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Conserved domains on  [gi|1767231507|ref|NP_001361961|]
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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 3.50e-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: 3.50e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507  37 LGKTICKATTEEVMAPKKKHLDYLLHCTNEPNVSIPSMANLLIERTQNPNWTVVYKALITIHNIMCYGNERFSQYLASCN 116
Cdd:cd16985     1 LAKAVCKATTHEVMGPKKKHLDYLVQCTNEPNVNIPQLADLLFERTQNSSWVVVFKALITTHHLMVYGNERFIQYLASRN 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1767231507 117 TTFNLTAFVDKVGGaGGYDMSTHVRRYAKYIGEKINTY 154
Cdd:cd16985    81 SLFNLSNFLDKSGS-QGYDMSTFIRRYAKYLNEKAISY 117
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
 391-512 1.19e-06

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: 51.91  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 391 QSSAAPAPQTADVTNPfgnfAAPSAFPTNVPPPAAHSAPFGVQPAPQHSAAPFYANLHQAP-PMQSQAPNEPENPFITAP 469
Cdd:PRK07764  398 APSAAAAAPAAAPAPA----AAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPsPPPAAAPSAQPAPAPAAA 473

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1767231507 470 AAPQMHNAPPVPPPPASQGAPAPinpfadPSATAASSAQPFGD 512
Cdd:PRK07764  474 PEPTAAPAPAPPAAPAPAAAPAA------PAAPAAPAGADDAA 510
 
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 3.50e-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: 3.50e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507  37 LGKTICKATTEEVMAPKKKHLDYLLHCTNEPNVSIPSMANLLIERTQNPNWTVVYKALITIHNIMCYGNERFSQYLASCN 116
Cdd:cd16985     1 LAKAVCKATTHEVMGPKKKHLDYLVQCTNEPNVNIPQLADLLFERTQNSSWVVVFKALITTHHLMVYGNERFIQYLASRN 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1767231507 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 2.41e-74

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: 2.41e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507  37 LGKTICKATTEEvMAPKKKHLDYLLHCTNEPNVSIPSMANLLIERTQNP-NWTVVYKALITIHNIMCYGNERFSQYLASC 115
Cdd:pfam07651   2 LEVAVVKATSHD-EAPPKEKHVREILVGTSSSAKLAALFWALSRRLPLTrSWVVAFKALILVHKLLREGHPSVLQELLRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 116 NTTFNLTAFVDKvgGAGGYDMSTHVRRYAKYIGEKINTYRMCAFD---FCKVKRG----REDGLLR--TMHTDKLLKTIP 186
Cdd:pfam07651  81 RRRISSLLRISS--FSLSWDYGAFIRAYAKYLDERLDFHRKLPRDpgtFERVEYGslvaVGDPNERylTMSMEDLLDSIP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 187 ILQNQIDALLEFSVTTSELNNGVINCSFILLFRDLIRLFACYNDGIINVLEKYFDMNKKQCRDALDTYKSFLTRLDKVAE 266
Cdd:pfam07651 159 KLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQFERLKE 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1767231507 267 FLRVAESVGIDRG-EIPDLTRAPASLLEALEAHL 299
Cdd:pfam07651 239 FYEVCKNLGYFRSlEIPKLPHIPPNLLEALEEYL 272
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
39-161 2.60e-29

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 112.72  E-value: 2.60e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507   39 KTICKATTEEVMAPKKKHLDYLLHCTNEPNVSIPSMANLLIERTQN-PNWTVVYKALITIHNIMCYGNER-FSQYLASCN 116
Cdd:smart00273   5 VKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDtKNWRVVYKALILLHYLLRNGSPRvILEALRNRN 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1767231507  117 TTFNLTAFVDKvgGAGGYDMSTHVRRYAKYIGEKINTYRMCAFDF 161
Cdd:smart00273  85 RILNLSDFQDI--DSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 391-512 1.19e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 51.91  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 391 QSSAAPAPQTADVTNPfgnfAAPSAFPTNVPPPAAHSAPFGVQPAPQHSAAPFYANLHQAP-PMQSQAPNEPENPFITAP 469
Cdd:PRK07764  398 APSAAAAAPAAAPAPA----AAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPsPPPAAAPSAQPAPAPAAA 473

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1767231507 470 AAPQMHNAPPVPPPPASQGAPAPinpfadPSATAASSAQPFGD 512
Cdd:PRK07764  474 PEPTAAPAPAPPAAPAPAAAPAA------PAAPAAPAGADDAA 510
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 383-591 2.72e-04

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 44.37  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 383 QPDLLDMfQSSAAPAPQTADvtnpfgnfAAPSAFPTNVPPPAAHSAPFGVQPAPQHsaapfyanlhqaPPMQSQAPnepE 462
Cdd:pfam03154 170 QPPVLQA-QSGAASPPSPPP--------PGTTQAATAGPTPSAPSVPPQGSPATSQ------------PPNQTQST---A 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 463 NPFITAPAAPQMHNAPPVPPPPASQGAPAP-----INPFADPSATAASSAQPFGDPgHQAAPFGYPNAHPDDLARMTAQM 537
Cdd:pfam03154 226 APHTLIQQTPTLHPQRLPSPHPPLQPMTQPpppsqVSPQPLPQPSLHGQMPPMPHS-LQTGPSHMQHPVPPQPFPLTPQS 304

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1767231507 538 SLNQqgyrAPAGwNTTTSAVSNNPFGATSAPQPMYTAPMGMYQQPFGAQPMWNP 591
Cdd:pfam03154 305 SQSQ----VPPG-PSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMP 353
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 396-519 7.55e-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: 42.55  E-value: 7.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 396 PAPQTADVTnPFGNFAAPSAFPTNVPPPAAhSAPFGVQPAPQHSAA-PFYANLHQAPPMqsqAPNEPENPFITAPAApqm 474
Cdd:cd23959   140 AEPQTAPVT-PFGQLPMFGQHPPPAKPLPA-AAAAQQSSASPGEVAsPFASGTVSASPF---ATATDTAPSSGAPDG--- 211

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1767231507 475 hnappvppppASQGAPAPiNPFAdPSATAASSAQPFGDPGHQAAP 519
Cdd:cd23959   212 ----------FPAEASAP-SPFA-APASAASFPAAPVANGEAATP 244
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 394-525 8.82e-03

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 38.98  E-value: 8.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 394 AAPAPQTADVTNPFGNFAAPSAFPTnVPPPAAHSAPFGVQPAPQHSAAPFYANLHQAPPMQSQAPNEPENPFITAPAAPQ 473
Cdd:NF040712  193 GRPLRPLATVPRLAREPADARPEEV-EPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPD 271

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1767231507 474 MHNAPPVPPPPASQGAPAPINPFADPSATA-ASSAQPFGDPGHQAAPFGYPNA 525
Cdd:NF040712  272 EATRDAGEPPAPGAAETPEAAEPPAPAPAApAAPAAPEAEEPARPEPPPAPKP 324
 
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 3.50e-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: 3.50e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507  37 LGKTICKATTEEVMAPKKKHLDYLLHCTNEPNVSIPSMANLLIERTQNPNWTVVYKALITIHNIMCYGNERFSQYLASCN 116
Cdd:cd16985     1 LAKAVCKATTHEVMGPKKKHLDYLVQCTNEPNVNIPQLADLLFERTQNSSWVVVFKALITTHHLMVYGNERFIQYLASRN 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1767231507 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 2.41e-74

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: 2.41e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507  37 LGKTICKATTEEvMAPKKKHLDYLLHCTNEPNVSIPSMANLLIERTQNP-NWTVVYKALITIHNIMCYGNERFSQYLASC 115
Cdd:pfam07651   2 LEVAVVKATSHD-EAPPKEKHVREILVGTSSSAKLAALFWALSRRLPLTrSWVVAFKALILVHKLLREGHPSVLQELLRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 116 NTTFNLTAFVDKvgGAGGYDMSTHVRRYAKYIGEKINTYRMCAFD---FCKVKRG----REDGLLR--TMHTDKLLKTIP 186
Cdd:pfam07651  81 RRRISSLLRISS--FSLSWDYGAFIRAYAKYLDERLDFHRKLPRDpgtFERVEYGslvaVGDPNERylTMSMEDLLDSIP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 187 ILQNQIDALLEFSVTTSELNNGVINCSFILLFRDLIRLFACYNDGIINVLEKYFDMNKKQCRDALDTYKSFLTRLDKVAE 266
Cdd:pfam07651 159 KLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQFERLKE 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1767231507 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 7.01e-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: 7.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507  37 LGKTICKATTEEVMAPKKKHLDYLLHCTNE--PNVSIPSMANLLIERTQNPNWTVVYKALITIHNIMCYGNERFSQYLAS 114
Cdd:cd03564     1 LDVAVVKATNHDEVPPKEKHVRKLLLATSNggGRADVAYIVHALAKRLHKKNWIVVLKTLIVIHRLLREGSPSFLEELLR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1767231507 115 CNTT-FNLTAFVDKvGGAGGYDMSTHVRRYAKYIGEKINTY 154
Cdd:cd03564    81 YSGHiFNLSNFKDD-SSPEAWDLSAFIRRYARYLEERLECF 120
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
39-161 2.60e-29

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 112.72  E-value: 2.60e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507   39 KTICKATTEEVMAPKKKHLDYLLHCTNEPNVSIPSMANLLIERTQN-PNWTVVYKALITIHNIMCYGNER-FSQYLASCN 116
Cdd:smart00273   5 VKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDtKNWRVVYKALILLHYLLRNGSPRvILEALRNRN 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1767231507  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 8.94e-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: 8.94e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507  34 GSQLGKTICKATTEEVMAPKKKHLDYLLHCTNEPnVSIPSMANLLIER--TQNPNWTVVYKALITIHNIMCYGNERFSQY 111
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNY-VEFPEIMKMLWKRlnDKGKNWRHIYKALTLLEYLLKNGSERVVDD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1767231507 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 1.27e-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: 1.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507  37 LGKTICKATTEEVMAPKKKHLDYLLHCTNEPNVSIPSMANLLIERTQNPNWTVVYKALITIHNIMCYGNERFSQYLASCN 116
Cdd:cd00197     1 FEKTVEKATSNENMGPDWPLIMEICDLINETNVGPKEAVDAIKKRINNKNPHVVLKALTLLEYCVKNCGERFHQEVASND 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1767231507 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 3.43e-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: 3.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507  39 KTICKATTEEVMAPKKKHLDYLLHCTNEPNVSIPSMANLLIERTQNPNWTVVYKALITIHNIMCYGN-ERFSQYLASCNT 117
Cdd:cd16988     3 KLVKGATKIKLAPPKAKYLDPILLATYSSDASFGEIVRALSRRLRDNSWTVVFKSLIVLHLMIREGEtDDVLLYYLSRPD 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1767231507 118 TFNLTAFVDKvGGAGGYDMSThVRRYAKYIGEKINTY 154
Cdd:cd16988    83 FLDLRKIRNG-SSAGSGQLQN-IQRYAAYLKERVKEY 117
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 391-512 1.19e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 51.91  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 391 QSSAAPAPQTADVTNPfgnfAAPSAFPTNVPPPAAHSAPFGVQPAPQHSAAPFYANLHQAP-PMQSQAPNEPENPFITAP 469
Cdd:PRK07764  398 APSAAAAAPAAAPAPA----AAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPsPPPAAAPSAQPAPAPAAA 473

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1767231507 470 AAPQMHNAPPVPPPPASQGAPAPinpfadPSATAASSAQPFGD 512
Cdd:PRK07764  474 PEPTAAPAPAPPAAPAPAAAPAA------PAAPAAPAGADDAA 510
ANTH_N_AP180_plant cd16987
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of plant Clathrin coat assembly ...
 41-150 1.47e-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: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507  41 ICKATTEEVMAPKKKHLDYLLHCTNepnvSIPSMANLLIE-------RTQNpnWTVVYKALITIHNIMCYGNERFSQYLA 113
Cdd:cd16987     5 VVKATSHDDAPPDEKYVREILSLGS----SSRAYASACVSalsrrlnRTRD--WVVALKCLMLLHRLLRDGSPILEQELS 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1767231507 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 2.16e-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: 2.16e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1767231507  39 KTICKATTEEVMAPKKKHLDYLlHCTNEPNVSIPSMANLLIERTQNPNWTVVYKALITIHNIMCYGNERFSQ 110
Cdd:cd16986     3 KAVNKATNKTDSPPKPKHVRTI-IVKSWTHQKGPQFYEELSKRLLLNNPVVQFKALVTLHKVLRDGPPELSL 73
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
394-595 2.58e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 47.56  E-value: 2.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 394 AAPAPQTADVTNPFGNFAAPSAFPTNVPPPAAHSAPFGVQPAPQHSAAPFYANLHQAPPMQSQAPNEPENPFITAPAAPQ 473
Cdd:PRK12323  388 AAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAA 467

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 474 mhnappvppppASQGAPAPINPFADPSATAASSA-QPFGDPGHQAAPFGYPNAHPDDLARMTAQMSLNQQGYRAPAGWNT 552
Cdd:PRK12323  468 -----------GPRPVAAAAAAAPARAAPAAAPApADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDD 536

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1767231507 553 TTSAVSNNPFGATSAPQPMYTAPMGMYQQPFGAQPMWNPAMAA 595
Cdd:PRK12323  537 AFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDG 579
PHA03378 PHA03378
EBNA-3B; Provisional
 317-525 6.70e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 46.21  E-value: 6.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 317 PHQFTTGFAFSQQPQPALGDAERQRYIELEQERLRQFEDQKKSINsanPFANDVASAAPAPATSAAQPDLLDMFQSSAAP 396
Cdd:PHA03378  600 PHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPITFN---VLVFPTPHQPPQVEITPYKPTWTQIGHIPYQP 676

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 397 APQTADVTNPF----GNFAAPSAFPTNVPPPAAhsAPFGVQPaPQhsAAPFYANLHQAPPMQSQAPNE---PENPFITAP 469
Cdd:PHA03378  677 SPTGANTMLPIqwapGTMQPPPRAPTPMRPPAA--PPGRAQR-PA--AATGRARPPAAAPGRARPPAAapgRARPPAAAP 751

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1767231507 470 AAPQMHNAPPVPPP--PASQGAPAPINPfadPSATAASSAQPFGDPGHQAAPFGYPNA 525
Cdd:PHA03378  752 GRARPPAAAPGRARppAAAPGAPTPQPP---PQAPPAPQQRPRGAPTPQPPPQAGPTS 806
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 362-531 6.74e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.13  E-value: 6.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 362 SANPFANDVASAAPAPATSAAQPDlldmfQSSAAPAPQTADVTNPFGNFAAPSAFPTNVPPPAAHSAPFGVQPAPQHSAA 441
Cdd:PRK07764  593 GAAGGEGPPAPASSGPPEEAARPA-----APAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 442 PFYANLHQAPP---MQSQAPNEPENPFITAPAAPQMHNAPPVPPPPASQGAPAPINPFADPSATAASSAQ---PFGDPGH 515
Cdd:PRK07764  668 GWPAKAGGAAPaapPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDpvpLPPEPDD 747

                         170
                  ....*....|....*.
gi 1767231507 516 QAAPFGYPNAHPDDLA 531
Cdd:PRK07764  748 PPDPAGAPAQPPPPPA 763
ANTH_N_Sla2p cd17007
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ...
 37-152 1.59e-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: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507  37 LGKTICKATTEEVMAPKKKHLDYLLHCTNEPNVSIPSMANLlieRTQN--PNWTVVYKALITIHNIMCYGNE-------R 107
Cdd:cd17007     1 LQVAIKKACSSDETAPKRKHVRACIVYTWDHKSSKPFWNAL---KTQPllSDEVQCFKALITIHKVLQEGHPsalkeaiR 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1767231507 108 FSQYLASCNTTFNLtafvdkvGGAGGYdmSTHVRRYAKYIGEKIN 152
Cdd:cd17007    78 NIEWLESLGRQSSG-------SGAKGY--GRLIKEYVRYLLDKLA 113
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 408-541 1.61e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 408 GNFAAPSAFPTNVPPPAAHSAPFGvQPAPQHSAAPFyanlHQAPPMQSQAPnepenpfitAPAAPQMHNAPPVPPPPASQ 487
Cdd:PRK07764  385 LGVAGGAGAPAAAAPSAAAAAPAA-APAPAAAAPAA----AAAPAPAAAPQ---------PAPAPAPAPAPPSPAGNAPA 450

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1767231507 488 GAPAPINPFADPSATAASSAQPFGDPGHQAAPFGYPNAHPDDLARMTAQMSLNQ 541
Cdd:PRK07764  451 GGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPA 504
flhF PRK06995
flagellar biosynthesis protein FlhF;
411-508 1.72e-04

flagellar biosynthesis protein FlhF;


Pssm-ID: 235904 [Multi-domain]  Cd Length: 484  Bit Score: 44.57  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 411 AAPSAFPTNVPPPAAHSAPFGVQPAPQHSAAPFY-ANLHQAPPMQSQAPNEPENPFITAPAAPQMHNAPPVPPPPASQGA 489
Cdd:PRK06995   60 AAAQPPPAAAPAAVSRPAAPAAEPAPWLVEHAKRlTAQREQLVARAAAPAAPEAQAPAAPAERAAAENAARRLARAAAAA 139

                          90
                  ....*....|....*....
gi 1767231507 490 PAPiNPFADPSATAASSAQ 508
Cdd:PRK06995  140 PRP-RVPADAAAAVADAVK 157
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 383-591 2.72e-04

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 44.37  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 383 QPDLLDMfQSSAAPAPQTADvtnpfgnfAAPSAFPTNVPPPAAHSAPFGVQPAPQHsaapfyanlhqaPPMQSQAPnepE 462
Cdd:pfam03154 170 QPPVLQA-QSGAASPPSPPP--------PGTTQAATAGPTPSAPSVPPQGSPATSQ------------PPNQTQST---A 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 463 NPFITAPAAPQMHNAPPVPPPPASQGAPAP-----INPFADPSATAASSAQPFGDPgHQAAPFGYPNAHPDDLARMTAQM 537
Cdd:pfam03154 226 APHTLIQQTPTLHPQRLPSPHPPLQPMTQPpppsqVSPQPLPQPSLHGQMPPMPHS-LQTGPSHMQHPVPPQPFPLTPQS 304

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1767231507 538 SLNQqgyrAPAGwNTTTSAVSNNPFGATSAPQPMYTAPMGMYQQPFGAQPMWNP 591
Cdd:pfam03154 305 SQSQ----VPPG-PSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMP 353
PHA03247 PHA03247
large tegument protein UL36; Provisional
 394-595 2.78e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 2.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507  394 AAPAPQTADVTNPFGNFAAPSAFPTNVPPPAAHSAPFGVQPAPQHSAAPfyANLHQAPPMQSQAPNEPENPFITAPAAPQ 473
Cdd:PHA03247  2731 ASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP--PRRLTRPAVASLSESRESLPSPWDPADPP 2808

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507  474 --MHNAPPVPPPPASQGAPAPINPFADPSATAASSA--QPFGDPGHQAAPFGypnahpdDLARmtaqmslnqqgyRAPAG 549
Cdd:PHA03247  2809 aaVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGppPPSLPLGGSVAPGG-------DVRR------------RPPSR 2869

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1767231507  550 WNTTTSAVSNNPFGATSAPQPMYTAPMGMYQQPFGAQPMWNPAMAA 595
Cdd:PHA03247  2870 SPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPP 2915
PHA03247 PHA03247
large tegument protein UL36; Provisional
 388-577 3.02e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 3.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507  388 DMFQSSAAPAPQTADVTNPFGNFAAPSAFPTNVPPPAAHSAPFGVQ----PAPQHSAAPFYANLHQAPPMQSQAPNEPEN 463
Cdd:PHA03247  2606 GDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERprddPAPGRVSRPRRARRLGRAAQASSPPQRPRR 2685

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507  464 PFITAPAAPQMHNAPPVPPPpasqgapapinPFADPSATAASSAQPFgDPGHQAAPFGYPNAHPDDLARMTAQMSLNQQG 543
Cdd:PHA03247  2686 RAARPTVGSLTSLADPPPPP-----------PTPEPAPHALVSATPL-PPGPAAARQASPALPAAPAPPAVPAGPATPGG 2753

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1767231507  544 YRAPAGWNTTTSAVSNN-PFGATSAPQPMYTAPMG 577
Cdd:PHA03247  2754 PARPARPPTTAGPPAPApPAAPAAGPPRRLTRPAV 2788
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 392-531 4.54e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 4.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 392 SSAAPAPQTAdvtnpfgnfAAPSAfptnVPPPAAHSAPFGVQPAPQHSAAPfyanlHQAPPMQSQAPNEPENPFITAPAA 471
Cdd:PRK07764  394 PAAAAPSAAA---------AAPAA----APAPAAAAPAAAAAPAPAAAPQP-----APAPAPAPAPPSPAGNAPAGGAPS 455

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 472 PQMHNAPPVPPPPASQGAPAPINPFADPSATAASSAQPFGDPGHQAAPfgypnAHPDDLA 531
Cdd:PRK07764  456 PPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAP-----AGADDAA 510
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 411-528 4.87e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 43.16  E-value: 4.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 411 AAPSAFPTNVPPPAAHSAPfgvQPAPQHSAAPFYAnlhQAPPMQSQAPNEPENPFITAPAAPQmhNAPPVPPPPASQGAP 490
Cdd:PRK14951  373 AAPAEKKTPARPEAAAPAA---APVAQAAAAPAPA---AAPAAAASAPAAPPAAAPPAPVAAP--AAAAPAAAPAAAPAA 444

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1767231507 491 APINPFADPSATAASSAQPF--GDPGHQAAPFGYPNAHPD 528
Cdd:PRK14951  445 VALAPAPPAQAAPETVAIPVrvAPEPAVASAAPAPAAAPA 484
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 396-519 7.55e-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: 42.55  E-value: 7.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 396 PAPQTADVTnPFGNFAAPSAFPTNVPPPAAhSAPFGVQPAPQHSAA-PFYANLHQAPPMqsqAPNEPENPFITAPAApqm 474
Cdd:cd23959   140 AEPQTAPVT-PFGQLPMFGQHPPPAKPLPA-AAAAQQSSASPGEVAsPFASGTVSASPF---ATATDTAPSSGAPDG--- 211

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1767231507 475 hnappvppppASQGAPAPiNPFAdPSATAASSAQPFGDPGHQAAP 519
Cdd:cd23959   212 ----------FPAEASAP-SPFA-APASAASFPAAPVANGEAATP 244
PHA03378 PHA03378
EBNA-3B; Provisional
 389-561 1.11e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 42.36  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 389 MFQSSAAPAPQTADVTNPfGNFAAPSAFPTNVPPPAAhsAPFGVQPAPQHSAAPFYANLHQAPPMQSQAPNEPENPFITA 468
Cdd:PHA03378  734 ARPPAAAPGRARPPAAAP-GRARPPAAAPGRARPPAA--APGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQAGPTSMQLM 810

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 469 PAA------PQMHNAPPVPPPPASQGAPAPINPfADPSATAASSAQPfgDPGH-------QAAPFGYPNAHPDDLARmta 535
Cdd:PHA03378  811 PRAapgqqgPTKQILRQLLTGGVKRGRPSLKKP-AALERQAAAGPTP--SPGSgtsdkivQAPVFYPPVLQPIQVMR--- 884

                         170       180
                  ....*....|....*....|....*.
gi 1767231507 536 qmslnQQGYRAPAGWNTTTSAVSNNP 561
Cdd:PHA03378  885 -----QLGSVRAAAASTVTQAPTEYT 905
PHA03247 PHA03247
large tegument protein UL36; Provisional
 394-598 2.13e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507  394 AAPAPQTADVT----NPFGNFAAPSAFPTNVPPPAAHSAPFGVQPAPQHSAAPFYANLHQAP--PMQSQAPNEPENPFIT 467
Cdd:PHA03247  2740 APPAVPAGPATpggpARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPwdPADPPAAVLAPAAALP 2819

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507  468 APAAPqmhnAPPVPPPPASQ-GAPAPINPFADPSATAASSAQPFGD-----PGHQAAPFGYPNAHPDdlARMTAQMSLNQ 541
Cdd:PHA03247  2820 PAASP----AGPLPPPTSAQpTAPPPPPGPPPPSLPLGGSVAPGGDvrrrpPSRSPAAKPAAPARPP--VRRLARPAVSR 2893

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1767231507  542 QgyrapagwnttTSAVSNNPFGATSAPQPMYTAPmGMYQQPFGAQPMWNPAMAAYGQ 598
Cdd:PHA03247  2894 S-----------TESFALPPDQPERPPQPQAPPP-PQPQPQPPPPPQPQPPPPPPPR 2938
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 392-498 2.38e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.85  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 392 SSAAPAPQTADVTNPfgnfAAPSAF---PTNVPPPAAHSAPFGVQPAPQHSAAPFYANLHQAPPMQSQAPNEPENPFITA 468
Cdd:PRK14951  389 PAAAPVAQAAAAPAP----AAAPAAaasAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPETVAIPV 464

                          90       100       110
                  ....*....|....*....|....*....|
gi 1767231507 469 PAAPQMHnAPPVPPPPASQGAPAPINPFAD 498
Cdd:PRK14951  465 RVAPEPA-VASAAPAPAAAPAAARLTPTEE 493
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 417-576 3.17e-03

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 40.48  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 417 PTNVPPPAAHSAPFGVQPAPqhSAAPfyanlHQAppmQSQAPNEPENPFITAPAAPQMHNAPPVPPPPASQGAPAPinpf 496
Cdd:PHA03269   23 NTNIPIPELHTSAATQKPDP--APAP-----HQA---ASRAPDPAVAPTSAASRKPDLAQAPTPAASEKFDPAPAP---- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 497 adpsaTAASSAQPfgDPGhqAAPFGYPNAHPDdlarmtAQMSLNQQGYRAPAGWNTTTSAVSNNP---FGATSAPQP-MY 572
Cdd:PHA03269   89 -----HQAASRAP--DPA--VAPQLAAAPKPD------AAEAFTSAAQAHEAPADAGTSAASKKPdpaAHTQHSPPPfAY 153


                  ....
gi 1767231507 573 TAPM 576
Cdd:PHA03269  154 TRSM 157
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
391-519 3.45e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.60  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 391 QSSAAPAPQTADVTNPFGNFAAPSAFPTNVPPPAAHSAPFG---------VQPAPQHSAAPFYANLHQAPPMQSQAPNEP 461
Cdd:PRK07003  394 SAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPAtadrgddaaDGDAPVPAKANARASADSRCDERDAQPPAD 473

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1767231507 462 ENPfITAPAAPQMHNAPPVPPPPASQGAPAPINPFADPSATAASSAQPFGDPGHQAAP 519
Cdd:PRK07003  474 SGS-ASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAP 530
PHA03378 PHA03378
EBNA-3B; Provisional
 391-591 3.61e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.44  E-value: 3.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 391 QSSAAPAPQTADVTNPfgNFAAPSAFPTNVPPPAAHsaPFGVQPAPQHsaAPFYANLHQAP--------PMQSQAPNEPE 462
Cdd:PHA03378  601 HPSQTPEPPTTQSHIP--ETSAPRQWPMPLRPIPMR--PLRMQPITFN--VLVFPTPHQPPqveitpykPTWTQIGHIPY 674

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 463 NPFITAPAA---PQMHNAPPVPPPPAS------QGAPAPINPfadPSATAASSAQPFGDPGHQAAPFGYPNAHPDDLARM 533
Cdd:PHA03378  675 QPSPTGANTmlpIQWAPGTMQPPPRAPtpmrppAAPPGRAQR---PAAATGRARPPAAAPGRARPPAAAPGRARPPAAAP 751

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1767231507 534 TAQmslnqqgyRAPAGWNTTTSAVSNNPFGATSAPQPMytAPMGMYQQPFGA-QPMWNP 591
Cdd:PHA03378  752 GRA--------RPPAAAPGRARPPAAAPGAPTPQPPPQ--APPAPQQRPRGApTPQPPP 800
PTZ00436 PTZ00436
60S ribosomal protein L19-like protein; Provisional
 391-527 4.44e-03

60S ribosomal protein L19-like protein; Provisional


Pssm-ID: 185616 [Multi-domain]  Cd Length: 357  Bit Score: 39.93  E-value: 4.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 391 QSSAAPAPQTAdvtnPFGNFAAPSAfPTNVPPPAAHSAPFGVQPAPQHSAAPfYANLHQAPPMQSQAPNEPENPFITAPA 470
Cdd:PTZ00436  224 KAAAAPAKAAA----PPAKAAAAPA-KAAAAPAKAAAPPAKAAAPPAKAAAP-PAKAAAPPAKAAAPPAKAAAPPAKAAA 297

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1767231507 471 APQMHNAppvpppPASQGAPAPINPFADPSATAASSAQPFGDPGHQAAPFGYPNAHP 527
Cdd:PTZ00436  298 APAKAAA------APAKAAAAPAKAAAPPAKAAAPPAKAATPPAKAAAPPAKAAAAP 348
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
391-509 4.89e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.22  E-value: 4.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 391 QSSAAPAPQTAdvtnpfgnfAAPSAFPTNVPPPAAHSAPFGVQPAPQhSAAPFYANLHQAPPMQSQAPNEPENPFITAPA 470
Cdd:PRK07003  376 VAGAVPAPGAR---------AAAAVGASAVPAVTAVTGAAGAALAPK-AAAAAAATRAEAPPAAPAPPATADRGDDAADG 445

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1767231507 471 APQMHNAPPVPPPPASQGAPAPINPFADPS--ATAASSAQP 509
Cdd:PRK07003  446 DAPVPAKANARASADSRCDERDAQPPADSGsaSAPASDAPP 486
PHA03247 PHA03247
large tegument protein UL36; Provisional
 395-577 7.16e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 7.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507  395 APAPQTADVTNPFGNFAAPSAFPtnvPPPAAHSAPfgvqPAPQHSAAPfyanLHQAPPMQSQAPNEPENPfiTAPAAPqm 474
Cdd:PHA03247  2711 APHALVSATPLPPGPAAARQASP---ALPAAPAPP----AVPAGPATP----GGPARPARPPTTAGPPAP--APPAAP-- 2775

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507  475 hnapPVPPPPAsqgAPAPINPFADPSATAASSAQpfgDPGHQAAPFGYPNAHPDDLARmtaqmslnqqgyraPAGWNTTT 554
Cdd:PHA03247  2776 ----AAGPPRR---LTRPAVASLSESRESLPSPW---DPADPPAAVLAPAAALPPAAS--------------PAGPLPPP 2831

                          170       180
                   ....*....|....*....|...
gi 1767231507  555 SAVSNNPFGATSAPQPMYTAPMG 577
Cdd:PHA03247  2832 TSAQPTAPPPPPGPPPPSLPLGG 2854
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
377-535 7.46e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 39.47  E-value: 7.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 377 PATSAAQPDLLDMFQSSAAPAPQTADVTNPFGNFAAPSAFPTNVPPPAAHSAPFGVQPAPQHSAAPfYANLHQAPPMQSQ 456
Cdd:PRK12323  412 AAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAA-AAPARAAPAAAPA 490

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1767231507 457 APNEPENPFITAPAAPqmhnAPPVPPPPASQGAPAPINPFADPSATAASSAQPFGDPGHQAAPFGYPNAHPDDLARMTA 535
Cdd:PRK12323  491 PADDDPPPWEELPPEF----ASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRP 565
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 394-525 8.82e-03

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 38.98  E-value: 8.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 394 AAPAPQTADVTNPFGNFAAPSAFPTnVPPPAAHSAPFGVQPAPQHSAAPFYANLHQAPPMQSQAPNEPENPFITAPAAPQ 473
Cdd:NF040712  193 GRPLRPLATVPRLAREPADARPEEV-EPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPD 271

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1767231507 474 MHNAPPVPPPPASQGAPAPINPFADPSATA-ASSAQPFGDPGHQAAPFGYPNA 525
Cdd:NF040712  272 EATRDAGEPPAPGAAETPEAAEPPAPAPAApAAPAAPEAEEPARPEPPPAPKP 324
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 392-518 9.29e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.20  E-value: 9.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767231507 392 SSAAPAPQTADVTNPFGNFAAPSAFPTNVPPPAAHSAPFGVQPAPQHSAAPFYANLHQAPPMQSQAPNEPENPFITAPAA 471
Cdd:PRK07764  680 APPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPP 759

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1767231507 472 PQMHNAPPVPPppasqGAPAPINPFADPSATAASSAQPFGDPGHQAA 518
Cdd:PRK07764  760 PPPAPAPAAAP-----AAAPPPSPPSEEEEMAEDDAPSMDDEDRRDA 801
 
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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