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Conserved domains on  [gi|2311270601|ref|NP_001399287|]
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epsin-1 isoform 6 [Mus musculus]

Protein Classification

ENTH domain-containing protein( domain architecture ID 13016662)

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

CATH:  1.25.40.90
Gene Ontology:  GO:0030276|GO:0005543|GO:0006897|GO:1901981|GO:0072659
PubMed:  10567358|27466364|14657269|12742163|22748146|11911874|29774507
SCOP:  4001355

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 2.41e-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: 2.41e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  19 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd16990     1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2311270601  99 NMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLRE 142
Cdd:cd16990    81 NIFAIQTLKDFQYIDRDGKDQGVNVREKAKQLVSLLKDDERLKN 124
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
 242-368 1.69e-07

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: 54.22  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601 242 PAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPW----GGAAPTPASGDPWRPAAptGPSVDPWGGTPAPAA 317
Cdd:PRK07764  649 APEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPaapaGAAPAQPAPAPAATPPA--GQADDPAAQPPQAAQ 726

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2311270601 318 GEGPTPdpwGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAA 368
Cdd:PRK07764  727 GASAPS---PAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAP 774
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 231-501 5.39e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.02  E-value: 5.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  231 SLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPtpasGDPWRPAAPTGPSVDPWG 310
Cdd:PHA03247  2694 SLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATP----GGPARPARPPTTAGPPAP 2769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  311 GTPA-PAAGEGPT-PDPWGSSDGGAPVSGPPSSDPW-----APAPAFSDPWGGSPAKPSSNGTAAVGGFDTEPDEFsdfd 383
Cdd:PHA03247  2770 APPAaPAAGPPRRlTRPAVASLSESRESLPSPWDPAdppaaVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGP---- 2845

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  384 rLRTALPTSGSSTGelellAGEVPARSPGafdmsgvGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNaalvdlDSLV 463
Cdd:PHA03247  2846 -PPPSLPLGGSVAP-----GGDVRRRPPS-------RSPAAKPAAPARPPVRRLARPAVSRSTESFALPP------DQPE 2906

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2311270601  464 SRPGPTPPGSKASNPFLPSGAPPTGPSVTNPFQPAPPA 501
Cdd:PHA03247  2907 RPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLA 2944
 
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 2.41e-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: 2.41e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  19 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd16990     1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2311270601  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 2.69e-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: 2.69e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  17 YSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLNDKGKNWRHIYKALTLLEYLLKNGSERVVDDL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2311270601  97 KENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRL 140
Cdd:pfam01417  81 RENIYIIRTLTDFHYIDENGKDQGINVRKKAKEILNLLEDDELL 124
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
18-144 8.05e-53

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 175.51  E-value: 8.05e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601   18 SEAEIKVREATSNDPWGPSSSLMSEIADLTYNV-VAFSEIMSMIWKRLNDHGkNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEkSSFAEIMAVLWRRLNDTK-NWRVVYKALILLHYLLRNGSPRVILEA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2311270601   97 KENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREER 144
Cdd:smart00273  80 LRNRNRILNLSDFQDIDSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 242-368 1.69e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 54.22  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601 242 PAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPW----GGAAPTPASGDPWRPAAptGPSVDPWGGTPAPAA 317
Cdd:PRK07764  649 APEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPaapaGAAPAQPAPAPAATPPA--GQADDPAAQPPQAAQ 726

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2311270601 318 GEGPTPdpwGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAA 368
Cdd:PRK07764  727 GASAPS---PAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAP 774
PHA03247 PHA03247
large tegument protein UL36; Provisional
 231-501 5.39e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.02  E-value: 5.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  231 SLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPtpasGDPWRPAAPTGPSVDPWG 310
Cdd:PHA03247  2694 SLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATP----GGPARPARPPTTAGPPAP 2769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  311 GTPA-PAAGEGPT-PDPWGSSDGGAPVSGPPSSDPW-----APAPAFSDPWGGSPAKPSSNGTAAVGGFDTEPDEFsdfd 383
Cdd:PHA03247  2770 APPAaPAAGPPRRlTRPAVASLSESRESLPSPWDPAdppaaVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGP---- 2845

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  384 rLRTALPTSGSSTGelellAGEVPARSPGafdmsgvGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNaalvdlDSLV 463
Cdd:PHA03247  2846 -PPPSLPLGGSVAP-----GGDVRRRPPS-------RSPAAKPAAPARPPVRRLARPAVSRSTESFALPP------DQPE 2906

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2311270601  464 SRPGPTPPGSKASNPFLPSGAPPTGPSVTNPFQPAPPA 501
Cdd:PHA03247  2907 RPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLA 2944
 
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 2.41e-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: 2.41e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  19 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd16990     1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2311270601  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 2.69e-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: 2.69e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  17 YSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLNDKGKNWRHIYKALTLLEYLLKNGSERVVDDL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2311270601  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 1.16e-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: 1.16e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  17 YSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:cd16991     2 YSSTQVKVRNATSNDPWGPSGDEMAEIAELTYDQHDFVEIMDMLDKRLNDKGKNWRHVAKALTVLDYLLHFGSENVVLWA 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2311270601  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 1.22e-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: 1.22e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  20 AEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKEN 99
Cdd:cd03571     1 LELLVREATSNEPWGPTGSQLAEIAQATFDYDDYQRIMKVLWKRLNDKGKNWRHVYKALTLLEYLLKNGSERVVDEFRDN 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2311270601 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 1.59e-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: 1.59e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  20 AEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKR-LNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd16989     1 IESKVREATNDDPWGPTGQLMQEIARYTFTYEQFPEVMNMLWKRmLKDNKKNWRRVYKSLLLLDYLLKNGSERVVTSARE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2311270601  99 NMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREERAHA 147
Cdd:cd16989    81 HIYDLRSLENYHFIDEKGKDQGINVRQKVKEIIELLQDDERLREERKKA 129
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
18-144 8.05e-53

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 175.51  E-value: 8.05e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601   18 SEAEIKVREATSNDPWGPSSSLMSEIADLTYNV-VAFSEIMSMIWKRLNDHGkNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEkSSFAEIMAVLWRRLNDTK-NWRVVYKALILLHYLLRNGSPRVILEA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2311270601   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 4.31e-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: 4.31e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  21 EIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLND-HGKNWRHVYKAMTLMEYLIKTGSERVSQQCKEN 99
Cdd:cd16992     2 ESKVREATNNDPWGASSTLMQEIAQGTYNYQQFNEIMPMIYKRFTEkAGSEWRQIYKALQLLEYLIKNGSERVVDDARGH 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2311270601 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 4.99e-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: 4.99e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  20 AEIKVREATSNDPWGPSSSLMSEIADLTYN-VVAFSEIMSMIWKRLNDHgkNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd00197     1 FEKTVEKATSNENMGPDWPLIMEICDLINEtNVGPKEAVDAIKKRINNK--NPHVVLKALTLLEYCVKNCGERFHQEVAS 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2311270601  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 1.20e-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: 1.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  20 AEIKVREAT-SNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHG-----KNWRHVYKAMTLMEYLIKTGSERVS 93
Cdd:cd16994     1 TELKVKQATdDNETSGATGTLMNEISVLTYSPKTLKEITQVLKKRLSGNSkksshKNCVHILKTLTLISYLINNGSNEFI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2311270601  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 9.05e-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: 9.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  21 EIKVREATSNDPWGPSSSLMSEIADLTYNVVAFsEIMSMIWKRLNDH-------------------GKNWRHVYKAMTLM 81
Cdd:cd16993     2 QIDIRRATNTDAWGPTPKHLAKVLRNRYQVPLY-LMTEYTLKRLVDHiatrpknlyekarkdyvnyGSEWRVVLKCLIVI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2311270601  82 EYLIKTGS--ERVSQ--QCKENMYAVQTLKDFQY---VDRDGKDQ--GVNVREKAKQLVALLRDEDRLREERA 145
Cdd:cd16993    81 EFLLLNVDtgDELNQvlSCLLNHKHIFTREIAQYkvkFSNDGKMEihERGIQKKCELILQLIEDSDFLRQERA 153
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 242-368 1.69e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 54.22  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601 242 PAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPW----GGAAPTPASGDPWRPAAptGPSVDPWGGTPAPAA 317
Cdd:PRK07764  649 APEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPaapaGAAPAQPAPAPAATPPA--GQADDPAAQPPQAAQ 726

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2311270601 318 GEGPTPdpwGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAA 368
Cdd:PRK07764  727 GASAPS---PAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAP 774
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 245-413 3.55e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 53.07  E-value: 3.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601 245 PQASDPWGGPAsvptavpvAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDP-WGGTPAPAAGEGPTP 323
Cdd:PRK07764  615 PAAPAAPAAPA--------APAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPaKAGGAAPAAPPPAPA 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601 324 DPWGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLA 403
Cdd:PRK07764  687 PAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAP 766

                         170
                  ....*....|
gi 2311270601 404 GEVPARSPGA 413
Cdd:PRK07764  767 AAAPAAAPPP 776
PHA03247 PHA03247
large tegument protein UL36; Provisional
 231-501 5.39e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.02  E-value: 5.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  231 SLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPtpasGDPWRPAAPTGPSVDPWG 310
Cdd:PHA03247  2694 SLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATP----GGPARPARPPTTAGPPAP 2769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  311 GTPA-PAAGEGPT-PDPWGSSDGGAPVSGPPSSDPW-----APAPAFSDPWGGSPAKPSSNGTAAVGGFDTEPDEFsdfd 383
Cdd:PHA03247  2770 APPAaPAAGPPRRlTRPAVASLSESRESLPSPWDPAdppaaVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGP---- 2845

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  384 rLRTALPTSGSSTGelellAGEVPARSPGafdmsgvGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNaalvdlDSLV 463
Cdd:PHA03247  2846 -PPPSLPLGGSVAP-----GGDVRRRPPS-------RSPAAKPAAPARPPVRRLARPAVSRSTESFALPP------DQPE 2906

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2311270601  464 SRPGPTPPGSKASNPFLPSGAPPTGPSVTNPFQPAPPA 501
Cdd:PHA03247  2907 RPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLA 2944
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 244-371 1.20e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 51.53  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601 244 PPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGA-APTPASGDPWRPAAPTGPSVDPWGGTPAPAagegpT 322
Cdd:PRK07764  591 APGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAaAPAEASAAPAPGVAAPEHHPKHVAVPDASD-----G 665

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2311270601 323 PDPWGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAAVGG 371
Cdd:PRK07764  666 GDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQA 714
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 240-502 3.87e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 49.78  E-value: 3.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  240 TTPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPwggtPAPAAGE 319
Cdd:PHA03307   113 SPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEE----TARAPSS 188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  320 GPTPDPWGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKpSSNGTAAVGGFDTEPDEFSDFDRLRTALPTSGSSTGEL 399
Cdd:PHA03307   189 PPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAA-DDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPT 267

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  400 ELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGSKASNPF 479
Cdd:PHA03307   268 RIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSP 347

                          250       260
                   ....*....|....*....|...
gi 2311270601  480 LPSGAPPTGPSvtnPFQPAPPAT 502
Cdd:PHA03307   348 SRSPSPSRPPP---PADPSSPRK 367
VHS cd03561
VHS (Vps27/Hrs/STAM) domain family; The VHS domain is present in Vps27 (Vacuolar Protein ...
 24-131 1.15e-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: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  24 VREATSNDPWGPSSSLMSEIADLtYNVVAFS--EIMSMIWKRLNDhgKNWRHVYKAMTLMEYLIKTGSERVSQQckenmy 101
Cdd:cd03561     5 VEKATSESLTEPDWALNLEICDL-VNSDPAQakDAVRALRKRLQS--KNPKVQLLALTLLETLVKNCGAPFHSE------ 75

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2311270601 102 aVQTLKDFQYVDR--DGKDQGVNVREKAKQLV 131
Cdd:cd03561    76 -VASRDFLQELVKlvKKKKTSPEVREKALALI 106
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 241-343 1.37e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.06  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601 241 TPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEG 320
Cdd:PRK07764  402 AAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPA 481

                          90       100
                  ....*....|....*....|...
gi 2311270601 321 PTPDPWGSSDGGAPVSGPPSSDP 343
Cdd:PRK07764  482 PAPPAAPAPAAAPAAPAAPAAPA 504
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 272-502 2.73e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.90  E-value: 2.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601 272 GGPAVPPAADPwGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDPWGSSDGG-------APVSGPPSSDPW 344
Cdd:PRK07764  400 SAAAAAPAAAP-APAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAaapsaqpAPAPAAAPEPTA 478

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601 345 APAPAFSDPWGGSPAKPSSNGTAAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELeLLAGEVPARSPG-----AFDMSGV 419
Cdd:PRK07764  479 APAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRERWPEILAAVPKRSRKTWAI-LLPEATVLGVRGdtlvlGFSTGGL 557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601 420 GGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAAlvdldsLVSRPGPTPPGSKASNPFLPSGAPPTGPSVTNPFQPAP 499
Cdd:PRK07764  558 ARRFASPGNAEVLVTALAEELGGDWQVEAVVGPAPG------AAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAG 631


                  ...
gi 2311270601 500 PAT 502
Cdd:PRK07764  632 AAA 634
PHA03247 PHA03247
large tegument protein UL36; Provisional
 274-509 7.21e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 7.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  274 PAVPPAADPWGGAAPTPASGDPWRPAAPTgpsvdpwggTPAPAAGEGPTPDPWGSSDGGAPVSGPPSSDPWAPAPAfsdp 353
Cdd:PHA03247   255 PAPPPVVGEGADRAPETARGATGPPPPPE---------AAAPNGAAAPPDGVWGAALAGAPLALPAPPDPPPPAPA---- 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  354 wGGSPAKPSSNGTAAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARS---PGAFDMSGVGGSLAESVGSP 430
Cdd:PHA03247   322 -GDAEEEDDEDGAMEVVSPLPRPRQHYPLGFPKRRRPTWTPPSSLEDLSAGRHHPKRaslPTRKRRSARHAATPFARGPG 400

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2311270601  431 PPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGSKASNPfLPSGAPPTGPSVTNPFQPAPPATLTLNQLR 509
Cdd:PHA03247   401 GDDQTRPAAPVPASVPTPAPTPVPASAPPPPATPLPSAEPGSDDGPAP-PPERQPPAPATEPAPDDPDDATRKALDALR 478
PHA03247 PHA03247
large tegument protein UL36; Provisional
 243-502 1.01e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  243 APPQASDPWGGP-----ASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPAS---GDPWRPAAPTGPSVDPWGGTPA 314
Cdd:PHA03247  2491 AAGAAPDPGGGGppdpdAPPAPSRLAPAILPDEPVGEPVHPRMLTWIRGLEELASddaGDPPPPLPPAAPPAAPDRSVPP 2570

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  315 PAAGEGPtPDPWGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAAvggfdTEPDEFSDFDRlrtalptsGS 394
Cdd:PHA03247  2571 PRPAPRP-SEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHA-----PDPPPPSPSPA--------AN 2636

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  395 STGELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGSK 474
Cdd:PHA03247  2637 EPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALV 2716

                          250       260
                   ....*....|....*....|....*...
gi 2311270601  475 ASNPFLPSGAPPTGPSVTNPFQPAPPAT 502
Cdd:PHA03247  2717 SATPLPPGPAAARQASPALPAAPAPPAV 2744
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
241-410 3.97e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.33  E-value: 3.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601 241 TPAPPQASdPWGGPASVPTAVPVAAAASdpwggpAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEG 320
Cdd:PRK12323  398 APAAPPAA-PAAAPAAAAAARAVAAAPA------RRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPR 470

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601 321 PTPDPwgssDGGAPVSGPPSSDPwAPAPAFSDPWGGSPAKPSSNGTAAVGGfDTEPDEFSDFDRLRTALPTSGSSTGELE 400
Cdd:PRK12323  471 PVAAA----AAAAPARAAPAAAP-APADDDPPPWEELPPEFASPAPAQPDA-APAGWVAESIPDPATADPDDAFETLAPA 544

                         170
                  ....*....|
gi 2311270601 401 LLAGEVPARS 410
Cdd:PRK12323  545 PAAAPAPRAA 554
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 273-371 5.08e-04

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 42.68  E-value: 5.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601 273 GPAVPPAADpwgGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDPWGSSDGGAPVSGPPSSDPWAPAPafsD 352
Cdd:PHA03264  263 GYEPPPAPS---GGSPAPPGDDRPEAKPEPGPVEDGAPGRETGGEGEGPEPAGRDGAAGGEPKPGPPRPAPDADRP---E 336

                          90
                  ....*....|....*....
gi 2311270601 353 PWGGSPAKPSSNGTAAVGG 371
Cdd:PHA03264  337 GWPSLEAITFPPPTPATPA 355
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 272-368 6.91e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.39  E-value: 6.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601 272 GGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGE-----GPTPDPWGSSDGGAPVSGPPSSDPWAP 346
Cdd:PRK14951  371 EAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPaaappAPVAAPAAAAPAAAPAAAPAAVALAPA 450

                          90       100
                  ....*....|....*....|..
gi 2311270601 347 APAFSDPWGGSPAKPSSNGTAA 368
Cdd:PRK14951  451 PPAQAAPETVAIPVRVAPEPAV 472
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 241-356 9.26e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.01  E-value: 9.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601 241 TPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEG 320
Cdd:PRK14951  380 TPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPET 459

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2311270601 321 PTPDPWGSSDGGAPVSGPPSSDPWAPAP----AFSDPWGG 356
Cdd:PRK14951  460 VAIPVRVAPEPAVASAAPAPAAAPAAARltptEEGDVWHA 499
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
240-379 9.70e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.17  E-value: 9.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601 240 TTPAPPQASDPWGGPASVPTAVPVAAAASDPwggPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGE 319
Cdd:PRK12323  372 AGPATAAAAPVAQPAPAAAAPAAAAPAPAAP---PAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAP 448

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601 320 GPTPDPWGSSDGGAPVSGPPSSDPwaPAPAFSDPWGGSPAKPSSNGTAAVGGFDTEPDEF 379
Cdd:PRK12323  449 APAPAPAAAPAAAARPAAAGPRPV--AAAAAAAPARAAPAAAPAPADDDPPPWEELPPEF 506
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
242-377 1.65e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 41.37  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601 242 PAPPQASDPWGG-PASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEG 320
Cdd:PRK07003  360 PAVTGGGAPGGGvPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRG 439

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2311270601 321 ptpdpwgssDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAAVGGFDTEPD 377
Cdd:PRK07003  440 ---------DDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPD 487
PHA03247 PHA03247
large tegument protein UL36; Provisional
 244-502 1.66e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  244 PPQASDP---WGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTP---ASGDPWRPAAPTGPSVDPWGGTPAPAA 317
Cdd:PHA03247  2673 AAQASSPpqrPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPpgpAAARQASPALPAAPAPPAVPAGPATPG 2752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  318 GEGPTPDPWGSSdgGAPVSGPPSSDPWAPAPAFSDPwGGSPAKPSSNgtaavggfdtepdefsdfdrlrtALPTSGSSTG 397
Cdd:PHA03247  2753 GPARPARPPTTA--GPPAPAPPAAPAAGPPRRLTRP-AVASLSESRE-----------------------SLPSPWDPAD 2806

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  398 ELELLAGEVPARSPGAFDMSGVggslaesvgSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGSKASN 477
Cdd:PHA03247  2807 PPAAVLAPAAALPPAASPAGPL---------PPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAA 2877

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2311270601  478 P--------FLPSGAPPTGPSVTNPFQPAPPAT 502
Cdd:PHA03247  2878 ParppvrrlARPAVSRSTESFALPPDQPERPPQ 2910
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
236-369 2.23e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.01  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601 236 ADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGGP--AVPPAADPWGG----AAPTPASGDPWRPAAPTGPSVDPW 309
Cdd:PRK12323  420 AAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPaaAARPAAAGPRPvaaaAAAAPARAAPAAAPAPADDDPPPW 499

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2311270601 310 GGTPAPAAGEGP-TPDPWGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAAV 369
Cdd:PRK12323  500 EELPPEFASPAPaQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPV 560
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 275-368 2.55e-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: 2.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  275 AVPPA-----ADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDPWGSSDGGAPVSGPPSSDPWAPAPA 349
Cdd:PRK12270    24 SVDPSwreffADYGPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAA 103

                           90       100
                   ....*....|....*....|..
gi 2311270601  350 FSDPWGGSPAKPSSN---GTAA 368
Cdd:PRK12270   104 AAAAPAAAAVEDEVTplrGAAA 125
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 240-325 2.62e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601 240 TTPAPPQASDPWGGPASVPTAVPVAAAASDpwggPAVPPAADPWGGAAPTPASGDPwrPAAPTGPSVDPWGGTPAPAAGE 319
Cdd:PRK07764  707 ATPPAGQADDPAAQPPQAAQGASAPSPAAD----DPVPLPPEPDDPPDPAGAPAQP--PPPPAPAPAAAPAAAPPPSPPS 780


                  ....*.
gi 2311270601 320 GPTPDP 325
Cdd:PRK07764  781 EEEEMA 786
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 215-368 2.87e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.54  E-value: 2.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  215 MAIEESKRETGGKEESSLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPwgGPAVPPAADPWGGAAPTPASGD 294
Cdd:PHA03307   239 SSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRER--SPSPSPSSPGSGPAPSSPRASS 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  295 PWRP--------AAPTGPSVDPWGGTPAPAAGEGPTPdpwGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGT 366
Cdd:PHA03307   317 SSSSsresssssTSSSSESSRGAAVSPGPSPSRSPSP---SRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAA 393


                   ..
gi 2311270601  367 AA 368
Cdd:PHA03307   394 VA 395
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 241-350 2.90e-03

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 40.48  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601 241 TPAPPQASDPWGGPASVPTAVPvaaaasDPWGGPAVPPAADPWGGAAPTPASGDPWRPA-APTGPSVDPWGGTPAPAAGE 319
Cdd:PHA03269   33 TSAATQKPDPAPAPHQAASRAP------DPAVAPTSAASRKPDLAQAPTPAASEKFDPApAPHQAASRAPDPAVAPQLAA 106

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2311270601 320 GPTPDPW-----GSSDGGAPVSGPPSSDPWAPAPAF 350
Cdd:PHA03269  107 APKPDAAeaftsAAQAHEAPADAGTSAASKKPDPAA 142
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 240-334 2.94e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 40.43  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601 240 TTPAPPQASDPWGGPASVPTAVPVAAAASDPwggPAVPPAADPWGGAAPTPA-SGDPWRPaAPTGPSVDPWGGTPAPAAG 318
Cdd:PRK14959  396 TIPTPGTQGPQGTAPAAGMTPSSAAPATPAP---SAAPSPRVPWDDAPPAPPrSGIPPRP-APRMPEASPVPGAPDSVAS 471

                          90
                  ....*....|....*.
gi 2311270601 319 EGPTPDPWGSSDGGAP 334
Cdd:PRK14959  472 ASDAPPTLGDPSDTAE 487
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 241-334 4.10e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.97  E-value: 4.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601 241 TPAPPQASDPWGGPASVPTAVPVAaaaSDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEG 320
Cdd:PRK07764  422 APAPAAAPQPAPAPAPAPAPPSPA---GNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPA 498

                          90
                  ....*....|....
gi 2311270601 321 PTPDPWGSSDGGAP 334
Cdd:PRK07764  499 APAAPAGADDAATL 512
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 247-490 6.51e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 39.38  E-value: 6.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  247 ASDPWGGPASVPTAVPVAAAASDPWGGPAV-PPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDP 325
Cdd:PHA03307    44 VSDSAELAAVTVVAGAAACDRFEPPTGPPPgPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPP 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  326 wgssDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAAVGGFDTEPD--EFSDFDRLRTALPTSGSSTGELELLA 403
Cdd:PHA03307   124 ----ASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQaaLPLSSPEETARAPSSPPAEPPPSTPP 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  404 GEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPES----FLGPNAALVDLDSLVSRPGPTPPGSKASNPf 479
Cdd:PHA03307   200 AAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESsgcgWGPENECPLPRPAPITLPTRIWEASGWNGP- 278

                          250
                   ....*....|.
gi 2311270601  480 lPSGAPPTGPS 490
Cdd:PHA03307   279 -SSRPGPASSS 288
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 301-370 7.01e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 39.28  E-value: 7.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601 301 PTGPSVDPWGGTPAPAAGEG-----PTPDPWG-----SSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAAVG 370
Cdd:PRK14959  373 PSGGGASAPSGSAAEGPASGgaatiPTPGTQGpqgtaPAAGMTPSSAAPATPAPSAAPSPRVPWDDAPPAPPRSGIPPRP 452
PHA03247 PHA03247
large tegument protein UL36; Provisional
 241-548 7.47e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 7.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  241 TPAPPQASDPWGGPASVPTAVPVAAAASDPWGG----PAVPPaaDPWGGAAPTPASGDPWRPAAPTGPSVDPwggTPAPA 316
Cdd:PHA03247  2552 PPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSrarrPDAPP--QSARPRAPVDDRGDPRGPAPPSPLPPDT---HAPDP 2626

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  317 AGEGPTPDPWGSSDGGAPVSGPPSSDPWAPAPAFSDPwggsPAKPSSNGTAAVGGFDTEPdefsdfDRLRTALPTSGSST 396
Cdd:PHA03247  2627 PPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSR----PRRARRLGRAAQASSPPQR------PRRRAARPTVGSLT 2696

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  397 GELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTptpptrkTPESFLGPNAALVDLdslvsrpGPTPPGSKAS 476
Cdd:PHA03247  2697 SLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPA-------APAPPAVPAGPATPG-------GPARPARPPT 2762

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2311270601  477 NPFLPSGAPPTGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNP 548
Cdd:PHA03247  2763 TAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSA 2834
PHA03247 PHA03247
large tegument protein UL36; Provisional
 273-502 9.17e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.15  E-value: 9.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  273 GPAVP-PAADPWGGAAPTpasgdpwrPAAPTGPSVDPWGGTPAPAAGEGPTPDPW---------GSSDGGAPvsgPPSSD 342
Cdd:PHA03247  2488 FPFAAgAAPDPGGGGPPD--------PDAPPAPSRLAPAILPDEPVGEPVHPRMLtwirgleelASDDAGDP---PPPLP 2556

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  343 PWAPAPAFSDPWGGSPAKPSSNGtAAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAG---------EVPARSPGA 413
Cdd:PHA03247  2557 PAAPPAAPDRSVPPPRPAPRPSE-PAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLppdthapdpPPPSPSPAA 2635

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  414 FDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNA--------------ALVDLDSLVSRPGPTPPGSKASNPF 479
Cdd:PHA03247  2636 NEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQAssppqrprrraarpTVGSLTSLADPPPPPPTPEPAPHAL 2715

                          250       260
                   ....*....|....*....|...
gi 2311270601  480 LPSGAPPTGPSVTNPFQPAPPAT 502
Cdd:PHA03247  2716 VSATPLPPGPAAARQASPALPAA 2738
PHA03247 PHA03247
large tegument protein UL36; Provisional
 242-377 9.65e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.15  E-value: 9.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  242 PAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAAdpwggaAPTPASGDPWRPAAPTGPSVDPWGGTPApaagEGP 321
Cdd:PHA03247  2889 PAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPP------QPQPPPPPPPRPQPPLAPTTDPAGAGEP----SGA 2958

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2311270601  322 TPDPWGSSDGGAPVSGP----PSSDPWAPAPAFSDPWGGSPAKPSSNGTAAVGGFDTEPD 377
Cdd:PHA03247  2959 VPQPWLGALVPGRVAVPrfrvPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETD 3018
 
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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