdQPLVNTlqrrkeKREPDPnggGPTTASGPPAAAEEAQRPrsmTVSAATRPGEEMEACEELALALSR 488
Cdd:PHA03247 2680 PQRPRRRAARPTV-GSLTSL------ADPPPP---PPTPEPAPHALVSATPLP---PGPAAARQASPALPAAPAPPAVPA 2746

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  489 GLQLDTQRSSRDSLQCSSGySTQTTTPCCSEDTIPSQVSDYDYFSVSGDQEADQQEFDKSstiPRNSDISQSYRRMFQAK 568
Cdd:PHA03247 2747 GPATPGGPARPARPPTTAG-PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPA---DPPAAVLAPAAALPPAA 2822

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  569 RPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSV-------RRGTIGAGPIPIKTPVIP----VKTPTVPDLPGVLPAPP 637
Cdd:PHA03247 2823 SPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVapggdvrRRPPSRSPAAKPAAPARPpvrrLARPAVSRSTESFALPP 2902

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  638 DGPEErgehsPESPsvgEGPQGVTSMPSSMWSGQASVNPPLPGPKPSIPEEHRQAIPESEAEDQEREPPSATVSPGQIPE 717
Cdd:PHA03247 2903 DQPER-----PPQP---QAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAV 2974

                         410
                  ....*....|.
gi 578816288  718 SDPADLSPRDT 728
Cdd:PHA03247 2975 PRFRVPQPAPS 2985
I-BAR_IMD_BAIAP2L1 cd07645
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Brain-specific ...
 28-200 7.32e-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: 44.91  E-value: 7.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  28 PVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHR----SIEAKLRQFSSALIdc 103
Cdd:cd07645   20 PGLRNLINLGKNYEKAVNAMVLAGKAYYDGVAKIGEIAAVSPV-SKELGHVLMEISDVHKklndSLEENFKKFHREII-- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288 104 liNPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKkvdtlGRGDI---QPQLDSALQDVNDKYLLL 180
Cdd:cd07645   97 --AELERKTDLDVKYMTATLKRYQTEHKNKLDSLEKSQADLKKIRRKSQ-----GRRNAskyEHKENEYLETVTSRQSDI 169

                        170       180
                 ....*....|....*....|
gi 578816288 181 EETEKQAVRKALIEERGRFC 200
Cdd:cd07645  170 QKFIADGCREALLEEKRRFC 189
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
 101-186 2.00e-04

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: 42.11  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288 101 IDCL--INPLQEQMEEWKKVANQLDKDhaKEykKARQEIKKKSSDTLKLQKKAKKVDTLGRGDIQPQLDSALQDVNDkyl 178
Cdd:cd21759   68 IKGLrkIRALEKQLKEMEEIASQLKKD--KD--KWTKQVKELKKEIDALIKKIKTNDMITRKEIDKLYNALVKKVDK--- 140


                 ....*...
gi 578816288 179 LLEETEKQ 186
Cdd:cd21759  141 QLAELQKK 148
WH2_WAS_WASL cd22064
Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein (WIP); ...
 729-755 2.57e-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: 38.61  E-value: 2.57e-04
                         10        20
                 ....*....|....*....|....*...
gi 578816288 729 PQGED-MLNAIRRGVKLKKTTTNDRSAP 755
Cdd:cd22064    2 QKGRGaLLGDIRKGMKLKKTVTNDRSAP 29
WH2_WAS_WASL-1 cd22076
Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein family ...
 734-755 1.10e-03

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


Pssm-ID: 409219 [Multi-domain]  Cd Length: 32  Bit Score: 36.87  E-value: 1.10e-03
                         10        20
                 ....*....|....*....|..
gi 578816288 734 MLNAIRRGVKLKKTTTNDRSAP 755
Cdd:cd22076    8 LLSDINKGKKLKKTVTNDRSAP 29
PHA03247 PHA03247
large tegument protein UL36; Provisional
 567-757 1.11e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  567 AKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKT---PTVPDLPGVLPAPPDGPEE- 642
Cdd:PHA03247 2766 PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAspaGPLPPPTSAQPTAPPPPPGp 2845

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  643 -------RGEHSPESPSVGEGPQGVT-------SMPSSMWSGQASVNP---PLPGPKPSiPEEHRQAIPESEAEDQEREP 705
Cdd:PHA03247 2846 pppslplGGSVAPGGDVRRRPPSRSPaakpaapARPPVRRLARPAVSRsteSFALPPDQ-PERPPQPQAPPPPQPQPQPP 2924

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578816288  706 PSATVSPGQIPESDP-ADLSPRDTPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 757
Cdd:PHA03247 2925 PPPQPQPPPPPPPRPqPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRF 2977
PHA03247 PHA03247
large tegument protein UL36; Provisional
 582-720 1.94e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  582 PAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPV-IPVKTPTVPDLPGVLPAPPDGPEERGE-HSPESPSVGEGPQG 659
Cdd:PHA03247  375 PKRASLPTRKRRSARHAATPFARGPGGDDQTRPAAPVpASVPTPAPTPVPASAPPPPATPLPSAEpGSDDGPAPPPERQP 454

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578816288  660 VTsmpssmwsgqasvnPPLPGPKPSIPEEHRQAIpESEAEDQEREPPSAtvSPGQIPESDP 720
Cdd:PHA03247  455 PA--------------PATEPAPDDPDDATRKAL-DALRERRPPEPPGA--DLAELLGRHP 498
WH2 pfam02205
WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in ...
 727-753 2.29e-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: 35.94  E-value: 2.29e-03
                          10        20
                  ....*....|....*....|....*...
gi 578816288  727 DTPQGEDMLNAIRRGVKLKKT-TTNDRS 753
Cdd:pfam02205   1 GGGGRGALLADIRAGKKLKKVeETNDRS 28
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 570-729 2.36e-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: 41.29  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  570 PASTAGLPTTLGPAMVTPGVATIrrTPSTKPSVRRGTIGAGPIPIKTPVIPVKTPTVPDLPGVLPAPP------DGPEER 643
Cdd:pfam03154 200 TPSAPSVPPQGSPATSQPPNQTQ--STAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPlpqpslHGQMPP 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288  644 GEHSPES-PSVGEGPQGVTSMPSSMWSGQASVnPPLPGPKPSIPEEHRQAIPESEAEDQEREPPSATVSPgQIPESDPAD 722
Cdd:pfam03154 278 MPHSLQTgPSHMQHPVPPQPFPLTPQSSQSQV-PPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLP-PAPLSMPHI 355


                  ....*..
gi 578816288  723 LSPRDTP 729
Cdd:pfam03154 356 KPPPTTP 362
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 608-754 2.59e-03

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 41.10  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288 608 GAGPIPIKTPVIPVKTPTVPDLPGVLPAPPDGPEERGEHSPESPSVGEGPQgvtsmpssmwsgqasvNPPLPGPKPSIPE 687
Cdd:PTZ00441 336 GKDGNPNEENLFPPGDDEVPDESNVPPNPPNVPGGSNSEFSSDVENPPNPP----------------NPDIPEQEPNIPE 399

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288 688 EHRQAIPES---EAEDQEREPPSATVSPGQIPESDPADLSPRDTPQGEDMLNAIRRGVKLKKTTTNDRSA 754
Cdd:PTZ00441 400 DSNKEVPEDvpmEPEDDRDNNFNEPKKPENKGDGQNEPVIPKPLDNERDQSNKNKQVNPGNRHNSEDRYT 469
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 110-195 9.87e-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: 37.18  E-value: 9.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288   110 EQMEEWKKVANQLD---KDHAKEYKKARQEIKKKSSdtlKLQKKAKKVDTLGRGDIQPQLDSALQDVNDKYLLLEE---T 183
Cdd:smart00935  11 QESPAGKAAQKQLEkefKKRQAELEKLEKELQKLKE---KLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQdlqK 87

                           90
                   ....*....|..
gi 578816288   184 EKQAVRKALIEE 195
Cdd:smart00935  88 RQQEELQKILDK 99
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 567-664 9.96e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 39.41  E-value: 9.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816288 567 AKRPASTAGLPTTLGPAMVTPGVAtirrtPSTKPSvrrgTIGAGPIPIKTPVIPVKTPTVPDLPGVLPAPPDGPEERGEH 646
Cdd:PRK14950 361 VPVPAPQPAKPTAAAPSPVRPTPA-----PSTRPK----AAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPESAPKL 431

                         90
                 ....*....|....*...
gi 578816288 647 SPESPSVGEGPQGVTSMP 664
Cdd:PRK14950 432 TRAAIPVDEKPKYTPPAP 449
 
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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