NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|976902975|gb|KVH90902|]
View 

ENTH/VHS-like protein [Cynara cardunculus var. scolymus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 25-146 1.25e-63

ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in endocytosis and cytoskeletal machinery. The function of the ENTH domain is unknown.


:

Pssm-ID: 426255  Cd Length: 124  Bit Score: 208.95  E-value: 1.25e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975   25 SIEQKVLDATSNEPWGPHGTHLADIAQASRNYHEYQMIMSVVWKRINDTGKNWRHVYKALTILDYLVANGSERVIDDIRE 104
Cdd:pfam01417   3 ETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLNDKGKNWRHIYKALTLLEYLLKNGSERVVDDLRE 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 976902975  105 HAYQISTLSTFQYIDSTGRDQGSNVRKKSQSLVALVNDKERI 146
Cdd:pfam01417  83 NIYIIRTLTDFHYIDENGKDQGINVRKKAKEILNLLEDDELL 124
PAT1 super family cl37801
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 443-618 1.57e-08

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


The actual alignment was detected with superfamily member pfam09770:

Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 58.51  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  443 APSQTAFQAQPDQLSTQTIFSSQTGQP--SLQTGYAP---QAGHPSSQtvfsAQPNQTTFPSSFPGQFGQPTLQPSFPSQ 517
Cdd:pfam09770 166 APKKAAAPAPAPQPAAQPASLPAPSRKmmSLEEVEAAmraQAKKPAQQ----PAPAPAQPPAAPPAQQAQQQQQFPPQIQ 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  518 GGPPMPHHGFQPPGAQ------SILQ--PGFSPQGGQPMPQPAFPAIGGNPPmPQPSFPAQGGQSISQPGFLAQGGNQSM 589
Cdd:pfam09770 242 QQQQPQQQPQQPQQHPgqghpvTILQrpQSPQPDPAQPSIQPQAQQFHQQPP-PVPVQPTQILQNPNRLSAARVGYPQNP 320

                         170       180
                  ....*....|....*....|....*....
gi 976902975  590 PQPSFPAQGGQSVLQAGFLAQGGHSMLQP 618
Cdd:pfam09770 321 QPGVQPAPAHQAHRQQGSFGRQAPIITHP 349
SF-CC1 super family cl36939
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
 157-265 1.90e-06

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


The actual alignment was detected with superfamily member TIGR01622:

Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 51.46  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  157 REKFRTSGGGMNRpyDDDRYEGRYGSRDEDhngygREKEWGDDRyGRDGGRYGeDGYRDDEYRGRSRSIDGDYGPRSRSS 236
Cdd:TIGR01622   7 RERLRDSSSAGDR--DRRRDKGRERSRDRS-----RDRERSRSR-RRDRHRDR-DYYRGRERRSRSRRPNRRYRPREKRR 77

                          90       100
                  ....*....|....*....|....*....
gi 976902975  237 DRERERAFEDDgHHSSRGSNVRAEDGPLD 265
Cdd:TIGR01622  78 RRGDSYRRRRD-DRRSRREKPRARDGTPE 105
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 463-818 2.76e-05

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 47.70  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  463 SSQTGQPSLQTGYAPQAGHPSSQtvfSAQPNQTTFPSSFPGQFGQPTLQPSFPSQGGPPMPHHGFQPPGAQSILQPGFSP 542
Cdd:pfam09606  54 SKKAAQQQQPQGGQGNGGMGGGQ---QGMPDPINALQNLAGQGTRPQMMGPMGPGPGGPMGQQMGGPGTASNLLASLGRP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  543 Q-----GGQPMPQPAFPAI---GGNPPMPQPSFPAQGGQSISQPG----------FLAQGGNQSMPQPSFPAQGGQSVLQ 604
Cdd:pfam09606 131 QmpmggAGFPSQMSRVGRMqpgGQAGGMMQPSSGQPGSGTPNQMGpnggpgqgqaGGMNGGQQGPMGGQMPPQMGVPGMP 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  605 AGFLAQGGHSMLQPGFPAQVPQPGFAAQGGHSMPQSGFAAQGGQSVLQPGfAPQGGQSASMISGFSQAGFPTktNPLSDI 684
Cdd:pfam09606 211 GPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMG-INQMQQMPQGVGGGAGQGGPG--QPMGPP 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  685 GIDFEAINRKEKRMEKPSKTPVTSNVTMGKAMGSGTGIGRagagtlraaSNPMVGSGMGITMGAPGPRPGFGAGYGGVNQ 764
Cdd:pfam09606 288 GQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQ---------QQMNQSVGQGGQVVALGGLNHLETWNPGNFG 358

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 976902975  765 PMGMNNMQQNMGIGMNIGQGFQMQQPPAGFPLGSaMPANYNPMLGRGAGYGQQP 818
Cdd:pfam09606 359 GLGANPMQRGQPGMMSSPSPVPGQQVRQVTPNQF-MRQSPQPSVPSPQGPGSQP 411
 
Name Accession Description Interval E-value
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 25-146 1.25e-63

ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in endocytosis and cytoskeletal machinery. The function of the ENTH domain is unknown.


Pssm-ID: 426255  Cd Length: 124  Bit Score: 208.95  E-value: 1.25e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975   25 SIEQKVLDATSNEPWGPHGTHLADIAQASRNYHEYQMIMSVVWKRINDTGKNWRHVYKALTILDYLVANGSERVIDDIRE 104
Cdd:pfam01417   3 ETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLNDKGKNWRHIYKALTLLEYLLKNGSERVVDDLRE 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 976902975  105 HAYQISTLSTFQYIDSTGRDQGSNVRKKSQSLVALVNDKERI 146
Cdd:pfam01417  83 NIYIIRTLTDFHYIDENGKDQGINVRKKAKEILNLLEDDELL 124
ENTH cd03571
Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is ...
 26-142 1.78e-63

Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, contributing to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340772  Cd Length: 117  Bit Score: 208.14  E-value: 1.78e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  26 IEQKVLDATSNEPWGPHGTHLADIAQASRNYHEYQMIMSVVWKRINDTGKNWRHVYKALTILDYLVANGSERVIDDIREH 105
Cdd:cd03571    1 LELLVREATSNEPWGPTGSQLAEIAQATFDYDDYQRIMKVLWKRLNDKGKNWRHVYKALTLLEYLLKNGSERVVDEFRDN 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 976902975 106 AYQISTLSTFQYIDSTGRDQGSNVRKKSQSLVALVND 142
Cdd:cd03571   81 LYLIRTLQDFQYVDENGDDQGINVREKAKQIVALLED 117
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
24-150 1.45e-45

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 159.33  E-value: 1.45e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975    24 PSIEQKVLDATSNEPWGPHGTHLADIAQASRNY-HEYQMIMSVVWKRINDTGkNWRHVYKALTILDYLVANGSERVIDDI 102
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEkSSFAEIMAVLWRRLNDTK-NWRVVYKALILLHYLLRNGSPRVILEA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 976902975   103 REHAYQISTLSTFQYIDSTGRDQGSNVRKKSQSLVALVNDKERIQEVR 150
Cdd:smart00273  80 LRNRNRILNLSDFQDIDSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 443-618 1.57e-08

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 58.51  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  443 APSQTAFQAQPDQLSTQTIFSSQTGQP--SLQTGYAP---QAGHPSSQtvfsAQPNQTTFPSSFPGQFGQPTLQPSFPSQ 517
Cdd:pfam09770 166 APKKAAAPAPAPQPAAQPASLPAPSRKmmSLEEVEAAmraQAKKPAQQ----PAPAPAQPPAAPPAQQAQQQQQFPPQIQ 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  518 GGPPMPHHGFQPPGAQ------SILQ--PGFSPQGGQPMPQPAFPAIGGNPPmPQPSFPAQGGQSISQPGFLAQGGNQSM 589
Cdd:pfam09770 242 QQQQPQQQPQQPQQHPgqghpvTILQrpQSPQPDPAQPSIQPQAQQFHQQPP-PVPVQPTQILQNPNRLSAARVGYPQNP 320

                         170       180
                  ....*....|....*....|....*....
gi 976902975  590 PQPSFPAQGGQSVLQAGFLAQGGHSMLQP 618
Cdd:pfam09770 321 QPGVQPAPAHQAHRQQGSFGRQAPIITHP 349
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
 157-265 1.90e-06

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 51.46  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  157 REKFRTSGGGMNRpyDDDRYEGRYGSRDEDhngygREKEWGDDRyGRDGGRYGeDGYRDDEYRGRSRSIDGDYGPRSRSS 236
Cdd:TIGR01622   7 RERLRDSSSAGDR--DRRRDKGRERSRDRS-----RDRERSRSR-RRDRHRDR-DYYRGRERRSRSRRPNRRYRPREKRR 77

                          90       100
                  ....*....|....*....|....*....
gi 976902975  237 DRERERAFEDDgHHSSRGSNVRAEDGPLD 265
Cdd:TIGR01622  78 RRGDSYRRRRD-DRRSRREKPRARDGTPE 105
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 463-818 2.76e-05

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 47.70  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  463 SSQTGQPSLQTGYAPQAGHPSSQtvfSAQPNQTTFPSSFPGQFGQPTLQPSFPSQGGPPMPHHGFQPPGAQSILQPGFSP 542
Cdd:pfam09606  54 SKKAAQQQQPQGGQGNGGMGGGQ---QGMPDPINALQNLAGQGTRPQMMGPMGPGPGGPMGQQMGGPGTASNLLASLGRP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  543 Q-----GGQPMPQPAFPAI---GGNPPMPQPSFPAQGGQSISQPG----------FLAQGGNQSMPQPSFPAQGGQSVLQ 604
Cdd:pfam09606 131 QmpmggAGFPSQMSRVGRMqpgGQAGGMMQPSSGQPGSGTPNQMGpnggpgqgqaGGMNGGQQGPMGGQMPPQMGVPGMP 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  605 AGFLAQGGHSMLQPGFPAQVPQPGFAAQGGHSMPQSGFAAQGGQSVLQPGfAPQGGQSASMISGFSQAGFPTktNPLSDI 684
Cdd:pfam09606 211 GPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMG-INQMQQMPQGVGGGAGQGGPG--QPMGPP 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  685 GIDFEAINRKEKRMEKPSKTPVTSNVTMGKAMGSGTGIGRagagtlraaSNPMVGSGMGITMGAPGPRPGFGAGYGGVNQ 764
Cdd:pfam09606 288 GQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQ---------QQMNQSVGQGGQVVALGGLNHLETWNPGNFG 358

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 976902975  765 PMGMNNMQQNMGIGMNIGQGFQMQQPPAGFPLGSaMPANYNPMLGRGAGYGQQP 818
Cdd:pfam09606 359 GLGANPMQRGQPGMMSSPSPVPGQQVRQVTPNQF-MRQSPQPSVPSPQGPGSQP 411
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 441-569 5.37e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 47.00  E-value: 5.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  441 PSAPSQTAFQAQPdQLSTQTIFSSQTGQPSLQ---TGYAPQAGHPSSQTVFSA---QPNQTTFPSSFPGQF--------- 505
Cdd:PRK10263  344 PPVASVDVPPAQP-TVAWQPVPGPQTGEPVIApapEGYPQQSQYAQPAVQYNEplqQPVQPQQPYYAPAAEqpaqqpyya 422

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 976902975  506 ---GQPTLQPSFPSQGGPPMPHHGFQPPGAQSILQPGFSPQGGQPMPQPAFPAIGGNPPMPQPSFPA 569
Cdd:PRK10263  423 papEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPV 489
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 489-609 7.57e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.87  E-value: 7.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  489 SAQPNQTTFPSSFPGQFGQPTLQPSFPSQ--GGPPMPHHGFQPPGAQSILQPGFSPQGGQPMPQ------PAFPAIGGNP 560
Cdd:TIGR01628 379 QPRMRQLPMGSPMGGAMGQPPYYGQGPQQqfNGQPLGWPRMSMMPTPMGPGGPLRPNGLAPMNAvrapsrNAQNAAQKPP 458

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 976902975  561 PMPQPSFPAQGGQSISQPgflaqggnqsMPQP-SFPAQGGQSVLQAGFLA 609
Cdd:TIGR01628 459 MQPVMYPPNYQSLPLSQD----------LPQPqSTASQGGQNKKLAQVLA 498
PRP38_assoc pfam12871
Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region ...
 202-242 2.64e-03

Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region found at the C-terminus of plant and metazoan pre-mRNA-splicing factor 38 proteins. The function is not known.


Pssm-ID: 463734 [Multi-domain]  Cd Length: 98  Bit Score: 37.83  E-value: 2.64e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 976902975  202 GRDGGRYGEDGYRDDEYRGRSRSIDGDYGPRSRSSDRERER 242
Cdd:pfam12871  55 SRSRSRDRRSRGTRDRRRDRDRDRYRSLRSRSRDRSRDRDR 95
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 144-258 2.99e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 41.04  E-value: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975 144 ERIQEVREKAAANREKFRTSGGGMNRPYDDDRYEGRYGSRDEDHNGyGREKEWGDDRYGRDGGRYGEDGYRDDEYRGRSR 223
Cdd:PRK12678 173 RRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREER-GRRDGGDRRGRRRRRDRRDARGDDNREDRGDRD 251

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 976902975 224 SIDGDYGpRSRSSDRERERafEDDGHHSSRGSNVR 258
Cdd:PRK12678 252 GDDGEGR-GGRRGRRFRDR--DRRGRRGGDGGNER 283
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 498-571 4.72e-03

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 38.62  E-value: 4.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975   498 PSSFPGQFGQPTL-----QPSFPSQGGPPMPHHGFQPPGAQSILQPGFSPQGGQPMP--QPAFPAIggnPPMPQPSFPAQ 570
Cdd:smart00818  80 HSMTPTQHHQPNLpqpaqQPFQPQPLQPPQPQQPMQPQPPVHPIPPLPPQPPLPPMFpmQPLPPLL---PDLPLEAWPAT 156


                   .
gi 976902975   571 G 571
Cdd:smart00818 157 D 157
 
Name Accession Description Interval E-value
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 25-146 1.25e-63

ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in endocytosis and cytoskeletal machinery. The function of the ENTH domain is unknown.


Pssm-ID: 426255  Cd Length: 124  Bit Score: 208.95  E-value: 1.25e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975   25 SIEQKVLDATSNEPWGPHGTHLADIAQASRNYHEYQMIMSVVWKRINDTGKNWRHVYKALTILDYLVANGSERVIDDIRE 104
Cdd:pfam01417   3 ETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLNDKGKNWRHIYKALTLLEYLLKNGSERVVDDLRE 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 976902975  105 HAYQISTLSTFQYIDSTGRDQGSNVRKKSQSLVALVNDKERI 146
Cdd:pfam01417  83 NIYIIRTLTDFHYIDENGKDQGINVRKKAKEILNLLEDDELL 124
ENTH cd03571
Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is ...
 26-142 1.78e-63

Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, contributing to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340772  Cd Length: 117  Bit Score: 208.14  E-value: 1.78e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  26 IEQKVLDATSNEPWGPHGTHLADIAQASRNYHEYQMIMSVVWKRINDTGKNWRHVYKALTILDYLVANGSERVIDDIREH 105
Cdd:cd03571    1 LELLVREATSNEPWGPTGSQLAEIAQATFDYDDYQRIMKVLWKRLNDKGKNWRHVYKALTLLEYLLKNGSERVVDEFRDN 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 976902975 106 AYQISTLSTFQYIDSTGRDQGSNVRKKSQSLVALVND 142
Cdd:cd03571   81 LYLIRTLQDFQYVDENGDDQGINVREKAKQIVALLED 117
ENTH_Ent1_Ent2 cd16991
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent1, Ent2, and similar proteins; This ...
 25-150 1.60e-54

Epsin N-Terminal Homology (ENTH) domain of Yeast Ent1, Ent2, and similar proteins; This subfamily is composed of the two orthologs of epsin in Saccharomyces cerevisiae, Epsin-1 (Ent1 or Ent1p) and Epsin-2 (Ent2 or Ent2p), and similar proteins. Yeast single epsin knockouts, either Ent1 and Ent2, are viable while the double knockout is not. Yeast epsins are required for endocytosis and localization of actin. Ent2 also plays a signaling role during cell division. The ENTH domain of Ent2 interacts with the septin organizing, Cdc42 GTPase activating protein, Bem3, leading to increased cytokinesis failure when overexpressed. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340788  Cd Length: 132  Bit Score: 184.40  E-value: 1.60e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  25 SIEQKVLDATSNEPWGPHGTHLADIAQASRNYHEYQMIMSVVWKRINDTGKNWRHVYKALTILDYLVANGSERVIDDIRE 104
Cdd:cd16991    4 STQVKVRNATSNDPWGPSGDEMAEIAELTYDQHDFVEIMDMLDKRLNDKGKNWRHVAKALTVLDYLLHFGSENVVLWAKE 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 976902975 105 HAYQISTLSTFQYIDSTGRDQGSNVRKKSQSLVALVNDKERIQEVR 150
Cdd:cd16991   84 NIYIIKTLREFQYIDDEGKDQGQNVRVKAKELTSLLLDDERLREER 129
ENTH_EpsinR cd16989
Epsin N-Terminal Homology (ENTH) domain of Epsin-related protein; Epsin-related protein ...
 26-153 6.74e-53

Epsin N-Terminal Homology (ENTH) domain of Epsin-related protein; Epsin-related protein (EpsinR) is also called clathrin interactor 1 (Clint), enthoprotin, or epsin-4. It is a clathrin-coated vesicle (CCV) protein that binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), clathrin, and the gamma appendage domain of the adaptor protein complex 1 (AP1). It contains an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. The ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. The ENTH domain of human epsinR binds directly to the helical bundle domain of the mouse SNARE Vti1b; soluble NSF attachment protein receptors (SNAREs) are type II transmembrane proteins that have critical roles in providing the specificity and energy for transport-vesicle fusion. Specific ENTH domains may also function as protein cargo selection/recognition modules. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340786  Cd Length: 130  Bit Score: 179.79  E-value: 6.74e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  26 IEQKVLDATSNEPWGPHGTHLADIAQASRNYHEYQMIMSVVWKRI-NDTGKNWRHVYKALTILDYLVANGSERVIDDIRE 104
Cdd:cd16989    1 IESKVREATNDDPWGPTGQLMQEIARYTFTYEQFPEVMNMLWKRMlKDNKKNWRRVYKSLLLLDYLLKNGSERVVTSARE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 976902975 105 HAYQISTLSTFQYIDSTGRDQGSNVRKKSQSLVALVNDKERIQEVREKA 153
Cdd:cd16989   81 HIYDLRSLENYHFIDEKGKDQGINVRQKVKEIIELLQDDERLREERKKA 129
ENTH_Epsin cd16990
Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an ...
 26-148 2.86e-52

Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an important role as accessory proteins in clathrin-mediated endocytosis. They are important factors in clathrin-coated vesicle (CCV) generation. They contribute to membrane deformation and play a key function as adaptor proteins, coupling various components of clathrin-mediated uptake. They also have an important role in selecting and recognizing cargo. Three isoforms have been identified in mammals, epsin-1 to -3, and these are conserved in vertebrates. Epsin-1 is highly enriched and represents the dominant isoform in the brain. It is required for proper synaptic vesicle retrieval and modulates the endocytic capacity of synaptic vesicles. Epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. The ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of CCVs. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340787  Cd Length: 124  Bit Score: 177.93  E-value: 2.86e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  26 IEQKVLDATSNEPWGPHGTHLADIAQASRNYHEYQMIMSVVWKRINDTGKNWRHVYKALTILDYLVANGSERVIDDIREH 105
Cdd:cd16990    2 AEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKEN 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 976902975 106 AYQISTLSTFQYIDSTGRDQGSNVRKKSQSLVALVNDKERIQE 148
Cdd:cd16990   82 IFAIQTLKDFQYIDRDGKDQGVNVREKAKQLVSLLKDDERLKN 124
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
24-150 1.45e-45

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 159.33  E-value: 1.45e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975    24 PSIEQKVLDATSNEPWGPHGTHLADIAQASRNY-HEYQMIMSVVWKRINDTGkNWRHVYKALTILDYLVANGSERVIDDI 102
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEkSSFAEIMAVLWRRLNDTK-NWRVVYKALILLHYLLRNGSPRVILEA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 976902975   103 REHAYQISTLSTFQYIDSTGRDQGSNVRKKSQSLVALVNDKERIQEVR 150
Cdd:smart00273  80 LRNRNRILNLSDFQDIDSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
ENTH_Ent3 cd16992
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent3 and similar proteins; This subfamily is ...
 27-145 4.94e-43

Epsin N-Terminal Homology (ENTH) domain of Yeast Ent3 and similar proteins; This subfamily is composed of one of two epsinR orthologs present in Saccharomyces cerevisiae, Epsin-3 (Ent3 or Ent3p), and similar proteins. Ent3 is an adaptor proteins at the Trans-Golgi Network (TGN); it cooperates with yeast SNARE Vti1p to regulate transport from the TGN to the prevacuolar endosome. Ent3 facilitates the interaction between Gga2p with both the endosomal syntaxin Pep12p and clathrin in the GGA-dependent transport to the late endosome. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. Similar to mammalian epsinR, The ENTH domain of Ent3 binds to the yeast SNARE Vti1p; soluble NSF attachment protein receptors (SNAREs) are type II transmembrane proteins that have critical roles in providing the specificity and energy for transport-vesicle fusion. Specific ENTH domains may also function as protein cargo selection/recognition modules. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340789  Cd Length: 121  Bit Score: 151.84  E-value: 4.94e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  27 EQKVLDATSNEPWGPHGTHLADIAQASRNYHEYQMIMSVVWKRIND-TGKNWRHVYKALTILDYLVANGSERVIDDIREH 105
Cdd:cd16992    2 ESKVREATNNDPWGASSTLMQEIAQGTYNYQQFNEIMPMIYKRFTEkAGSEWRQIYKALQLLEYLIKNGSERVVDDARGH 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 976902975 106 AYQISTLSTFQYIDSTGRDQGSNVRKKSQSLVALVNDKER 145
Cdd:cd16992   82 LTLIKMLRSFHYIDDKGKDQGINVRNRAKELIELLSDDEK 121
VHS_ENTH_ANTH cd00197
VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a ...
 27-139 7.82e-19

VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a VHS, CID, ENTH, or ANTH domain. The VHS domain is present in Vps27 (Vacuolar Protein Sorting), Hrs (Hepatocyte growth factor-regulated tyrosine kinase substrate) and STAM (Signal Transducing Adaptor Molecule). It is located at the N-termini of proteins involved in intracellular membrane trafficking. The CTD-Interacting Domain (CID) is present in several RNA-processing factors and binds tightly to the carboxy-terminal domain (CTD) of RNA polymerase II (RNAP II or Pol II). The epsin N-terminal homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. A set of proteins previously designated as harboring an ENTH domain in fact contains a highly similar, yet unique module referred to as an AP180 N-Terminal Homology (ANTH) domain. VHS, ENTH, and ANTH domains are structurally similar and are composed of a superhelix of eight alpha helices. ENTH and ANTH (E/ANTH) domains bind both inositol phospholipids and proteins and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. E/ANTH domain-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340764  Cd Length: 115  Bit Score: 82.86  E-value: 7.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  27 EQKVLDATSNEPWGPHGTHLADIAQASRNYHE-YQMIMSVVWKRINDtgKNWRHVYKALTILDYLVANGSERVIDDIREH 105
Cdd:cd00197    2 EKTVEKATSNENMGPDWPLIMEICDLINETNVgPKEAVDAIKKRINN--KNPHVVLKALTLLEYCVKNCGERFHQEVASN 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 976902975 106 AYQIStLSTFQYIDSTGRDQGSNVRKKSQSLVAL 139
Cdd:cd00197   80 DFAVE-LLKFDKSGLLGDDVSTNVREKAIELVQL 112
ENTH_Ent4 cd16994
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent4 and similar proteins; Yeast Epsin-4 ...
 27-144 4.02e-10

Epsin N-Terminal Homology (ENTH) domain of Yeast Ent4 and similar proteins; Yeast Epsin-4 (Ent4 or Ent4p) has been reported to be involved in the Trans-Golgi Network (TGN)-to-vacuole sorting of Arn1p, a transporter for the uptake of ferrichrome, an important nutritional source of iron. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340791  Cd Length: 126  Bit Score: 58.07  E-value: 4.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  27 EQKVLDAT-SNEPWGPHGTHLADIAQASRNYHEYQMIMSVVWKRINDTG-----KNWRHVYKALTILDYLVANGSERVID 100
Cdd:cd16994    2 ELKVKQATdDNETSGATGTLMNEISVLTYSPKTLKEITQVLKKRLSGNSkksshKNCVHILKTLTLISYLINNGSNEFIA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 976902975 101 DIREHAYQISTLSTFQYIDSTGRDQGSNVRKKSQSLVALVNDKE 144
Cdd:cd16994   82 WLRSNLYLIERLKDFEVQDNRDLPMANQIRSLSQDICELINDDE 125
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 443-618 1.57e-08

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 58.51  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  443 APSQTAFQAQPDQLSTQTIFSSQTGQP--SLQTGYAP---QAGHPSSQtvfsAQPNQTTFPSSFPGQFGQPTLQPSFPSQ 517
Cdd:pfam09770 166 APKKAAAPAPAPQPAAQPASLPAPSRKmmSLEEVEAAmraQAKKPAQQ----PAPAPAQPPAAPPAQQAQQQQQFPPQIQ 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  518 GGPPMPHHGFQPPGAQ------SILQ--PGFSPQGGQPMPQPAFPAIGGNPPmPQPSFPAQGGQSISQPGFLAQGGNQSM 589
Cdd:pfam09770 242 QQQQPQQQPQQPQQHPgqghpvTILQrpQSPQPDPAQPSIQPQAQQFHQQPP-PVPVQPTQILQNPNRLSAARVGYPQNP 320

                         170       180
                  ....*....|....*....|....*....
gi 976902975  590 PQPSFPAQGGQSVLQAGFLAQGGHSMLQP 618
Cdd:pfam09770 321 QPGVQPAPAHQAHRQQGSFGRQAPIITHP 349
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
 157-265 1.90e-06

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 51.46  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  157 REKFRTSGGGMNRpyDDDRYEGRYGSRDEDhngygREKEWGDDRyGRDGGRYGeDGYRDDEYRGRSRSIDGDYGPRSRSS 236
Cdd:TIGR01622   7 RERLRDSSSAGDR--DRRRDKGRERSRDRS-----RDRERSRSR-RRDRHRDR-DYYRGRERRSRSRRPNRRYRPREKRR 77

                          90       100
                  ....*....|....*....|....*....
gi 976902975  237 DRERERAFEDDgHHSSRGSNVRAEDGPLD 265
Cdd:TIGR01622  78 RRGDSYRRRRD-DRRSRREKPRARDGTPE 105
ENTH_Ent5 cd16993
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent5 and similar proteins; This subfamily is ...
 33-156 1.10e-05

Epsin N-Terminal Homology (ENTH) domain of Yeast Ent5 and similar proteins; This subfamily is composed of one of two epsinR orthologs present in Saccharomyces cerevisiae, Epsin-5 (Ent5 or Ent5p), and similar proteins. Ent5 is required, together with Ent3 and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body. It is also required for protein transport from the Trans-Golgi Network (TGN) to the vacuole. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340790  Cd Length: 158  Bit Score: 46.30  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  33 ATSNEPWGPHGTHLADIAQasrnyHEYQ----MIMSVVWKRIND-------------------TGKNWRHVYKALTILDY 89
Cdd:cd16993    8 ATNTDAWGPTPKHLAKVLR-----NRYQvplyLMTEYTLKRLVDhiatrpknlyekarkdyvnYGSEWRVVLKCLIVIEF 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 976902975  90 LVANGSE-RVIDDIRE---HAYQISTLSTFQY---IDSTGRDQ--GSNVRKKSQSLVALVNDKERIQEVREKAAAN 156
Cdd:cd16993   83 LLLNVDTgDELNQVLScllNHKHIFTREIAQYkvkFSNDGKMEihERGIQKKCELILQLIEDSDFLRQERAKNKKN 158
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 463-818 2.76e-05

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 47.70  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  463 SSQTGQPSLQTGYAPQAGHPSSQtvfSAQPNQTTFPSSFPGQFGQPTLQPSFPSQGGPPMPHHGFQPPGAQSILQPGFSP 542
Cdd:pfam09606  54 SKKAAQQQQPQGGQGNGGMGGGQ---QGMPDPINALQNLAGQGTRPQMMGPMGPGPGGPMGQQMGGPGTASNLLASLGRP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  543 Q-----GGQPMPQPAFPAI---GGNPPMPQPSFPAQGGQSISQPG----------FLAQGGNQSMPQPSFPAQGGQSVLQ 604
Cdd:pfam09606 131 QmpmggAGFPSQMSRVGRMqpgGQAGGMMQPSSGQPGSGTPNQMGpnggpgqgqaGGMNGGQQGPMGGQMPPQMGVPGMP 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  605 AGFLAQGGHSMLQPGFPAQVPQPGFAAQGGHSMPQSGFAAQGGQSVLQPGfAPQGGQSASMISGFSQAGFPTktNPLSDI 684
Cdd:pfam09606 211 GPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMG-INQMQQMPQGVGGGAGQGGPG--QPMGPP 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  685 GIDFEAINRKEKRMEKPSKTPVTSNVTMGKAMGSGTGIGRagagtlraaSNPMVGSGMGITMGAPGPRPGFGAGYGGVNQ 764
Cdd:pfam09606 288 GQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQ---------QQMNQSVGQGGQVVALGGLNHLETWNPGNFG 358

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 976902975  765 PMGMNNMQQNMGIGMNIGQGFQMQQPPAGFPLGSaMPANYNPMLGRGAGYGQQP 818
Cdd:pfam09606 359 GLGANPMQRGQPGMMSSPSPVPGQQVRQVTPNQF-MRQSPQPSVPSPQGPGSQP 411
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 441-569 5.37e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 47.00  E-value: 5.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  441 PSAPSQTAFQAQPdQLSTQTIFSSQTGQPSLQ---TGYAPQAGHPSSQTVFSA---QPNQTTFPSSFPGQF--------- 505
Cdd:PRK10263  344 PPVASVDVPPAQP-TVAWQPVPGPQTGEPVIApapEGYPQQSQYAQPAVQYNEplqQPVQPQQPYYAPAAEqpaqqpyya 422

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 976902975  506 ---GQPTLQPSFPSQGGPPMPHHGFQPPGAQSILQPGFSPQGGQPMPQPAFPAIGGNPPMPQPSFPA 569
Cdd:PRK10263  423 papEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPV 489
VHS cd03561
VHS (Vps27/Hrs/STAM) domain family; The VHS domain is present in Vps27 (Vacuolar Protein ...
 26-155 6.81e-05

VHS (Vps27/Hrs/STAM) domain family; The VHS domain is present in Vps27 (Vacuolar Protein Sorting), Hrs (Hepatocyte growth factor-regulated tyrosine kinase substrate) and STAM (Signal Transducing Adaptor Molecule). It has a superhelical structure similar to that of the ARM (Armadillo) repeats and is present at the N-termini of proteins involved in intracellular membrane trafficking. There are four general groups of VHS domain containing proteins based on their association with other domains. The first group consists of proteins of the STAM/EAST/Hbp family, which has the domain composition of VHS-SH3-ITAM. The second consists of proteins with a FYVE domain C-terminal to VHS. The third consists of GGA proteins with a domain composition of VHS-GAT (GGA and TOM)-GAE (Gamma-Adaptin Ear) domain. The fourth consists of proteins with a VHS domain alone or with domains other than those mentioned above. In GGA proteins, VHS domains are involved in cargo recognition in trans-Golgi, thereby having a general membrane targeting/cargo recognition role in vesicular trafficking.


Pssm-ID: 340765  Cd Length: 131  Bit Score: 43.41  E-value: 6.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  26 IEQKVLDATS----NEPWgPHGTHLADIAQASRNYHEYqmIMSVVWKRINDtgKNWRHVYKALTILDYLVANGSERVidd 101
Cdd:cd03561    1 VEELVEKATSesltEPDW-ALNLEICDLVNSDPAQAKD--AVRALRKRLQS--KNPKVQLLALTLLETLVKNCGAPF--- 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 976902975 102 ireHAyQISTlstfqyidstgrdqgsnvRKKSQSLVALVNDKERIQEVREKAAA 155
Cdd:cd03561   73 ---HS-EVAS------------------RDFLQELVKLVKKKKTSPEVREKALA 104
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 440-583 1.02e-04

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 46.18  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  440 PPSAPSQTAFQAQPDQLSTQTIFSSQTGQPSLQTGYAPQAGHP-------SSQTVFSAQpnqttfPSSFPGQFGQPTLQP 512
Cdd:pfam09770 220 QPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPvtilqrpQSPQPDPAQ------PSIQPQAQQFHQQPP 293

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 976902975  513 SFPSQggppmPHHGFQPPGAQSILQPGfSPQGGQPMPQPAfpaiGGNPPMPQPSFPAQGGQSISQPGFLAQ 583
Cdd:pfam09770 294 PVPVQ-----PTQILQNPNRLSAARVG-YPQNPQPGVQPA----PAHQAHRQQGSFGRQAPIITHPQQLAQ 354
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 528-821 2.00e-04

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 45.00  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  528 QPPGAQSILQPGFSPQGGQPMPQPA-----FPAIGGNPPMPQPSFPAQGGQSISQPGFLAQGGNQsmpqpsfpaqggQSV 602
Cdd:pfam09606  59 QQQQPQGGQGNGGMGGGQQGMPDPInalqnLAGQGTRPQMMGPMGPGPGGPMGQQMGGPGTASNL------------LAS 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  603 LQAGFLAQGGHSMLQPGFPAQVPQPGfAAQGGHSMPQSGFAAQGGQSVLQPGFAPQGGQSASMISGfsQAGFPTKTNPLS 682
Cdd:pfam09606 127 LGRPQMPMGGAGFPSQMSRVGRMQPG-GQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGG--QQGPMGGQMPPQ 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  683 digidfeainrkekrmekpsktpvtsnvtMGKAMGSGTGIGRAGAGTLRAASNPMVGSGMGitmGAPGPRPGFGagyggv 762
Cdd:pfam09606 204 -----------------------------MGVPGMPGPADAGAQMGQQAQANGGMNPQQMG---GAPNQVAMQQ------ 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 976902975  763 nQPMGMNNMQQNMGIGMNigqgfQMQQPPAGFPLGSAMPANYNPMLGRGAGYGQQPYGG 821
Cdd:pfam09606 246 -QQPQQQGQQSQLGMGIN-----QMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVM 298
PHA03247 PHA03247
large tegument protein UL36; Provisional
 372-596 6.60e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 6.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  372 ASPGKTPFDDPFGDGPFRAAPSTDGYLAQQSPS-PFTDEPPNSVAPTSGNNSgfgdtfdqTIDILADILPPSAPSQTAFQ 450
Cdd:PHA03247 2765 GPPAPAPPAAPAAGPPRRLTRPAVASLSESRESlPSPWDPADPPAAVLAPAA--------ALPPAASPAGPLPPPTSAQP 2836

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  451 AQPDQLSTQTIFSSQTG------------QPSLQTGYAPQA-GHPSSQTVFSAQPNQTTFPSSFPGQFGQPTLQPSFPSQ 517
Cdd:PHA03247 2837 TAPPPPPGPPPPSLPLGgsvapggdvrrrPPSRSPAAKPAApARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPP 2916

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  518 GGPPMPHHgfQPPGAQSILQPgfspqggQPMPQPAFPAIGGNPPMPQPSfpaqGGQSISQPGFLAQGGNQ------SMPQ 591
Cdd:PHA03247 2917 PQPQPQPP--PPPQPQPPPPP-------PPRPQPPLAPTTDPAGAGEPS----GAVPQPWLGALVPGRVAvprfrvPQPA 2983


                  ....*
gi 976902975  592 PSFPA 596
Cdd:PHA03247 2984 PSREA 2988
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 489-609 7.57e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.87  E-value: 7.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  489 SAQPNQTTFPSSFPGQFGQPTLQPSFPSQ--GGPPMPHHGFQPPGAQSILQPGFSPQGGQPMPQ------PAFPAIGGNP 560
Cdd:TIGR01628 379 QPRMRQLPMGSPMGGAMGQPPYYGQGPQQqfNGQPLGWPRMSMMPTPMGPGGPLRPNGLAPMNAvrapsrNAQNAAQKPP 458

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 976902975  561 PMPQPSFPAQGGQSISQPgflaqggnqsMPQP-SFPAQGGQSVLQAGFLA 609
Cdd:TIGR01628 459 MQPVMYPPNYQSLPLSQD----------LPQPqSTASQGGQNKKLAQVLA 498
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
 142-261 9.15e-04

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 42.57  E-value: 9.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  142 DKERIQEvrekaaanREKFRTSGGGMNRPYDDDRYEGRYGSRDEDHngYGREKEWGDDRYGRDGGRYGEDGYRDDEYRGR 221
Cdd:TIGR01642   2 DEEPDRE--------REKSRGRDRDRSSERPRRRSRDRSRFRDRHR--RSRERSYREDSRPRDRRRYDSRSPRSLRYSSV 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 976902975  222 SRSIDgdyGPRSRSSDRERERAFEDDGHHSSRGSNVRAED 261
Cdd:TIGR01642  72 RRSRD---RPRRRSRSVRSIEQHRRRLRDRSPSNQWRKDD 108
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 440-671 1.07e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 42.72  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  440 PPSAPSQTAFQAQPDQLSTQTIFSSQTGQPS--LQTGYAP----------QA-----GHPSSQtvfSAQPNQTTFPSSFP 502
Cdd:pfam09770 107 PAARAAQSSAQPPASSLPQYQYASQQSQQPSkpVRTGYEKykepepipdlQVdaslwGVAPKK---AAAPAPAPQPAAQP 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  503 GQFGQPT--------LQPSFPSQGGPPMPHHGFQPPGAQSILQPGFSPQGGQPMPQPAFPAIGGNPPMPQPSFPAQGGQ- 573
Cdd:pfam09770 184 ASLPAPSrkmmsleeVEAAMRAQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPv 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  574 SISQpgflaqggnQSMPQPSFPAQGGQSVLQAGFLAQGGHSMLQPGFPAQVPQPGFAAQGGHSmpqsgfaaQGGQSVLQP 653
Cdd:pfam09770 264 TILQ---------RPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQILQNPNRLSAARVGYP--------QNPQPGVQP 326

                         250
                  ....*....|....*...
gi 976902975  654 GFAPQGGQSASMISGFSQ 671
Cdd:pfam09770 327 APAHQAHRQQGSFGRQAP 344
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 440-596 1.36e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975 440 PPSAPSQTAFQAQPDQLSTQTIFSSQTGQPSLQTGYAPQAGHPSSQTVFSAQPNQTTFPSSFPGQFGQPTLQPS-FPSQG 518
Cdd:PRK07764 619 AAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAApAGAAP 698

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 976902975 519 GPPMPHHGFQPPGAQSILQPGFSPQGGQPMPQPAFPAIGGNPPMPQPSFPAQGGQSISQPGFLAQGGNQSMPQPSFPA 596
Cdd:PRK07764 699 AQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPP 776
ANTH_N cd03564
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ...
 26-115 2.41e-03

ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal Homology) domain family is composed of Adaptor Protein 180 (AP180), Clathrin Assembly Lymphoid Myeloid Leukemia protein (CALM), and similar proteins. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ANTH-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that the ANTH domain is a universal component of the machinery for clathrin-mediated membrane budding. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains.


Pssm-ID: 340767  Cd Length: 120  Bit Score: 38.79  E-value: 2.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  26 IEQKVLDATSNEPWGPHGTHLADIAQASRNYHEYQMIMSVV---WKRINDtgKNWRHVYKALTILDYLVANGSERVIDDI 102
Cdd:cd03564    1 LDVAVVKATNHDEVPPKEKHVRKLLLATSNGGGRADVAYIVhalAKRLHK--KNWIVVLKTLIVIHRLLREGSPSFLEEL 78

                         90
                 ....*....|...
gi 976902975 103 REHAYQISTLSTF 115
Cdd:cd03564   79 LRYSGHIFNLSNF 91
PRP38_assoc pfam12871
Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region ...
 202-242 2.64e-03

Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region found at the C-terminus of plant and metazoan pre-mRNA-splicing factor 38 proteins. The function is not known.


Pssm-ID: 463734 [Multi-domain]  Cd Length: 98  Bit Score: 37.83  E-value: 2.64e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 976902975  202 GRDGGRYGEDGYRDDEYRGRSRSIDGDYGPRSRSSDRERER 242
Cdd:pfam12871  55 SRSRSRDRRSRGTRDRRRDRDRDRYRSLRSRSRDRSRDRDR 95
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 144-258 2.99e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 41.04  E-value: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975 144 ERIQEVREKAAANREKFRTSGGGMNRPYDDDRYEGRYGSRDEDHNGyGREKEWGDDRYGRDGGRYGEDGYRDDEYRGRSR 223
Cdd:PRK12678 173 RRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREER-GRRDGGDRRGRRRRRDRRDARGDDNREDRGDRD 251

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 976902975 224 SIDGDYGpRSRSSDRERERafEDDGHHSSRGSNVR 258
Cdd:PRK12678 252 GDDGEGR-GGRRGRRFRDR--DRRGRRGGDGGNER 283
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 498-571 4.72e-03

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 38.62  E-value: 4.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975   498 PSSFPGQFGQPTL-----QPSFPSQGGPPMPHHGFQPPGAQSILQPGFSPQGGQPMP--QPAFPAIggnPPMPQPSFPAQ 570
Cdd:smart00818  80 HSMTPTQHHQPNLpqpaqQPFQPQPLQPPQPQQPMQPQPPVHPIPPLPPQPPLPPMFpmQPLPPLL---PDLPLEAWPAT 156


                   .
gi 976902975   571 G 571
Cdd:smart00818 157 D 157
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 400-627 5.94e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.45  E-value: 5.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  400 QQSPSPFTDEPpnSVAPTSGNNSGFGDTFDQTIDILADILPPSAPSQTAFQAQPDQLSTQTIFSSQTGQPSLQTGYAPQA 479
Cdd:PRK10263  361 QPVPGPQTGEP--VIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAP 438

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  480 GHPSSQTVFSAQPNQTTFPSsfpgqfgQPTLQPSFPSQGGPPMPHHGFQPPGAQSilQPGFSPQGG-------------- 545
Cdd:PRK10263  439 EQPVAGNAWQAEEQQSTFAP-------QSTYQTEQTYQQPAAQEPLYQQPQPVEQ--QPVVEPEPVveetkparpplyyf 509

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  546 ------------------QPMPQPAFPAIGGNPPMPQPSFPAQGG-QSISQPGFLAQGGNQSMPQPSFPAQGGQSVLQag 606
Cdd:PRK10263  510 eeveekrarereqlaawyQPIPEPVKEPEPIKSSLKAPSVAAVPPvEAAAAVSPLASGVKKATLATGAAATVAAPVFS-- 587

                         250       260
                  ....*....|....*....|...
gi 976902975  607 fLAQGG--HSMLQPGFPAQVPQP 627
Cdd:PRK10263  588 -LANSGgpRPQVKEGIGPQLPRP 609
PRP38_assoc pfam12871
Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region ...
 172-247 6.60e-03

Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region found at the C-terminus of plant and metazoan pre-mRNA-splicing factor 38 proteins. The function is not known.


Pssm-ID: 463734 [Multi-domain]  Cd Length: 98  Bit Score: 36.68  E-value: 6.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975  172 DDDRYEGRYGSRDEDHNGyGREKEWGDDRY---------------GRDGGRYGEDGYRDDEYRGRSRSIDGDYGPRSRSS 236
Cdd:pfam12871   9 DLDEEEEEDEEEDEEASD-ESERASLSRKRrsrsrrrsstrdrsrSRSRSRSRDRRSRGTRDRRRDRDRDRYRSLRSRSR 87

                          90
                  ....*....|.
gi 976902975  237 DRERERAFEDD 247
Cdd:pfam12871  88 DRSRDRDRDRR 98
PHA03378 PHA03378
EBNA-3B; Provisional
 369-666 8.22e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 8.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975 369 PRGASPGKTPFD-DPFGDGPFRAAPSTDGYLAQQSPspftDEPPNsVAPTSgnnsgFGDTFDQTIDILADILPPSAPSQT 447
Cdd:PHA03378 616 PETSAPRQWPMPlRPIPMRPLRMQPITFNVLVFPTP----HQPPQ-VEITP-----YKPTWTQIGHIPYQPSPTGANTML 685

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975 448 AFQAQPDQLSTQtifssqtgqPSLQTGYAPQAGHPSSQTVFSAQPNQTTFPSSFPGQFGQPTLQPsfpsqgGPPMPhhgf 527
Cdd:PHA03378 686 PIQWAPGTMQPP---------PRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAP------GRARP---- 746

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975 528 qPPGAQSILQPgfsPQGGQPMPQPAFPAIGGNPPMPQPSFPAQGGQsisQPgflaQGGNQSMPQPsfpaQGGQSVLQAGF 607
Cdd:PHA03378 747 -PAAAPGRARP---PAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQ---RP----RGAPTPQPPP----QAGPTSMQLMP 811

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 976902975 608 LAQGGhsmlQPGFPAQVPQPGFAAQGGHSMPQSGFAAQGG-QSVLQPGFAPQGGQSASMI 666
Cdd:PHA03378 812 RAAPG----QQGPTKQILRQLLTGGVKRGRPSLKKPAALErQAAAGPTPSPGSGTSDKIV 867
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH