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Conserved domains on  [gi|1767231509|ref|NP_001361962|]
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Phosphatidylinositol-binding clathrin assembly protein unc-11 [Caenorhabditis elegans]

Protein Classification

ANTH domain-containing protein( domain architecture ID 13016467)

ANTH (AP180 N-Terminal Homology) domain-containing protein may act as clathrin coat assembly protein; similar to Caenorhabditis elegans phosphatidylinositol-binding clathrin assembly protein unc-11

CATH:  1.20.58.150|1.25.40.90
Gene Ontology:  GO:0048268|GO:0030136|GO:0005545|GO:0030276
PubMed:  22748146|12740367|12742163

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANTH_N_AP180 cd16985
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of adaptor protein 180 (AP180) ...
 37-154 1.03e-77

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of adaptor protein 180 (AP180) subfamily; The Adaptor Protein 180 (AP180) subfamily members are phosphatidylinositol-binding clathrin assembly proteins, including mammalian clathrin coat assembly protein AP180 and Clathrin Assembly Lymphoid Myeloid Leukemia protein (CALM), Drosophila LAP (also called Like-AP180 or AP180), and Caenorhabditis elegans Uncoordinated protein 11 (unc-11, also called AP180-like adaptor protein). They are components of the adaptor complexes which link clathrin to receptors in coated vesicles. AP180 and CALM play important roles in clathrin-mediated endocytosis. AP180, also called 91 kDa synaptosomal-associated protein (SNAP91) or phosphoprotein F1-20, is a brain-specific clathrin-binding protein which stimulates clathrin assembly during the recycling of synaptic vesicles. CALM, also called phosphatidylinositol binding clathrin assembly protein (PICALM), is ubiquitously expressed. Members of this subfamily contain ANTH domains, which bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains of the Adaptor Protein 180 (AP180) subfamily.


:

Pssm-ID: 340782  Cd Length: 117  Bit Score: 241.17  E-value: 1.03e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509  37 LGKTICKATTEEVMAPKKKHLDYLLHCTNEPNVSIPSMANLLIERTQNPNWTVVYKALITIHNIMCYGNERFSQYLASCN 116
Cdd:cd16985     1 LAKAVCKATTHEVMGPKKKHLDYLVQCTNEPNVNIPQLADLLFERTQNSSWVVVFKALITTHHLMVYGNERFIQYLASRN 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1767231509 117 TTFNLTAFVDKVGGaGGYDMSTHVRRYAKYIGEKINTY 154
Cdd:cd16985    81 SLFNLSNFLDKSGS-QGYDMSTFIRRYAKYLNEKAISY 117
KREPA super family cl49620
Kinetoplastid RNA Editing Protein A (KREPA); The KREPA 1-6 (TbMP81, 63, 42, 24, 19, and 18, ...
 364-528 3.66e-04

Kinetoplastid RNA Editing Protein A (KREPA); The KREPA 1-6 (TbMP81, 63, 42, 24, 19, and 18, respectively) proteins are components of the RNA editing complex of parasitic protozoans such as Trypanosoma and Leishmania species. These parasites have a uniquely organized mitochondrial genome, the kinetoplast. Most kinetoplast-transcribed mRNAs are cryptic and encode multiple subunits for the electron transport chain following maturation through a uridine insertion/deletion process called RNA editing. KREPAs participate in the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. The editosome, a high molecular mass enzyme complex, carries out the reaction with the help of critical enzymes and structural proteins. Five related editosome proteins KREPA1 (TbMP81), KREPA2 (TbMP63), KREPA3 (TbMP42), KREPA4 (TbMP24), KREPA5 (TbMP19), and KREPA6 (TbMP18) play critical roles in the structure and auxiliary functions of the editing process without any predicted catalytic function. The KREPA1, KREPA2, and KREPA3 proteins contain C2H2 zinc finger motifs and KREPA4 and KREPA6, contain RNA-binding domains but all have a conserved C-terminal sequences that resemble an oligonucleotide-binding (OB)-fold domain. Thus, this group of five proteins is likely to be involved in protein-protein and/or protein-RNA interactions. RNA editing is crucial for the parasite's survival in both its bloodstream and procyclic form life cycle stages which allows the parasite to adapt to its environment and maintain its viability.


The actual alignment was detected with superfamily member cd23959:

Pssm-ID: 483960 [Multi-domain]  Cd Length: 424  Bit Score: 43.32  E-value: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509 364 NPFANDVASAAPAPATSAAQPDLLDMFQSSAAPAPQT---------ADVTNPF---GNFAAPSAFPTNVPPP-----AAH 426
Cdd:cd23959    67 NPFDGPGLVTASTVSDCYVGNANFYEVDMSDAFAMAPdeslgpfraARVPNPFsasSSTQRETHKTAQVAPPkaepqTAP 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509 427 SAPFGVQPAPQHSAAPFYANLHQAPPMQSQAPNGHQAAPF--GYPNAHPDDLARMTAQMSLNQQGYRAPAgwntttSAVS 504
Cdd:cd23959   147 VTPFGQLPMFGQHPPPAKPLPAAAAAQQSSASPGEVASPFasGTVSASPFATATDTAPSSGAPDGFPAEA------SAPS 220

                         170       180
                  ....*....|....*....|....
gi 1767231509 505 nnPFGATSAPQPMYTAPMGMYQQP 528
Cdd:cd23959   221 --PFAAPASAASFPAAPVANGEAA 242
 
Name Accession Description Interval E-value
ANTH_N_AP180 cd16985
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of adaptor protein 180 (AP180) ...
 37-154 1.03e-77

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of adaptor protein 180 (AP180) subfamily; The Adaptor Protein 180 (AP180) subfamily members are phosphatidylinositol-binding clathrin assembly proteins, including mammalian clathrin coat assembly protein AP180 and Clathrin Assembly Lymphoid Myeloid Leukemia protein (CALM), Drosophila LAP (also called Like-AP180 or AP180), and Caenorhabditis elegans Uncoordinated protein 11 (unc-11, also called AP180-like adaptor protein). They are components of the adaptor complexes which link clathrin to receptors in coated vesicles. AP180 and CALM play important roles in clathrin-mediated endocytosis. AP180, also called 91 kDa synaptosomal-associated protein (SNAP91) or phosphoprotein F1-20, is a brain-specific clathrin-binding protein which stimulates clathrin assembly during the recycling of synaptic vesicles. CALM, also called phosphatidylinositol binding clathrin assembly protein (PICALM), is ubiquitously expressed. Members of this subfamily contain ANTH domains, which bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains of the Adaptor Protein 180 (AP180) subfamily.


Pssm-ID: 340782  Cd Length: 117  Bit Score: 241.17  E-value: 1.03e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509  37 LGKTICKATTEEVMAPKKKHLDYLLHCTNEPNVSIPSMANLLIERTQNPNWTVVYKALITIHNIMCYGNERFSQYLASCN 116
Cdd:cd16985     1 LAKAVCKATTHEVMGPKKKHLDYLVQCTNEPNVNIPQLADLLFERTQNSSWVVVFKALITTHHLMVYGNERFIQYLASRN 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1767231509 117 TTFNLTAFVDKVGGaGGYDMSTHVRRYAKYIGEKINTY 154
Cdd:cd16985    81 SLFNLSNFLDKSGS-QGYDMSTFIRRYAKYLNEKAISY 117
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 37-299 7.16e-75

ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.


Pssm-ID: 400137  Cd Length: 272  Bit Score: 239.51  E-value: 7.16e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509  37 LGKTICKATTEEvMAPKKKHLDYLLHCTNEPNVSIPSMANLLIERTQNP-NWTVVYKALITIHNIMCYGNERFSQYLASC 115
Cdd:pfam07651   2 LEVAVVKATSHD-EAPPKEKHVREILVGTSSSAKLAALFWALSRRLPLTrSWVVAFKALILVHKLLREGHPSVLQELLRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509 116 NTTFNLTAFVDKvgGAGGYDMSTHVRRYAKYIGEKINTYRMCAFD---FCKVKRG----REDGLLR--TMHTDKLLKTIP 186
Cdd:pfam07651  81 RRRISSLLRISS--FSLSWDYGAFIRAYAKYLDERLDFHRKLPRDpgtFERVEYGslvaVGDPNERylTMSMEDLLDSIP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509 187 ILQNQIDALLEFSVTTSELNNGVINCSFILLFRDLIRLFACYNDGIINVLEKYFDMNKKQCRDALDTYKSFLTRLDKVAE 266
Cdd:pfam07651 159 KLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQFERLKE 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1767231509 267 FLRVAESVGIDRG-EIPDLTRAPASLLEALEAHL 299
Cdd:pfam07651 239 FYEVCKNLGYFRSlEIPKLPHIPPNLLEALEEYL 272
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
39-161 2.11e-29

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 112.72  E-value: 2.11e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509   39 KTICKATTEEVMAPKKKHLDYLLHCTNEPNVSIPSMANLLIERTQN-PNWTVVYKALITIHNIMCYGNER-FSQYLASCN 116
Cdd:smart00273   5 VKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDtKNWRVVYKALILLHYLLRNGSPRvILEALRNRN 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1767231509  117 TTFNLTAFVDKvgGAGGYDMSTHVRRYAKYIGEKINTYRMCAFDF 161
Cdd:smart00273  85 RILNLSDFQDI--DSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 364-528 3.66e-04

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 43.32  E-value: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509 364 NPFANDVASAAPAPATSAAQPDLLDMFQSSAAPAPQT---------ADVTNPF---GNFAAPSAFPTNVPPP-----AAH 426
Cdd:cd23959    67 NPFDGPGLVTASTVSDCYVGNANFYEVDMSDAFAMAPdeslgpfraARVPNPFsasSSTQRETHKTAQVAPPkaepqTAP 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509 427 SAPFGVQPAPQHSAAPFYANLHQAPPMQSQAPNGHQAAPF--GYPNAHPDDLARMTAQMSLNQQGYRAPAgwntttSAVS 504
Cdd:cd23959   147 VTPFGQLPMFGQHPPPAKPLPAAAAAQQSSASPGEVASPFasGTVSASPFATATDTAPSSGAPDGFPAEA------SAPS 220

                         170       180
                  ....*....|....*....|....
gi 1767231509 505 nnPFGATSAPQPMYTAPMGMYQQP 528
Cdd:cd23959   221 --PFAAPASAASFPAAPVANGEAA 242
PHA03247 PHA03247
large tegument protein UL36; Provisional
 395-533 1.05e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509  395 APAPQTADVTNPFGNFAAPSAFPtnvPPPAAHSAPfgvqPAPQHSAAPFYANLHQAPPMQSQAPnghQAAPFGYPNAHPD 474
Cdd:PHA03247  2711 APHALVSATPLPPGPAAARQASP---ALPAAPAPP----AVPAGPATPGGPARPARPPTTAGPP---APAPPAAPAAGPP 2780

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1767231509  475 DLARMTAQMSLNQQGYRAPAGWNTTTSAVsnnPFGATSAPQPMYTAPMGMYQQPFGAQP 533
Cdd:PHA03247  2781 RRLTRPAVASLSESRESLPSPWDPADPPA---AVLAPAAALPPAASPAGPLPPPTSAQP 2836
 
Name Accession Description Interval E-value
ANTH_N_AP180 cd16985
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of adaptor protein 180 (AP180) ...
 37-154 1.03e-77

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of adaptor protein 180 (AP180) subfamily; The Adaptor Protein 180 (AP180) subfamily members are phosphatidylinositol-binding clathrin assembly proteins, including mammalian clathrin coat assembly protein AP180 and Clathrin Assembly Lymphoid Myeloid Leukemia protein (CALM), Drosophila LAP (also called Like-AP180 or AP180), and Caenorhabditis elegans Uncoordinated protein 11 (unc-11, also called AP180-like adaptor protein). They are components of the adaptor complexes which link clathrin to receptors in coated vesicles. AP180 and CALM play important roles in clathrin-mediated endocytosis. AP180, also called 91 kDa synaptosomal-associated protein (SNAP91) or phosphoprotein F1-20, is a brain-specific clathrin-binding protein which stimulates clathrin assembly during the recycling of synaptic vesicles. CALM, also called phosphatidylinositol binding clathrin assembly protein (PICALM), is ubiquitously expressed. Members of this subfamily contain ANTH domains, which bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains of the Adaptor Protein 180 (AP180) subfamily.


Pssm-ID: 340782  Cd Length: 117  Bit Score: 241.17  E-value: 1.03e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509  37 LGKTICKATTEEVMAPKKKHLDYLLHCTNEPNVSIPSMANLLIERTQNPNWTVVYKALITIHNIMCYGNERFSQYLASCN 116
Cdd:cd16985     1 LAKAVCKATTHEVMGPKKKHLDYLVQCTNEPNVNIPQLADLLFERTQNSSWVVVFKALITTHHLMVYGNERFIQYLASRN 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1767231509 117 TTFNLTAFVDKVGGaGGYDMSTHVRRYAKYIGEKINTY 154
Cdd:cd16985    81 SLFNLSNFLDKSGS-QGYDMSTFIRRYAKYLNEKAISY 117
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 37-299 7.16e-75

ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.


Pssm-ID: 400137  Cd Length: 272  Bit Score: 239.51  E-value: 7.16e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509  37 LGKTICKATTEEvMAPKKKHLDYLLHCTNEPNVSIPSMANLLIERTQNP-NWTVVYKALITIHNIMCYGNERFSQYLASC 115
Cdd:pfam07651   2 LEVAVVKATSHD-EAPPKEKHVREILVGTSSSAKLAALFWALSRRLPLTrSWVVAFKALILVHKLLREGHPSVLQELLRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509 116 NTTFNLTAFVDKvgGAGGYDMSTHVRRYAKYIGEKINTYRMCAFD---FCKVKRG----REDGLLR--TMHTDKLLKTIP 186
Cdd:pfam07651  81 RRRISSLLRISS--FSLSWDYGAFIRAYAKYLDERLDFHRKLPRDpgtFERVEYGslvaVGDPNERylTMSMEDLLDSIP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509 187 ILQNQIDALLEFSVTTSELNNGVINCSFILLFRDLIRLFACYNDGIINVLEKYFDMNKKQCRDALDTYKSFLTRLDKVAE 266
Cdd:pfam07651 159 KLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQFERLKE 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1767231509 267 FLRVAESVGIDRG-EIPDLTRAPASLLEALEAHL 299
Cdd:pfam07651 239 FYEVCKNLGYFRSlEIPKLPHIPPNLLEALEEYL 272
ANTH_N cd03564
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ...
 37-154 5.50e-31

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


Pssm-ID: 340767  Cd Length: 120  Bit Score: 116.99  E-value: 5.50e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509  37 LGKTICKATTEEVMAPKKKHLDYLLHCTNE--PNVSIPSMANLLIERTQNPNWTVVYKALITIHNIMCYGNERFSQYLAS 114
Cdd:cd03564     1 LDVAVVKATNHDEVPPKEKHVRKLLLATSNggGRADVAYIVHALAKRLHKKNWIVVLKTLIVIHRLLREGSPSFLEELLR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1767231509 115 CNTT-FNLTAFVDKvGGAGGYDMSTHVRRYAKYIGEKINTY 154
Cdd:cd03564    81 YSGHiFNLSNFKDD-SSPEAWDLSAFIRRYARYLEERLECF 120
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
39-161 2.11e-29

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 112.72  E-value: 2.11e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509   39 KTICKATTEEVMAPKKKHLDYLLHCTNEPNVSIPSMANLLIERTQN-PNWTVVYKALITIHNIMCYGNER-FSQYLASCN 116
Cdd:smart00273   5 VKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDtKNWRVVYKALILLHYLLRNGSPRvILEALRNRN 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1767231509  117 TTFNLTAFVDKvgGAGGYDMSTHVRRYAKYIGEKINTYRMCAFDF 161
Cdd:smart00273  85 RILNLSDFQDI--DSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 34-157 7.72e-26

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: 102.64  E-value: 7.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509  34 GSQLGKTICKATTEEVMAPKKKHLDYLLHCTNEPnVSIPSMANLLIER--TQNPNWTVVYKALITIHNIMCYGNERFSQY 111
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNY-VEFPEIMKMLWKRlnDKGKNWRHIYKALTLLEYLLKNGSERVVDD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1767231509 112 L-ASCNTTFNLTAFvdKVGGAGGYDMSTHVRRYAKYIGEKINTYRMC 157
Cdd:pfam01417  80 LrENIYIIRTLTDF--HYIDENGKDQGINVRKKAKEILNLLEDDELL 124
VHS_ENTH_ANTH cd00197
VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a ...
 37-151 1.11e-24

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: 99.04  E-value: 1.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509  37 LGKTICKATTEEVMAPKKKHLDYLLHCTNEPNVSIPSMANLLIERTQNPNWTVVYKALITIHNIMCYGNERFSQYLASCN 116
Cdd:cd00197     1 FEKTVEKATSNENMGPDWPLIMEICDLINETNVGPKEAVDAIKKRINNKNPHVVLKALTLLEYCVKNCGERFHQEVASND 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1767231509 117 TTFNLTAFVDKvgGAGGYDMSTHVRRYAKYIGEKI 151
Cdd:cd00197    81 FAVELLKFDKS--GLLGDDVSTNVREKAIELVQLW 113
ANTH_N_YAP180 cd16988
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of yeast clathrin coat assembly ...
 39-154 3.10e-19

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of yeast clathrin coat assembly protein AP180 (YAP180) and similar proteins; This subfamily includes yeast clathrin coat assembly protein AP180 (YAP180) and similar proteins. There are two YAP180 proteins in Saccharomyces cerevisiae, AP180A (yAP180A or YAP1801) and AP180B (yAP180B or YAP1802). They are involved in endocytosis and clathrin cage assembly. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains of plant clathrin coat assembly protein AP180 and similar proteins.


Pssm-ID: 340785  Cd Length: 117  Bit Score: 83.39  E-value: 3.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509  39 KTICKATTEEVMAPKKKHLDYLLHCTNEPNVSIPSMANLLIERTQNPNWTVVYKALITIHNIMCYGN-ERFSQYLASCNT 117
Cdd:cd16988     3 KLVKGATKIKLAPPKAKYLDPILLATYSSDASFGEIVRALSRRLRDNSWTVVFKSLIVLHLMIREGEtDDVLLYYLSRPD 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1767231509 118 TFNLTAFVDKvGGAGGYDMSThVRRYAKYIGEKINTY 154
Cdd:cd16988    83 FLDLRKIRNG-SSAGSGQLQN-IQRYAAYLKERVKEY 117
ANTH_N_AP180_plant cd16987
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of plant Clathrin coat assembly ...
 41-150 1.33e-05

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of plant Clathrin coat assembly protein AP180 and similar proteins; This subfamily is composed of plant clathrin coat assembly protein AP180 and other ANTH domain containing proteins that are yet to be characterized. Arabidopsis thaliana AP180 (At-AP180) is a binding partner of plant alphaC-adaptin; it functions as a clathrin assembly protein that promotes the formation of cages with an almost uniform size distribution. In addition to At-AP180, Arabidopsis thaliana contains many ANTH domain containing proteins labelled as putative clathrin assembly proteins included in this subfamily such as At4g02650, At5g10410, At2g25430, and At1g33340, among others. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains of plant clathrin coat assembly protein AP180 and similar proteins.


Pssm-ID: 340784  Cd Length: 122  Bit Score: 44.54  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509  41 ICKATTEEVMAPKKKHLDYLLHCTNepnvSIPSMANLLIE-------RTQNpnWTVVYKALITIHNIMCYGNERFSQYLA 113
Cdd:cd16987     5 VVKATSHDDAPPDEKYVREILSLGS----SSRAYASACVSalsrrlnRTRD--WVVALKCLMLLHRLLRDGSPILEQELS 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1767231509 114 SCNTT----FNLTAFVDKVGGAGGyDMSTHVRRYAKYIGEK 150
Cdd:cd16987    79 LAPSGgrnpLNLSDFRDGSSSKSW-DFSAFVRAYAAYLDER 118
ANTH_N_Sla2p_HIP1_like cd16986
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; ...
 39-110 1.96e-05

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; Members of the Sla2p/HIP1/HIP1R subfamily share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. Both HIP1 and HIP1R promote clathrin assembly in vitro. Yeast Sla2p, is a regulator of membrane cytoskeleton assembly. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. While the ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome, mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively. This model describes the N-terminal region of ANTH domains of the Sla2p/HIP1/HIP1R subfamily.


Pssm-ID: 340783  Cd Length: 117  Bit Score: 43.91  E-value: 1.96e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1767231509  39 KTICKATTEEVMAPKKKHLDYLlHCTNEPNVSIPSMANLLIERTQNPNWTVVYKALITIHNIMCYGNERFSQ 110
Cdd:cd16986     3 KAVNKATNKTDSPPKPKHVRTI-IVKSWTHQKGPQFYEELSKRLLLNNPVVQFKALVTLHKVLRDGPPELSL 73
ANTH_N_Sla2p cd17007
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ...
 37-152 1.44e-04

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; This subfamily is composed of Saccharomyces cerevisiae Sla2 protein (Sla2p, also called transmembrane protein MOP2), Schizosaccharomyces pombe endocytosis protein End4 (End4p, also called Sla2 protein homolog), and similar proteins. In yeast, cells lacking Sla2p have severe defects in actin organization, cell morphology, and endocytosis, suggesting roles in these processes. Sla2p regulates the Eps15-like Arp2/3 complex activator, Pan1p, controlling actin polymerization during endocytosis. In fission yeast, End4p has been implicated in cellular morphogenesis. Sla2p contains an N-terminal ANTH, a central colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domains f Sla2p and similar proteins.


Pssm-ID: 340804  Cd Length: 115  Bit Score: 41.52  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509  37 LGKTICKATTEEVMAPKKKHLDYLLHCTNEPNVSIPSMANLlieRTQN--PNWTVVYKALITIHNIMCYGNE-------R 107
Cdd:cd17007     1 LQVAIKKACSSDETAPKRKHVRACIVYTWDHKSSKPFWNAL---KTQPllSDEVQCFKALITIHKVLQEGHPsalkeaiR 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1767231509 108 FSQYLASCNTTFNLtafvdkvGGAGGYdmSTHVRRYAKYIGEKIN 152
Cdd:cd17007    78 NIEWLESLGRQSSG-------SGAKGY--GRLIKEYVRYLLDKLA 113
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 364-528 3.66e-04

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 43.32  E-value: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509 364 NPFANDVASAAPAPATSAAQPDLLDMFQSSAAPAPQT---------ADVTNPF---GNFAAPSAFPTNVPPP-----AAH 426
Cdd:cd23959    67 NPFDGPGLVTASTVSDCYVGNANFYEVDMSDAFAMAPdeslgpfraARVPNPFsasSSTQRETHKTAQVAPPkaepqTAP 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509 427 SAPFGVQPAPQHSAAPFYANLHQAPPMQSQAPNGHQAAPF--GYPNAHPDDLARMTAQMSLNQQGYRAPAgwntttSAVS 504
Cdd:cd23959   147 VTPFGQLPMFGQHPPPAKPLPAAAAAQQSSASPGEVASPFasGTVSASPFATATDTAPSSGAPDGFPAEA------SAPS 220

                         170       180
                  ....*....|....*....|....
gi 1767231509 505 nnPFGATSAPQPMYTAPMGMYQQP 528
Cdd:cd23959   221 --PFAAPASAASFPAAPVANGEAA 242
PHA03247 PHA03247
large tegument protein UL36; Provisional
 395-533 1.05e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509  395 APAPQTADVTNPFGNFAAPSAFPtnvPPPAAHSAPfgvqPAPQHSAAPFYANLHQAPPMQSQAPnghQAAPFGYPNAHPD 474
Cdd:PHA03247  2711 APHALVSATPLPPGPAAARQASP---ALPAAPAPP----AVPAGPATPGGPARPARPPTTAGPP---APAPPAAPAAGPP 2780

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1767231509  475 DLARMTAQMSLNQQGYRAPAGWNTTTSAVsnnPFGATSAPQPMYTAPMGMYQQPFGAQP 533
Cdd:PHA03247  2781 RRLTRPAVASLSESRESLPSPWDPADPPA---AVLAPAAALPPAASPAGPLPPPTSAQP 2836
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 391-477 3.23e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509 391 QSSAAPAPQTADVTNPfgnfaAPSAFPTNVPPPAAHSAPFGVQPAPQHSAAPFYANLHQAPPMQSQAPNGHQAAPFG-YP 469
Cdd:PRK07764  428 APQPAPAPAPAPAPPS-----PAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAApAA 502


                  ....*...
gi 1767231509 470 NAHPDDLA 477
Cdd:PRK07764  503 PAGADDAA 510
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 362-545 3.34e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 3.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509 362 SANPFANDVASAAPAPATSAAQPDlldmfQSSAAPAPQTADVTNPFGNFAAPSAFPTNVPPPAAHSAPFGVQPAPQHSAA 441
Cdd:PRK07764  593 GAAGGEGPPAPASSGPPEEAARPA-----APAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509 442 PFYANLHQAPPMQSQAPNGHQAAPFGYPNAHPDDLARMTAQMSLNQQGYRAPAGWNTTTSAVSNNPFGATSAPQPMYTAP 521
Cdd:PRK07764  668 GWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDD 747

                         170       180
                  ....*....|....*....|....*.
gi 1767231509 522 MGMYQQPFG--AQPMWNPAMAAYGQQ 545
Cdd:PRK07764  748 PPDPAGAPAqpPPPPAPAPAAAPAAA 773
dnaA PRK14086
chromosomal replication initiator protein DnaA;
413-532 3.65e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 40.19  E-value: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509 413 PSAFPTNVPPPAAHSAP------FGVQPAPQHSAAPFYANlHQAPPMQSQAPNGHQAAPFGYPNAHPDDLARMTaqmsln 486
Cdd:PRK14086   90 PSAGEPAPPPPHARRTSepelprPGRRPYEGYGGPRADDR-PPGLPRQDQLPTARPAYPAYQQRPEPGAWPRAA------ 162

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1767231509 487 qqgyrAPAGWNTTTSAvsnNPFGATSAPQPMYTAPMGMYQQPFGAQ 532
Cdd:PRK14086  163 -----DDYGWQQQRLG---FPPRAPYASPASYAPEQERDREPYDAG 200
PHA03247 PHA03247
large tegument protein UL36; Provisional
 394-523 4.20e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 4.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509  394 AAPAPQTADVTNPFGNFAAPSAFPTNVPPPAAHSAPfgvqPAPQHSAAPfyanlHQAPPMQSQAPNGHQAAPFGYPNAHP 473
Cdd:PHA03247  2731 ASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGP----PAPAPPAAP-----AAGPPRRLTRPAVASLSESRESLPSP 2801

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1767231509  474 DDLARMTAQMS---LNQQGYRAPAGWNTTTSAVSNNPFGATSAPQPMYTAPMG 523
Cdd:PHA03247  2802 WDPADPPAAVLapaAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGG 2854
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 391-537 4.75e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.07  E-value: 4.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509  391 QSSAAPAP---QTADVTNPFGNFAAPSAFPTNVP-----PPAAHSAPFGVQPAPQHSAApfyANLHQAPPMQSQAPNGHQ 462
Cdd:PRK10263   331 QSWAAPVEpvtQTPPVASVDVPPAQPTVAWQPVPgpqtgEPVIAPAPEGYPQQSQYAQP---AVQYNEPLQQPVQPQQPY 407

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767231509  463 AAPFGYPNAHPDDLARMTAQMSlnQQGYRAPAGWN-TTTSAVSNNPFGATSAPQPMYTaPMGMYQQPFGAQPMWNP 537
Cdd:PRK10263   408 YAPAAEQPAQQPYYAPAPEQPA--QQPYYAPAPEQpVAGNAWQAEEQQSTFAPQSTYQ-TEQTYQQPAAQEPLYQQ 480
PHA03378 PHA03378
EBNA-3B; Provisional
 317-537 7.62e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.28  E-value: 7.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509 317 PHQFTTGFAFSQQPQPALGDAERQRYIELEQERLRQFEDQKKSINsanPFANDVASAAPAPATSAAQPDLLDMFQSSAAP 396
Cdd:PHA03378  600 PHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPITFN---VLVFPTPHQPPQVEITPYKPTWTQIGHIPYQP 676

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231509 397 APQTADVTNPfgnfaaPSAFPTNVPPPAAHSAPFGVQPAPQHSAAPFYANLHQAPPmqSQAPNGHQAAPFGYPNAHPDDL 476
Cdd:PHA03378  677 SPTGANTMLP------IQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARP--PAAAPGRARPPAAAPGRARPPA 748

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1767231509 477 ARMTAQmslnqqgyRAPAGWNTTTSAVSNNPFGATSAPQPMytAPMGMYQQPFGA-QPMWNP 537
Cdd:PHA03378  749 AAPGRA--------RPPAAAPGRARPPAAAPGAPTPQPPPQ--APPAPQQRPRGApTPQPPP 800
 
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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