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Conserved domains on  [gi|6093894|sp|O42393|]
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RecName: Full=43 kDa receptor-associated protein of the synapse; Short=RAPsyn; AltName: Full=43 kDa postsynaptic protein; AltName: Full=Acetylcholine receptor-associated 43 kDa protein

Protein Classification

TPR and RING-H2_Rapsyn domain-containing protein (domain architecture ID 11721581)

protein containing domains SNAP, TPR, TPR_12, and RING-H2_Rapsyn

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SNAP super family cl24038
Soluble N-ethylmaleimide-sensitive factor (NSF) Attachment Protein family; Members of the ...
1-80 1.66e-40

Soluble N-ethylmaleimide-sensitive factor (NSF) Attachment Protein family; Members of the soluble NSF attachment protein (SNAP) family are involved in intracellular membrane trafficking, including vesicular transport between the endoplasmic reticulum and Golgi apparatus. Higher eukaryotes contain three isoforms of SNAPs: alpha, beta, and gamma. Alpha-SNAP is universally present in eukaryotes and acts as an adaptor protein between SNARE (integral membrane SNAP receptor) and NSF for recruitment to the 20S complex. Beta-SNAP is brain-specific and shares high sequence identity (about 85%) with alpha-SNAP. Gamma-SNAP is weakly related (about 20-25% identity) to the two other isoforms, and is ubiquitous. It may help regulate the activity of the 20S complex. The X-ray structures of vertebrate gamma-SNAP and yeast Sec17, a SNAP family member, show similar all-helical structures consisting of an N-terminal extended twisted sheet of four Tetratricopeptide repeat (TPR)-like helical hairpins and a C-terminal helical bundle.


The actual alignment was detected with superfamily member pfam10579:

Pssm-ID: 329252  Cd Length: 80  Bit Score: 138.50  E-value: 1.66e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894      1 MGQDQTKQQIEKGLHLYQSNQTEKALQVWMRVLEKSADPAGRFRVLGCLITAHAEMGRYKDMLKFAVVQIDTARELEDPN 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 2.57e-24

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: 94.42  E-value: 2.57e-24
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 6093894  360 ELYCGMCGESIGEKNNQLQALPCSHFFHLKCLQTN--GTRGCPNCRR 404
Cdd:cd16478   1 ELYCGMCGESIGEKNESLQALPCSHIFHLKCLQTNlnGTRGCPNCRR 47
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
9-239 2.93e-07

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


:

Pssm-ID: 223533 [Multi-domain]  Cd Length: 291  Bit Score: 51.39  E-value: 2.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894    9 QIEKGLHLYQSNQTEKALQVWMRVLEKSADPAgRFRVLGCLITAHAEMGRYKDMLKFavvqIDTARELEDPNYLTEGYLN 88
Cdd:COG0457  62 LLLLALALLKLGRLEEALELLEKALELELLPN-LAEALLNLGLLLEALGKYEEALEL----LEKALALDPDPDLAEALLA 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894   89 LArSNEKLCEFQKTISYCKTCLNMQGttvSLQLNGQVSLSMGNAFLGLSIFQKALECFEKALRYAHNNDDKMLEcrvccS 168
Cdd:COG0457 137 LG-ALYELGDYEEALELYEKALELDP---ELNELAEALLALGALLEALGRYEEALELLEKALKLNPDDDAEALL-----N 207
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6093894  169 LGNFYAQIKDYEKALFFPCKAAELVNDYgagwslkyrAMSQYHMAVAYRKLGRLADAMDCCEESMKIALQH 239
Cdd:COG0457 208 LGLLYLKLGKYEEALEYYEKALELDPDN---------AEALYNLALLLLELGRYEEALEALEKALELDPDL 269
TPR_12 pfam13424
Tetratricopeptide repeat;
204-278 8.82e-05

Tetratricopeptide repeat;


:

Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 40.45  E-value: 8.82e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6093894    204 YRAMSQYHMAVAYRKLGRLADAMDCCEESMKIA--LQHGDRPLQALCLLCFADIHLSRRDVQTAFPRYDSAMSIMTE 278
Cdd:pfam13424   1 DVATALNNLAAVLRRLGRYDEALELLEKALEIArrLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
 
Name Accession Description Interval E-value
Rapsyn_N pfam10579
Rapsyn N-terminal myristoylation and linker region; Neuromuscular junction formation relies ...
1-80 1.66e-40

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: 138.50  E-value: 1.66e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894      1 MGQDQTKQQIEKGLHLYQSNQTEKALQVWMRVLEKSADPAGRFRVLGCLITAHAEMGRYKDMLKFAVVQIDTARELEDPN 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 2.57e-24

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: 94.42  E-value: 2.57e-24
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 6093894  360 ELYCGMCGESIGEKNNQLQALPCSHFFHLKCLQTN--GTRGCPNCRR 404
Cdd:cd16478   1 ELYCGMCGESIGEKNESLQALPCSHIFHLKCLQTNlnGTRGCPNCRR 47
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
9-239 2.93e-07

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


Pssm-ID: 223533 [Multi-domain]  Cd Length: 291  Bit Score: 51.39  E-value: 2.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894    9 QIEKGLHLYQSNQTEKALQVWMRVLEKSADPAgRFRVLGCLITAHAEMGRYKDMLKFavvqIDTARELEDPNYLTEGYLN 88
Cdd:COG0457  62 LLLLALALLKLGRLEEALELLEKALELELLPN-LAEALLNLGLLLEALGKYEEALEL----LEKALALDPDPDLAEALLA 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894   89 LArSNEKLCEFQKTISYCKTCLNMQGttvSLQLNGQVSLSMGNAFLGLSIFQKALECFEKALRYAHNNDDKMLEcrvccS 168
Cdd:COG0457 137 LG-ALYELGDYEEALELYEKALELDP---ELNELAEALLALGALLEALGRYEEALELLEKALKLNPDDDAEALL-----N 207
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6093894  169 LGNFYAQIKDYEKALFFPCKAAELVNDYgagwslkyrAMSQYHMAVAYRKLGRLADAMDCCEESMKIALQH 239
Cdd:COG0457 208 LGLLYLKLGKYEEALEYYEKALELDPDN---------AEALYNLALLLLELGRYEEALEALEKALELDPDL 269
TPR_12 pfam13424
Tetratricopeptide repeat;
204-278 8.82e-05

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 40.45  E-value: 8.82e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6093894    204 YRAMSQYHMAVAYRKLGRLADAMDCCEESMKIA--LQHGDRPLQALCLLCFADIHLSRRDVQTAFPRYDSAMSIMTE 278
Cdd:pfam13424   1 DVATALNNLAAVLRRLGRYDEALELLEKALEIArrLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
363-403 7.35e-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: 7.35e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 6093894  363 CGMCGESIgEKNNQLQALPCSHFFHLKCLQT--NGTR-GCPNCR 403
Cdd:COG5540 326 CAICMSNF-IKNDRLRVLPCDHRFHVGCVDKwlLGYSnKCPVCR 368
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
62-291 8.94e-04

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 41.22  E-value: 8.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894     62 MLKFAVVQIDTARELEDPNYLT----------EGYLNLARSNEKLCEFQKTISYCKTCLNMQGTTVSLqlngqvsLSM-G 130
Cdd:TIGR02917 536 ILALAGLYLRTGNEEEAVAWLEkaaelnpqeiEPALALAQYYLGKGQLKKALAILNEAADAAPDSPEA-------WLMlG 608
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894    131 NAFLGLSIFQKALECFEKALRYAHNNDDKMLEcrvccsLGNFYAQIKDYEKALffpckaaelvndygagWSLKyRAMSQY 210
Cdd:TIGR02917 609 RAQLAAGDLNKAVSSFKKLLALQPDSALALLL------LADAYAVMKNYAKAI----------------TSLK-RALELK 665
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894    211 -HMAVAYRKLGRLADAMDCCEESMKIALQ-HGDRPLQALCLLCFADIHLSRRDVQTAFPRYDSAMSIMTEIGN--RLGQI 286
Cdd:TIGR02917 666 pDNTEAQIGLAQLLLAAKRTESAKKIAKSlQKQHPKAALGFELEGDLYLRQKDYPAAIQAYRKALKRAPSSQNaiKLHRA 745

                  ....*
gi 6093894    287 QVLLG 291
Cdd:TIGR02917 746 LLASG 750
zf-RING_2 pfam13639
Ring finger domain;
363-403 5.20e-03

Ring finger domain;


Pssm-ID: 338865 [Multi-domain]  Cd Length: 44  Bit Score: 34.68  E-value: 5.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 6093894    363 CGMCGESIgEKNNQLQALPCSHFFHLKC----LQTNGTrgCPNCR 403
Cdd:pfam13639   3 CPICLEEF-EEGDKVVILPCGHHFHRECldkwLRSSNT--CPLCR 44
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
144-236 8.86e-03

BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It is known to have a role in endosomal targeting. ESCRT-III subunit Snf7 binds to a conserved hydrophobic patch in the BRO1 domain that is required for protein complex formation and for the protein-sorting function of BRO1.


Pssm-ID: 335214  Cd Length: 374  Bit Score: 37.93  E-value: 8.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894    144 ECF-EKALRyahnndDKM---LECRVCCSLGNFYAQIKDYekalffpCKAAELVNDYGAGW----SLK---YRAMSQYHM 212
Cdd:pfam03097 182 ECFwEKAIK------DNKkdsLIAKLAAQVSELYEEALEA-------LKKPVLSDLFDKEWishvQAKahhFKALAQYRQ 248
                          90       100       110
                  ....*....|....*....|....*....|.
gi 6093894    213 AVAY---RKLG----RLADAMDCCEESMKIA 236
Cdd:pfam03097 249 ALADeeaKKYGeeiaRLQLALSLLKEALKSK 279
 
Name Accession Description Interval E-value
Rapsyn_N pfam10579
Rapsyn N-terminal myristoylation and linker region; Neuromuscular junction formation relies ...
1-80 1.66e-40

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: 138.50  E-value: 1.66e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894      1 MGQDQTKQQIEKGLHLYQSNQTEKALQVWMRVLEKSADPAGRFRVLGCLITAHAEMGRYKDMLKFAVVQIDTARELEDPN 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 2.57e-24

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: 94.42  E-value: 2.57e-24
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 6093894  360 ELYCGMCGESIGEKNNQLQALPCSHFFHLKCLQTN--GTRGCPNCRR 404
Cdd:cd16478   1 ELYCGMCGESIGEKNESLQALPCSHIFHLKCLQTNlnGTRGCPNCRR 47
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
9-239 2.93e-07

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


Pssm-ID: 223533 [Multi-domain]  Cd Length: 291  Bit Score: 51.39  E-value: 2.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894    9 QIEKGLHLYQSNQTEKALQVWMRVLEKSADPAgRFRVLGCLITAHAEMGRYKDMLKFavvqIDTARELEDPNYLTEGYLN 88
Cdd:COG0457  62 LLLLALALLKLGRLEEALELLEKALELELLPN-LAEALLNLGLLLEALGKYEEALEL----LEKALALDPDPDLAEALLA 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894   89 LArSNEKLCEFQKTISYCKTCLNMQGttvSLQLNGQVSLSMGNAFLGLSIFQKALECFEKALRYAHNNDDKMLEcrvccS 168
Cdd:COG0457 137 LG-ALYELGDYEEALELYEKALELDP---ELNELAEALLALGALLEALGRYEEALELLEKALKLNPDDDAEALL-----N 207
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6093894  169 LGNFYAQIKDYEKALFFPCKAAELVNDYgagwslkyrAMSQYHMAVAYRKLGRLADAMDCCEESMKIALQH 239
Cdd:COG0457 208 LGLLYLKLGKYEEALEYYEKALELDPDN---------AEALYNLALLLLELGRYEEALEALEKALELDPDL 269
RING-H2 cd16448
H2 subclass of RING (RING-H2) finger and its variants; RING finger is a specialized type of ...
363-403 6.50e-07

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: 45.52  E-value: 6.50e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 6093894  363 CGMCGESIGEKNNQLQALPCSHFFHLKCLQ---TNGTRGCPNCR 403
Cdd:cd16448   1 CAICLEEFEEGDCPVRLLPCGHVFHKSCIDkwlESGNRTCPLCR 44
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
60-317 4.21e-05

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


Pssm-ID: 223533 [Multi-domain]  Cd Length: 291  Bit Score: 44.84  E-value: 4.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894   60 KDMLKFAVVQIDTARELEDPNYLTEGYLNLARSNEKLCEFQKTISYCKTCLNMQgttvSLQLNGQVSLSMGNAFLGLSIF 139
Cdd:COG0457  36 LGELAEALELLEEALELLPNSDLAGLLLLLALALLKLGRLEEALELLEKALELE----LLPNLAEALLNLGLLLEALGKY 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894  140 QKALECFEKALRYAHNNDDKMLECRVCC--SLGNFYAQIKDYEKALFFPCKAAELVNDYgagwslkyramsqYHMAVAYR 217
Cdd:COG0457 112 EEALELLEKALALDPDPDLAEALLALGAlyELGDYEEALELYEKALELDPELNELAEAL-------------LALGALLE 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894  218 KLGRLADAMDCCEESMKIalqhgDRPLQALCLLCFADIHLSRRDVQTAFPRYDSAMSIMTEIgnrlgqIQVLLGVAKCWM 297
Cdd:COG0457 179 ALGRYEEALELLEKALKL-----NPDDDAEALLNLGLLYLKLGKYEEALEYYEKALELDPDN------AEALYNLALLLL 247
                       250       260
                ....*....|....*....|
gi 6093894  298 IQKELDKALESIEKAQELAE 317
Cdd:COG0457 248 ELGRYEEALEALEKALELDP 267
TPR_12 pfam13424
Tetratricopeptide repeat;
204-278 8.82e-05

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 40.45  E-value: 8.82e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6093894    204 YRAMSQYHMAVAYRKLGRLADAMDCCEESMKIA--LQHGDRPLQALCLLCFADIHLSRRDVQTAFPRYDSAMSIMTE 278
Cdd:pfam13424   1 DVATALNNLAAVLRRLGRYDEALELLEKALEIArrLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
RING-H2_RNF167 cd16797
RING finger, H2 subclass, found in RING finger protein 167 (RNF167) and similar proteins; ...
363-404 5.81e-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: 37.33  E-value: 5.81e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 6093894  363 CGMCGESIgEKNNQLQALPCSHFFHLKCLQ---TNGTRGCPNCRR 404
Cdd:cd16797   3 CAICLDEY-EEGDKLRVLPCSHAYHSKCVDpwlTQTKKTCPVCKQ 46
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
363-403 7.35e-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: 7.35e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 6093894  363 CGMCGESIgEKNNQLQALPCSHFFHLKCLQT--NGTR-GCPNCR 403
Cdd:COG5540 326 CAICMSNF-IKNDRLRVLPCDHRFHVGCVDKwlLGYSnKCPVCR 368
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
62-291 8.94e-04

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 41.22  E-value: 8.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894     62 MLKFAVVQIDTARELEDPNYLT----------EGYLNLARSNEKLCEFQKTISYCKTCLNMQGTTVSLqlngqvsLSM-G 130
Cdd:TIGR02917 536 ILALAGLYLRTGNEEEAVAWLEkaaelnpqeiEPALALAQYYLGKGQLKKALAILNEAADAAPDSPEA-------WLMlG 608
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894    131 NAFLGLSIFQKALECFEKALRYAHNNDDKMLEcrvccsLGNFYAQIKDYEKALffpckaaelvndygagWSLKyRAMSQY 210
Cdd:TIGR02917 609 RAQLAAGDLNKAVSSFKKLLALQPDSALALLL------LADAYAVMKNYAKAI----------------TSLK-RALELK 665
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894    211 -HMAVAYRKLGRLADAMDCCEESMKIALQ-HGDRPLQALCLLCFADIHLSRRDVQTAFPRYDSAMSIMTEIGN--RLGQI 286
Cdd:TIGR02917 666 pDNTEAQIGLAQLLLAAKRTESAKKIAKSlQKQHPKAALGFELEGDLYLRQKDYPAAIQAYRKALKRAPSSQNaiKLHRA 745

                  ....*
gi 6093894    287 QVLLG 291
Cdd:TIGR02917 746 LLASG 750
RING-H2_RNF13_like cd16665
RING finger, H2 subclass, found in RING finger protein 13 (RNF13), RING finger protein 167 ...
363-404 2.03e-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: 35.85  E-value: 2.03e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 6093894  363 CGMCGESIGEKNnQLQALPCSHFFHLKCLQ---TNGTRGCPNCRR 404
Cdd:cd16665   3 CAICLDDYEEGD-KLRILPCSHAYHCKCIDpwlTQNRRTCPVCKR 46
TPR COG0790
TPR repeat [Signal transduction mechanisms];
139-316 2.08e-03

TPR repeat [Signal transduction mechanisms];


Pssm-ID: 223861 [Multi-domain]  Cd Length: 292  Bit Score: 39.64  E-value: 2.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894  139 FQKALECFEKAlryAHNNDDKMlecrvCCSLGNFYAQ----IKDYEKALFFPCKAAELVNDYGAGwslkyramSQYHMAV 214
Cdd:COG0790  93 KTKAADWYRCA---AADGLAEA-----LFNLGLMYANgrgvPLDLVKALKYYEKAAKLGNVEAAL--------AMYRLGL 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894  215 AYRKlGRLADAMD-----CCEESMKIALQhGDRPLQALCLLCFADIHLSRRDVQTAFPRYD-SAMSIMTEIGNRLGQI-Q 287
Cdd:COG0790 157 AYLS-GLQALAVAyddkkALYLYRKAAEL-GNPDAQLLLGRMYEKGLGVPRDLKKAFRWYKkAAEQGDGAACYNLGLMyL 234
                       170       180       190
                ....*....|....*....|....*....|...
gi 6093894  288 VLLGVAKCWMIQKE----LDKALESIEKAQELA 316
Cdd:COG0790 235 NGEGVKKAAFLTAAkeedKKQALEWLQKACELG 267
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
146-315 2.09e-03

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 40.07  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894    146 FEKALRYAHNNDDKMLecrvccSLGNFYAQIKDYEKALFFPCKAAELVNDYGAgwslKYRAMSQYhmavaYRKLGRLADA 225
Cdd:TIGR02917 522 FEKVLTIDPKNLRAIL------ALAGLYLRTGNEEEAVAWLEKAAELNPQEIE----PALALAQY-----YLGKGQLKKA 586
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894    226 MDCCEESMKIAlqhgDRPLQALCLLcfADIHLSRRDVQTAFPRYDSAMSIMTEignrlgQIQVLLGVAKCWMIQKELDKA 305
Cdd:TIGR02917 587 LAILNEAADAA----PDSPEAWLML--GRAQLAAGDLNKAVSSFKKLLALQPD------SALALLLLADAYAVMKNYAKA 654
                         170
                  ....*....|
gi 6093894    306 LESIEKAQEL 315
Cdd:TIGR02917 655 ITSLKRALEL 664
RING-H2_RNF115 cd16800
RING finger, H2 subclass, found in RING finger protein 115 (RNF115) and similar proteins; ...
361-404 2.09e-03

RING finger, H2 subclass, found in RING finger protein 115 (RNF115) and similar proteins; RNF115, also known as Rab7-interacting ring finger protein (Rabring 7), or zinc finger protein 364 (ZNF364), or breast cancer-associated gene 2 (BCA2), is an E3 ubiquitin-protein ligase that is an endogenous inhibitor of adenosine monophosphate-activated protein kinase (AMPK) activation and its inhibition increases the efficacy of metformin in breast cancer cells. It also functions as a co-factor in the restriction imposed by tetherin on HIV-1, and targets HIV-1 Gag for lysosomal degradation, impairing virus assembly and release, in a tetherin-independent manner. Moreover, RNF115 is a Rab7-binding protein that stimulates c-Myc degradation through mono-ubiquitination of MM-1. It also plays crucial roles as a Rab7 target protein in vesicle traffic to late endosome/lysosome and lysosome biogenesis. Furthermore, RNF115 and the related protein, RNF126 associate with the epidermal growth factor receptor (EGFR) and promote ubiquitylation of EGFR, suggesting they play a role in the ubiquitin-dependent sorting and downregulation of membrane receptors. RNF115 contains an N-terminal BCA2 Zinc-finger domain (BZF), the AKT-phosphorylation sites, and the C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 319714 [Multi-domain]  Cd Length: 47  Bit Score: 35.74  E-value: 2.09e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 6093894  361 LYCGMCGE--SIGEknnQLQALPCSHFFHLKC----LQTNGTrgCPNCRR 404
Cdd:cd16800   1 LECPVCKEdyTVEE---QVRQLPCNHFFHSDCivpwLELHDT--CPVCRK 45
RING-H2_DZIP3 cd16460
RING finger, H2 subclass, found in DAZ (deleted in azoospermia)-interacting protein 3 (DZIP3) ...
363-403 2.34e-03

RING finger, H2 subclass, found in DAZ (deleted in azoospermia)-interacting protein 3 (DZIP3) and similar proteins; DZIP3, also known as RNA-binding ubiquitin ligase of 138 kDa (RUL138) or 2A-HUB protein, is an RNA-binding E3 ubiquitin-protein ligase that interacts with coactivator-associated arginine methyltransferase 1 (CARM1) and acts as a transcriptional coactivator of estrogen receptor (ER) alpha. It is also a histone H2A ubiquitin ligase that catalyzes monoubiquitination of H2A at lysine 119, functioning as a combinatoric component of the repression machinery required for repressing a specific chemokine gene expression program, critically modulating migratory responses to Toll-like receptors (TLR) activation. DZIP3 contains a C3H2C3-type RING-H2 finger at the C-terminus.


Pssm-ID: 319374 [Multi-domain]  Cd Length: 43  Bit Score: 35.39  E-value: 2.34e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 6093894  363 CGMCGESIGEKNnqLQALPCSHFFHLKCLQT--NGTRGCPNCR 403
Cdd:cd16460   3 CVICHENLSPEN--LSVLPCAHKFHSQCIRPwlMQQRTCPTCR 43
RING-H2_BRAP2 cd16457
RING finger, H2 subclass, found in BRCA1-associated protein (BRAP2) and similar proteins; ...
363-403 2.43e-03

RING finger, H2 subclass, found in BRCA1-associated protein (BRAP2) and similar proteins; BRAP2, also known as impedes mitogenic signal propagation (IMP), RING finger protein 52, or renal carcinoma antigen NY-REN-63, is a novel cytoplasmic protein interacting with the two functional nuclear localization signal (NLS) motifs of BRCA1, a nuclear protein linked to breast cancer. It also binds to the SV40 large T antigen NLS motif and the bipartite NLS motif found in mitosin. BRAP2 serves as a cytoplasmic retention protein and plays a role in in the regulation of nuclear protein transport. It contains an N-terminal RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), followed by a C3H2C3-type RING-H2 finger and a UBP-type zinc finger.


Pssm-ID: 319371 [Multi-domain]  Cd Length: 44  Bit Score: 35.33  E-value: 2.43e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 6093894  363 CGMCGESIGEKNNQLQALPCSHFFHLKCLQTNGTRGCPNCR 403
Cdd:cd16457   3 CPVCLERMDESVSGILTILCNHSFHCDCLKRWGDSTCPVCR 43
RING1-H2_RNF32 cd16677
RING finger 1, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; ...
363-403 2.68e-03

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: 35.38  E-value: 2.68e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 6093894  363 CGMCGESIGEKNNQLqaLPCSHFFHLKCLQT----NGTRGCPNCR 403
Cdd:cd16677   2 CVICKEDFGLQQQVL--LSCSHVFHRACLESferfSGKKTCPMCR 44
RING-H2_PA-TM-RING cd16454
RING finger, H2 subclass, found in the PA-TM-RING ubiquitin ligase family; The PA-TM-RING ...
363-403 4.58e-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: 34.58  E-value: 4.58e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 6093894  363 CGMCGESIGEkNNQLQALPCSHFFHLKC----LQTNGTrgCPNCR 403
Cdd:cd16454   2 CAICLEEFED-GEEVRVLPCNHLFHSNCidpwLEQHAT--CPLCR 43
zf-RING_2 pfam13639
Ring finger domain;
363-403 5.20e-03

Ring finger domain;


Pssm-ID: 338865 [Multi-domain]  Cd Length: 44  Bit Score: 34.68  E-value: 5.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 6093894    363 CGMCGESIgEKNNQLQALPCSHFFHLKC----LQTNGTrgCPNCR 403
Cdd:pfam13639   3 CPICLEEF-EEGDKVVILPCGHHFHRECldkwLRSSNT--CPLCR 44
RING-H2_RNF38_like cd16472
RING finger, H2 subclass, found in RING finger proteins RNF38, RNF44, and similar proteins; ...
372-403 6.23e-03

RING finger, H2 subclass, found in RING finger proteins RNF38, RNF44, and similar proteins; The family includes RING finger proteins RNF38, RNF44, and similar proteins. RNF38 is a nuclear E3 ubiquitin protein ligase that plays a role in regulating p53. RNF44 is an uncharacterized RING finger protein that shows high sequence similarity with RNF38. Both RNF38 and RNF44 contain a coiled-coil motif, a KIL motif (Lys-X2-Ile/Leu-X2-Ile/Leu, X can be any amino acid), and a C3H2C3-type RING-H2 finger. In addition, RNF38 harbors two potential nuclear localization signals.


Pssm-ID: 319386 [Multi-domain]  Cd Length: 45  Bit Score: 34.38  E-value: 6.23e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 6093894  372 EKNNQLQALPCSHFFHLKC----LQTNgtRGCPNCR 403
Cdd:cd16472  12 EARQLLRVLPCSHEFHAKCvdkwLKTN--RTCPICR 45
RING-H2_PJA1_2 cd16465
RING finger, H2 subclass, found in protein E3 ubiquitin-protein ligase Praja-1, Praja-2, and ...
363-404 7.04e-03

RING finger, H2 subclass, found in protein E3 ubiquitin-protein ligase Praja-1, Praja-2, and similar proteins; The family includes two highly similar E3 ubiquitin-protein ligases Praja-1 and Praja-2. Praja-1, also known as RING finger protein 70, is a RING-H2 finger ubiquitin ligase encoded by gene PJA1, a novel human X chromosome gene abundantly expressed in brain. It has been implicated in bone and liver development, as well as memory formation and X-linked mental retardation (MRX). Praja-1 interacts with and activates the ubiquitin-conjugating enzyme UbcH5B, and shows E2-dependent E3 ubiquitin ligase activity. It is a 3-deazaneplanocin A (DZNep)-induced ubiquitin ligase that directly ubiquitinates individual polycomb repressive complex 2 (PRC2) subunits in a cell free system, which leads to their proteasomal degradation. It also plays an important role in neuronal plasticity, which is the basis for learning and memory. Moreover, Praja-1 ubiquitinates embryonic liver fodrin (ELF) and Smad3, but not Smad4, in a transforming growth factor-beta (TGF-beta)-dependent manner. It controls ELF abundance through ubiquitin-mediated degradation, and further regulates TGF-beta signaling, which plays a key role in the suppression of gastric carcinoma. Furthermore, Praja-1 regulates the transcription function of the homeodomain protein Dlx5 by controlling the stability of the Dlx/Msx-interacting MAGE/Necdin family protein, Dlxin-1, via an ubiquitin-dependent degradation pathway. Praja-2, also known as RING finger protein 131, or NEURODAP1, or KIAA0438, is an E2-dependent E3 ubiquitin ligase that interacts with and activates the ubiquitin-conjugating enzyme UbcH5B. It functions as an A-kinase anchoring protein (AKAP)-like E3 ubiquitin ligase that plays a critical role in controlling cyclic AMP (cAMP) dependent PKA activity and pro-survival signaling, and further promotes cell proliferation and growth. Praja-2 is also involved in protein sorting at the postsynaptic density region of axosomatic synapses and possibly plays a role in synaptic communication and plasticity. Moreover, Praja-2, together with the AMPK-related kinase SIK2 and the CDK5 activator CDK5R1/p35, forms a SIK2-p35-PJA2 complex that plays an essential role for glucose homeostasis in pancreatic beta cell functional compensation. Furthermore, Praja-2 ubiquitylates and degrades Mob, a core component of NDR/LATS kinase and a positive regulator of the tumor-suppressor Hippo signaling. Both Praja-1 and Praja-2 contain a potential nuclear localization signal (NLS) and a C-terminal C3H2C3-type RING-H2 motif.


Pssm-ID: 319379 [Multi-domain]  Cd Length: 46  Bit Score: 34.28  E-value: 7.04e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 6093894  363 CGMCGESIgEKNNQLQALPCSHFFHLKC----LQTNGTrgCPNCRR 404
Cdd:cd16465   2 CPICCCEY-VKDEIATELPCHHLFHKLCitawLQKSGT--CPVCRH 44
RING-H2_synoviolin cd16479
RING finger, H2 subclass, found in synoviolin and similar proteins; Synoviolin, also known as ...
380-403 8.22e-03

RING finger, H2 subclass, found in synoviolin and similar proteins; Synoviolin, also known as synovial apoptosis inhibitor 1 (Syvn1), Hrd1, or Der3, is an endoplasmic reticulum (ER)-anchoring E3 ubiquitin ligase that functions as a suppressor of ER stress-induced apoptosis and plays a role in homeostasis maintenance. It also targets tumor suppressor gene p53 for proteasomal degradation, suggesting the crosstalk between ER associated degradation (ERAD) and p53 mediated apoptotic pathway under ER stress. Moreover, Synoviolin controls body weight and mitochondrial biogenesis through negative regulation of the thermogenic coactivator peroxisome proliferator-activated receptor coactivator (PGC)-1beta. It upregulates amyloid beta production by targeting a negative regulator of gamma-secretase, Retention in endoplasmic reticulum 1 (Rer1), for degradation. It is also involved in the degradation of endogenous immature nicastrin, and affects amyloid beta-protein generation. Moreover, Synoviolin is highly expressed in rheumatoid synovial cells and may be involved in the pathogenesis of rheumatoid arthritis (RA). It functions as an anti-apoptotic factor that is responsible for the outgrowth of synovial cells during the development of RA. It promotes inositol-requiring enzyme 1 (IRE1) ubiquitination and degradation in synovial fibroblasts with collagen-induced arthritis. Furthermore, the upregulation of Synoviolin may represent a protective response against neurodegeneration in Parkinson"s disease (PD). In addition, Synoviolin is involved in liver fibrogenesis. Synoviolin contains a C3H2C2-type RING-H2 finger.


Pssm-ID: 319393 [Multi-domain]  Cd Length: 43  Bit Score: 33.81  E-value: 8.22e-03
                        10        20
                ....*....|....*....|....*.
gi 6093894  380 LPCSHFFHLKCLQTNGTRG--CPNCR 403
Cdd:cd16479  18 LPCGHIFHLSCLRSWLQRQqtCPTCR 43
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
141-225 8.38e-03

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 38.14  E-value: 8.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894    141 KALECFEKALRYAHNNDDKMlecrvcCSLGNFYAQIKDYEKALFFPCKAAELVNDYGAgwslkyramSQYHMAVAYRKLG 220
Cdd:TIGR02917 821 RALEYAERALKLAPNIPAIL------DTLGWLLVEKGEADRALPLLRKAVNIAPEAAA---------IRYHLALALLATG 885

                  ....*
gi 6093894    221 RLADA 225
Cdd:TIGR02917 886 RKAEA 890
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
144-236 8.86e-03

BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It is known to have a role in endosomal targeting. ESCRT-III subunit Snf7 binds to a conserved hydrophobic patch in the BRO1 domain that is required for protein complex formation and for the protein-sorting function of BRO1.


Pssm-ID: 335214  Cd Length: 374  Bit Score: 37.93  E-value: 8.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6093894    144 ECF-EKALRyahnndDKM---LECRVCCSLGNFYAQIKDYekalffpCKAAELVNDYGAGW----SLK---YRAMSQYHM 212
Cdd:pfam03097 182 ECFwEKAIK------DNKkdsLIAKLAAQVSELYEEALEA-------LKKPVLSDLFDKEWishvQAKahhFKALAQYRQ 248
                          90       100       110
                  ....*....|....*....|....*....|.
gi 6093894    213 AVAY---RKLG----RLADAMDCCEESMKIA 236
Cdd:pfam03097 249 ALADeeaKKYGeeiaRLQLALSLLKEALKSK 279
 
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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