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Conserved domains on  [gi|1720383834|ref|XP_030104310|]
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protein MTSS 1 isoform X27 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
I-BAR_IMD_MIM cd07643
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; ...
 7-241 7.93e-163

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. Members of this subfamily include missing in metastasis (MIM) or metastasis suppressor 1 (MTSS1), metastasis suppressor 1-like (MTSSL) or ABBA (Actin-Bundling protein with BAIAP2 homology), and similar proteins. They contain an N-terminal IMD and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. MIM was originally identified as a missing transcript from metastatic bladder and prostate cancer cells. It is a scaffold protein that functions in a signaling pathway between the PDGF receptor, Src kinases, and actin assembly. It may also function as a cofactor of the Sonic hedgehog (Shh) transcriptional pathway and may participate in tumor development and progression via this pathway. ABBA regulates actin and plasma membrane dynamics to promote the extension of radial glia, which is important in neuronal migration, axon guidance and neurogenesis. The IMD domain of MIM binds and bundles actin filaments, binds membranes, and interacts with the small GTPase Rac.


:

Pssm-ID: 153327  Cd Length: 231  Bit Score: 467.31  E-value: 7.93e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834   7 KECSALGGLFQTIISDMKGSYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGGTREIGSALTRMCMRH 86
Cdd:cd07643     1 KECSALGGLFQAIINDMKGSYPLWEDFVSKATKLHSQLRATIVATSAFLDAFQKIADAATNTRGATKEIGSALTRMCMRH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  87 RSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKvdaqGRGDIQPQL 166
Cdd:cd07643    81 KSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIRLQKKARK----GKGDLQPQL 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720383834 167 DSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTISEDLKSLTMDPHKLP 241
Cdd:cd07643   157 DSAMQDVNDKYLLLEETEKKAVRNALIEERGRFCTFVSFLKPVLDEEISMLGEVTHLQTIMEDLASLTADPHKLP 231
WH2_MTSS1 cd22060
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein ...
 663-693 1.40e-13

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


:

Pssm-ID: 409203  Cd Length: 31  Bit Score: 64.73  E-value: 1.40e-13
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1720383834 663 ESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 693
Cdd:cd22060     1 DEPQGEDMLSAIRRGVKLRKTVTNDRSAPRI 31
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 503-693 2.19e-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: 48.01  E-value: 2.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  503 AKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKT---PTVPDLPGVLPSPPDGPEER 579
Cdd:PHA03247  2766 PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAspaGPLPPPTSAQPTAPPPPPGP 2845

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  580 GEHS----------------PESPSAGEGPQGVSNIPSSLWSGQAPVNP--PLPGPKPSIPeehRQAIPESEAEDQERDP 641
Cdd:PHA03247  2846 PPPSlplggsvapggdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSteSFALPPDQPE---RPPQPQAPPPPQPQPQ 2922

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720383834  642 PSATVSPGPIPESDP---ADLSPRESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 693
Cdd:PHA03247  2923 PPPPPQPQPPPPPPPrpqPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRF 2977
 
Name Accession Description Interval E-value
I-BAR_IMD_MIM cd07643
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; ...
 7-241 7.93e-163

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. Members of this subfamily include missing in metastasis (MIM) or metastasis suppressor 1 (MTSS1), metastasis suppressor 1-like (MTSSL) or ABBA (Actin-Bundling protein with BAIAP2 homology), and similar proteins. They contain an N-terminal IMD and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. MIM was originally identified as a missing transcript from metastatic bladder and prostate cancer cells. It is a scaffold protein that functions in a signaling pathway between the PDGF receptor, Src kinases, and actin assembly. It may also function as a cofactor of the Sonic hedgehog (Shh) transcriptional pathway and may participate in tumor development and progression via this pathway. ABBA regulates actin and plasma membrane dynamics to promote the extension of radial glia, which is important in neuronal migration, axon guidance and neurogenesis. The IMD domain of MIM binds and bundles actin filaments, binds membranes, and interacts with the small GTPase Rac.


Pssm-ID: 153327  Cd Length: 231  Bit Score: 467.31  E-value: 7.93e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834   7 KECSALGGLFQTIISDMKGSYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGGTREIGSALTRMCMRH 86
Cdd:cd07643     1 KECSALGGLFQAIINDMKGSYPLWEDFVSKATKLHSQLRATIVATSAFLDAFQKIADAATNTRGATKEIGSALTRMCMRH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  87 RSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKvdaqGRGDIQPQL 166
Cdd:cd07643    81 KSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIRLQKKARK----GKGDLQPQL 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720383834 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 6.96e-114

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: 341.47  E-value: 6.96e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  16 FQTIISDMKgsyPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHRSIEAKLRQ 95
Cdd:pfam08397   1 YKTIMEQFN---PALENFIYKGNNYLSALRTTVEAAEAYFDAFQKVGEMATNSRG-SRELGSALTQMCMRHRSIESKLEQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  96 FSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKvdaqGRGDIQPQLDSALQDVND 175
Cdd:pfam08397  77 FVQAFHGGLLNPLEENTELDKKFANQLDKDYAKEYRHARAELKKCSSELLKLQKKADK----GKGDQQPQLDEALQDVND 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720383834 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 ...
 663-693 1.40e-13

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


Pssm-ID: 409203  Cd Length: 31  Bit Score: 64.73  E-value: 1.40e-13
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1720383834 663 ESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 693
Cdd:cd22060     1 DEPQGEDMLSAIRRGVKLRKTVTNDRSAPRI 31
PHA03247 PHA03247
large tegument protein UL36; Provisional
 503-693 2.19e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 2.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  503 AKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKT---PTVPDLPGVLPSPPDGPEER 579
Cdd:PHA03247  2766 PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAspaGPLPPPTSAQPTAPPPPPGP 2845

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  580 GEHS----------------PESPSAGEGPQGVSNIPSSLWSGQAPVNP--PLPGPKPSIPeehRQAIPESEAEDQERDP 641
Cdd:PHA03247  2846 PPPSlplggsvapggdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSteSFALPPDQPE---RPPQPQAPPPPQPQPQ 2922

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720383834  642 PSATVSPGPIPESDP---ADLSPRESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 693
Cdd:PHA03247  2923 PPPPPQPQPPPPPPPrpqPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRF 2977
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 110-195 1.14e-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: 39.87  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  110 EQMEEWKKVANQLD---KDHAKEYKKARQEIKKKSSdtlKLQKKAKKVDAQGRGDIQPQLDSALQDVNDKYLLLEE---T 183
Cdd:smart00935  11 QESPAGKAAQKQLEkefKKRQAELEKLEKELQKLKE---KLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQdlqK 87

                           90
                   ....*....|..
gi 1720383834  184 EKQAVRKALIEE 195
Cdd:smart00935  88 RQQEELQKILDK 99
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 457-665 1.75e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.68  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834 457 TIPSQVSDYDYFSVSgDQEAEQQEFD--------KSSTIPRNSDISQSYRRMFQAKRPASTAGLPTTLGPAMVTPGVATI 528
Cdd:pfam03154 144 TSPSIPSPQDNESDS-DSSAQQQILQtqppvlqaQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQ 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834 529 rrTPSTKPSVRRGTIGAGPIPIKTPVIPVKTPTVPDLPGVLPSPP------DGPEERGEHSPES-PSAGEGPQGVSNIPS 601
Cdd:pfam03154 223 --STAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPlpqpslHGQMPPMPHSLQTgPSHMQHPVPPQPFPL 300

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720383834 602 SLWSGQAPVnPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPgPIPESDPADLSPRESP 665
Cdd:pfam03154 301 TPQSSQSQV-PPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLP-PAPLSMPHIKPPPTTP 362
WH2 pfam02205
WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in ...
 664-689 9.81e-03

WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in WASP and Scar1 (mammalian homolog) to be the region that interacts with actin.


Pssm-ID: 460490  Cd Length: 28  Bit Score: 34.01  E-value: 9.81e-03
                          10        20
                  ....*....|....*....|....*..
gi 1720383834 664 SPQGEDMLNAIRRGVKLKKT-TTNDRS 689
Cdd:pfam02205   2 GGGRGALLADIRAGKKLKKVeETNDRS 28
 
Name Accession Description Interval E-value
I-BAR_IMD_MIM cd07643
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; ...
 7-241 7.93e-163

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. Members of this subfamily include missing in metastasis (MIM) or metastasis suppressor 1 (MTSS1), metastasis suppressor 1-like (MTSSL) or ABBA (Actin-Bundling protein with BAIAP2 homology), and similar proteins. They contain an N-terminal IMD and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. MIM was originally identified as a missing transcript from metastatic bladder and prostate cancer cells. It is a scaffold protein that functions in a signaling pathway between the PDGF receptor, Src kinases, and actin assembly. It may also function as a cofactor of the Sonic hedgehog (Shh) transcriptional pathway and may participate in tumor development and progression via this pathway. ABBA regulates actin and plasma membrane dynamics to promote the extension of radial glia, which is important in neuronal migration, axon guidance and neurogenesis. The IMD domain of MIM binds and bundles actin filaments, binds membranes, and interacts with the small GTPase Rac.


Pssm-ID: 153327  Cd Length: 231  Bit Score: 467.31  E-value: 7.93e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834   7 KECSALGGLFQTIISDMKGSYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGGTREIGSALTRMCMRH 86
Cdd:cd07643     1 KECSALGGLFQAIINDMKGSYPLWEDFVSKATKLHSQLRATIVATSAFLDAFQKIADAATNTRGATKEIGSALTRMCMRH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  87 RSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKvdaqGRGDIQPQL 166
Cdd:cd07643    81 KSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTIRLQKKARK----GKGDLQPQL 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720383834 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 6.96e-114

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: 341.47  E-value: 6.96e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  16 FQTIISDMKgsyPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHRSIEAKLRQ 95
Cdd:pfam08397   1 YKTIMEQFN---PALENFIYKGNNYLSALRTTVEAAEAYFDAFQKVGEMATNSRG-SRELGSALTQMCMRHRSIESKLEQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  96 FSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKvdaqGRGDIQPQLDSALQDVND 175
Cdd:pfam08397  77 FVQAFHGGLLNPLEENTELDKKFANQLDKDYAKEYRHARAELKKCSSELLKLQKKADK----GKGDQQPQLDEALQDVND 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720383834 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 4.29e-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: 264.61  E-value: 4.29e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  10 SALGGLFQTIISDMKG-SYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHRS 88
Cdd:cd07605     1 EELNRLTENIYKNIKEqFNPVLRNLIKAGKKYQKALQALSQAAKVFFDALAKIGELASQSRG-SQELGEALKQIVDTHKS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  89 IEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKVdaqGRGDIQPQLDS 168
Cdd:cd07605    80 IEASLEQVAKAFHGELILPLEKKLELDQKVINKFEKDYKKEYKQKREDLDKARSELKKLQKKSQKS---GTGKYQEKLDQ 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720383834 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 2.15e-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: 77.87  E-value: 2.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  19 IISDMKGSYPVWEDFINKAGKLQSQLRTtvvaAAAFLDAFQKVADMATNtrggtrEIGSALTRMCMRHRSIEAKLRQFSS 98
Cdd:cd07307     2 LDELEKLLKKLIKDTKKLLDSLKELPAA----AEKLSEALQELGKELPD------LSNTDLGEALEKFGKIQKELEEFRD 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  99 ALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKvdaqgrGDIQPQLDSALQDVNDKYL 178
Cdd:cd07307    72 QLEQKLENKVIEPLKEYLKKDLKEIKKRRKKLDKARLDYDAAREKLKKLRKKKKD------SSKLAEAEEELQEAKEKYE 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1720383834 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 ...
 663-693 1.40e-13

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


Pssm-ID: 409203  Cd Length: 31  Bit Score: 64.73  E-value: 1.40e-13
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1720383834 663 ESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 693
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 2.13e-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: 2.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  15 LFQTIISDMKgsyPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHRSIEAKLR 94
Cdd:cd07646    12 VYKTIMEQFN---PSLRNFIAMGKNYEKALASVTFAAKGYFDALVKMGELASESQG-SKELGDVLFQMAEVHRQIQNQLE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  95 QfssaLIDCLINPLQEQMEewKKVanQLDKDH-AKEYKKARQEIKKKSSDTLKLQKKAKKVDAQGRGDIQPQL--DSALQ 171
Cdd:cd07646    88 E----MLKSFHNELLTQLE--QKV--ELDSRYlTAALKKYQTEHRSKGESLEKCQAELKKLRKKSQGSKNPQKysDKELQ 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1720383834 172 DV---NDKYLLLEETEKQAVRKALIEERGRFC 200
Cdd:cd07646   160 YIeaiSNKQGELENYVSDGYKTALTEERRRYC 191
PHA03247 PHA03247
large tegument protein UL36; Provisional
 503-693 2.19e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 2.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  503 AKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKT---PTVPDLPGVLPSPPDGPEER 579
Cdd:PHA03247  2766 PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAspaGPLPPPTSAQPTAPPPPPGP 2845

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  580 GEHS----------------PESPSAGEGPQGVSNIPSSLWSGQAPVNP--PLPGPKPSIPeehRQAIPESEAEDQERDP 641
Cdd:PHA03247  2846 PPPSlplggsvapggdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSteSFALPPDQPE---RPPQPQAPPPPQPQPQ 2922

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720383834  642 PSATVSPGPIPESDP---ADLSPRESPQGEDMLNAIRRGVKLKKTTTNDRSAPRF 693
Cdd:PHA03247  2923 PPPPPQPQPPPPPPPrpqPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRF 2977
I-BAR_IMD_BAIAP2L1 cd07645
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Brain-specific ...
 28-200 3.53e-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: 45.68  E-value: 3.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  28 PVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGgTREIGSALTRMCMRHR----SIEAKLRQFSSALIdc 103
Cdd:cd07645    20 PGLRNLINLGKNYEKAVNAMVLAGKAYYDGVAKIGEIAAVSPV-SKELGHVLMEISDVHKklndSLEENFKKFHREII-- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834 104 liNPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAkkvdaQGRGDI---QPQLDSALQDVNDKYLLL 180
Cdd:cd07645    97 --AELERKTDLDVKYMTATLKRYQTEHKNKLDSLEKSQADLKKIRRKS-----QGRRNAskyEHKENEYLETVTSRQSDI 169

                         170       180
                  ....*....|....*....|
gi 1720383834 181 EETEKQAVRKALIEERGRFC 200
Cdd:cd07645   170 QKFIADGCREALLEEKRRFC 189
PHA03247 PHA03247
large tegument protein UL36; Provisional
 506-667 3.99e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 3.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  506 PASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPvKTPTVPDLPGVLPSPPDGPEERGEHSPE 585
Cdd:PHA03247  2713 HALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTT-AGPPAPAPPAAPAAGPPRRLTRPAVASL 2791

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  586 SPSAGEGPqgvsnipssLWSGQAPVNPPLPGPKPSIPEEHRQAIPEseaedqerdPPSATVSPGPiPESDPADLSPRESP 665
Cdd:PHA03247  2792 SESRESLP---------SPWDPADPPAAVLAPAAALPPAASPAGPL---------PPPTSAQPTA-PPPPPGPPPPSLPL 2852


                   ..
gi 1720383834  666 QG 667
Cdd:PHA03247  2853 GG 2854
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 544-692 7.08e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 46.11  E-value: 7.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834 544 GAGPIPIKTPVIPVKTPTVPDLPGVLPSPPDGP------EERGEHSPESPSAGEGPQGVSNIPSslwsgqaPVNPPLPGP 617
Cdd:PTZ00441  336 GKDGNPNEENLFPPGDDEVPDESNVPPNPPNVPggsnseFSSDVENPPNPPNPDIPEQEPNIPE-------DSNKEVPED 408

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720383834 618 KPSIPEEHR-QAIPESEAEDQERDPPSATVSPGPIP-ESDPADLSPRESPQGEDmlNAIRRGVKLKKTTTNDRSAPR 692
Cdd:PTZ00441  409 VPMEPEDDRdNNFNEPKKPENKGDGQNEPVIPKPLDnERDQSNKNKQVNPGNRH--NSEDRYTRPHGRNNENRNYNN 483
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 503-676 7.73e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 7.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  503 AKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSvrrgtiGAGPIPIKTPVIPVKTPtVPDLPGVLPSPPdGPEERGEH 582
Cdd:PHA03307    79 APANESRSTPTWSLSTLAPASPAREGSPTPPGPSS------PDPPPPTPPPASPPPSP-APDLSEMLRPVG-SPGPPPAA 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  583 SPESPSAGEGPqgvsnipsslwSGQAPVNPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPGPIPESDPADLSPR 662
Cdd:PHA03307   151 SPPAAGASPAA-----------VASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASS 219

                          170
                   ....*....|....
gi 1720383834  663 ESPQGEDMLNAIRR 676
Cdd:PHA03307   220 PAPAPGRSAADDAG 233
WH2_WAS_WASL cd22064
Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein (WIP); ...
 664-691 1.79e-04

Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein (WIP); This family contains the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) found in WAS/WASL-interacting protein family (WIPF, also known as WASP-interacting protein or WIP). Human WIP protein is proline rich and has high sequence similarity to yeast protein verprolin (included in this model). WIP forms complexes with WASP/N-WASP and modulates their function in vivo. It is involved in the regulation of endocytosis and participates in several cellular processes, some of which are relevant in cancer and may be dependent on different oncogenic stimuli. WIP interacts directly with mammalian actin-binding protein-1 (mABP1) via the SH3 domain during platelet-derived growth factor (PDGF)-mediated dorsal ruffle formation. WIP family includes members 1 (WAS/WASL-interacting protein family member 1) or WIPF1), 2 (WIPF2) and 3 (WIPF3). Aberrant expression of WIPF1 contributes to the invasion and metastasis of several malignancies such breast cancer, glioma and colorectal cancer; it has been identified as an oncoprotein in human pancreatic ductal adenocarcinoma (PDAC) and is associated with poor survival. WIPF2 may be an important regulator of the actin cytoskeleton. WIPF2 binds to N-WASP, regulating actin dynamics close to the plasma membrane; N-WASP in turn controls the second phase insulin secretion through the regulation of the Arp2/3 complex. WIPF3, along with LIPA (lysosomal acid lipase A), are expressed in microphages and are involved in pathological abdominal aortic aneurysm (AAA), a serious condition of the aorta. In yeast, verprolin is involved in cytoskeletal organization and cellular growth. It may exert its effects on the cytoskeleton directly, or indirectly via proline-binding proteins, such as profilin, or via proteins possessing SH3 domains.


Pssm-ID: 409207 [Multi-domain]  Cd Length: 29  Bit Score: 38.99  E-value: 1.79e-04
                          10        20
                  ....*....|....*....|....*....
gi 1720383834 664 SPQGED-MLNAIRRGVKLKKTTTNDRSAP 691
Cdd:cd22064     1 EQKGRGaLLGDIRKGMKLKKTVTNDRSAP 29
PHA03247 PHA03247
large tegument protein UL36; Provisional
 503-665 2.07e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  503 AKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPS-------------------VRRGTIGAGP----IPIKTPVIPVKT 559
Cdd:PHA03247  2809 AAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPgppppslplggsvapggdvRRRPPSRSPAakpaAPARPPVRRLAR 2888

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  560 PTVPDLPGVLPSPPDGPEErgehsPESPSAGEGPQGVSNIPSSlwsGQAPVNPPLPGPKPSIPEEHRQAIPESEAEDQER 639
Cdd:PHA03247  2889 PAVSRSTESFALPPDQPER-----PPQPQAPPPPQPQPQPPPP---PQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVP 2960

                          170       180
                   ....*....|....*....|....*....
gi 1720383834  640 DPPSATVSPGPIP---ESDPADLSPRESP 665
Cdd:PHA03247  2961 QPWLGALVPGRVAvprFRVPQPAPSREAP 2989
PHA03247 PHA03247
large tegument protein UL36; Provisional
 523-667 2.65e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 2.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  523 PGVATIRRTPSTK-PSVRRGTIGAGPIPIKTPVIPvKTPTVPdLPGVLPSPPDGPEE--------RGEHSPESPSAGEGP 593
Cdd:PHA03247  2475 PGAPVYRRPAEARfPFAAGAAPDPGGGGPPDPDAP-PAPSRL-APAILPDEPVGEPVhprmltwiRGLEELASDDAGDPP 2552

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  594 QGVSNIPSSLWSGQApVNPPLPGPKPSIP----EEHRQAIPESEAEDQ----ERDPPSATVSPGPIPesdPADLSPRESP 665
Cdd:PHA03247  2553 PPLPPAAPPAAPDRS-VPPPRPAPRPSEPavtsRARRPDAPPQSARPRapvdDRGDPRGPAPPSPLP---PDTHAPDPPP 2628


                   ..
gi 1720383834  666 QG 667
Cdd:PHA03247  2629 PS 2630
PHA03247 PHA03247
large tegument protein UL36; Provisional
 518-659 6.95e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 6.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  518 PAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPV-IPVKTPTVPDLPGVLPSPPDGPEERGEhspesPSAGEGPqgv 596
Cdd:PHA03247   375 PKRASLPTRKRRSARHAATPFARGPGGDDQTRPAAPVpASVPTPAPTPVPASAPPPPATPLPSAE-----PGSDDGP--- 446

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720383834  597 snipsslwsgqapvnPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPGPiPESDPADL 659
Cdd:PHA03247   447 ---------------APPPERQPPAPATEPAPDDPDDATRKALDALRERRPPEP-PGADLAEL 493
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 110-195 1.14e-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: 39.87  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  110 EQMEEWKKVANQLD---KDHAKEYKKARQEIKKKSSdtlKLQKKAKKVDAQGRGDIQPQLDSALQDVNDKYLLLEE---T 183
Cdd:smart00935  11 QESPAGKAAQKQLEkefKKRQAELEKLEKELQKLKE---KLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQdlqK 87

                           90
                   ....*....|..
gi 1720383834  184 EKQAVRKALIEE 195
Cdd:smart00935  88 RQQEELQKILDK 99
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 556-650 1.48e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 41.53  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834 556 PVKTPTVPDLPGVLPSPPDGPEERGEHSPESPSA-GEGPQGVSNIPSSLWSGQAPVNPPLPGP-KPSIPEEHRQAIPESE 633
Cdd:PHA03264  263 GYEPPPAPSGGSPAPPGDDRPEAKPEPGPVEDGApGRETGGEGEGPEPAGRDGAAGGEPKPGPpRPAPDADRPEGWPSLE 342

                          90
                  ....*....|....*..
gi 1720383834 634 AEDQerdPPSATVSPGP 650
Cdd:PHA03264  343 AITF---PPPTPATPAV 356
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 457-665 1.75e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.68  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834 457 TIPSQVSDYDYFSVSgDQEAEQQEFD--------KSSTIPRNSDISQSYRRMFQAKRPASTAGLPTTLGPAMVTPGVATI 528
Cdd:pfam03154 144 TSPSIPSPQDNESDS-DSSAQQQILQtqppvlqaQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQ 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834 529 rrTPSTKPSVRRGTIGAGPIPIKTPVIPVKTPTVPDLPGVLPSPP------DGPEERGEHSPES-PSAGEGPQGVSNIPS 601
Cdd:pfam03154 223 --STAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPlpqpslHGQMPPMPHSLQTgPSHMQHPVPPQPFPL 300

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720383834 602 SLWSGQAPVnPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPgPIPESDPADLSPRESP 665
Cdd:pfam03154 301 TPQSSQSQV-PPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLP-PAPLSMPHIKPPPTTP 362
PHA03247 PHA03247
large tegument protein UL36; Provisional
 476-692 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 1720383834  476 AEQQEFDKSSTIPRNSDISQSYRRMFQAKRPASTA------GLPTTLGPAM---------VTPGVATIRRTPSTK-PSVR 539
Cdd:PHA03247  2646 VPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPqrprrrAARPTVGSLTsladpppppPTPEPAPHALVSATPlPPGP 2725

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  540 RGTIGAGPIPIKTPVIPvKTPTVPDLPGVLPSPPDGPEERGEHSPESPSA-GEGPQGVSNIPSSlwsgqAPVNPPLPG-P 617
Cdd:PHA03247  2726 AAARQASPALPAAPAPP-AVPAGPATPGGPARPARPPTTAGPPAPAPPAApAAGPPRRLTRPAV-----ASLSESRESlP 2799

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720383834  618 KPSIPEEHRQAIPESEAEDQERDPPSATVSPGPIPESDPADLSPRESPQGEDMLNAIRRGVKLKKTTTNDRSAPR 692
Cdd:PHA03247  2800 SPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAK 2874
WH2_WAS_WASL-1 cd22076
Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein family ...
 670-691 2.10e-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: 36.10  E-value: 2.10e-03
                          10        20
                  ....*....|....*....|..
gi 1720383834 670 MLNAIRRGVKLKKTTTNDRSAP 691
Cdd:cd22076     8 LLSDINKGKKLKKTVTNDRSAP 29
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
 101-176 3.52e-03

calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).


Pssm-ID: 409646 [Multi-domain]  Cd Length: 149  Bit Score: 38.64  E-value: 3.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720383834 101 IDCL--INPLQEQMEEWKKVANQLDKDhaKEykKARQEIKKKSSDTLKLQKKAKKVDAQGRGDIQPQLDSALQDVNDK 176
Cdd:cd21759    68 IKGLrkIRALEKQLKEMEEIASQLKKD--KD--KWTKQVKELKKEIDALIKKIKTNDMITRKEIDKLYNALVKKVDKQ 141
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 502-680 3.84e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834 502 QAKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRrGTIGAGPIPIKTPVIPvkTPTVPDLPGVLPSPPDGPEERGE 581
Cdd:PRK07764  632 AAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW-PAKAGGAAPAAPPPAP--APAAPAAPAGAAPAQPAPAPAAT 708

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834 582 HSPE-SPSAGEGPQGVSNIPSSLWSGQAPVNPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPGPIPESDPADLS 660
Cdd:PRK07764  709 PPAGqADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAED 788

                         170       180
                  ....*....|....*....|
gi 1720383834 661 PRESPQGEDMLNAIRRGVKL 680
Cdd:PRK07764  789 DAPSMDDEDRRDAEEVAMEL 808
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 518-668 3.90e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.54  E-value: 3.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  518 PAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKTPTV-PDLPGVLPSPPDGPEERGEHSPESPsAGEGPQGV 596
Cdd:PHA03307    53 VTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPaSPAREGSPTPPGPSSPDPPPPTPPP-ASPPPSPA 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  597 SNIPSSLWSGQAPVNPPL---------PGPKPSIPEEHRQ-AIPESEAEDQERDPPSATVSPGPIPesDPADLSPRESPQ 666
Cdd:PHA03307   132 PDLSEMLRPVGSPGPPPAasppaagasPAAVASDAASSRQaALPLSSPEETARAPSSPPAEPPPST--PPAAASPRPPRR 209


                   ..
gi 1720383834  667 GE 668
Cdd:PHA03307   210 SS 211
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 503-676 5.03e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.15  E-value: 5.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  503 AKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRG----TIGAGPIPIKTPVIPVKTPTVPDLPGVLPSPPDGPEE 578
Cdd:PHA03307   157 ASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPstppAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASS 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834  579 RGEHSPESPSAGEGPQGvsnipsslwsgQAPVNPPLPGPKPSIPEEHRQAIPE--------SEAEDQERDPPSATVSPGP 650
Cdd:PHA03307   237 SDSSSSESSGCGWGPEN-----------ECPLPRPAPITLPTRIWEASGWNGPssrpgpasSSSSPRERSPSPSPSSPGS 305

                          170       180
                   ....*....|....*....|....*.
gi 1720383834  651 IPESDPADLSPRESPQGEDMLNAIRR 676
Cdd:PHA03307   306 GPAPSSPRASSSSSSSRESSSSSTSS 331
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 427-661 5.86e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.14  E-value: 5.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834 427 QLDVQRSSRDSLQCSSGYSTQTTTPCCSEDTIPSQVSDYDYFSVSgdqeaeQQEFDKSSTIPRNSDISQSYRRMFQAKRP 506
Cdd:pfam03154 163 QQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVP------PQGSPATSQPPNQTQSTAAPHTLIQQTPT 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834 507 ASTAGLPTTLGPAMVTPGVATIRRTP--STKPSVRRGTIGAGPIPIKT--PVIPVKTPTVPdlpgvLPSPPDGPEERGEH 582
Cdd:pfam03154 237 LHPQRLPSPHPPLQPMTQPPPPSQVSpqPLPQPSLHGQMPPMPHSLQTgpSHMQHPVPPQP-----FPLTPQSSQSQVPP 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834 583 SPESPSAGEGPQGVSNIPS--SLWSGQAPVN---PPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATvspGPIPESDPA 657
Cdd:pfam03154 312 GPSPAAPGQSQQRIHTPPSqsQLQSQQPPREqplPPAPLSMPHIKPPPTTPIPQLPNPQSHKHPPHLS---GPSPFQMNS 388


                  ....
gi 1720383834 658 DLSP 661
Cdd:pfam03154 389 NLPP 392
PHA03418 PHA03418
hypothetical E4 protein; Provisional
 535-619 6.11e-03

hypothetical E4 protein; Provisional


Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 38.95  E-value: 6.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834 535 KPSVRRGTIGAGPIPIKTPVIPVKTPTVPDLPGVLPSPPDG--------PEERGEHSPESPSAGEGPQgvsnipsslwSG 606
Cdd:PHA03418  102 RPGKRSKADEHGPAPGRAALAPFKLDLDQDPLHGDPDPPPGatggqgeePPEGGEESQPPLGEGEGAV----------EG 171

                          90
                  ....*....|...
gi 1720383834 607 QAPVNPPLPGPKP 619
Cdd:PHA03418  172 HPPPLPPAPEPKP 184
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 503-684 8.33e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 39.41  E-value: 8.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834 503 AKRPASTAGLPTTLGPAMVTPGVAtirrtPSTKPSvrrgTIGAGPIPIKTPVIPVKTPTvpdlpgvlPSPPDgpeergeh 582
Cdd:PRK14950  361 VPVPAPQPAKPTAAAPSPVRPTPA-----PSTRPK----AAAAANIPPKEPVRETATPP--------PVPPR-------- 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834 583 spespsagegpqgvsnipsslwsgqaPVNPPLPGPKPSIPEEHRQAIPESEAEDQERDPP-----SATVSPGPIPE---- 653
Cdd:PRK14950  416 --------------------------PVAPPVPHTPESAPKLTRAAIPVDEKPKYTPPAPpkeeeKALIADGDVLEqlea 469

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1720383834 654 --SDPADLSPRESPQGEDMLNAIRRGVKLKKTT 684
Cdd:PRK14950  470 iwKQILRDVPPRSPAVQALLSSGVRPVSVEKNT 502
PHA03378 PHA03378
EBNA-3B; Provisional
 518-676 9.04e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.28  E-value: 9.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834 518 PAMVTPGVATIRRTPSTKPSVRRgTIGAGPIPIKTPVIPVKTPTVPDLPGVLPSPPDGPEERGEHSPESPSAGEGPQGVS 597
Cdd:PHA03378  673 PYQPSPTGANTMLPIQWAPGTMQ-PPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAP 751

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383834 598 NIPSSLWSGQAPVNPPLPGPKPSIPEEHRQAIPESeaedqeRDPPSATVSPGPIPESDPAD--LSPRESPQGEDMLNAIR 675
Cdd:PHA03378  752 GRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAP------QQRPRGAPTPQPPPQAGPTSmqLMPRAAPGQQGPTKQIL 825


                  .
gi 1720383834 676 R 676
Cdd:PHA03378  826 R 826
WH2 pfam02205
WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in ...
 664-689 9.81e-03

WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in WASP and Scar1 (mammalian homolog) to be the region that interacts with actin.


Pssm-ID: 460490  Cd Length: 28  Bit Score: 34.01  E-value: 9.81e-03
                          10        20
                  ....*....|....*....|....*..
gi 1720383834 664 SPQGEDMLNAIRRGVKLKKT-TTNDRS 689
Cdd:pfam02205   2 GGGRGALLADIRAGKKLKKVeETNDRS 28
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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