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Conserved domains on  [gi|145559521|sp|Q13702|]
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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; AltName: Full=RING finger protein 205

Protein Classification

tetratricopeptide repeat protein( domain architecture ID 11721572)

tetratricopeptide repeat (TPR) protein may adopt a right-handed helical structure with an amphipathic channel and may function as an interaction scaffold in the formation of multi-protein complexes

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 3.81e-34

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: 451671 [Multi-domain]  Cd Length: 80  Bit Score: 122.05  E-value: 3.81e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521    1 MGQDQTKQQIEKGLQLYQSNQTEKALQVWTKVLEKSSDLMGRFRVLGCLVTAHSEMGRYKEMLKFAVVQIDTARELEDAD 80
Cdd:pfam10579   1 LGQDIAKQKIEKGLKLYEQNDQEAALRTWMKALKGTCDPEDCFQLLGCLIQAHMDMGKFKEAIEFGHAQIGIAEELDDPD 80
RING-H2_Rapsyn cd16478
RING finger, H2 subclass, found in 43 kDa receptor-associated protein of the synapse (Rapsyn) ...
 360-404 1.29e-22

RING finger, H2 subclass, found in 43 kDa receptor-associated protein of the synapse (Rapsyn) and similar proteins; Rapsyn, also known as acetylcholine receptor (AChR)-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 AChR in the postsynaptic membrane of the motor endplate. 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 AChR 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: 438141 [Multi-domain]  Cd Length: 48  Bit Score: 89.83  E-value: 1.29e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 145559521 360 ELYCGLCGESIGEKNSRLQALPCSHIFHLRCLQNN---GTRSCPNCRR 404
Cdd:cd16478    1 ELFCGMCGESIGEKNEQLQALPCSHIFHLKCLQTNlrgGTRGCPNCRR 48
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
84-328 2.15e-10

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


:

Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 60.79  E-value: 2.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521  84 ESYLNLARSNEKLCEFHKTISYCKTCLGLPGTRAGAQLGgqvslsMGNAFLGLSVFQKALESFEKALRYAHNNDDAMLec 163
Cdd:COG0457    9 EAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYN------LGLAYLRLGRYEEALADYEQALELDPDDAEALN-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521 164 rvccSLGSFYAQVKDYEKALFFPCKAAELVNNYGKGWslkyramsqYHMAVAYRLLGRLGSAMECCEESMKIAlqhgdrP 243
Cdd:COG0457   81 ----NLGLALQALGRYEEALEDYDKALELDPDDAEAL---------YNLGLALLELGRYDEAIEAYERALELD------P 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521 244 LQALCLLCFADIHRSRGDLETAFPRYDSAMSIMTEIGNRLGQVQALLGVAKCWVARKALDKALDAIERAQDLAEEVGNKL 323
Cdd:COG0457  142 DDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAE 221


                 ....*
gi 145559521 324 SQLKL 328
Cdd:COG0457  222 LLLLA 226
 
Name Accession Description Interval E-value
Rapsyn_N pfam10579
Rapsyn N-terminal myristoylation and linker region; Neuromuscular junction formation relies ...
 1-80 3.81e-34

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: 431369 [Multi-domain]  Cd Length: 80  Bit Score: 122.05  E-value: 3.81e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521    1 MGQDQTKQQIEKGLQLYQSNQTEKALQVWTKVLEKSSDLMGRFRVLGCLVTAHSEMGRYKEMLKFAVVQIDTARELEDAD 80
Cdd:pfam10579   1 LGQDIAKQKIEKGLKLYEQNDQEAALRTWMKALKGTCDPEDCFQLLGCLIQAHMDMGKFKEAIEFGHAQIGIAEELDDPD 80
RING-H2_Rapsyn cd16478
RING finger, H2 subclass, found in 43 kDa receptor-associated protein of the synapse (Rapsyn) ...
 360-404 1.29e-22

RING finger, H2 subclass, found in 43 kDa receptor-associated protein of the synapse (Rapsyn) and similar proteins; Rapsyn, also known as acetylcholine receptor (AChR)-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 AChR in the postsynaptic membrane of the motor endplate. 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 AChR 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: 438141 [Multi-domain]  Cd Length: 48  Bit Score: 89.83  E-value: 1.29e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 145559521 360 ELYCGLCGESIGEKNSRLQALPCSHIFHLRCLQNN---GTRSCPNCRR 404
Cdd:cd16478    1 ELFCGMCGESIGEKNEQLQALPCSHIFHLKCLQTNlrgGTRGCPNCRR 48
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
84-328 2.15e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 60.79  E-value: 2.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521  84 ESYLNLARSNEKLCEFHKTISYCKTCLGLPGTRAGAQLGgqvslsMGNAFLGLSVFQKALESFEKALRYAHNNDDAMLec 163
Cdd:COG0457    9 EAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYN------LGLAYLRLGRYEEALADYEQALELDPDDAEALN-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521 164 rvccSLGSFYAQVKDYEKALFFPCKAAELVNNYGKGWslkyramsqYHMAVAYRLLGRLGSAMECCEESMKIAlqhgdrP 243
Cdd:COG0457   81 ----NLGLALQALGRYEEALEDYDKALELDPDDAEAL---------YNLGLALLELGRYDEAIEAYERALELD------P 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521 244 LQALCLLCFADIHRSRGDLETAFPRYDSAMSIMTEIGNRLGQVQALLGVAKCWVARKALDKALDAIERAQDLAEEVGNKL 323
Cdd:COG0457  142 DDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAE 221


                 ....*
gi 145559521 324 SQLKL 328
Cdd:COG0457  222 LLLLA 226
TPR_12 pfam13424
Tetratricopeptide repeat;
204-278 1.84e-05

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 42.37  E-value: 1.84e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145559521  204 YRAMSQYHMAVAYRLLGRLGSAMECCEESMKIA--LQHGDRPLQALCLLCFADIHRSRGDLETAFPRYDSAMSIMTE 278
Cdd:pfam13424   1 DVATALNNLAAVLRRLGRYDEALELLEKALEIArrLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
 363-403 1.07e-04

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


Pssm-ID: 227827 [Multi-domain]  Cd Length: 374  Bit Score: 44.22  E-value: 1.07e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 145559521 363 CGLCGESIgEKNSRLQALPCSHIFHLRCLQN--NGTR-SCPNCR 403
Cdd:COG5540  326 CAICMSNF-IKNDRLRVLPCDHRFHVGCVDKwlLGYSnKCPVCR 368
zf-RING_2 pfam13639
Ring finger domain;
363-403 1.08e-04

Ring finger domain;


Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 39.31  E-value: 1.08e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 145559521  363 CGLCGESIgEKNSRLQALPCSHIFHLRCLQN--NGTRSCPNCR 403
Cdd:pfam13639   3 CPICLEEF-EEGDKVVVLPCGHHFHRECLDKwlRSSNTCPLCR 44
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 5-156 3.00e-04

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 40.56  E-value: 3.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521   5 QTKQQIEKGLQLYQSNQTEKALQVWTKVLEKSSDLMGRFRVLGclvTAHSEMGRYKEmlkfAVVQIDTARELEDADFllE 84
Cdd:COG4783    3 CAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLG---EILLQLGDLDE----AIVLLHEALELDPDEP--E 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145559521  85 SYLNLARSNEKLCEFHKTISYCKTCLGLPGTRAGAQLGgqvslsMGNAFLGLSVFQKALESFEKALRYAHNN 156
Cdd:COG4783   74 ARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLR------LARAYRALGRPDEAIAALEKALELDPDD 139
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 62-291 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: 40.45  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521   62 MLKFAVVQIDTARELEDADFL----------LESYLNLARSNEKLCEFHKTISYCKTCLglpgtrAGAQLGGQVSLSMGN 131
Cdd:TIGR02917 536 ILALAGLYLRTGNEEEAVAWLekaaelnpqeIEPALALAQYYLGKGQLKKALAILNEAA------DAAPDSPEAWLMLGR 609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521  132 AFLGLSVFQKALESFEKALRYAHNNDDAMLEcrvccsLGSFYAQVKDYEKALffpckaaelvnnygkgWSLKyRAMSQY- 210
Cdd:TIGR02917 610 AQLAAGDLNKAVSSFKKLLALQPDSALALLL------LADAYAVMKNYAKAI----------------TSLK-RALELKp 666

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521  211 HMAVAYRLLGRLGSAMECCEESMKIALQ-HGDRPLQALCLLCFADIHRSRGDLETAFPRYDSAMSIMTEIGNRLGQVQAL 289
Cdd:TIGR02917 667 DNTEAQIGLAQLLLAAKRTESAKKIAKSlQKQHPKAALGFELEGDLYLRQKDYPAAIQAYRKALKRAPSSQNAIKLHRAL 746


                  ..
gi 145559521  290 LG 291
Cdd:TIGR02917 747 LA 748
 
Name Accession Description Interval E-value
Rapsyn_N pfam10579
Rapsyn N-terminal myristoylation and linker region; Neuromuscular junction formation relies ...
 1-80 3.81e-34

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: 431369 [Multi-domain]  Cd Length: 80  Bit Score: 122.05  E-value: 3.81e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521    1 MGQDQTKQQIEKGLQLYQSNQTEKALQVWTKVLEKSSDLMGRFRVLGCLVTAHSEMGRYKEMLKFAVVQIDTARELEDAD 80
Cdd:pfam10579   1 LGQDIAKQKIEKGLKLYEQNDQEAALRTWMKALKGTCDPEDCFQLLGCLIQAHMDMGKFKEAIEFGHAQIGIAEELDDPD 80
RING-H2_Rapsyn cd16478
RING finger, H2 subclass, found in 43 kDa receptor-associated protein of the synapse (Rapsyn) ...
 360-404 1.29e-22

RING finger, H2 subclass, found in 43 kDa receptor-associated protein of the synapse (Rapsyn) and similar proteins; Rapsyn, also known as acetylcholine receptor (AChR)-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 AChR in the postsynaptic membrane of the motor endplate. 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 AChR 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: 438141 [Multi-domain]  Cd Length: 48  Bit Score: 89.83  E-value: 1.29e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 145559521 360 ELYCGLCGESIGEKNSRLQALPCSHIFHLRCLQNN---GTRSCPNCRR 404
Cdd:cd16478    1 ELFCGMCGESIGEKNEQLQALPCSHIFHLKCLQTNlrgGTRGCPNCRR 48
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
84-328 2.15e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 60.79  E-value: 2.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521  84 ESYLNLARSNEKLCEFHKTISYCKTCLGLPGTRAGAQLGgqvslsMGNAFLGLSVFQKALESFEKALRYAHNNDDAMLec 163
Cdd:COG0457    9 EAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYN------LGLAYLRLGRYEEALADYEQALELDPDDAEALN-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521 164 rvccSLGSFYAQVKDYEKALFFPCKAAELVNNYGKGWslkyramsqYHMAVAYRLLGRLGSAMECCEESMKIAlqhgdrP 243
Cdd:COG0457   81 ----NLGLALQALGRYEEALEDYDKALELDPDDAEAL---------YNLGLALLELGRYDEAIEAYERALELD------P 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521 244 LQALCLLCFADIHRSRGDLETAFPRYDSAMSIMTEIGNRLGQVQALLGVAKCWVARKALDKALDAIERAQDLAEEVGNKL 323
Cdd:COG0457  142 DDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAE 221


                 ....*
gi 145559521 324 SQLKL 328
Cdd:COG0457  222 LLLLA 226
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 9-329 2.28e-10

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 60.90  E-value: 2.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521   9 QIEKGLQLYQSNQTEKALQVWTKVLEKSSDlmgrfrvlgcLVTAHSEMGRYKEMLKfavvqidtarELEDAdflLESYLN 88
Cdd:COG2956   11 WYFKGLNYLLNGQPDKAIDLLEEALELDPE----------TVEAHLALGNLYRRRG----------EYDRA---IRIHQK 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521  89 LARSNEKlcefhktisycktclglpgtRAGAQLG-GQVSLSMGNaflglsvFQKALESFEKALRYAHNNDDAMLEcrvcc 167
Cdd:COG2956   68 LLERDPD--------------------RAEALLElAQDYLKAGL-------LDRAEELLEKLLELDPDDAEALRL----- 115

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521 168 sLGSFYAQVKDYEKALFFpckAAELVNNYGKgwslkyRAMSQYHMAVAYRLLGRLGSAMECCEEsmkiALQHGDRPLQAL 247
Cdd:COG2956  116 -LAEIYEQEGDWEKAIEV---LERLLKLGPE------NAHAYCELAELYLEQGDYDEAIEALEK----ALKLDPDCARAL 181

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521 248 CLLcfADIHRSRGDLETAFPRYDSAMSIMTEignrlgQVQALLGVAKCWVARKALDKALDAIERAQDLAEEVGNKLSQLK 327
Cdd:COG2956  182 LLL--AELYLEQGDYEEAIAALERALEQDPD------YLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALAD 253


                 ..
gi 145559521 328 LH 329
Cdd:COG2956  254 LL 255
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
52-307 4.90e-09

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 56.55  E-value: 4.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521  52 AHSEMGRYKEmlkfAVVQIDTARELEDADFllESYLNLARSNEKLCEFHKTISYCKTCLGLPGTRAGAQLggqvslSMGN 131
Cdd:COG0457   17 AYRRLGRYEE----AIEDYEKALELDPDDA--EALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALN------NLGL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521 132 AFLGLSVFQKALESFEKALRYAHNNDDAMLecrvccSLGSFYAQVKDYEKALFFPCKAAELVNNYgkgwslkyrAMSQYH 211
Cdd:COG0457   85 ALQALGRYEEALEDYDKALELDPDDAEALY------NLGLALLELGRYDEAIEAYERALELDPDD---------ADALYN 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521 212 MAVAYRLLGRLGSAMECCEESMKIALQHGDRPLQALCLLCFADIHRSRGDLETAFPRYDSAMSIMTEIGNRLGQVQALLG 291
Cdd:COG0457  150 LGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALAL 229

                        250
                 ....*....|....*.
gi 145559521 292 VAKCWVARKALDKALD 307
Cdd:COG0457  230 LLALRLAALALYQYRA 245
COG3899 COG3899
Predicted ATPase [General function prediction only];
142-318 2.81e-07

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 52.94  E-value: 2.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521  142 ALESFEKALRYAHNNDDAMLECRVCCSLGSFYAQVKDYEKA--LFFPCKAAELVNNYGKGWSLKYRAMSQYHMAVAYRLL 219
Cdd:COG3899   724 ALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAeaLLERALAARALAALAALRHGNPPASARAYANLGLLLL 803

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521  220 GRLGSAMECCEESMKIALQHGDRPLQALCLLCFADIHRSRGDLETAFPRYDSAMSIMTEIGNRLGQVQALLGVAKCWVAR 299
Cdd:COG3899   804 GDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAA 883

                         170
                  ....*....|....*....
gi 145559521  300 KALDKALDAIERAQDLAEE 318
Cdd:COG3899   884 AALAAAAAAAARLLAAAAA 902
RING-H2 cd16448
H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type ...
 363-403 5.06e-07

H2 subclass of RING (RING-H2) fingers and its variants; The 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 into 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 patterns while some lack a single Cys or His residue at typical Zn ligand positions (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 the 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: 438112 [Multi-domain]  Cd Length: 43  Bit Score: 45.86  E-value: 5.06e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 145559521 363 CGLCGESIGEKnSRLQALPCSHIFHLRCLQN---NGTRSCPNCR 403
Cdd:cd16448    1 CVICLEEFEEG-DVVRLLPCGHVFHLACILRwleSGNNTCPLCR 43
RING-H2_RNF32_rpt1 cd16677
first RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; ...
 363-405 5.77e-06

first RING finger, 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, proteins with double RING-H2 fingers may act as scaffolds for binding several proteins that function in the same pathway. This model corresponds to the first RING-H2 finger.


Pssm-ID: 438339 [Multi-domain]  Cd Length: 49  Bit Score: 43.06  E-value: 5.77e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 145559521 363 CGLCGESIGEKNSRLqaLPCSHIFHLRCLQN----NGTRSCPNCRRS 405
Cdd:cd16677    2 CPICLEDFGLQQQVL--LSCSHVFHRACLESferfSGKKTCPMCRKE 46
TPR_12 pfam13424
Tetratricopeptide repeat;
204-278 1.84e-05

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 42.37  E-value: 1.84e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145559521  204 YRAMSQYHMAVAYRLLGRLGSAMECCEESMKIA--LQHGDRPLQALCLLCFADIHRSRGDLETAFPRYDSAMSIMTE 278
Cdd:pfam13424   1 DVATALNNLAAVLRRLGRYDEALELLEKALEIArrLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
139-236 2.46e-05

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 42.85  E-value: 2.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521 139 FQKALESFEKALRYAHNNDDAMLecrvccSLGSFYAQVKDYEKALFFPcKAAELVNNYgkgwslkyrAMSQYHMAVAYRL 218
Cdd:COG3063    8 LEEAEEYYEKALELDPDNADALN------NLGLLLLEQGRYDEAIALE-KALKLDPNN---------AEALLNLAELLLE 71

                         90
                 ....*....|....*...
gi 145559521 219 LGRLGSAMECCEESMKIA 236
Cdd:COG3063   72 LGDYDEALAYLERALELD 89
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 129-273 3.35e-05

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 46.14  E-value: 3.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521 129 MGNAFLGLSVFQKALESFEKALRYAHNNDDAmlecrvCCSLGSFYAQVKDYEKALFFPCKAAELVNNYgkgwslkyrAMS 208
Cdd:COG3914  118 LGNLLLALGRLEEALAALRRALALNPDFAEA------YLNLGEALRRLGRLEEAIAALRRALELDPDN---------AEA 182

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145559521 209 QYHMAVAYRLLGRLGSAMECCEESMKIALQHgdrpLQALCLLCFADIHRSRGDLETAFPRYDSAM 273
Cdd:COG3914  183 LNNLGNALQDLGRLEEAIAAYRRALELDPDN----ADAHSNLLFALRQACDWEVYDRFEELLAAL 243
RING-HC_MKRN cd16521
RING finger, HC subclass, found in the makorin (MKRN) proteins; The MKRN protein subfamily ...
 363-403 4.16e-05

RING finger, HC subclass, found in the makorin (MKRN) proteins; The MKRN protein subfamily includes ribonucleoproteins that are characterized by a variety of zinc-finger motifs, including typical arrays of one to four C3H1-type zinc fingers and a C3HC4-type RING-HC finger. Another motif rich in Cys and His residues (CH), with so far unknown function, is also generally present in MKRN proteins. MKRN proteins may have E3 ubiquitin ligase activity.


Pssm-ID: 438184 [Multi-domain]  Cd Length: 53  Bit Score: 40.72  E-value: 4.16e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 145559521 363 CGLCGESIGEKNSRLQALP-CSHIFHLRCL---------QNNGTRSCPNCR 403
Cdd:cd16521    3 CGICMEVVLEKERRFGILSnCNHVFCLECIrewrsskdfENSIVRSCPICR 53
RING-H2_synoviolin cd16479
RING finger, H2 subclass, found in synoviolin and similar proteins; Synoviolin, also known as ...
 363-403 7.07e-05

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 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: 438142 [Multi-domain]  Cd Length: 43  Bit Score: 40.03  E-value: 7.07e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 145559521 363 CGLCGESIGEKNSRLqalPCSHIFHLRCLQNNGTR--SCPNCR 403
Cdd:cd16479    4 CIICREEMTVGAKKL---PCGHIFHLSCLRSWLQRqqTCPTCR 43
RING-H2_BRAP2 cd16457
RING finger, H2 subclass, found in BRCA1-associated protein (BRAP2) and similar proteins; ...
 363-403 1.03e-04

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 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: 438121 [Multi-domain]  Cd Length: 44  Bit Score: 39.58  E-value: 1.03e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 145559521 363 CGLCGESIGEKNSRLQALPCSHIFHLRCLQNNGTRSCPNCR 403
Cdd:cd16457    3 CPVCLERMDESVSGILTILCNHSFHCSCLSKWGDSSCPVCR 43
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
 363-403 1.07e-04

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


Pssm-ID: 227827 [Multi-domain]  Cd Length: 374  Bit Score: 44.22  E-value: 1.07e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 145559521 363 CGLCGESIgEKNSRLQALPCSHIFHLRCLQN--NGTR-SCPNCR 403
Cdd:COG5540  326 CAICMSNF-IKNDRLRVLPCDHRFHVGCVDKwlLGYSnKCPVCR 368
zf-RING_2 pfam13639
Ring finger domain;
363-403 1.08e-04

Ring finger domain;


Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 39.31  E-value: 1.08e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 145559521  363 CGLCGESIgEKNSRLQALPCSHIFHLRCLQN--NGTRSCPNCR 403
Cdd:pfam13639   3 CPICLEEF-EEGDKVVVLPCGHHFHRECLDKwlRSSNTCPLCR 44
HRD1 COG5243
HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein ...
 373-405 2.38e-04

HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227568 [Multi-domain]  Cd Length: 491  Bit Score: 43.04  E-value: 2.38e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 145559521 373 KNSRLQALPCSHIFHLRCLQNNGTRS--CPNCRRS 405
Cdd:COG5243  309 LDMTPKRLPCGHILHLHCLKNWLERQqtCPICRRP 343
RING-H2_RNF38-like cd16472
RING finger, H2 subclass, found in RING finger proteins RNF38, RNF44, and similar proteins; ...
 372-403 2.56e-04

RING finger, H2 subclass, found in RING finger proteins RNF38, RNF44, and similar proteins; This subfamily 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 to 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: 438135 [Multi-domain]  Cd Length: 46  Bit Score: 38.47  E-value: 2.56e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 145559521 372 EKNSRLQALPCSHIFHLRC----LQNNgtRSCPNCR 403
Cdd:cd16472   13 EKRQLLRVLPCSHEFHAKCidkwLKTN--RTCPICR 46
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
206-315 2.73e-04

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 42.30  E-value: 2.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521 206 AMSQYHMAVAYRLLGRLGSAMECCEESMKIALQHGdrplQALCLLcfADIHRSRGDLETAFPRYDSAMSImteignRLGQ 285
Cdd:COG0457    8 AEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDA----EALYNL--GLAYLRLGRYEEALADYEQALEL------DPDD 75

                         90       100       110
                 ....*....|....*....|....*....|
gi 145559521 286 VQALLGVAKCWVARKALDKALDAIERAQDL 315
Cdd:COG0457   76 AEALNNLGLALQALGRYEEALEDYDKALEL 105
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 5-156 3.00e-04

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 40.56  E-value: 3.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521   5 QTKQQIEKGLQLYQSNQTEKALQVWTKVLEKSSDLMGRFRVLGclvTAHSEMGRYKEmlkfAVVQIDTARELEDADFllE 84
Cdd:COG4783    3 CAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLG---EILLQLGDLDE----AIVLLHEALELDPDEP--E 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145559521  85 SYLNLARSNEKLCEFHKTISYCKTCLGLPGTRAGAQLGgqvslsMGNAFLGLSVFQKALESFEKALRYAHNN 156
Cdd:COG4783   74 ARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLR------LARAYRALGRPDEAIAALEKALELDPDD 139
RING-H2_RNF167 cd16797
RING finger, H2 subclass, found in RING finger protein 167 (RNF167) and similar proteins; ...
 363-404 3.10e-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 AMPA-type glutamate receptor subunit 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: 38.10  E-value: 3.10e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 145559521 363 CGLCGESIgEKNSRLQALPCSHIFHLRCLQ---NNGTRSCPNCRR 404
Cdd:cd16797    3 CAICLDEY-EEGDKLRVLPCSHAYHSKCVDpwlTQTKKTCPVCKQ 46
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 52-268 3.30e-04

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 43.06  E-value: 3.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521  52 AHSEMGRYKEmlkfAVVQIDTARELeDADFLlESYLNLARSNEKLCEFHKTISYCKTCLGLPGTRAGAQLggqvslSMGN 131
Cdd:COG3914   87 LLQALGRYEE----ALALYRRALAL-NPDNA-EALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYL------NLGE 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521 132 AFLGLSVFQKALESFEKALRYAHNNDDAMlecrvcCSLGSFYAQVKDYEKALFFPCKAAELVNNYGKGWSLKYRAMSQYH 211
Cdd:COG3914  155 ALRRLGRLEEAIAALRRALELDPDNAEAL------NNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALRQAC 228

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145559521 212 MAVAYRLLGRLGSAMECCEESMK----IALQHGDRPLQALCLLCFADIHRSRGDLETAFPR 268
Cdd:COG3914  229 DWEVYDRFEELLAALARGPSELSpfalLYLPDDDPAELLALARAWAQLVAAAAAPELPPPP 289
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 3.79e-04

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: 438118 [Multi-domain]  Cd Length: 43  Bit Score: 38.02  E-value: 3.79e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 145559521 363 CGLCGESIgEKNSRLQALPCSHIFHLRC----LQNNGTrsCPNCR 403
Cdd:cd16454    2 CAICLEEF-KEGEKVRVLPCNHLFHKDCidpwLEQHNT--CPLCR 43
RING-H2_DZIP3 cd16460
RING finger, H2 subclass, found in DAZ (deleted in azoospermia)-interacting protein 3 (DZIP3) ...
 363-403 5.94e-04

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 combinatorial 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: 438123 [Multi-domain]  Cd Length: 47  Bit Score: 37.52  E-value: 5.94e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 145559521 363 CGLCGESIGEKNsRLQALPCSHIFHLRCLQN--NGTRSCPNCR 403
Cdd:cd16460    3 CVICHEAFSDGD-RLLVLPCAHKFHTQCIGPwlDGQQTCPTCR 44
RING-H2_RNF12 cd16674
RING finger, H2 subclass, found in RING finger protein 12 (RNF12) and similar proteins; RNF12, ...
 363-410 8.59e-04

RING finger, H2 subclass, found in RING finger protein 12 (RNF12) and similar proteins; RNF12, also known as LIM domain-interacting RING finger protein or RING finger LIM domain-binding protein (R-LIM), is an E3 ubiquitin-protein ligase encoded by gene RLIM that is crucial for normal embryonic development in some species and for normal X inactivation in mice. It thus functions as a major sex-specific epigenetic regulator of female mouse nurturing tissues. RNF12 is widely expressed during embryogenesis, and mainly localizes to the cell nucleus, where it regulates the levels of many proteins, including CLIM, LMO, HDAC2, TRF1, SMAD7, and REX1, by proteasomal degradation. Its functional activity is regulated by phosphorylation-dependent nucleocytoplasmic shuttling. It is negatively regulated by pluripotency factors in embryonic stem cells. p53 represses its transcription through Sp1. RNF12 is the primary factor responsible for X chromosome inactivation (XCI) in female placental mammals. It is an indispensable factor in up-regulation of Xist transcription, thereby leading to initiation of random XCI. It also targets REX1, an inhibitor of XCI, for proteasomal degradation. RNF12 also acts as a co-regulator for a range of transcription factors, particularly those containing a LIM homeodomain, and modulates the formation of transcriptional multiprotein complexes. It is a negative regulator of Smad7, which in turn negatively regulates the signaling of type I receptors from the transforming growth factor beta (TGF-beta) superfamily. In addition, paternal RNF12 is a critical survival factor for milk-producing alveolar cells. RNF12 contains an nuclear localization signal (NLS) and a C3H2C3-type RING-H2 finger.


Pssm-ID: 438336 [Multi-domain]  Cd Length: 51  Bit Score: 37.01  E-value: 8.59e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 145559521 363 CGLCGESIGEKNsRLQALPCSHIFHLRC----LQNNGTrsCPNCRRSSMKPG 410
Cdd:cd16674    3 CSVCITEYTEGN-KLRKLPCSHEYHVHCidrwLSENST--CPICRRAVLASG 51
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 83-183 9.18e-04

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 39.22  E-value: 9.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521  83 LESYLNLARSNEKLCEFHKTISYCKTCLGLPGTRAGAQLGgqvslsMGNAFLGLSVFQKALESFEKALRYAHNNDDAMLE 162
Cdd:COG4235   17 AEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLD------LAEALLAAGDTEEAEELLERALALDPDNPEALYL 90

                         90       100
                 ....*....|....*....|.
gi 145559521 163 crvccsLGSFYAQVKDYEKAL 183
Cdd:COG4235   91 ------LGLAAFQQGDYAEAI 105
RING-H2_TRAIP cd16480
RING finger, H2 subclass, found in TRAF-interacting protein (TRAIP) and similar proteins; ...
 362-403 1.05e-03

RING finger, H2 subclass, found in TRAF-interacting protein (TRAIP) and similar proteins; TRAIP, also known as RING finger protein 206 (RNF206) or TRIP, is a ubiquitously expressed nucleolar E3 ubiquitin ligase important for cellular proliferation and differentiation. It is found near mitotic chromosomes and functions as a regulator of the spindle assembly checkpoint. TRAIP interacts with tumor necrosis factor (TNF)-receptor-associated factor (TRAF) proteins and inhibits TNF-alpha-mediated nuclear factor (NF)-kappaB activation. It also interacts with two tumor suppressors CYLD and spleen tyrosine kinase (Syk), and DNA polymerase eta, which facilitates translesional synthesis after DNA damage. TRAIP contains an N-terminal C3H2C2-type RING-H2 finger and an extended coiled-coil domain.


Pssm-ID: 438143 [Multi-domain]  Cd Length: 43  Bit Score: 36.64  E-value: 1.05e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 145559521 362 YCGLCGESIGekNSR-LQALPCSHIFHLRCLQN--NGTRSCPNCR 403
Cdd:cd16480    1 YCTICSDFFD--NSRdVAAIHCGHTFHYDCLLQwfDTSRTCPQCR 43
TPR_12 pfam13424
Tetratricopeptide repeat;
249-318 1.55e-03

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 36.98  E-value: 1.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145559521  249 LLCFADIHRSRGDLETAFPRYDSAMSIMTEI--GNRLGQVQALLGVAKCWVARKALDKALDAIERAQDLAEE 318
Cdd:pfam13424   6 LNNLAAVLRRLGRYDEALELLEKALEIARRLlgPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
RING-H2_RNF126-like cd16667
RING finger, H2 subclass, found in RING finger proteins RNF126, RNF115, and similar proteins; ...
 363-403 1.87e-03

RING finger, H2 subclass, found in RING finger proteins RNF126, RNF115, and similar proteins; This subfamily includes RING finger proteins RNF126, RNF115, and similar proteins. RNF126 is a Bag6-dependent E3 ubiquitin ligase that is involved in the mislocalized protein (MLP) pathway of quality control. It regulates the retrograde sorting of the cation-independent mannose 6-phosphate receptor (CI-MPR). RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation, and could be a novel therapeutic target in breast and prostate cancers. It is also able to ubiquitylate cytidine deaminase (AID), a poorly soluble protein that is essential for antibody diversification. 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; this inhibition increases the efficacy of metformin in breast cancer cells. It also functions as a cofactor 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. RNF115 and 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. Both of them contain an N-terminal BCA2 Zinc-finger domain (BZF), AKT-phosphorylation sites, and a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438329 [Multi-domain]  Cd Length: 43  Bit Score: 35.74  E-value: 1.87e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 145559521 363 CGLCGE--SIGEKnsrLQALPCSHIFHLRCL-----QNNgtrSCPNCR 403
Cdd:cd16667    2 CAVCKEdfEVGEE---VRQLPCKHLFHPDCIvpwleLHN---SCPVCR 43
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 205-318 1.97e-03

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 38.25  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521 205 RAMSQYHMAVAYRLLGRLGSAMECCEEsmkiALQHGDRPLQALCLLcfADIHRSRGDLETAFPRYDSAMSIMTEignrlg 284
Cdd:COG4783    3 CAEALYALAQALLLAGDYDEAEALLEK----ALELDPDNPEAFALL--GEILLQLGDLDEAIVLLHEALELDPD------ 70

                         90       100       110
                 ....*....|....*....|....*....|....
gi 145559521 285 QVQALLGVAKCWVARKALDKALDAIERAQDLAEE 318
Cdd:COG4783   71 EPEARLNLGLALLKAGDYDEALALLEKALKLDPE 104
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 62-291 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: 40.45  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521   62 MLKFAVVQIDTARELEDADFL----------LESYLNLARSNEKLCEFHKTISYCKTCLglpgtrAGAQLGGQVSLSMGN 131
Cdd:TIGR02917 536 ILALAGLYLRTGNEEEAVAWLekaaelnpqeIEPALALAQYYLGKGQLKKALAILNEAA------DAAPDSPEAWLMLGR 609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521  132 AFLGLSVFQKALESFEKALRYAHNNDDAMLEcrvccsLGSFYAQVKDYEKALffpckaaelvnnygkgWSLKyRAMSQY- 210
Cdd:TIGR02917 610 AQLAAGDLNKAVSSFKKLLALQPDSALALLL------LADAYAVMKNYAKAI----------------TSLK-RALELKp 666

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521  211 HMAVAYRLLGRLGSAMECCEESMKIALQ-HGDRPLQALCLLCFADIHRSRGDLETAFPRYDSAMSIMTEIGNRLGQVQAL 289
Cdd:TIGR02917 667 DNTEAQIGLAQLLLAAKRTESAKKIAKSlQKQHPKAALGFELEGDLYLRQKDYPAAIQAYRKALKRAPSSQNAIKLHRAL 746


                  ..
gi 145559521  290 LG 291
Cdd:TIGR02917 747 LA 748
RING-H2_RNF111 cd16681
RING finger, H2 subclass, found in RING finger protein 111 (RNF111) and similar proteins; ...
 357-403 2.24e-03

RING finger, H2 subclass, found in RING finger protein 111 (RNF111) and similar proteins; RNF111, also known as Arkadia, is a nuclear E3 ubiquitin-protein ligase that targets intracellular effectors and modulators of transforming growth factor beta (TGF-beta)/Nodal-related signaling for polyubiquitination and proteasome-dependent degradation. It acts as an amplifier of Nodal signals, and enhances the dorsalizing activity of limiting amounts of Xnr1, a Nodal homolog, and requires Nodal signaling for its function. The loss of RNF111 results in early embryonic lethality, with defects attributed to compromised Nodal signaling. RNF111 also regulates tumor metastasis by modulation of the TGF-beta pathway. Its ubiquitination can be modulated by the four and a half LIM-only protein 2 (FHL2) that activates TGF-beta signal transduction. Furthermore, RNF111 interacts with the clathrin-adaptor 2 (AP2) complex and regulates endocytosis of certain cell surface receptors, leading to modulation of epidermal growth factor (EGF) and possibly other signaling pathways. In addition, RNF111 has been identified as a small ubiquitin-like modifier (SUMO)-binding protein with clustered SUMO-interacting motifs (SIMs) that together form a SUMO-binding domain (SBD). It thus functions as a SUMO-targeted ubiquitin ligase (STUbL) that directly links nonproteolytic ubiquitylation and SUMOylation in the DNA damage response, as well as triggers degradation of signal-induced polysumoylated proteins, such as the promyelocytic leukemia protein (PML). The N-terminal half of RNF111 harbors three SIMs. Its C-terminal half show high sequence similarity with RING finger protein 165 (RNF165), where it contains two serine rich domains, two nuclear localization signals, an NRG-TIER domain, and a C-terminal C3H2C3-type RING-H2 finger that is required for polyubiqutination and proteasome-dependent degradation of phosphorylated forms of Smad2/3 and three major negative regulators of TGF-beta signaling, Smad7, SnoN and c-Ski.


Pssm-ID: 438343 [Multi-domain]  Cd Length: 61  Bit Score: 36.19  E-value: 2.24e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 145559521 357 EETELYCGLCgESIGEKNSRLQALPCSHIFHLRCLQN--NGTRSCPNCR 403
Cdd:cd16681    7 EDTEEKCTIC-LSILEEGEDVRRLPCMHLFHQVCVDQwlITNKKCPICR 54
RING-H2_AMFR cd16455
RING finger, H2 subclass, found in autocrine motility factor receptor (AMFR) and similar ...
 363-405 2.89e-03

RING finger, H2 subclass, found in autocrine motility factor receptor (AMFR) and similar proteins; AMFR, also known as AMF receptor, or RING finger protein 45, or ER-protein gp78, is an internalizing cell surface glycoprotein localized in both plasma membrane caveolae and the endoplasmic reticulum (ER). It is involved in the regulation of cellular adhesion, proliferation, motility and apoptosis, as well as in the process of learning and memory. AMFR also functions as a RING finger-dependent ubiquitin protein ligase (E3) implicated in the degradation from the ER. AMFR contains an N-terminal RING-H2 finger and a C-terminal ubiquitin-associated (UBA)-like CUE domain.


Pssm-ID: 438119 [Multi-domain]  Cd Length: 44  Bit Score: 35.50  E-value: 2.89e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 145559521 363 CGLCGESIgeknSRLQALPCSHIFHLRCLQN--NGTRSCPNCRRS 405
Cdd:cd16455    3 CAICWESM----QSARKLPCGHLFHNSCLRSwlEQDTSCPTCRMS 43
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 139-236 2.99e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 38.02  E-value: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521 139 FQKALESFEKALRYAHNNDDAMLecrvccSLGSFYAQVKDYEKALFFPCKAAELVNNYgkgwslkyrAMSQYHMAVAYRL 218
Cdd:COG5010   70 FEESLALLEQALQLDPNNPELYY------NLALLYSRSGDKDEAKEYYEKALALSPDN---------PNAYSNLAALLLS 134

                         90
                 ....*....|....*...
gi 145559521 219 LGRLGSAMECCEESMKIA 236
Cdd:COG5010  135 LGQDDEAKAALQRALGTS 152
RING-H2_TUL1-like cd23117
RING finger, H2 subclass, found in Saccharomyces cerevisiae transmembrane E3 ubiquitin-protein ...
 381-405 4.44e-03

RING finger, H2 subclass, found in Saccharomyces cerevisiae transmembrane E3 ubiquitin-protein ligase 1 (TUL1) and similar proteins; This subfamily includes Saccharomyces cerevisiae TUL1, Schizosaccharomyces pombe DSC E3 ubiquitin ligase complex subunit 1 (DSC1), and Arabidopsis thaliana protein FLYING SAUCER 2 (FLY2). TUL1 is the catalytic component of DSC E3 ubiquitin ligase complexes that tag proteins present in Golgi, endosome and vacuole membranes and function in protein homeostasis under non-stress conditions, and support a role in protein quality control. It mediates ubiquitination of vacuolar proteins such as CPS1, PPN1, PEP12 and other proteins containing exposed hydrophilic residues within their transmembrane domains, leading to their sorting into internal vesicles in late endosomes. TUL1 also targets the unpalmitoylated endosomal SNARE TLG1 to the multivesicular body (MVB) pathway. DSC1, also known as defective for SREBP cleavage protein 1, is the catalytic component of the DSC E3 ubiquitin ligase complex required for the sre1 transcriptional activator proteolytic cleavage to release the soluble transcription factor from the membrane in low oxygen or sterol conditions. FLY2 acts as an E3 ubiquitin-protein ligase that may be involved in xylem development. Members of this subfamily contain a C3H2C3-type RING-H2 finger.


Pssm-ID: 438479 [Multi-domain]  Cd Length: 59  Bit Score: 35.45  E-value: 4.44e-03
                         10        20
                 ....*....|....*....|....*..
gi 145559521 381 PCSHIFHLRCLQN--NGTRSCPNCRRS 405
Cdd:cd23117   30 PCNHIFHTNCLERwmDIKLECPTCRRP 56
RING-HC_EHV1-like cd23130
RING finger, HC subclass, found in Equid alphaherpesvirus 1 (Equine herpesvirus 1/EHV-1) ...
 362-404 4.51e-03

RING finger, HC subclass, found in Equid alphaherpesvirus 1 (Equine herpesvirus 1/EHV-1) regulatory protein and similar proteins; EHV-1 regulatory protein belongs to the Vmw110 (IPC0) protein family. It contains a typical C3HC4-type RING-HC finger and binds zinc stably.


Pssm-ID: 438492 [Multi-domain]  Cd Length: 51  Bit Score: 35.02  E-value: 4.51e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 145559521 362 YCGLCGEsigEKNSRLQALPCSHIFHLRCLQNNGTRS--CPNCRR 404
Cdd:cd23130    2 VCPICLD---DPEDEAITLPCLHQFCYTCILRWLQTSptCPLCKT 43
RING-H2_RHA1-like cd23121
RING finger, H2 subclass, found in Arabidopsis thaliana RING-H2 finger A1a (RHA1A), A1b (RHA1B) ...
 363-403 4.66e-03

RING finger, H2 subclass, found in Arabidopsis thaliana RING-H2 finger A1a (RHA1A), A1b (RHA1B) and similar proteins; This subfamily includes Arabidopsis thaliana RHA1A, RHA1B and XERICO. RHA1A is a probable E3 ubiquitin-protein ligase that may possess E3 ubiquitin ligase activity in vitro. RHA1B possesses E3 ubiquitin-protein ligase activity when associated with the E2 enzyme UBC8 in vitro. XERICO functions on abscisic acid homeostasis at post-translational level, probably through ubiquitin/proteasome-dependent substrate-specific degradation. Members of this subfamily contain a C3H2C3-type RING-H2 finger.


Pssm-ID: 438483 [Multi-domain]  Cd Length: 50  Bit Score: 35.15  E-value: 4.66e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 145559521 363 CGLCGESIGEKNSRLQALPCSHIFHLRCL-----QNNGTrsCPNCR 403
Cdd:cd23121    4 CAICLSDFNSDEKLRQLPKCGHIFHHHCLdrwirYNKIT--CPLCR 47
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 124-278 4.78e-03

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 37.09  E-value: 4.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521 124 QVSLSMGNAFLGLSVFQKALESFEKALRYAHNNDDAMlecrvcCSLGSFYAQVKDYEKALffpckaaelvNNYGKGWSL- 202
Cdd:COG4783    5 EALYALAQALLLAGDYDEAEALLEKALELDPDNPEAF------ALLGEILLQLGDLDEAI----------VLLHEALELd 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145559521 203 KYRAMSQYHMAVAYRLLGRLGSAMECCEESMKIALQHGDrplqALCLLcfADIHRSRGDLETAFPRYDSAMSIMTE 278
Cdd:COG4783   69 PDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPE----AYLRL--ARAYRALGRPDEAIAALEKALELDPD 138
RING-H2_RNF13 cd16796
RING finger, H2 subclass, found in RING finger protein 13 (RNF13) and similar proteins; RNF13 ...
 363-408 5.56e-03

RING finger, H2 subclass, found in RING finger protein 13 (RNF13) and similar proteins; 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. It functions as an important regulator of inositol-requiring transmembrane kinase/endonuclease IRE1alpha, mediating endoplasmic reticulum (ER) stress-induced apoptosis through the activation of the IRE1alpha-TRAF2-JNK signaling pathway. Moreover, RNF13 is involved in the regulation of the soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor (SNARE) complex via the ubiquitination of snapin, a SNAP25-interacting protein, which thereby controls synaptic function. In addition, RNF13 participates in regulating the function of satellite cells by modulating cytokine composition. RNF13 is evolutionarily conserved among many metazoans and contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.


Pssm-ID: 438450 [Multi-domain]  Cd Length: 59  Bit Score: 35.02  E-value: 5.56e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 145559521 363 CGLCGESIgEKNSRLQALPCSHIFHLRCLQ---NNGTRSCPNCRRSSMK 408
Cdd:cd16796   11 CAICLDEY-EEGDKLRILPCSHAYHCKCVDpwlTKTKKTCPVCKQKVVP 58
RING-H2_RNF103 cd16473
RING finger, H2 subclass, found in RING finger protein 103 (RNF103) and similar proteins; ...
 363-408 6.98e-03

RING finger, H2 subclass, found in RING finger protein 103 (RNF103) and similar proteins; RNF103, also known as KF-1 or zinc finger protein 103 homolog (Zfp-103), is an endoplasmic reticulum (ER)-resident E3 ubiquitin-protein ligase that is widely expressed in many different organs, including brain, heart, kidney, spleen, and lung. It is involved in the ER-associated degradation (ERAD) pathway by interacting with components of the ERAD pathway, including Derlin-1 and VCP. RNF103 contains several hydrophobic regions at its N-terminal and middle regions, as well as a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438136 [Multi-domain]  Cd Length: 55  Bit Score: 34.56  E-value: 6.98e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 145559521 363 CGLCGESIgEKNSRLQALPCSHIFHLRCLQ---NNGTRSCPNCRRSSMK 408
Cdd:cd16473    7 CAICLENY-QNGDLLRGLPCGHVFHQNCIDvwlERDNHCCPVCRWPVYK 54
TPR_MalT pfam17874
MalT-like TPR region; This entry contains a series of TPR repeats.
 212-324 7.07e-03

MalT-like TPR region; This entry contains a series of TPR repeats.


Pssm-ID: 436107 [Multi-domain]  Cd Length: 336  Bit Score: 38.06  E-value: 7.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521  212 MAVAYRLLGRLGSAMECCEESMKIALQHGDRPLQALCLLCFADIHRSRGDLETAFPRYDSAMSIMTEIGnrlGQVQALLG 291
Cdd:pfam17874  46 LGEAYLCLGDLDAALQAMREAEALARRADSPHVTLWALLQQGEILRAQGRLHQALETYQQALQLARDHG---LQHLPLHG 122

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 145559521  292 VAKCWVAR-----KALDKALDAIERAQDLAEEVGNKLS 324
Cdd:pfam17874 123 FLLVGLADllyewNDLEEAEQHAQQGIQLGRQWEPDAA 160
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 173-307 8.60e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 36.86  E-value: 8.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559521 173 YAQVKDYEKALFFPCKAAELVNNYGKGWSLKYRAMSQYHMAVAYRLLGRLGSAMECCEESMKIAlqhgdrPLQALCLLCF 252
Cdd:COG5010   21 RTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLD------PNNPELYYNL 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 145559521 253 ADIHRSRGDLETAFPRYDSAMSIM---TEIGNRLGQVQALLGVAKcwVARKALDKALD 307
Cdd:COG5010   95 ALLYSRSGDKDEAKEYYEKALALSpdnPNAYSNLAALLLSLGQDD--EAKAALQRALG 150
RING-H2_RNF126 cd16801
RING finger, H2 subclass, found in RING finger protein 126 (RNF126) and similar proteins; ...
 363-404 9.40e-03

RING finger, H2 subclass, found in RING finger protein 126 (RNF126) and similar proteins; RNF126 is a Bag6-dependent E3 ubiquitin ligase that is involved in the mislocalized protein (MLP) pathway of quality control. It regulates the retrograde sorting of the cation-independent mannose 6-phosphate receptor (CI-MPR). Moreover, RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation, and could be a novel therapeutic target in breast and prostate cancers. It is also able to ubiquitylate cytidine deaminase (AID), a poorly soluble protein that is essential for antibody diversification. In addition, RNF126 and the related protein, RNF115 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. RNF126 contains an N-terminal BCA2 Zinc-finger domain (BZF), the AKT-phosphorylation sites, and the C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438453 [Multi-domain]  Cd Length: 44  Bit Score: 34.19  E-value: 9.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 145559521 363 CGLCGE--SIGEKnsrLQALPCSHIFHLRC----LQNNGTrsCPNCRR 404
Cdd:cd16801    2 CPVCKEdyTVGEN---VRQLPCNHLFHNDCivpwLEQHDT--CPVCRK 44
RING-H2_RNF130 cd16803
RING finger, H2 subclass, found in RING finger protein 130 (RNF130) and similar proteins; ...
 362-408 9.86e-03

RING finger, H2 subclass, found in RING finger protein 130 (RNF130) and similar proteins; RNF130, also known as Goliath homolog (H-Goliath), is a paralog of RNF128, also known as gene related to anergy in lymphocytes protein (GRAIL). It is a transmembrane E3 ubiquitin-protein ligase expressed in leukocytes. It has a self-ubiquitination property, and controls the development of T cell clonal anergy by ubiquitination. RNF130 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.


Pssm-ID: 319717 [Multi-domain]  Cd Length: 49  Bit Score: 34.18  E-value: 9.86e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 145559521 362 YCGLCGESIgEKNSRLQALPCSHIFHLRCLQN--NGTRSCPNCRRSSMK 408
Cdd:cd16803    2 HCAVCIEGY-KQNDVVRILPCKHVFHKSCVDPwlNEHCTCPMCKLNILK 49
 
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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