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Conserved domains on  [gi|19071955|dbj|BAB85679|]
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rapsyn [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Rapsyn_N pfam10579
Rapsyn N-terminal myristoylation and linker region; Neuromuscular junction formation relies ...
1-80 1.63e-44

Rapsyn N-terminal myristoylation and linker region; Neuromuscular junction formation relies upon the clustering of acetylcholine receptors and other proteins in the muscle membrane. Rapsyn is a peripheral membrane protein that is selectively concentrated at the neuromuscular junction and is essential for the formation of synaptic acetylcholine receptor aggregates. Acetylcholine receptors fail to aggregate beneath nerve terminals in mice where rapsyn has been knocked out. The N-terminal six amino acids of rapsyn are its myristoylation site, and myristoylation is necessary for the targeting of the protein to the membrane.


:

Pssm-ID: 313739  Cd Length: 80  Bit Score: 148.90  E-value: 1.63e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071955     1 MGQDQTKQQIEKGLKLYQSNDTEKALYVWMKVLRKTSDPGGKFRVLGCLITAHSEMGKYKEMLQFSLAQINTAREMEDPD 80
Cdd:pfam10579   1 MGQDQTKQQIEKGLRLYQSNNTEKALRTWRKVLKKTCDREGCFRVLGCLITAHSEMGKYKEMLEFGHQQIGTARELEDPD 80
RING-H2_Rapsyn cd16478
RING finger, H2 subclass, found in 43 kDa receptor-associated protein of the synapse (Rapsyn) ...
360-404 6.80e-23

RING finger, H2 subclass, found in 43 kDa receptor-associated protein of the synapse (Rapsyn) and similar proteins; Rapsyn, also known as acetylcholine receptor-associated 43 kDa protein or RING finger protein 205 (RNF205), is a 43 kDa postsynaptic protein that plays an essential role in the clustering and maintenance of acetylcholine receptor (AChR) in the postsynaptic membrane of the motor endplate (EP). AChRs enable the transport of rapsyn from the Golgi complex to the plasma membrane through a molecule-specific interaction. Rapsyn also mediates subsynaptic anchoring of protein kinase A (PKA) type I in close proximity to the postsynaptic membrane, which is essential for synapse maintenance. Its mutations in humans cause endplate acetylcholine-receptor deficiency and myasthenic syndrome. Rapsyn contains an N-terminal myristoylation signal required for membrane association, seven tetratricopeptide repeats (TPRs) that subserve rapsyn self-association, a coiled-coil domain responsible for the binding of determinants within the long cytoplasmic loop of each AChR subunit, a C3H2C3-type RING-H2 finger that binds to the cytoplasmic domain of beta-dystroglycan and to S-NRAP and links rapsyn to the subsynaptic cytoskeleton, and a serine phosphorylation site.


:

Pssm-ID: 319392 [Multi-domain]  Cd Length: 47  Bit Score: 90.57  E-value: 6.80e-23
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 19071955 360 ELYCGMCGESIGEKNQQLQALPCSHIFHLKCLQTN--GTKGCPKCHR 404
Cdd:cd16478   1 ELYCGMCGESIGEKNESLQALPCSHIFHLKCLQTNlnGTRGCPNCRR 47
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
9-266 1.24e-05

Tetratricopeptide (TPR) repeat [General function prediction only];


:

Pssm-ID: 223533 [Multi-domain]  Cd Length: 291  Bit Score: 46.38  E-value: 1.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071955   9 QIEKGLKLYQSNDTEKALYVWMKVLRKTSDPGgKFRVLGCLITAHSEMGKYKEmlqfSLAQINTAREMEDPDYLTEGYLN 88
Cdd:COG0457  62 LLLLALALLKLGRLEEALELLEKALELELLPN-LAEALLNLGLLLEALGKYEE----ALELLEKALALDPDPDLAEALLA 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071955  89 LArSNEKLCDFQKTVSYCETCLNMQGttvSLQLNGQVCLSMGNAYLGLSVFQKALVSYEKALRYAHNNDDKMLEcrvccS 168
Cdd:COG0457 137 LG-ALYELGDYEEALELYEKALELDP---ELNELAEALLALGALLEALGRYEEALELLEKALKLNPDDDAEALL-----N 207
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071955 169 LGNFYIQLKDFEKALFFPCKAAELVNDYgkgwslkyrAMSQYHMSVAYKKLMRLPDAMECCEESMKIalqhgDRPLQALC 248
Cdd:COG0457 208 LGLLYLKLGKYEEALEYYEKALELDPDN---------AEALYNLALLLLELGRYEEALEALEKALEL-----DPDLYNLG 273
                       250
                ....*....|....*...
gi 19071955 249 LLNFADIHRCQKDVDKAF 266
Cdd:COG0457 274 LALLLLLAEALELLEKAD 291
TPR_12 pfam13424
Tetratricopeptide repeat;
249-318 3.41e-05

Tetratricopeptide repeat;


:

Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 41.60  E-value: 3.41e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19071955   249 LLNFADIHRCQKDVDKAFPRYESSMCIMSEI--GNRLGQASIYVGVGKCWILQKEYDKALDSLQRANDLAEA 318
Cdd:pfam13424   6 LNNLAAVLRRLGRYDEALELLEKALEIARRLlgPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
 
Name Accession Description Interval E-value
Rapsyn_N pfam10579
Rapsyn N-terminal myristoylation and linker region; Neuromuscular junction formation relies ...
1-80 1.63e-44

Rapsyn N-terminal myristoylation and linker region; Neuromuscular junction formation relies upon the clustering of acetylcholine receptors and other proteins in the muscle membrane. Rapsyn is a peripheral membrane protein that is selectively concentrated at the neuromuscular junction and is essential for the formation of synaptic acetylcholine receptor aggregates. Acetylcholine receptors fail to aggregate beneath nerve terminals in mice where rapsyn has been knocked out. The N-terminal six amino acids of rapsyn are its myristoylation site, and myristoylation is necessary for the targeting of the protein to the membrane.


Pssm-ID: 313739  Cd Length: 80  Bit Score: 148.90  E-value: 1.63e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071955     1 MGQDQTKQQIEKGLKLYQSNDTEKALYVWMKVLRKTSDPGGKFRVLGCLITAHSEMGKYKEMLQFSLAQINTAREMEDPD 80
Cdd:pfam10579   1 MGQDQTKQQIEKGLRLYQSNNTEKALRTWRKVLKKTCDREGCFRVLGCLITAHSEMGKYKEMLEFGHQQIGTARELEDPD 80
RING-H2_Rapsyn cd16478
RING finger, H2 subclass, found in 43 kDa receptor-associated protein of the synapse (Rapsyn) ...
360-404 6.80e-23

RING finger, H2 subclass, found in 43 kDa receptor-associated protein of the synapse (Rapsyn) and similar proteins; Rapsyn, also known as acetylcholine receptor-associated 43 kDa protein or RING finger protein 205 (RNF205), is a 43 kDa postsynaptic protein that plays an essential role in the clustering and maintenance of acetylcholine receptor (AChR) in the postsynaptic membrane of the motor endplate (EP). AChRs enable the transport of rapsyn from the Golgi complex to the plasma membrane through a molecule-specific interaction. Rapsyn also mediates subsynaptic anchoring of protein kinase A (PKA) type I in close proximity to the postsynaptic membrane, which is essential for synapse maintenance. Its mutations in humans cause endplate acetylcholine-receptor deficiency and myasthenic syndrome. Rapsyn contains an N-terminal myristoylation signal required for membrane association, seven tetratricopeptide repeats (TPRs) that subserve rapsyn self-association, a coiled-coil domain responsible for the binding of determinants within the long cytoplasmic loop of each AChR subunit, a C3H2C3-type RING-H2 finger that binds to the cytoplasmic domain of beta-dystroglycan and to S-NRAP and links rapsyn to the subsynaptic cytoskeleton, and a serine phosphorylation site.


Pssm-ID: 319392 [Multi-domain]  Cd Length: 47  Bit Score: 90.57  E-value: 6.80e-23
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 19071955 360 ELYCGMCGESIGEKNQQLQALPCSHIFHLKCLQTN--GTKGCPKCHR 404
Cdd:cd16478   1 ELYCGMCGESIGEKNESLQALPCSHIFHLKCLQTNlnGTRGCPNCRR 47
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
9-266 1.24e-05

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 223533 [Multi-domain]  Cd Length: 291  Bit Score: 46.38  E-value: 1.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071955   9 QIEKGLKLYQSNDTEKALYVWMKVLRKTSDPGgKFRVLGCLITAHSEMGKYKEmlqfSLAQINTAREMEDPDYLTEGYLN 88
Cdd:COG0457  62 LLLLALALLKLGRLEEALELLEKALELELLPN-LAEALLNLGLLLEALGKYEE----ALELLEKALALDPDPDLAEALLA 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071955  89 LArSNEKLCDFQKTVSYCETCLNMQGttvSLQLNGQVCLSMGNAYLGLSVFQKALVSYEKALRYAHNNDDKMLEcrvccS 168
Cdd:COG0457 137 LG-ALYELGDYEEALELYEKALELDP---ELNELAEALLALGALLEALGRYEEALELLEKALKLNPDDDAEALL-----N 207
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071955 169 LGNFYIQLKDFEKALFFPCKAAELVNDYgkgwslkyrAMSQYHMSVAYKKLMRLPDAMECCEESMKIalqhgDRPLQALC 248
Cdd:COG0457 208 LGLLYLKLGKYEEALEYYEKALELDPDN---------AEALYNLALLLLELGRYEEALEALEKALEL-----DPDLYNLG 273
                       250
                ....*....|....*...
gi 19071955 249 LLNFADIHRCQKDVDKAF 266
Cdd:COG0457 274 LALLLLLAEALELLEKAD 291
TPR_12 pfam13424
Tetratricopeptide repeat;
204-273 1.62e-05

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 42.37  E-value: 1.62e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19071955   204 YRAMSQYHMSVAYKKLMRLPDAMECCEESMKIA--LQHGDRPLQALCLLNFADIHRCQKDVDKAFPRYESSM 273
Cdd:pfam13424   1 DVATALNNLAAVLRRLGRYDEALELLEKALEIArrLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERAL 72
TPR_12 pfam13424
Tetratricopeptide repeat;
249-318 3.41e-05

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 41.60  E-value: 3.41e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19071955   249 LLNFADIHRCQKDVDKAFPRYESSMCIMSEI--GNRLGQASIYVGVGKCWILQKEYDKALDSLQRANDLAEA 318
Cdd:pfam13424   6 LNNLAAVLRRLGRYDEALELLEKALEIARRLlgPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
363-402 8.03e-04

RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227827 [Multi-domain]  Cd Length: 374  Bit Score: 41.13  E-value: 8.03e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 19071955 363 CGMCGESIgEKNQQLQALPCSHIFHLKCLQT--NGTK-GCPKC 402
Cdd:COG5540 326 CAICMSNF-IKNDRLRVLPCDHRFHVGCVDKwlLGYSnKCPVC 367
zf-RING_11 pfam17123
RING-like zinc finger;
363-391 3.41e-03

RING-like zinc finger;


Pssm-ID: 339895 [Multi-domain]  Cd Length: 29  Bit Score: 34.41  E-value: 3.41e-03
                          10        20
                  ....*....|....*....|....*....
gi 19071955   363 CGMCGESIGEKnQQLQALPCSHIFHLKCL 391
Cdd:pfam17123   2 CSICLDEFEPG-QALRVLPCSHVFHYKCI 29
 
Name Accession Description Interval E-value
Rapsyn_N pfam10579
Rapsyn N-terminal myristoylation and linker region; Neuromuscular junction formation relies ...
1-80 1.63e-44

Rapsyn N-terminal myristoylation and linker region; Neuromuscular junction formation relies upon the clustering of acetylcholine receptors and other proteins in the muscle membrane. Rapsyn is a peripheral membrane protein that is selectively concentrated at the neuromuscular junction and is essential for the formation of synaptic acetylcholine receptor aggregates. Acetylcholine receptors fail to aggregate beneath nerve terminals in mice where rapsyn has been knocked out. The N-terminal six amino acids of rapsyn are its myristoylation site, and myristoylation is necessary for the targeting of the protein to the membrane.


Pssm-ID: 313739  Cd Length: 80  Bit Score: 148.90  E-value: 1.63e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071955     1 MGQDQTKQQIEKGLKLYQSNDTEKALYVWMKVLRKTSDPGGKFRVLGCLITAHSEMGKYKEMLQFSLAQINTAREMEDPD 80
Cdd:pfam10579   1 MGQDQTKQQIEKGLRLYQSNNTEKALRTWRKVLKKTCDREGCFRVLGCLITAHSEMGKYKEMLEFGHQQIGTARELEDPD 80
RING-H2_Rapsyn cd16478
RING finger, H2 subclass, found in 43 kDa receptor-associated protein of the synapse (Rapsyn) ...
360-404 6.80e-23

RING finger, H2 subclass, found in 43 kDa receptor-associated protein of the synapse (Rapsyn) and similar proteins; Rapsyn, also known as acetylcholine receptor-associated 43 kDa protein or RING finger protein 205 (RNF205), is a 43 kDa postsynaptic protein that plays an essential role in the clustering and maintenance of acetylcholine receptor (AChR) in the postsynaptic membrane of the motor endplate (EP). AChRs enable the transport of rapsyn from the Golgi complex to the plasma membrane through a molecule-specific interaction. Rapsyn also mediates subsynaptic anchoring of protein kinase A (PKA) type I in close proximity to the postsynaptic membrane, which is essential for synapse maintenance. Its mutations in humans cause endplate acetylcholine-receptor deficiency and myasthenic syndrome. Rapsyn contains an N-terminal myristoylation signal required for membrane association, seven tetratricopeptide repeats (TPRs) that subserve rapsyn self-association, a coiled-coil domain responsible for the binding of determinants within the long cytoplasmic loop of each AChR subunit, a C3H2C3-type RING-H2 finger that binds to the cytoplasmic domain of beta-dystroglycan and to S-NRAP and links rapsyn to the subsynaptic cytoskeleton, and a serine phosphorylation site.


Pssm-ID: 319392 [Multi-domain]  Cd Length: 47  Bit Score: 90.57  E-value: 6.80e-23
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 19071955 360 ELYCGMCGESIGEKNQQLQALPCSHIFHLKCLQTN--GTKGCPKCHR 404
Cdd:cd16478   1 ELYCGMCGESIGEKNESLQALPCSHIFHLKCLQTNlnGTRGCPNCRR 47
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
9-266 1.24e-05

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 223533 [Multi-domain]  Cd Length: 291  Bit Score: 46.38  E-value: 1.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071955   9 QIEKGLKLYQSNDTEKALYVWMKVLRKTSDPGgKFRVLGCLITAHSEMGKYKEmlqfSLAQINTAREMEDPDYLTEGYLN 88
Cdd:COG0457  62 LLLLALALLKLGRLEEALELLEKALELELLPN-LAEALLNLGLLLEALGKYEE----ALELLEKALALDPDPDLAEALLA 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071955  89 LArSNEKLCDFQKTVSYCETCLNMQGttvSLQLNGQVCLSMGNAYLGLSVFQKALVSYEKALRYAHNNDDKMLEcrvccS 168
Cdd:COG0457 137 LG-ALYELGDYEEALELYEKALELDP---ELNELAEALLALGALLEALGRYEEALELLEKALKLNPDDDAEALL-----N 207
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071955 169 LGNFYIQLKDFEKALFFPCKAAELVNDYgkgwslkyrAMSQYHMSVAYKKLMRLPDAMECCEESMKIalqhgDRPLQALC 248
Cdd:COG0457 208 LGLLYLKLGKYEEALEYYEKALELDPDN---------AEALYNLALLLLELGRYEEALEALEKALEL-----DPDLYNLG 273
                       250
                ....*....|....*...
gi 19071955 249 LLNFADIHRCQKDVDKAF 266
Cdd:COG0457 274 LALLLLLAEALELLEKAD 291
TPR_12 pfam13424
Tetratricopeptide repeat;
204-273 1.62e-05

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 42.37  E-value: 1.62e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19071955   204 YRAMSQYHMSVAYKKLMRLPDAMECCEESMKIA--LQHGDRPLQALCLLNFADIHRCQKDVDKAFPRYESSM 273
Cdd:pfam13424   1 DVATALNNLAAVLRRLGRYDEALELLEKALEIArrLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERAL 72
RING-H2 cd16448
H2 subclass of RING (RING-H2) finger and its variants; RING finger is a specialized type of ...
363-402 1.96e-05

H2 subclass of RING (RING-H2) finger and its variants; RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized as two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have different Cys/His pattern. Some lack a single Cys or His residues at typical Zn ligand positions. Especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well. This family corresponds to H2 subclass of RING (RING-H2) finger proteins that are characterized by containing C3H2C3-type canonical RING-H2 fingers or noncanonical RING-H2 finger variants, including C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type modified RING-H2 fingers. The canonical RING-H2 finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-H-X2-C-X(4-48)-C-X2-C, X is any amino acid and the number of X residues varies in different fingers. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-H2 finger can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serves as a scaffold for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 319362 [Multi-domain]  Cd Length: 44  Bit Score: 41.28  E-value: 1.96e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 19071955 363 CGMCGESIGEKNQQLQALPCSHIFHLKCLQ---TNGTKGCPKC 402
Cdd:cd16448   1 CAICLEEFEEGDCPVRLLPCGHVFHKSCIDkwlESGNRTCPLC 43
TPR_12 pfam13424
Tetratricopeptide repeat;
249-318 3.41e-05

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 41.60  E-value: 3.41e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19071955   249 LLNFADIHRCQKDVDKAFPRYESSMCIMSEI--GNRLGQASIYVGVGKCWILQKEYDKALDSLQRANDLAEA 318
Cdd:pfam13424   6 LNNLAAVLRRLGRYDEALELLEKALEIARRLlgPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
RING1-H2_RNF32 cd16677
RING finger 1, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; ...
363-402 2.64e-04

RING finger 1, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; RNF32 is mainly expressed in testis spermatogenesis, most likely in spermatocytes and/or in spermatids, suggesting a possible role in sperm formation. RNF32 contains two C3H2C3-type RING-H2 fingers separated by an IQ domain of unknown function. Although the biological function of RNF32 remains unclear, the protein with double RING-H2 fingers may act as a scaffold for binding several proteins that function in the same pathway. This family corresponds to the first RING-H2 finger.


Pssm-ID: 319591 [Multi-domain]  Cd Length: 44  Bit Score: 38.08  E-value: 2.64e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 19071955 363 CGMCGESIGEKNQQLqaLPCSHIFHLKCLQT----NGTKGCPKC 402
Cdd:cd16677   2 CVICKEDFGLQQQVL--LSCSHVFHRACLESferfSGKKTCPMC 43
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
363-402 8.03e-04

RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227827 [Multi-domain]  Cd Length: 374  Bit Score: 41.13  E-value: 8.03e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 19071955 363 CGMCGESIgEKNQQLQALPCSHIFHLKCLQT--NGTK-GCPKC 402
Cdd:COG5540 326 CAICMSNF-IKNDRLRVLPCDHRFHVGCVDKwlLGYSnKCPVC 367
RING-H2_RNF167 cd16797
RING finger, H2 subclass, found in RING finger protein 167 (RNF167) and similar proteins; ...
363-402 8.20e-04

RING finger, H2 subclass, found in RING finger protein 167 (RNF167) and similar proteins; RNF167, also known as RING105, is an endosomal/lysosomal E3 ubiquitin-protein ligase involved in alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) ubiquitination. It ubiquitinates GluA2 and regulates its surface expression, and thus acts as a selective regulator of AMPAR-mediated neurotransmission. It acts as an endosomal membrane protein which ubiquitylates vesicle-associated membrane protein 3 (VAMP3) and regulates endosomal trafficking. Moreover, RNF167 plays a role in the regulation of TSSC5 (tumor-suppressing subchromosomal transferable fragment cDNA, also known as ORCTL2/IMPT1/BWR1A/SLC22A1L), which can function in concert with the ubiquitin-conjugating enzyme UbcH6. RNF167 is widely conserved in metazoans and contains an N-terminal signal peptide, a protease-associated (PA) domain, two transmembrane domains (TM1 and TM2), and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.


Pssm-ID: 319711 [Multi-domain]  Cd Length: 46  Bit Score: 36.95  E-value: 8.20e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 19071955 363 CGMCGESIgEKNQQLQALPCSHIFHLKCLQ---TNGTKGCPKC 402
Cdd:cd16797   3 CAICLDEY-EEGDKLRVLPCSHAYHSKCVDpwlTQTKKTCPVC 44
RING-H2_PA-TM-RING cd16454
RING finger, H2 subclass, found in the PA-TM-RING ubiquitin ligase family; The PA-TM-RING ...
363-402 2.00e-03

RING finger, H2 subclass, found in the PA-TM-RING ubiquitin ligase family; The PA-TM-RING family represents a group of transmembrane-type E3 ubiquitin ligases, which has been characterized by an N-terminal transient signal peptide, a PA (protease-associated) domain, a TM (transmembrane) domain, as well as a C-terminal C3H2C3-type RING-H2 finger domain. It includes RNF13, RNF167, ZNRF4 (zinc and RING finger 4), GRAIL (gene related to anergy in lymphocytes)/RNF128, RNF130, RNF133, RNF148, RNF149 and RNF150 (which are more closely related), as well as RNF43 and ZNRF3 which have substantially longer C-terminal tail extensions compared with the others. PA-TM-RING proteins are expressed at low levels in all mammalian tissues and species, but they are not present in yeast. They play a common regulatory role in intracellular trafficking/sorting, suggesting that abrogation of their function may result in dysregulation of cellular signaling events in cancer.


Pssm-ID: 319368 [Multi-domain]  Cd Length: 43  Bit Score: 35.74  E-value: 2.00e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 19071955 363 CGMCGESIGEkNQQLQALPCSHIFHLKC----LQTNGTkgCPKC 402
Cdd:cd16454   2 CAICLEEFED-GEEVRVLPCNHLFHSNCidpwLEQHAT--CPLC 42
zf-RING_11 pfam17123
RING-like zinc finger;
363-391 3.41e-03

RING-like zinc finger;


Pssm-ID: 339895 [Multi-domain]  Cd Length: 29  Bit Score: 34.41  E-value: 3.41e-03
                          10        20
                  ....*....|....*....|....*....
gi 19071955   363 CGMCGESIGEKnQQLQALPCSHIFHLKCL 391
Cdd:pfam17123   2 CSICLDEFEPG-QALRVLPCSHVFHYKCI 29
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
129-382 5.68e-03

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 223533 [Multi-domain]  Cd Length: 291  Bit Score: 38.29  E-value: 5.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071955 129 MGNAYLGLSVFQKALVSYEKALRYAHNNDDKMLECRvccsLGNFYIQLKDFEKALFFPCKAAELVNDYgkgwslkYRAMS 208
Cdd:COG0457  29 GLALLELLGELAEALELLEEALELLPNSDLAGLLLL----LALALLKLGRLEEALELLEKALELELLP-------NLAEA 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071955 209 QYHMSVAYKKLMRLPDAMECCEEsmkiALQHGDRPLQALCLLNFAdIHRCQKDVDKAFPRYESSMCIMSEIGNRlgqASI 288
Cdd:COG0457  98 LLNLGLLLEALGKYEEALELLEK----ALALDPDPDLAEALLALG-ALYELGDYEEALELYEKALELDPELNEL---AEA 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19071955 289 YVGVGKCWILQKEYDKALDSLQRANDLAEAIgnklcILKVHSLCEGIYRCKEQQEELREQVVKFLQCVEELELYCGMCGE 368
Cdd:COG0457 170 LLALGALLEALGRYEEALELLEKALKLNPDD-----DAEALLNLGLLYLKLGKYEEALEYYEKALELDPDNAEALYNLAL 244
                       250
                ....*....|....
gi 19071955 369 SIGEKNQQLQALPC 382
Cdd:COG0457 245 LLLELGRYEEALEA 258
RING-H2_RNF13_like cd16665
RING finger, H2 subclass, found in RING finger protein 13 (RNF13), RING finger protein 167 ...
363-404 7.47e-03

RING finger, H2 subclass, found in RING finger protein 13 (RNF13), RING finger protein 167 (RNF167), and similar proteins; This subfamily includes RING finger protein 13 (RNF13), RING finger protein 167 (RNF167), Zinc/RING finger protein 4 (ZNRF4), and similar proteins, which belong to a larger PA-TM-RING ubiquitin ligase family that has been characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane domain (TM), and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence. RNF13 is a widely expressed membrane-associated E3 ubiquitin-protein ligase that is functionally significant in the regulation of cancer development, muscle cell growth, and neuronal development. Its expression is developmentally regulated during myogenesis and is upregulated in various tumors. RNF13 negatively regulates cell proliferation through its E3 ligase activity. RNF167, also known as RING105, is an endosomal/lysosomal E3 ubiquitin-protein ligase involved in alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) ubiquitination. It acts as an endosomal membrane protein which ubiquitylates vesicle-associated membrane protein 3 (VAMP3) and regulates endosomal trafficking. Moreover, RNF167 plays a role in the regulation of TSSC5 (tumor-suppressing subchromosomal transferable fragment cDNA; also known as ORCTL2/IMPT1/BWR1A/SLC22A1L), which can function in concert with the ubiquitin-conjugating enzyme UbcH6. ZNRF4, also known as RING finger protein 204 (RNF204), or Nixin, is an endoplasmic reticulum (ER) membrane-anchored ubiquitin ligase that physically interacts with the ER-localized chaperone calnexin in a glycosylation-independent manner, induces calnexin ubiquitination, and p97-dependent degradation, indicating an ER-associated degradation-like mechanism of calnexin turnover. The murine protein sperizin (spermatid-specific ring zinc finger) is a homolog of human ZNRF4. It is specifically expressed in Haploid germ cells and involved in spermatogenesis.


Pssm-ID: 319579 [Multi-domain]  Cd Length: 46  Bit Score: 33.92  E-value: 7.47e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 19071955 363 CGMCGESIGEKnQQLQALPCSHIFHLKCLQ---TNGTKGCPKCHR 404
Cdd:cd16665   3 CAICLDDYEEG-DKLRILPCSHAYHCKCIDpwlTQNRRTCPVCKR 46
RING-HC_TRIM9 cd16755
RING finger, HC subclass, found in tripartite motif-containing protein 9 (TRIM9) and similar ...
358-405 9.30e-03

RING finger, HC subclass, found in tripartite motif-containing protein 9 (TRIM9) and similar proteins; TRIM9, human ortholog of rat Spring, also known as RING finger protein 91 (RNF91), is a brain-specific E3 ubiquitin-protein ligase collaborating with an E2 ubiquitin conjugating enzyme UBCH5b. TRIM9 plays an important role in the regulation of neuronal functions and participates in the neurodegenerative disorders through its ligase activity. It interacts with the WD repeat region of beta-transducin repeat-containing protein (beta-TrCP) through its N-terminal degron motif depending on the phosphorylation status, and thus negatively regulates nuclear factor-kappaB (NF-kappaB) activation in the NF-kappaB pro-inflammatory signaling pathway. Moreover, TRIM9 acts as a critical catalytic link between Netrin-1 and exocytic soluble NSF attachment receptor protein (SNARE) machinery in murine cortical neurons. It promotes SNARE-mediated vesicle fusion and axon branching in a Netrin-dependent manner. TRIM9 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319669 [Multi-domain]  Cd Length: 52  Bit Score: 34.25  E-value: 9.30e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19071955 358 ELELYCGMCGESIGEKnqqlQALPCSHIFHLKC-----LQT---NGTKGCPKCHRS 405
Cdd:cd16755   1 EEELKCPVCGSFYREP----IILPCSHNLCLACarnilVQTperNSCLTCPQCHRS 52
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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