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Conserved domains on  [gi|1042818015|ref|NP_001308192|]
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epsin-1 isoform d [Homo sapiens]

Protein Classification

ENTH domain-containing protein; epsin; epsin( domain architecture ID 13016790)

ENTH (Epsin N-Terminal Homology) domain-containing protein may be involved in clathrin-mediated endocytosis; similar to epsin family proteins that play an important role as accessory proteins in clathrin-mediated endocytosis; epsin plays an important role as accessory proteins in clathrin-mediated endocytosis; epsin plays an important role as accessory proteins in clathrin-mediated endocytosis

Gene Ontology:  GO:0030276|GO:0005543|GO:0006897
PubMed:  10567358

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ENTH_Epsin cd16990
Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an ...
 19-142 4.74e-99

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: 296.19  E-value: 4.74e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  19 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd16990     1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1042818015  99 NMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLRE 142
Cdd:cd16990    81 NIFAIQTLKDFQYIDRDGKDQGVNVREKAKQLVSLLKDDERLKN 124
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
 265-453 3.79e-08

DNA polymerase III subunits gamma and tau; Validated


The actual alignment was detected with superfamily member PRK07764:

Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 56.53  E-value: 3.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015 265 TAPAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPPVPPAADPWGGPAPTPAS------------GDPWRPAAPAGPSVD 332
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAApapgvaapehhpKHVAVPDASDGGDGW 669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015 333 PWGGTPAPAAGEGPTPDPWGSSDGGVPVSGPSASDPWTPAPA--FSDPWGGSPAKPSTNGTTAGGFDTEPDEFSDFDRLR 410
Cdd:PRK07764  670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAgqADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP 749

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1042818015 411 TALPTSGSSAGELELLAGEVPARSPGAFDMSGVRGSLAEAVGS 453
Cdd:PRK07764  750 DPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPS 792
 
Name Accession Description Interval E-value
ENTH_Epsin cd16990
Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an ...
 19-142 4.74e-99

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: 296.19  E-value: 4.74e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  19 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd16990     1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1042818015  99 NMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLRE 142
Cdd:cd16990    81 NIFAIQTLKDFQYIDRDGKDQGVNVREKAKQLVSLLKDDERLKN 124
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 17-140 4.72e-73

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: 228.98  E-value: 4.72e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  17 YSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLNDKGKNWRHIYKALTLLEYLLKNGSERVVDDL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1042818015  97 KENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRL 140
Cdd:pfam01417  81 RENIYIIRTLTDFHYIDENGKDQGINVRKKAKEILNLLEDDELL 124
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
18-144 1.22e-52

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 175.51  E-value: 1.22e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015   18 SEAEIKVREATSNDPWGPSSSLMSEIADLTYNV-VAFSEIMSMIWKRLNDHGkNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEkSSFAEIMAVLWRRLNDTK-NWRVVYKALILLHYLLRNGSPRVILEA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1042818015   97 KENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREER 144
Cdd:smart00273  80 LRNRNRILNLSDFQDIDSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 265-453 3.79e-08

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 56.53  E-value: 3.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015 265 TAPAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPPVPPAADPWGGPAPTPAS------------GDPWRPAAPAGPSVD 332
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAApapgvaapehhpKHVAVPDASDGGDGW 669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015 333 PWGGTPAPAAGEGPTPDPWGSSDGGVPVSGPSASDPWTPAPA--FSDPWGGSPAKPSTNGTTAGGFDTEPDEFSDFDRLR 410
Cdd:PRK07764  670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAgqADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP 749

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1042818015 411 TALPTSGSSAGELELLAGEVPARSPGAFDMSGVRGSLAEAVGS 453
Cdd:PRK07764  750 DPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPS 792
MSCRAMM_ClfB NF033845
MSCRAMM family adhesin clumping factor ClfB; Clumping factor B is an MSCRAMM (Microbial ...
 294-407 4.88e-05

MSCRAMM family adhesin clumping factor ClfB; Clumping factor B is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468203 [Multi-domain]  Cd Length: 871  Bit Score: 46.48  E-value: 4.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015 294 DPWGGPPVPPAADPWGGPAPTPasgdpwrpaapaGPSVDPwggTPAPAAGEGPTPDPWGSSDGGVPVSGPSASDPWTPAP 373
Cdd:NF033845  545 DPTPGPPVDPEPSPEPEPEPTP------------DPEPSP---DPDPEPSPDPDPDSDSDSDSGSDSDSGSDSDSDSDSD 609

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1042818015 374 AFSDPWGGSPAKPSTNGTTAGGFDTEPDEFSDFD 407
Cdd:NF033845  610 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 643
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
 300-396 7.51e-03

Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.


Pssm-ID: 429334  Cd Length: 301  Bit Score: 38.75  E-value: 7.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015 300 PVPPAADPWGGPAPTPASGDPWRPAAPAGPSVDPwGGTPAPAAGEGPTPDPWGSSDGGVPvsgPSASDPWTPAPAFSDPW 379
Cdd:pfam07174  34 PAVAHADPEPAPPPPSTATAPPAPPPPPPAPAAP-APPPPPAAPNAPNAPPPPADPNAPP---PPPADPNAPPPPAVDPN 109

                          90
                  ....*....|....*..
gi 1042818015 380 GGSPAKPStngTTAGGF 396
Cdd:pfam07174 110 APEPGRID---NAVGGF 123
 
Name Accession Description Interval E-value
ENTH_Epsin cd16990
Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an ...
 19-142 4.74e-99

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: 296.19  E-value: 4.74e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  19 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd16990     1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1042818015  99 NMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLRE 142
Cdd:cd16990    81 NIFAIQTLKDFQYIDRDGKDQGVNVREKAKQLVSLLKDDERLKN 124
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 17-140 4.72e-73

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: 228.98  E-value: 4.72e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  17 YSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLNDKGKNWRHIYKALTLLEYLLKNGSERVVDDL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1042818015  97 KENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRL 140
Cdd:pfam01417  81 RENIYIIRTLTDFHYIDENGKDQGINVRKKAKEILNLLEDDELL 124
ENTH_Ent1_Ent2 cd16991
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent1, Ent2, and similar proteins; This ...
 17-144 2.00e-70

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: 222.53  E-value: 2.00e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  17 YSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:cd16991     2 YSSTQVKVRNATSNDPWGPSGDEMAEIAELTYDQHDFVEIMDMLDKRLNDKGKNWRHVAKALTVLDYLLHFGSENVVLWA 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1042818015  97 KENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREER 144
Cdd:cd16991    82 KENIYIIKTLREFQYIDDEGKDQGQNVRVKAKELTSLLLDDERLREER 129
ENTH cd03571
Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is ...
 20-136 2.04e-65

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: 208.91  E-value: 2.04e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  20 AEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKEN 99
Cdd:cd03571     1 LELLVREATSNEPWGPTGSQLAEIAQATFDYDDYQRIMKVLWKRLNDKGKNWRHVYKALTLLEYLLKNGSERVVDEFRDN 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1042818015 100 MYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRD 136
Cdd:cd03571    81 LYLIRTLQDFQYVDENGDDQGINVREKAKQIVALLED 117
ENTH_EpsinR cd16989
Epsin N-Terminal Homology (ENTH) domain of Epsin-related protein; Epsin-related protein ...
 20-147 2.57e-60

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: 195.97  E-value: 2.57e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  20 AEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKR-LNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd16989     1 IESKVREATNDDPWGPTGQLMQEIARYTFTYEQFPEVMNMLWKRmLKDNKKNWRRVYKSLLLLDYLLKNGSERVVTSARE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1042818015  99 NMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREERAHA 147
Cdd:cd16989    81 HIYDLRSLENYHFIDEKGKDQGINVRQKVKEIIELLQDDERLREERKKA 129
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
18-144 1.22e-52

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 175.51  E-value: 1.22e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015   18 SEAEIKVREATSNDPWGPSSSLMSEIADLTYNV-VAFSEIMSMIWKRLNDHGkNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEkSSFAEIMAVLWRRLNDTK-NWRVVYKALILLHYLLRNGSPRVILEA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1042818015   97 KENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREER 144
Cdd:smart00273  80 LRNRNRILNLSDFQDIDSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
ENTH_Ent3 cd16992
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent3 and similar proteins; This subfamily is ...
 21-139 6.08e-46

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: 157.61  E-value: 6.08e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  21 EIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLND-HGKNWRHVYKAMTLMEYLIKTGSERVSQQCKEN 99
Cdd:cd16992     2 ESKVREATNNDPWGASSTLMQEIAQGTYNYQQFNEIMPMIYKRFTEkAGSEWRQIYKALQLLEYLIKNGSERVVDDARGH 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1042818015 100 MYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDR 139
Cdd:cd16992    82 LTLIKMLRSFHYIDDKGKDQGINVRNRAKELIELLSDDEK 121
VHS_ENTH_ANTH cd00197
VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a ...
 20-136 6.64e-41

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: 143.72  E-value: 6.64e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  20 AEIKVREATSNDPWGPSSSLMSEIADLTYN-VVAFSEIMSMIWKRLNDHgkNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd00197     1 FEKTVEKATSNENMGPDWPLIMEICDLINEtNVGPKEAVDAIKKRINNK--NPHVVLKALTLLEYCVKNCGERFHQEVAS 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1042818015  99 NMYAVQTLKdFQYVDRDGKDQGVNVREKAKQLVALLRD 136
Cdd:cd00197    79 NDFAVELLK-FDKSGLLGDDVSTNVREKAIELVQLWAS 115
ENTH_Ent4 cd16994
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent4 and similar proteins; Yeast Epsin-4 ...
 20-138 1.28e-21

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: 90.43  E-value: 1.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  20 AEIKVREAT-SNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHG-----KNWRHVYKAMTLMEYLIKTGSERVS 93
Cdd:cd16994     1 TELKVKQATdDNETSGATGTLMNEISVLTYSPKTLKEITQVLKKRLSGNSkksshKNCVHILKTLTLISYLINNGSNEFI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1042818015  94 QQCKENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDED 138
Cdd:cd16994    81 AWLRSNLYLIERLKDFEVQDNRDLPMANQIRSLSQDICELINDDE 125
ENTH_Ent5 cd16993
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent5 and similar proteins; This subfamily is ...
 21-145 9.52e-09

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: 54.78  E-value: 9.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  21 EIKVREATSNDPWGPSSSLMSEIADLTYNVVAFsEIMSMIWKRLNDH-------------------GKNWRHVYKAMTLM 81
Cdd:cd16993     2 QIDIRRATNTDAWGPTPKHLAKVLRNRYQVPLY-LMTEYTLKRLVDHiatrpknlyekarkdyvnyGSEWRVVLKCLIVI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1042818015  82 EYLIKTGS--ERVSQ--QCKENMYAVQTLKDFQY---VDRDGKDQ--GVNVREKAKQLVALLRDEDRLREERA 145
Cdd:cd16993    81 EFLLLNVDtgDELNQvlSCLLNHKHIFTREIAQYkvkFSNDGKMEihERGIQKKCELILQLIEDSDFLRQERA 153
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 265-453 3.79e-08

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 56.53  E-value: 3.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015 265 TAPAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPPVPPAADPWGGPAPTPAS------------GDPWRPAAPAGPSVD 332
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAApapgvaapehhpKHVAVPDASDGGDGW 669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015 333 PWGGTPAPAAGEGPTPDPWGSSDGGVPVSGPSASDPWTPAPA--FSDPWGGSPAKPSTNGTTAGGFDTEPDEFSDFDRLR 410
Cdd:PRK07764  670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAgqADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP 749

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1042818015 411 TALPTSGSSAGELELLAGEVPARSPGAFDMSGVRGSLAEAVGS 453
Cdd:PRK07764  750 DPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPS 792
PHA03247 PHA03247
large tegument protein UL36; Provisional
 267-525 6.34e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.63  E-value: 6.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  267 PAPAPTtdPWGGPAPMAAAVPTAAPTSDPWGGPPVPPAADPW----GGPAPT---PASGDPWRPAAPAGPSVDPWGGTPA 339
Cdd:PHA03247  2708 PEPAPH--ALVSATPLPPGPAAARQASPALPAAPAPPAVPAGpatpGGPARParpPTTAGPPAPAPPAAPAAGPPRRLTR 2785

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  340 PAAGE-----GPTPDPWGSSDGGVPVSGPSASDPWTPAPAFSDPwggspaKPSTNGTTAGGFDTEPdefsdfdrLRTALP 414
Cdd:PHA03247  2786 PAVASlsesrESLPSPWDPADPPAAVLAPAAALPPAASPAGPLP------PPTSAQPTAPPPPPGP--------PPPSLP 2851

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  415 TSGSSAGelellAGEVPARSPGafdmsgvRGSLAEAVGSPPPAATPTPTPPTRKTPESFLGPNaalvdlDSLVSRPGPTP 494
Cdd:PHA03247  2852 LGGSVAP-----GGDVRRRPPS-------RSPAAKPAAPARPPVRRLARPAVSRSTESFALPP------DQPERPPQPQA 2913

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1042818015  495 PGAKASNPFLPGGGPATGPSVTNPFQPAPPA 525
Cdd:PHA03247  2914 PPPPQPQPQPPPPPQPQPPPPPPPRPQPPLA 2944
PHA03247 PHA03247
large tegument protein UL36; Provisional
 268-526 1.76e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 1.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  268 APAPTTDPWGGPAPMAAAVPTAAPTS-----DPWGGPPVPPAADPWGGPAPTPAS---GDPWRPAAPAGPSVDPWGGTPA 339
Cdd:PHA03247  2491 AAGAAPDPGGGGPPDPDAPPAPSRLApailpDEPVGEPVHPRMLTWIRGLEELASddaGDPPPPLPPAAPPAAPDRSVPP 2570

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  340 PAAGEGPtPDPWGSSDGGVPVSGPSASDPWTPAPAFSDPWGGSPAKPSTNGTTAggfdTEPDEFSDFDRlrtalptsGSS 419
Cdd:PHA03247  2571 PRPAPRP-SEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHA----PDPPPPSPSPA--------ANE 2637

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  420 AGELELLAGEVPARSPGAFDMSGVRGSLAEAVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGAKA 499
Cdd:PHA03247  2638 PDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVS 2717

                          250       260
                   ....*....|....*....|....*..
gi 1042818015  500 SNPFLPGGGPATGPSVTNPFQPAPPAT 526
Cdd:PHA03247  2718 ATPLPPGPAAARQASPALPAAPAPPAV 2744
VHS cd03561
VHS (Vps27/Hrs/STAM) domain family; The VHS domain is present in Vps27 (Vacuolar Protein ...
 24-131 1.21e-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: 44.95  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  24 VREATSNDPWGPSSSLMSEIADLtYNVVAFS--EIMSMIWKRLNDhgKNWRHVYKAMTLMEYLIKTGSERVSQQckenmy 101
Cdd:cd03561     5 VEKATSESLTEPDWALNLEICDL-VNSDPAQakDAVRALRKRLQS--KNPKVQLLALTLLETLVKNCGAPFHSE------ 75

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1042818015 102 aVQTLKDFQYVDR--DGKDQGVNVREKAKQLV 131
Cdd:cd03561    76 -VASRDFLQELVKlvKKKKTSPEVREKALALI 106
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
261-432 2.37e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 47.18  E-value: 2.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015 261 ADVFTAPAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPPVPPAADPWGGPAPTPASGDPwRPAAPAGPSVDPWGGTP-- 338
Cdd:PRK12323  404 AAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAAR-PAAAGPRPVAAAAAAAPar 482

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015 339 -APAAGEGPTPD---PWGSSDGGVPVSGPSASDPWTP---APAFSDPWGGSPAKPSTNGTTAGGFDTEPDEFSDFDRLRT 411
Cdd:PRK12323  483 aAPAAAPAPADDdppPWEELPPEFASPAPAQPDAAPAgwvAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVA 562

                         170       180
                  ....*....|....*....|.
gi 1042818015 412 ALPTSGSSAGELELLAGEVPA 432
Cdd:PRK12323  563 PRPPRASASGLPDMFDGDWPA 583
MSCRAMM_ClfB NF033845
MSCRAMM family adhesin clumping factor ClfB; Clumping factor B is an MSCRAMM (Microbial ...
 294-407 4.88e-05

MSCRAMM family adhesin clumping factor ClfB; Clumping factor B is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468203 [Multi-domain]  Cd Length: 871  Bit Score: 46.48  E-value: 4.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015 294 DPWGGPPVPPAADPWGGPAPTPasgdpwrpaapaGPSVDPwggTPAPAAGEGPTPDPWGSSDGGVPVSGPSASDPWTPAP 373
Cdd:NF033845  545 DPTPGPPVDPEPSPEPEPEPTP------------DPEPSP---DPDPEPSPDPDPDSDSDSDSGSDSDSGSDSDSDSDSD 609

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1042818015 374 AFSDPWGGSPAKPSTNGTTAGGFDTEPDEFSDFD 407
Cdd:NF033845  610 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 643
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 266-453 1.98e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.39  E-value: 1.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  266 APAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPPVPPAADPWGGPAPTPASGDPwrPAAPAGPSVDPWGGTPAPAAGEG 345
Cdd:PHA03307    81 ANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLS--EMLRPVGSPGPPPAASPPAAGAS 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  346 PTP---DPWGSSDGGVPVSGPSASDPWTPAPAFSDPW--------GGSPAKPSTNGTTAGGFDTEPDEFSDFDRLRTALP 414
Cdd:PHA03307   159 PAAvasDAASSRQAALPLSSPEETARAPSSPPAEPPPstppaaasPRPPRRSSPISASASSPAPAPGRSAADDAGASSSD 238

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1042818015  415 TSGS-SAGELELLAGEVPARSPGAFDMSGVRGSLAEAVGS 453
Cdd:PHA03307   239 SSSSeSSGCGWGPENECPLPRPAPITLPTRIWEASGWNGP 278
PHA03247 PHA03247
large tegument protein UL36; Provisional
 266-523 3.02e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 3.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  266 APAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPPVPPAADPWGGPAPTPASGdPWRPAAP---------AGPSVDPWGG 336
Cdd:PHA03247  2630 SPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQR-PRRRAARptvgsltslADPPPPPPTP 2708

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  337 TPAPAAGEGPTPDPWGSSDGGVPVSGPSAsDPWTPAPAFSDPWGGSPAKPSTNGTTAGGFDTEPDEFSDFDRLRTALPTS 416
Cdd:PHA03247  2709 EPAPHALVSATPLPPGPAAARQASPALPA-APAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPA 2787

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  417 GSSAGELELLAGEVPARSPGAFDMSGVRGSLAEAVGSPPP-----AATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPG 491
Cdd:PHA03247  2788 VASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPlppptSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP 2867

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1042818015  492 PTPPGAKASNPFLPGGGPATGPSVTNPFQPAP 523
Cdd:PHA03247  2868 SRSPAAKPAAPARPPVRRLARPAVSRSTESFA 2899
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 265-526 6.44e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.85  E-value: 6.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  265 TAPAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPPVPPAADPWGGPAPTPASGDPWRPAAPAGPSVDPwggtPAPAAGE 344
Cdd:PHA03307   113 SPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEE----TARAPSS 188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  345 GPTPDPWGSSDGGVPVSGPSASDPWTPAPAFSDPWGGSPAKPSTNGTTAGGFDTEPDEFSDFDRLRTALPTSGSSAGELE 424
Cdd:PHA03307   189 PPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTR 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  425 LLAGEVPARSPGAFDMSGVRGSLAEAVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGAKASNPFL 504
Cdd:PHA03307   269 IWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPS 348

                          250       260
                   ....*....|....*....|..
gi 1042818015  505 PGGGPATGPSvtnPFQPAPPAT 526
Cdd:PHA03307   349 RSPSPSRPPP---PADPSSPRK 367
PHA03247 PHA03247
large tegument protein UL36; Provisional
 265-372 7.07e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 7.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  265 TAPAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGP-PVPPAADPWGGPAPTPASGDPWRPAAPAGPSVDPWGGTPAPAAG 343
Cdd:PHA03247  2765 GPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPsPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPG 2844

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1042818015  344 EGPTPDPWGSS---DGGVPVSGPSASDPWTPA 372
Cdd:PHA03247  2845 PPPPSLPLGGSvapGGDVRRRPPSRSPAAKPA 2876
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
265-442 7.11e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.56  E-value: 7.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015 265 TAPAPAPTTDPWGGPAPMAAAVPTAAPTSDPwggPPVPPAADPWGGPAPTPASGDPWRPAAPAGPSVDPWGGTPAPAAGE 344
Cdd:PRK12323  393 AAAAPAPAAPPAAPAAAPAAAAAARAVAAAP---ARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGP 469

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015 345 GPTPD-----PWGSSDGGVPVSGPSASDPWTPAPAFSDPWGGSPAKPSTNGTTAGGFDTEPDEFSDFDRLRTALPTSGSS 419
Cdd:PRK12323  470 RPVAAaaaaaPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAP 549

                         170       180
                  ....*....|....*....|...
gi 1042818015 420 AGELELLAGEVPARSPGAFDMSG 442
Cdd:PRK12323  550 APRAAAATEPVVAPRPPRASASG 572
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 266-379 7.12e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 7.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015 266 APAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPPVPPAADPWGGPAPTPASGDPWRPAAPAGPSVDPWGGTPAPAAGEG 345
Cdd:PRK07764  402 AAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPA 481

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1042818015 346 PTPDPWGSSDGGVPV-SGPSASDPWTPAPAFSDPW 379
Cdd:PRK07764  482 PAPPAAPAPAAAPAApAAPAAPAGADDAATLRERW 516
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
261-433 9.28e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.17  E-value: 9.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015 261 ADVFTAPAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGP---PVPPAADPWGGPA---PTPASGDPWRPAAPAGPSVDPW 334
Cdd:PRK12323  420 AAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPaaaARPAAAGPRPVAAaaaAAPARAAPAAAPAPADDDPPPW 499

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015 335 GGTPAPAAGEGP-TPDPWGSSDGGVPVSGPSASDPWTPAPAFSDPWGGSPAKPSTNGTTAGGFDTEPDEFSDfdrlrtal 413
Cdd:PRK12323  500 EELPPEFASPAPaQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASAS-------- 571

                         170       180
                  ....*....|....*....|
gi 1042818015 414 PTSGSSAGELELLAGEVPAR 433
Cdd:PRK12323  572 GLPDMFDGDWPALAARLPVR 591
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 262-365 2.92e-03

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 40.64  E-value: 2.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015  262 DVFTAPAPAPTTDPwggpapmaaAVPTAAPTSDPWGGPPVPPAADPWGGPAPTPASGDPWRPAAPAGPSVDPWGGTPAPA 341
Cdd:PRK12270    31 EFFADYGPGSTAAP---------TAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPA 101

                           90       100
                   ....*....|....*....|....
gi 1042818015  342 AGEGPTPDPWGSSDGGVPVSGPSA 365
Cdd:PRK12270   102 AAAAAAPAAAAVEDEVTPLRGAAA 125
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 263-374 7.38e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.20  E-value: 7.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015 263 VFTAPAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPPVPPAA-DPWGGPAPTPASGDPWRPAAPAGPSVDPWGGTPA-- 339
Cdd:PRK07764  386 GVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAApQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSaq 465

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1042818015 340 PAAGEGPTPDPWGSSDGGVPVSGPSASDPWTPAPA 374
Cdd:PRK07764  466 PAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAP 500
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
 300-396 7.51e-03

Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.


Pssm-ID: 429334  Cd Length: 301  Bit Score: 38.75  E-value: 7.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015 300 PVPPAADPWGGPAPTPASGDPWRPAAPAGPSVDPwGGTPAPAAGEGPTPDPWGSSDGGVPvsgPSASDPWTPAPAFSDPW 379
Cdd:pfam07174  34 PAVAHADPEPAPPPPSTATAPPAPPPPPPAPAAP-APPPPPAAPNAPNAPPPPADPNAPP---PPPADPNAPPPPAVDPN 109

                          90
                  ....*....|....*..
gi 1042818015 380 GGSPAKPStngTTAGGF 396
Cdd:pfam07174 110 APEPGRID---NAVGGF 123
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 277-390 8.11e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.20  E-value: 8.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015 277 GGPAPMAAAVPTAAPTSdpwgGPPVPPAADPwGGPAPTPASGDPWRPAAPAGPsvdpwggTPAPAAGEGPTPDPWGSSDG 356
Cdd:PRK07764  384 RLGVAGGAGAPAAAAPS----AAAAAPAAAP-APAAAAPAAAAAPAPAAAPQP-------APAPAPAPAPPSPAGNAPAG 451

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1042818015 357 GVPVS--GPSASDPWTPAPAFSDPWGGSPAKPSTNG 390
Cdd:PRK07764  452 GAPSPppAAAPSAQPAPAPAAAPEPTAAPAPAPPAA 487
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 265-381 8.58e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 38.93  E-value: 8.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042818015 265 TAPAPAPTTDPWGGPAPMAAAVPTAAptsdpwggPPVPPAADPWGGPAPTPASGDPWRPAAPAGPSVDPWGGTPAPAAGE 344
Cdd:PRK14951  387 AAPAAAPVAQAAAAPAPAAAPAAAAS--------APAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPE 458

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1042818015 345 GP------TPDPwGSSDGGVPVSGPSASDPWTPAPAFsDPWGG 381
Cdd:PRK14951  459 TVaipvrvAPEP-AVASAAPAPAAAPAAARLTPTEEG-DVWHA 499
PRK10952 PRK10952
proline/glycine betaine ABC transporter permease ProW;
292-327 9.27e-03

proline/glycine betaine ABC transporter permease ProW;


Pssm-ID: 236805  Cd Length: 355  Bit Score: 38.53  E-value: 9.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1042818015 292 TSDPWGGPPVP----PAADPWGGPAPTPASGDP--WRPAAPA 327
Cdd:PRK10952    5 QNNPWDTTPAAdsaaQSADAWGTPAGAPTDGGGadWLNSAPA 46
 
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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