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Conserved domains on  [gi|1034662253|ref|XP_016869577|]
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protein MTSS 1 isoform X7 [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; ...
 7-237 6.02e-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: 477.71  E-value: 6.02e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253   7 KECSALGGLFQTIISDMKGSYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGGTREIGSALTRMCMRH 86
Cdd:cd07643     1 KECSALGGLFQAIINDMKGSYPLWEDFVSKATKLHSQLRATIVATSAFLDAFQKIADAATNTRGATKEIGSALTRMCMRH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  87 RSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKGRGDIQPQLDSAL 166
Cdd:cd07643    81 KSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIRLQKKARKGKGDLQPQLDSAM 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034662253 167 QDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTISEDLKSLTMDPHKLP 237
Cdd:cd07643   161 QDVNDKYLLLEETEKKAVRNALIEERGRFCTFVSFLKPVLDEEISMLGEVTHLQTIMEDLASLTADPHKLP 231
WH2_MTSS1 cd22060
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein ...
 808-838 7.20e-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: 7.20e-14
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1034662253 808 DTPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 838
Cdd:cd22060     1 DEPQGEDMLSAIRRGVKLRKTVTNDRSAPRI 31
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 648-809 5.03e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 5.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  648 AKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPS-------------------VRRGTIGAGPIPIKTPVIP----VKT 704
Cdd:PHA03247  2809 AAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPgppppslplggsvapggdvRRRPPSRSPAAKPAAPARPpvrrLAR 2888

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  705 PTVPDLPGVLPAPPDGPEErgehsPESPsvgEGPQGVTSMPSSMWSGQASVNPPLPGPKPSIPEEHRQAIPESEAEDQER 784
Cdd:PHA03247  2889 PAVSRSTESFALPPDQPER-----PPQP---QAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVP 2960

                          170       180
                   ....*....|....*....|....*
gi 1034662253  785 EPPSATVSPGQIPESDPADLSPRDT 809
Cdd:PHA03247  2961 QPWLGALVPGRVAVPRFRVPQPAPS 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; ...
 7-237 6.02e-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: 477.71  E-value: 6.02e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253   7 KECSALGGLFQTIISDMKGSYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGGTREIGSALTRMCMRH 86
Cdd:cd07643     1 KECSALGGLFQAIINDMKGSYPLWEDFVSKATKLHSQLRATIVATSAFLDAFQKIADAATNTRGATKEIGSALTRMCMRH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  87 RSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKGRGDIQPQLDSAL 166
Cdd:cd07643    81 KSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIRLQKKARKGKGDLQPQLDSAM 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034662253 167 QDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTISEDLKSLTMDPHKLP 237
Cdd:cd07643   161 QDVNDKYLLLEETEKKAVRNALIEERGRFCTFVSFLKPVLDEEISMLGEVTHLQTIMEDLASLTADPHKLP 231
IMD pfam08397
IRSp53/MIM homology domain; The N-terminal predicted helical stretch of the insulin receptor ...
 16-236 3.01e-117

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: 354.57  E-value: 3.01e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  16 FQTIISDMKgsyPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHRSIEAKLRQ 95
Cdd:pfam08397   1 YKTIMEQFN---PALENFIYKGNNYLSALRTTVEAAEAYFDAFQKVGEMATNSRG-SRELGSALTQMCMRHRSIESKLEQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  96 FSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKGRGDIQPQLDSALQDVNDKYLL 175
Cdd:pfam08397  77 FVQAFHGGLLNPLEENTELDKKFANQLDKDYAKEYRHARAELKKCSSELLKLQKKADKGKGDQQPQLDEALQDVNDKYLL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034662253 176 LEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGE-ITHLQTISEDLKSLTMDPHKL 236
Cdd:pfam08397 157 LEETVSQAVRAALIEERRRFCFLIEKLLPVSNTELQMLGEaITHLQNIVLLWKELTSEPHRL 218
WH2_MTSS1 cd22060
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein ...
 808-838 7.20e-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: 7.20e-14
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1034662253 808 DTPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 838
Cdd:cd22060     1 DEPQGEDMLSAIRRGVKLRKTVTNDRSAPRI 31
PHA03247 PHA03247
large tegument protein UL36; Provisional
 648-809 5.03e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 5.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  648 AKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPS-------------------VRRGTIGAGPIPIKTPVIP----VKT 704
Cdd:PHA03247  2809 AAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPgppppslplggsvapggdvRRRPPSRSPAAKPAAPARPpvrrLAR 2888

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  705 PTVPDLPGVLPAPPDGPEErgehsPESPsvgEGPQGVTSMPSSMWSGQASVNPPLPGPKPSIPEEHRQAIPESEAEDQER 784
Cdd:PHA03247  2889 PAVSRSTESFALPPDQPER-----PPQP---QAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVP 2960

                          170       180
                   ....*....|....*....|....*
gi 1034662253  785 EPPSATVSPGQIPESDPADLSPRDT 809
Cdd:PHA03247  2961 QPWLGALVPGRVAVPRFRVPQPAPS 2985
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 651-810 8.41e-04

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: 43.22  E-value: 8.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253 651 PASTAGLPTTLGPAMVTPGVATIrrTPSTKPSVRRGTIGAGPIPIKTPVIPVKTPTVPDLPGVLPAPP------DGPEER 724
Cdd:pfam03154 200 TPSAPSVPPQGSPATSQPPNQTQ--STAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPlpqpslHGQMPP 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253 725 GEHSPES-PSVGEGPQGVTSMPSSMWSGQASVnPPLPGPKPSIPEEHRQAIPESEAEDQEREPPSATVSPgQIPESDPAD 803
Cdd:pfam03154 278 MPHSLQTgPSHMQHPVPPQPFPLTPQSSQSQV-PPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLP-PAPLSMPHI 355


                  ....*..
gi 1034662253 804 LSPRDTP 810
Cdd:pfam03154 356 KPPPTTP 362
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 108-193 3.45e-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: 38.72  E-value: 3.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  108 LQEQMEEWKKVANQLDKDHAK----EYKKARQEIKKKSSDtlkLQKKAKKGRGDIQPQLDSALQDVNDKYllleeteKQA 183
Cdd:smart00935  34 LEKLEKELQKLKEKLQKDAATlseaAREKKEKELQKKVQE---FQRKQQKLQQDLQKRQQEELQKILDKI-------NKA 103

                           90
                   ....*....|
gi 1034662253  184 VrKALIEERG 193
Cdd:smart00935 104 I-KEVAKKKG 112
WH2 pfam02205
WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in ...
 808-834 3.53e-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: 35.55  E-value: 3.53e-03
                          10        20
                  ....*....|....*....|....*...
gi 1034662253 808 DTPQGEDMLNAIRRGVKLKKT-TTNDRS 834
Cdd:pfam02205   1 GGGGRGALLADIRAGKKLKKVeETNDRS 28
 
Name Accession Description Interval E-value
I-BAR_IMD_MIM cd07643
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; ...
 7-237 6.02e-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: 477.71  E-value: 6.02e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253   7 KECSALGGLFQTIISDMKGSYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGGTREIGSALTRMCMRH 86
Cdd:cd07643     1 KECSALGGLFQAIINDMKGSYPLWEDFVSKATKLHSQLRATIVATSAFLDAFQKIADAATNTRGATKEIGSALTRMCMRH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  87 RSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKGRGDIQPQLDSAL 166
Cdd:cd07643    81 KSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIRLQKKARKGKGDLQPQLDSAM 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034662253 167 QDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTISEDLKSLTMDPHKLP 237
Cdd:cd07643   161 QDVNDKYLLLEETEKKAVRNALIEERGRFCTFVSFLKPVLDEEISMLGEVTHLQTIMEDLASLTADPHKLP 231
IMD pfam08397
IRSp53/MIM homology domain; The N-terminal predicted helical stretch of the insulin receptor ...
 16-236 3.01e-117

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: 354.57  E-value: 3.01e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  16 FQTIISDMKgsyPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHRSIEAKLRQ 95
Cdd:pfam08397   1 YKTIMEQFN---PALENFIYKGNNYLSALRTTVEAAEAYFDAFQKVGEMATNSRG-SRELGSALTQMCMRHRSIESKLEQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  96 FSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKGRGDIQPQLDSALQDVNDKYLL 175
Cdd:pfam08397  77 FVQAFHGGLLNPLEENTELDKKFANQLDKDYAKEYRHARAELKKCSSELLKLQKKADKGKGDQQPQLDEALQDVNDKYLL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034662253 176 LEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGE-ITHLQTISEDLKSLTMDPHKL 236
Cdd:pfam08397 157 LEETVSQAVRAALIEERRRFCFLIEKLLPVSNTELQMLGEaITHLQNIVLLWKELTSEPHRL 218
I-BAR_IMD cd07605
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module ...
 10-230 2.45e-83

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: 2.45e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  10 SALGGLFQTIISDMKG-SYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHRS 88
Cdd:cd07605     1 EELNRLTENIYKNIKEqFNPVLRNLIKAGKKYQKALQALSQAAKVFFDALAKIGELASQSRG-SQELGEALKQIVDTHKS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  89 IEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKK-GRGDIQPQLDSALQ 167
Cdd:cd07605    80 IEASLEQVAKAFHGELILPLEKKLELDQKVINKFEKDYKKEYKQKREDLDKARSELKKLQKKSQKsGTGKYQEKLDQALE 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034662253 168 DVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISM-LGEITHLQTISEDLKSLT 230
Cdd:cd07605   160 ELNDKQKELEAFVSQGLRDALLEERRRYCFLVDKHCSVAKHEIAYhAKAMTLLSTRLPLWQELC 223
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 19-216 5.94e-17

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


Pssm-ID: 153271 [Multi-domain]  Cd Length: 194  Bit Score: 79.80  E-value: 5.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  19 IISDMKGSYPVWEDFINKAGKLQSQLRTtvvaAAAFLDAFQKVADMATNtrggtrEIGSALTRMCMRHRSIEAKLRQFSS 98
Cdd:cd07307     2 LDELEKLLKKLIKDTKKLLDSLKELPAA----AEKLSEALQELGKELPD------LSNTDLGEALEKFGKIQKELEEFRD 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  99 ALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKGRGDiqPQLDSALQDVNDKYLLLEE 178
Cdd:cd07307    72 QLEQKLENKVIEPLKEYLKKDLKEIKKRRKKLDKARLDYDAAREKLKKLRKKKKDSSKL--AEAEEELQEAKEKYEELRE 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1034662253 179 TEKQAVRKaLIEERGR-----FCTFISMLRPVIEEEISMLGEI 216
Cdd:cd07307   150 ELIEDLNK-LEEKRKElflslLLSFIEAQSEFFKEVLKILEQL 191
WH2_MTSS1 cd22060
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein ...
 808-838 7.20e-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: 7.20e-14
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1034662253 808 DTPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 838
Cdd:cd22060     1 DEPQGEDMLSAIRRGVKLRKTVTNDRSAPRI 31
I-BAR_IMD_IRSp53 cd07646
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Insulin Receptor ...
 15-196 2.21e-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: 61.48  E-value: 2.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  15 LFQTIISDMKgsyPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHRSIEAKLR 94
Cdd:cd07646    12 VYKTIMEQFN---PSLRNFIAMGKNYEKALASVTFAAKGYFDALVKMGELASESQG-SKELGDVLFQMAEVHRQIQNQLE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  95 QFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAkKGRGDIQPQLDSALQDV---ND 171
Cdd:cd07646    88 EMLKSFHNELLTQLEQKVELDSRYLTAALKKYQTEHRSKGESLEKCQAELKKLRKKS-QGSKNPQKYSDKELQYIeaiSN 166

                         170       180
                  ....*....|....*....|....*
gi 1034662253 172 KYLLLEETEKQAVRKALIEERGRFC 196
Cdd:cd07646   167 KQGELENYVSDGYKTALTEERRRYC 191
I-BAR_IMD_BAIAP2L1 cd07645
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Brain-specific ...
 28-196 1.95e-06

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


Pssm-ID: 153329  Cd Length: 226  Bit Score: 49.92  E-value: 1.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  28 PVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHR----SIEAKLRQFSSALIdc 103
Cdd:cd07645    20 PGLRNLINLGKNYEKAVNAMVLAGKAYYDGVAKIGEIAAVSPV-SKELGHVLMEISDVHKklndSLEENFKKFHREII-- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253 104 liNPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKGRGDIQPQLDSA--LQDVNDKYLLLEETEK 181
Cdd:cd07645    97 --AELERKTDLDVKYMTATLKRYQTEHKNKLDSLEKSQADLKKIRRKSQGRRNASKYEHKENeyLETVTSRQSDIQKFIA 174

                         170
                  ....*....|....*
gi 1034662253 182 QAVRKALIEERGRFC 196
Cdd:cd07645   175 DGCREALLEEKRRFC 189
WH2_WAS_WASL cd22064
Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein (WIP); ...
 810-836 3.42e-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: 3.42e-04
                          10        20
                  ....*....|....*....|....*...
gi 1034662253 810 PQGED-MLNAIRRGVKLKKTTTNDRSAP 836
Cdd:cd22064     2 QKGRGaLLGDIRKGMKLKKTVTNDRSAP 29
PHA03247 PHA03247
large tegument protein UL36; Provisional
 648-809 5.03e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 5.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  648 AKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPS-------------------VRRGTIGAGPIPIKTPVIP----VKT 704
Cdd:PHA03247  2809 AAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPgppppslplggsvapggdvRRRPPSRSPAAKPAAPARPpvrrLAR 2888

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  705 PTVPDLPGVLPAPPDGPEErgehsPESPsvgEGPQGVTSMPSSMWSGQASVNPPLPGPKPSIPEEHRQAIPESEAEDQER 784
Cdd:PHA03247  2889 PAVSRSTESFALPPDQPER-----PPQP---QAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVP 2960

                          170       180
                   ....*....|....*....|....*
gi 1034662253  785 EPPSATVSPGQIPESDPADLSPRDT 809
Cdd:PHA03247  2961 QPWLGALVPGRVAVPRFRVPQPAPS 2985
PHA03247 PHA03247
large tegument protein UL36; Provisional
 651-812 7.36e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 7.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  651 PASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKTPTvpdlpgvlPAPPDGPEERGEHSPE 730
Cdd:PHA03247  2713 HALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA--------PAPPAAPAAGPPRRLT 2784

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  731 SPSVGEGPQGVTSMPSSmwSGQASVNPPLPGPKPSIPEEHRQAIPEseaedqerePPSATVSPGQiPESDPADLSPRDTP 810
Cdd:PHA03247  2785 RPAVASLSESRESLPSP--WDPADPPAAVLAPAAALPPAASPAGPL---------PPPTSAQPTA-PPPPPGPPPPSLPL 2852


                   ..
gi 1034662253  811 QG 812
Cdd:PHA03247  2853 GG 2854
PHA03247 PHA03247
large tegument protein UL36; Provisional
 648-838 8.00e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 8.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  648 AKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKT---PTVPDLPGVLPAPPDGPEE- 723
Cdd:PHA03247  2766 PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAspaGPLPPPTSAQPTAPPPPPGp 2845

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  724 -------RGEHSPESPSVGEGPQGVT-------SMPSSMWSGQASVNP---PLPGPKPSiPEEHRQAIPESEAEDQEREP 786
Cdd:PHA03247  2846 pppslplGGSVAPGGDVRRRPPSRSPaakpaapARPPVRRLARPAVSRsteSFALPPDQ-PERPPQPQAPPPPQPQPQPP 2924

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034662253  787 PSATVSPGQIPESDP-ADLSPRDTPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 838
Cdd:PHA03247  2925 PPPQPQPPPPPPPRPqPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRF 2977
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 651-810 8.41e-04

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: 43.22  E-value: 8.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253 651 PASTAGLPTTLGPAMVTPGVATIrrTPSTKPSVRRGTIGAGPIPIKTPVIPVKTPTVPDLPGVLPAPP------DGPEER 724
Cdd:pfam03154 200 TPSAPSVPPQGSPATSQPPNQTQ--STAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPlpqpslHGQMPP 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253 725 GEHSPES-PSVGEGPQGVTSMPSSMWSGQASVnPPLPGPKPSIPEEHRQAIPESEAEDQEREPPSATVSPgQIPESDPAD 803
Cdd:pfam03154 278 MPHSLQTgPSHMQHPVPPQPFPLTPQSSQSQV-PPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLP-PAPLSMPHI 355


                  ....*..
gi 1034662253 804 LSPRDTP 810
Cdd:pfam03154 356 KPPPTTP 362
WH2_WAS_WASL-1 cd22076
Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein family ...
 815-836 1.37e-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: 1.37e-03
                          10        20
                  ....*....|....*....|..
gi 1034662253 815 MLNAIRRGVKLKKTTTNDRSAP 836
Cdd:cd22076     8 LLSDINKGKKLKKTVTNDRSAP 29
PHA03247 PHA03247
large tegument protein UL36; Provisional
 663-801 1.64e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  663 PAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPV-IPVKTPTVPDLPGVLPAPPDGPEERGE-HSPESPSVGEGPQG 740
Cdd:PHA03247   375 PKRASLPTRKRRSARHAATPFARGPGGDDQTRPAAPVpASVPTPAPTPVPASAPPPPATPLPSAEpGSDDGPAPPPERQP 454

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034662253  741 VTsmpssmwsgqasvnPPLPGPKPSIPEEHRQAIpESEAEDQEREPPSAtvSPGQIPESDP 801
Cdd:PHA03247   455 PA--------------PATEPAPDDPDDATRKAL-DALRERRPPEPPGA--DLAELLGRHP 498
PHA03247 PHA03247
large tegument protein UL36; Provisional
 621-810 1.71e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  621 ADQQEFDKSSTIPRNSDISQSYRRMFQAKRPASTA------GLPTTLGPAM---------VTPGVATIRRTPSTK-PSVR 684
Cdd:PHA03247  2646 VPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPqrprrrAARPTVGSLTsladpppppPTPEPAPHALVSATPlPPGP 2725

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  685 RGTIGAGPIPIKTPVIPvKTPTVPDLPGVLPAPPDGPEERGEHSPESPSVGEGPQGVTSMPSSMWSGQASVNpplPGPKP 764
Cdd:PHA03247  2726 AAARQASPALPAAPAPP-AVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRE---SLPSP 2801

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1034662253  765 SIPEEHRQAIPESEAEdqerEPPSATVSPGQIPESDPADLSPRDTP 810
Cdd:PHA03247  2802 WDPADPPAAVLAPAAA----LPPAASPAGPLPPPTSAQPTAPPPPP 2843
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 689-835 2.10e-03

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 41.49  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253 689 GAGPIPIKTPVIPVKTPTVPDLPGVLPAPPDGPEERGEHSPESPSVGEGPQgvtsmpssmwsgqasvNPPLPGPKPSIPE 768
Cdd:PTZ00441  336 GKDGNPNEENLFPPGDDEVPDESNVPPNPPNVPGGSNSEFSSDVENPPNPP----------------NPDIPEQEPNIPE 399

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253 769 EHRQAIPES---EAEDQEREPPSATVSPGQIPESDPADLSPRDTPQGEDMLNAIRRGVKLKKTTTNDRSA 835
Cdd:PTZ00441  400 DSNKEVPEDvpmEPEDDRDNNFNEPKKPENKGDGQNEPVIPKPLDNERDQSNKNKQVNPGNRHNSEDRYT 469
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 108-193 3.45e-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: 38.72  E-value: 3.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034662253  108 LQEQMEEWKKVANQLDKDHAK----EYKKARQEIKKKSSDtlkLQKKAKKGRGDIQPQLDSALQDVNDKYllleeteKQA 183
Cdd:smart00935  34 LEKLEKELQKLKEKLQKDAATlseaAREKKEKELQKKVQE---FQRKQQKLQQDLQKRQQEELQKILDKI-------NKA 103

                           90
                   ....*....|
gi 1034662253  184 VrKALIEERG 193
Cdd:smart00935 104 I-KEVAKKKG 112
WH2 pfam02205
WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in ...
 808-834 3.53e-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: 35.55  E-value: 3.53e-03
                          10        20
                  ....*....|....*....|....*...
gi 1034662253 808 DTPQGEDMLNAIRRGVKLKKT-TTNDRS 834
Cdd:pfam02205   1 GGGGRGALLADIRAGKKLKKVeETNDRS 28
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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