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Conserved domains on  [gi|71990236|ref|NP_505798|]
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Vacuolar protein-sorting-associated protein 36 [Caenorhabditis elegans]

Protein Classification

Vps36_ESCRT-II and EAP30 domain-containing protein( domain architecture ID 10569134)

Vps36_ESCRT-II and EAP30 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EAP30 pfam04157
EAP30/Vps36 family; This family includes EAP30 as well as the Vps36 protein. Vps36 is involved ...
 152-369 1.65e-67

EAP30/Vps36 family; This family includes EAP30 as well as the Vps36 protein. Vps36 is involved in Golgi to endosome trafficking. EAP30 is a subunit of the ELL complex. The ELL is an 80-kDa RNA polymerase II transcription factor. ELL interacts with three other proteins to form the complex known as ELL complex. The ELL complex is capable of increasing that catalytic rate of transcription elongation, but is unable to repress initiation of transcription by RNA polymerase II as is the case of ELL. EAP30 is thought to lead to the derepression of ELL's transcriptional inhibitory activity.


:

Pssm-ID: 461201  Cd Length: 210  Bit Score: 212.09  E-value: 1.65e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990236   152 VGISGIERRLAENHQKTHETITQAFDDMSKLMETAREMVALSKSISEKVRSRKGEISEdetiaFKSYLLSLGVsDPVTKS 231
Cdd:pfam04157   1 VGIAALEQRQEQQQEQYEELLSSAFEDLEALMEKFKELVEFAEKHKKKIKKNPEFRAQ-----FQSMCASLGV-DPLTFW 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990236   232 TF-VGSDSEYFQKLAKEISDVLYEHIKENGGMCALPEVYCRINRARGMELLSPEDVMNACGALSRiNSPLELHRFPSGVL 310
Cdd:pfam04157  75 WMsLLGVGDFYYELAVQIVEVCLATRDENGGLISLDDLYARVNRARGVELISPDDLLRAIKLLEL-VLGSRLRKFKSGLL 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 71990236   311 VVQLKSASMDSTVGQTLEFVSKleRASANELAESLGITVILARERLLAAEESGLICRDD 369
Cdd:pfam04157 154 VVQLELNTDQTEVASRLGGLGG--YVTASELADNLGWSVARAKEVLEDLEREGLLWRDE 210
Vps36_ESCRT-II pfam11605
Vacuolar protein sorting protein 36 Vps36; Vps36 is a subunit of ESCRT-II, a protein involved ...
 2-89 1.77e-27

Vacuolar protein sorting protein 36 Vps36; Vps36 is a subunit of ESCRT-II, a protein involved in driving protein sorting from endosomes to lysosomes. The GLUE domain of Vps36 allows for a tight interaction to occur between the protein and Vps28, a subunit of ESCRT-I. This interaction is critical for ubiquitinated cargo progression from early to late endosomes.


:

Pssm-ID: 402964  Cd Length: 92  Bit Score: 103.93  E-value: 1.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990236     2 NRLSWYTP-GESTEELLCQAGHVGIYEGDLKQTNFEQGTASLTMQRIIWADSSDPDR---RLVLHHSLVISMEKHHKSMF 77
Cdd:pfam11605   1 ERNTSGRPvLRENEVDIYVQDNVGLYQGDQKILNRQNGRLYLTTHRIIYVDSADPKKvslSLPLKLVYSISEKEYSSGFL 80

                          90
                  ....*....|..
gi 71990236    78 SKGGKIVVKLEK 89
Cdd:pfam11605  81 RSSPKIILFLKP 92
 
Name Accession Description Interval E-value
EAP30 pfam04157
EAP30/Vps36 family; This family includes EAP30 as well as the Vps36 protein. Vps36 is involved ...
 152-369 1.65e-67

EAP30/Vps36 family; This family includes EAP30 as well as the Vps36 protein. Vps36 is involved in Golgi to endosome trafficking. EAP30 is a subunit of the ELL complex. The ELL is an 80-kDa RNA polymerase II transcription factor. ELL interacts with three other proteins to form the complex known as ELL complex. The ELL complex is capable of increasing that catalytic rate of transcription elongation, but is unable to repress initiation of transcription by RNA polymerase II as is the case of ELL. EAP30 is thought to lead to the derepression of ELL's transcriptional inhibitory activity.


Pssm-ID: 461201  Cd Length: 210  Bit Score: 212.09  E-value: 1.65e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990236   152 VGISGIERRLAENHQKTHETITQAFDDMSKLMETAREMVALSKSISEKVRSRKGEISEdetiaFKSYLLSLGVsDPVTKS 231
Cdd:pfam04157   1 VGIAALEQRQEQQQEQYEELLSSAFEDLEALMEKFKELVEFAEKHKKKIKKNPEFRAQ-----FQSMCASLGV-DPLTFW 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990236   232 TF-VGSDSEYFQKLAKEISDVLYEHIKENGGMCALPEVYCRINRARGMELLSPEDVMNACGALSRiNSPLELHRFPSGVL 310
Cdd:pfam04157  75 WMsLLGVGDFYYELAVQIVEVCLATRDENGGLISLDDLYARVNRARGVELISPDDLLRAIKLLEL-VLGSRLRKFKSGLL 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 71990236   311 VVQLKSASMDSTVGQTLEFVSKleRASANELAESLGITVILARERLLAAEESGLICRDD 369
Cdd:pfam04157 154 VVQLELNTDQTEVASRLGGLGG--YVTASELADNLGWSVARAKEVLEDLEREGLLWRDE 210
Vps36_ESCRT-II pfam11605
Vacuolar protein sorting protein 36 Vps36; Vps36 is a subunit of ESCRT-II, a protein involved ...
 2-89 1.77e-27

Vacuolar protein sorting protein 36 Vps36; Vps36 is a subunit of ESCRT-II, a protein involved in driving protein sorting from endosomes to lysosomes. The GLUE domain of Vps36 allows for a tight interaction to occur between the protein and Vps28, a subunit of ESCRT-I. This interaction is critical for ubiquitinated cargo progression from early to late endosomes.


Pssm-ID: 402964  Cd Length: 92  Bit Score: 103.93  E-value: 1.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990236     2 NRLSWYTP-GESTEELLCQAGHVGIYEGDLKQTNFEQGTASLTMQRIIWADSSDPDR---RLVLHHSLVISMEKHHKSMF 77
Cdd:pfam11605   1 ERNTSGRPvLRENEVDIYVQDNVGLYQGDQKILNRQNGRLYLTTHRIIYVDSADPKKvslSLPLKLVYSISEKEYSSGFL 80

                          90
                  ....*....|..
gi 71990236    78 SKGGKIVVKLEK 89
Cdd:pfam11605  81 RSSPKIILFLKP 92
PH-GRAM-like_Eap45 cd13226
Pleckstrin homology-like domain or GLUE (GRAM-like ubiquitin-binding in Eap45) domain of Eap45; ...
 1-128 2.66e-21

Pleckstrin homology-like domain or GLUE (GRAM-like ubiquitin-binding in Eap45) domain of Eap45; ESCRT complexes form the main machinery driving protein sorting from endosomes to lysosomes. Human/yeast ESCRT-I consists of Tsg101/Vps23, Vps28/Vps28, and a Vps37 homolog/Vps37. Human/yeast ESCRT-II is composed of EAP20/Vps25, EAP30/Vps22, and EAP45/Vps36. Yeast ESCRT-III consists Vps2, Vps20, Vps24, and Snf7 subunits. In contrast, there are three Human paralogs of Snf7 (hSnf7-1/CHMP4A, hSnf7-2/CHMP4B, and hSnf7-3/CHMP4C) and two paralogs of Vps2 (CHMP2A and CHMP2B). Yeast ESCRT-I links directly to ESCRT-II, through a tight interaction of Vps28 (ESCRT-I) with the yeast-specific zinc-finger insertion within the GLUE domain of Vps36. The Vps36 subunit (ESCRT-II) binds ubiquitin using one of its two NZF zinc fingers in its N-terminal region. Human Vps36, EAP45, also binds ubiquitin despite having no NZF domain. Instead, mammalian ESCRT-II interacts with Ub through the Eap45 GLUE domain directly. While yeast Vps36 GLUE shows a preference for the singly phosphorylated PI(3)P, while Eap45 GLUE preferentially binds the triply phosphorylated phosphatidylinositol PI(3,4,5)P3. Structurally, Eap45 GLUE only has a PH-like fold since it lacks the secondary structure element corresponding to the 4 strand, unlike that of yeast Vps36 GLUE. ESCRT-II also interacts with ESCRT-III via a EAP20(Vps25)/CHMP6(Vps20) interaction. The interactions of ESCRT-II GLUE domain with membranes, ESCRT-I, and ubiquitin are critical for ubiquitinated cargo progression from early to late endosomes. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275408 [Multi-domain]  Cd Length: 129  Bit Score: 88.55  E-value: 2.66e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990236   1 MNRLSWYT----PGESteeLLCQAGHVGIYEGDLKqTNFEQGTASLTMQRIIWADSSDPDRRLVLHHSLVISMEKHHKSM 76
Cdd:cd13226   1 MDRFMWCDgllfPNET---LVIQQRGVRIYDGDEK-TKFDSGELVLTSHRLIWRDQKQIERCLSLPLSLIVFIEEEESGG 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 71990236  77 FSKGGKIVVKL-EKPKAGNIGPVNSSHYETLRLVFRHGGEDDFFKKYEDAVRR 128
Cdd:cd13226  77 FGKSAKIVVHLhPAPPNKEPGPKQSSPYNYIKLSFKEGGQSEFYRALSEELTR 129
COG2345 COG2345
Predicted transcriptional regulator, ArsR family [Transcription];
316-367 4.69e-05

Predicted transcriptional regulator, ArsR family [Transcription];


Pssm-ID: 441914 [Multi-domain]  Cd Length: 217  Bit Score: 44.14  E-value: 4.69e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71990236 316 SASMDSTVGQTLEFVSKLERASANELAESLGITVILARERLLAAEESGLICR 367
Cdd:COG2345   8 AALADPTRRRILELLKRAGPVTAAELAEALGLTPNAVRRHLDALEEEGLVER 59
 
Name Accession Description Interval E-value
EAP30 pfam04157
EAP30/Vps36 family; This family includes EAP30 as well as the Vps36 protein. Vps36 is involved ...
 152-369 1.65e-67

EAP30/Vps36 family; This family includes EAP30 as well as the Vps36 protein. Vps36 is involved in Golgi to endosome trafficking. EAP30 is a subunit of the ELL complex. The ELL is an 80-kDa RNA polymerase II transcription factor. ELL interacts with three other proteins to form the complex known as ELL complex. The ELL complex is capable of increasing that catalytic rate of transcription elongation, but is unable to repress initiation of transcription by RNA polymerase II as is the case of ELL. EAP30 is thought to lead to the derepression of ELL's transcriptional inhibitory activity.


Pssm-ID: 461201  Cd Length: 210  Bit Score: 212.09  E-value: 1.65e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990236   152 VGISGIERRLAENHQKTHETITQAFDDMSKLMETAREMVALSKSISEKVRSRKGEISEdetiaFKSYLLSLGVsDPVTKS 231
Cdd:pfam04157   1 VGIAALEQRQEQQQEQYEELLSSAFEDLEALMEKFKELVEFAEKHKKKIKKNPEFRAQ-----FQSMCASLGV-DPLTFW 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990236   232 TF-VGSDSEYFQKLAKEISDVLYEHIKENGGMCALPEVYCRINRARGMELLSPEDVMNACGALSRiNSPLELHRFPSGVL 310
Cdd:pfam04157  75 WMsLLGVGDFYYELAVQIVEVCLATRDENGGLISLDDLYARVNRARGVELISPDDLLRAIKLLEL-VLGSRLRKFKSGLL 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 71990236   311 VVQLKSASMDSTVGQTLEFVSKleRASANELAESLGITVILARERLLAAEESGLICRDD 369
Cdd:pfam04157 154 VVQLELNTDQTEVASRLGGLGG--YVTASELADNLGWSVARAKEVLEDLEREGLLWRDE 210
Vps36_ESCRT-II pfam11605
Vacuolar protein sorting protein 36 Vps36; Vps36 is a subunit of ESCRT-II, a protein involved ...
 2-89 1.77e-27

Vacuolar protein sorting protein 36 Vps36; Vps36 is a subunit of ESCRT-II, a protein involved in driving protein sorting from endosomes to lysosomes. The GLUE domain of Vps36 allows for a tight interaction to occur between the protein and Vps28, a subunit of ESCRT-I. This interaction is critical for ubiquitinated cargo progression from early to late endosomes.


Pssm-ID: 402964  Cd Length: 92  Bit Score: 103.93  E-value: 1.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990236     2 NRLSWYTP-GESTEELLCQAGHVGIYEGDLKQTNFEQGTASLTMQRIIWADSSDPDR---RLVLHHSLVISMEKHHKSMF 77
Cdd:pfam11605   1 ERNTSGRPvLRENEVDIYVQDNVGLYQGDQKILNRQNGRLYLTTHRIIYVDSADPKKvslSLPLKLVYSISEKEYSSGFL 80

                          90
                  ....*....|..
gi 71990236    78 SKGGKIVVKLEK 89
Cdd:pfam11605  81 RSSPKIILFLKP 92
PH-GRAM-like_Eap45 cd13226
Pleckstrin homology-like domain or GLUE (GRAM-like ubiquitin-binding in Eap45) domain of Eap45; ...
 1-128 2.66e-21

Pleckstrin homology-like domain or GLUE (GRAM-like ubiquitin-binding in Eap45) domain of Eap45; ESCRT complexes form the main machinery driving protein sorting from endosomes to lysosomes. Human/yeast ESCRT-I consists of Tsg101/Vps23, Vps28/Vps28, and a Vps37 homolog/Vps37. Human/yeast ESCRT-II is composed of EAP20/Vps25, EAP30/Vps22, and EAP45/Vps36. Yeast ESCRT-III consists Vps2, Vps20, Vps24, and Snf7 subunits. In contrast, there are three Human paralogs of Snf7 (hSnf7-1/CHMP4A, hSnf7-2/CHMP4B, and hSnf7-3/CHMP4C) and two paralogs of Vps2 (CHMP2A and CHMP2B). Yeast ESCRT-I links directly to ESCRT-II, through a tight interaction of Vps28 (ESCRT-I) with the yeast-specific zinc-finger insertion within the GLUE domain of Vps36. The Vps36 subunit (ESCRT-II) binds ubiquitin using one of its two NZF zinc fingers in its N-terminal region. Human Vps36, EAP45, also binds ubiquitin despite having no NZF domain. Instead, mammalian ESCRT-II interacts with Ub through the Eap45 GLUE domain directly. While yeast Vps36 GLUE shows a preference for the singly phosphorylated PI(3)P, while Eap45 GLUE preferentially binds the triply phosphorylated phosphatidylinositol PI(3,4,5)P3. Structurally, Eap45 GLUE only has a PH-like fold since it lacks the secondary structure element corresponding to the 4 strand, unlike that of yeast Vps36 GLUE. ESCRT-II also interacts with ESCRT-III via a EAP20(Vps25)/CHMP6(Vps20) interaction. The interactions of ESCRT-II GLUE domain with membranes, ESCRT-I, and ubiquitin are critical for ubiquitinated cargo progression from early to late endosomes. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275408 [Multi-domain]  Cd Length: 129  Bit Score: 88.55  E-value: 2.66e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990236   1 MNRLSWYT----PGESteeLLCQAGHVGIYEGDLKqTNFEQGTASLTMQRIIWADSSDPDRRLVLHHSLVISMEKHHKSM 76
Cdd:cd13226   1 MDRFMWCDgllfPNET---LVIQQRGVRIYDGDEK-TKFDSGELVLTSHRLIWRDQKQIERCLSLPLSLIVFIEEEESGG 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 71990236  77 FSKGGKIVVKL-EKPKAGNIGPVNSSHYETLRLVFRHGGEDDFFKKYEDAVRR 128
Cdd:cd13226  77 FGKSAKIVVHLhPAPPNKEPGPKQSSPYNYIKLSFKEGGQSEFYRALSEELTR 129
PH-GRAM-like_Vps36 cd13227
Pleckstrin homology-like domain or GLUE (GRAM-like ubiquitin-binding in Eap45) domain of Vps36; ...
 22-55 1.35e-06

Pleckstrin homology-like domain or GLUE (GRAM-like ubiquitin-binding in Eap45) domain of Vps36; ESCRT complexes form the main machinery driving protein sorting from endosomes to lysosomes. Yeast/human ESCRT-I consists of Vps23/Tsg101, Vps28/Vps28, and Vps37/Vps37 homolog. Yeast/human ESCRT-II is composed of Vps25/EAP20, Vps22/EAP30, and Vps36/EAP45. Yeast ESCRT-III consists Vps2, Vps20, Vps24, and Snf7 subunits. In contrast, there are three human paralogs of Snf7 (hSnf7-1/CHMP4A, hSnf7-2/CHMP4B, and hSnf7-3/CHMP4C) and two paralogs of Vps2 (CHMP2A and CHMP2B). Yeast ESCRT-I links directly to ESCRT-II, through a tight interaction of Vps28 (ESCRT-I) with the yeast-specific zinc-finger insertion within the GLUE domain of Vps36. The Vps36 subunit (ESCRT-II) binds ubiquitin using one of its two NZF zinc fingers in its N-terminal region. Human Vps36, EAP45, also binds ubiquitin despite having no NZF domain. Instead, mammalian ESCRT-II interacts with Ub through the Eap45 GLUE domain itself. The yeast Vps36 GLUE has a complete PH domain, wherease Eap45 GLUE only has a PH-like fold since it lacks the secondary structure element corresponding to the 4 strand. ESCRT-II also interacts with ESCRT-III via a Vps25(EAP20)/Vps20(CHMP6) interaction. Structure 2CAY is missing this insertion that contains 2 NZF zinc fingers. It is a split PH domain, with a noncanonical lipid binding pocket that binds PI(3)P. The interactions of ESCRT-II GLUE domain with membranes, ESCRT-I, and ubiquitin are critical for ubiquitinated cargo progression from early to late endosomes. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275409 [Multi-domain]  Cd Length: 119  Bit Score: 46.94  E-value: 1.35e-06
                        10        20        30
                ....*....|....*....|....*....|....
gi 71990236  22 HVGIYEGDLKQTNFEQGTASLTMQRIIWADSSDP 55
Cdd:cd13227  26 NVGLYHGKSKILNRQNGRIYLTSQRIIYVDDDDP 59
COG2345 COG2345
Predicted transcriptional regulator, ArsR family [Transcription];
316-367 4.69e-05

Predicted transcriptional regulator, ArsR family [Transcription];


Pssm-ID: 441914 [Multi-domain]  Cd Length: 217  Bit Score: 44.14  E-value: 4.69e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71990236 316 SASMDSTVGQTLEFVSKLERASANELAESLGITVILARERLLAAEESGLICR 367
Cdd:COG2345   8 AALADPTRRRILELLKRAGPVTAAELAEALGLTPNAVRRHLDALEEEGLVER 59
 
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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