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Conserved domains on  [gi|224967081|ref|NP_033049|]
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43 kDa receptor-associated protein of the synapse [Mus musculus]

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 2.59e-38

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: 132.72  E-value: 2.59e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967081    1 MGQDQTKQQIEKGLQLYQSNQTEKALQVWMKVLEKGSDLVGRFRVLGCLVTAHSEMGRYKEMLKFAVVQIDTARGLEDAD 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 3.49e-23

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


:

Pssm-ID: 319392 [Multi-domain]  Cd Length: 47  Bit Score: 91.34  E-value: 3.49e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 224967081 360 ELYCGLCGESIGERNSRLQALPCSHIFHLRCLQNN--GTRSCPNCRR 404
Cdd:cd16478    1 ELYCGMCGESIGEKNESLQALPCSHIFHLKCLQTNlnGTRGCPNCRR 47
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
9-239 1.41e-05

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


:

Pssm-ID: 223533 [Multi-domain]  Cd Length: 291  Bit Score: 46.38  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967081   9 QIEKGLQLYQSNQTEKALQVWMKVLEKGSDLvGRFRVLGCLVTAHSEMGRYKEMLK--FAVVQIDTARGLEDADFLLESY 86
Cdd:COG0457   62 LLLLALALLKLGRLEEALELLEKALELELLP-NLAEALLNLGLLLEALGKYEEALEllEKALALDPDPDLAEALLALGAL 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967081  87 LNLARSNEKLCEFHKTISYCKTCLGLpgtragaqlgGQVSLSMGNAFLGLSLFQKALESFEKALRYAHNNDDTMLEcrvc 166
Cdd:COG0457  141 YELGDYEEALELYEKALELDPELNEL----------AEALLALGALLEALGRYEEALELLEKALKLNPDDDAEALL---- 206
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224967081 167 cSLGSFYAQVKDYEKALFFPCKAAELVNDYgkgwslkyrAMSQYHMAVAYRLLGHLGSAMECCEESMKIALQH 239
Cdd:COG0457  207 -NLGLLYLKLGKYEEALEYYEKALELDPDN---------AEALYNLALLLLELGRYEEALEALEKALELDPDL 269
TPR_12 pfam13424
Tetratricopeptide repeat;
204-278 2.98e-04

Tetratricopeptide repeat;


:

Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 38.91  E-value: 2.98e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224967081  204 YRAMSQYHMAVAYRLLGHLGSAMECCEESMKIA--LQHGDRPLQALCLLCFADIHRSRGDLETAFPRYDSAMSIMTE 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 2.59e-38

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: 132.72  E-value: 2.59e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967081    1 MGQDQTKQQIEKGLQLYQSNQTEKALQVWMKVLEKGSDLVGRFRVLGCLVTAHSEMGRYKEMLKFAVVQIDTARGLEDAD 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 3.49e-23

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


Pssm-ID: 319392 [Multi-domain]  Cd Length: 47  Bit Score: 91.34  E-value: 3.49e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 224967081 360 ELYCGLCGESIGERNSRLQALPCSHIFHLRCLQNN--GTRSCPNCRR 404
Cdd:cd16478    1 ELYCGMCGESIGEKNESLQALPCSHIFHLKCLQTNlnGTRGCPNCRR 47
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
9-239 1.41e-05

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


Pssm-ID: 223533 [Multi-domain]  Cd Length: 291  Bit Score: 46.38  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967081   9 QIEKGLQLYQSNQTEKALQVWMKVLEKGSDLvGRFRVLGCLVTAHSEMGRYKEMLK--FAVVQIDTARGLEDADFLLESY 86
Cdd:COG0457   62 LLLLALALLKLGRLEEALELLEKALELELLP-NLAEALLNLGLLLEALGKYEEALEllEKALALDPDPDLAEALLALGAL 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967081  87 LNLARSNEKLCEFHKTISYCKTCLGLpgtragaqlgGQVSLSMGNAFLGLSLFQKALESFEKALRYAHNNDDTMLEcrvc 166
Cdd:COG0457  141 YELGDYEEALELYEKALELDPELNEL----------AEALLALGALLEALGRYEEALELLEKALKLNPDDDAEALL---- 206
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224967081 167 cSLGSFYAQVKDYEKALFFPCKAAELVNDYgkgwslkyrAMSQYHMAVAYRLLGHLGSAMECCEESMKIALQH 239
Cdd:COG0457  207 -NLGLLYLKLGKYEEALEYYEKALELDPDN---------AEALYNLALLLLELGRYEEALEALEKALELDPDL 269
zf-RING_2 pfam13639
Ring finger domain;
363-403 1.29e-04

Ring finger domain;


Pssm-ID: 338865 [Multi-domain]  Cd Length: 44  Bit Score: 38.91  E-value: 1.29e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 224967081  363 CGLCGESIgERNSRLQALPCSHIFHLRCLQN--NGTRSCPNCR 403
Cdd:pfam13639   3 CPICLEEF-EEGDKVVILPCGHHFHRECLDKwlRSSNTCPLCR 44
TPR_12 pfam13424
Tetratricopeptide repeat;
204-278 2.98e-04

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 38.91  E-value: 2.98e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224967081  204 YRAMSQYHMAVAYRLLGHLGSAMECCEESMKIA--LQHGDRPLQALCLLCFADIHRSRGDLETAFPRYDSAMSIMTE 278
Cdd:pfam13424   1 DVATALNNLAAVLRRLGRYDEALELLEKALEIArrLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
363-403 3.10e-04

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


Pssm-ID: 227827 [Multi-domain]  Cd Length: 374  Bit Score: 42.29  E-value: 3.10e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 224967081 363 CGLCGESIgERNSRLQALPCSHIFHLRCLQN--NGTR-SCPNCR 403
Cdd:COG5540  326 CAICMSNF-IKNDRLRVLPCDHRFHVGCVDKwlLGYSnKCPVCR 368
 
Name Accession Description Interval E-value
Rapsyn_N pfam10579
Rapsyn N-terminal myristoylation and linker region; Neuromuscular junction formation relies ...
1-80 2.59e-38

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: 132.72  E-value: 2.59e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967081    1 MGQDQTKQQIEKGLQLYQSNQTEKALQVWMKVLEKGSDLVGRFRVLGCLVTAHSEMGRYKEMLKFAVVQIDTARGLEDAD 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 3.49e-23

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


Pssm-ID: 319392 [Multi-domain]  Cd Length: 47  Bit Score: 91.34  E-value: 3.49e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 224967081 360 ELYCGLCGESIGERNSRLQALPCSHIFHLRCLQNN--GTRSCPNCRR 404
Cdd:cd16478    1 ELYCGMCGESIGEKNESLQALPCSHIFHLKCLQTNlnGTRGCPNCRR 47
RING-H2 cd16448
H2 subclass of RING (RING-H2) finger and its variants; RING finger is a specialized type of ...
363-403 1.45e-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: 47.45  E-value: 1.45e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 224967081 363 CGLCGESIGERNSRLQALPCSHIFHLRCLQN---NGTRSCPNCR 403
Cdd:cd16448    1 CAICLEEFEEGDCPVRLLPCGHVFHKSCIDKwleSGNRTCPLCR 44
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
9-239 1.41e-05

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


Pssm-ID: 223533 [Multi-domain]  Cd Length: 291  Bit Score: 46.38  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967081   9 QIEKGLQLYQSNQTEKALQVWMKVLEKGSDLvGRFRVLGCLVTAHSEMGRYKEMLK--FAVVQIDTARGLEDADFLLESY 86
Cdd:COG0457   62 LLLLALALLKLGRLEEALELLEKALELELLP-NLAEALLNLGLLLEALGKYEEALEllEKALALDPDPDLAEALLALGAL 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967081  87 LNLARSNEKLCEFHKTISYCKTCLGLpgtragaqlgGQVSLSMGNAFLGLSLFQKALESFEKALRYAHNNDDTMLEcrvc 166
Cdd:COG0457  141 YELGDYEEALELYEKALELDPELNEL----------AEALLALGALLEALGRYEEALELLEKALKLNPDDDAEALL---- 206
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224967081 167 cSLGSFYAQVKDYEKALFFPCKAAELVNDYgkgwslkyrAMSQYHMAVAYRLLGHLGSAMECCEESMKIALQH 239
Cdd:COG0457  207 -NLGLLYLKLGKYEEALEYYEKALELDPDN---------AEALYNLALLLLELGRYEEALEALEKALELDPDL 269
RING1-H2_RNF32 cd16677
RING finger 1, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; ...
363-403 5.99e-05

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: 40.01  E-value: 5.99e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 224967081 363 CGLCGESIGERNSRLqaLPCSHIFHLRCLQN----NGTRSCPNCR 403
Cdd:cd16677    2 CVICKEDFGLQQQVL--LSCSHVFHRACLESferfSGKKTCPMCR 44
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 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: 39.59  E-value: 7.07e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 224967081 363 CGLCGESIGERNSRLqalPCSHIFHLRCLQNNGTR--SCPNCR 403
Cdd:cd16479    4 CIICREEMVSGAKKL---PCGHIFHLSCLRSWLQRqqTCPTCR 43
zf-RING_2 pfam13639
Ring finger domain;
363-403 1.29e-04

Ring finger domain;


Pssm-ID: 338865 [Multi-domain]  Cd Length: 44  Bit Score: 38.91  E-value: 1.29e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 224967081  363 CGLCGESIgERNSRLQALPCSHIFHLRCLQN--NGTRSCPNCR 403
Cdd:pfam13639   3 CPICLEEF-EEGDKVVILPCGHHFHRECLDKwlRSSNTCPLCR 44
RING-H2_BRAP2 cd16457
RING finger, H2 subclass, found in BRCA1-associated protein (BRAP2) and similar proteins; ...
363-403 2.55e-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 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: 38.03  E-value: 2.55e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 224967081 363 CGLCGESIGERNSRLQALPCSHIFHLRCLQNNGTRSCPNCR 403
Cdd:cd16457    3 CPVCLERMDESVSGILTILCNHSFHCDCLKRWGDSTCPVCR 43
TPR_12 pfam13424
Tetratricopeptide repeat;
204-278 2.98e-04

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 38.91  E-value: 2.98e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224967081  204 YRAMSQYHMAVAYRLLGHLGSAMECCEESMKIA--LQHGDRPLQALCLLCFADIHRSRGDLETAFPRYDSAMSIMTE 278
Cdd:pfam13424   1 DVATALNNLAAVLRRLGRYDEALELLEKALEIArrLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
363-403 3.10e-04

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


Pssm-ID: 227827 [Multi-domain]  Cd Length: 374  Bit Score: 42.29  E-value: 3.10e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 224967081 363 CGLCGESIgERNSRLQALPCSHIFHLRCLQN--NGTR-SCPNCR 403
Cdd:COG5540  326 CAICMSNF-IKNDRLRVLPCDHRFHVGCVDKwlLGYSnKCPVCR 368
RING-H2_RNF167 cd16797
RING finger, H2 subclass, found in RING finger protein 167 (RNF167) and similar proteins; ...
363-404 3.41e-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: 38.10  E-value: 3.41e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 224967081 363 CGLCGESIgERNSRLQALPCSHIFHLRCLQ---NNGTRSCPNCRR 404
Cdd:cd16797    3 CAICLDEY-EEGDKLRVLPCSHAYHSKCVDpwlTQTKKTCPVCKQ 46
HRD1 COG5243
HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein ...
373-405 4.74e-04

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


Pssm-ID: 227568 [Multi-domain]  Cd Length: 491  Bit Score: 41.88  E-value: 4.74e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 224967081 373 RNSRLQALPCSHIFHLRCLQNNGTRS--CPNCRRS 405
Cdd:COG5243  309 LDMTPKRLPCGHILHLHCLKNWLERQqtCPICRRP 343
RING-H2_DZIP3 cd16460
RING finger, H2 subclass, found in DAZ (deleted in azoospermia)-interacting protein 3 (DZIP3) ...
363-403 6.12e-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 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: 37.31  E-value: 6.12e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 224967081 363 CGLCGESIGERNsrLQALPCSHIFHLRCLQN--NGTRSCPNCR 403
Cdd:cd16460    3 CVICHENLSPEN--LSVLPCAHKFHSQCIRPwlMQQRTCPTCR 43
RING-H2_AMFR cd16455
RING finger, H2 subclass, found in autocrine motility factor receptor (AMFR) and similar ...
363-405 7.74e-04

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 degradation from the ER. AMFR contains an N-terminal RING-H2 finger and a C-terminal ubiquitin-associated (UBA)-like CUE domain.


Pssm-ID: 319369 [Multi-domain]  Cd Length: 44  Bit Score: 36.96  E-value: 7.74e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 224967081 363 CGLCGESIGerNSRlqALPCSHIFHLRCLQN--NGTRSCPNCRRS 405
Cdd:cd16455    3 CAICWESMQ--TAR--KLPCGHLFHNSCLRSwlEQDTSCPTCRRS 43
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 1.09e-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: 36.51  E-value: 1.09e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 224967081 363 CGLCGESIgERNSRLQALPCSHIFHLRCLQN--NGTRSCPNCR 403
Cdd:cd16454    2 CAICLEEF-EDGEEVRVLPCNHLFHSNCIDPwlEQHATCPLCR 43
RING-H2_RNF126_like cd16667
RING finger, H2 subclass, found in RING finger proteins RNF126, RNF115, and similar proteins; ...
363-403 1.42e-03

RING finger, H2 subclass, found in RING finger proteins RNF126, RNF115, and similar proteins; The family 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 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. 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), the AKT-phosphorylation sites, and the C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 319581 [Multi-domain]  Cd Length: 43  Bit Score: 36.14  E-value: 1.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 224967081 363 CGLCGESIGERNSRLQaLPCSHIFHLRCL-----QNNgtrSCPNCR 403
Cdd:cd16667    2 CAVCKEDFKVGEKVRQ-LPCNHVFHPDCIvpwleQHN---TCPVCR 43
RING-H2_RNF13_like cd16665
RING finger, H2 subclass, found in RING finger protein 13 (RNF13), RING finger protein 167 ...
363-404 2.43e-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: 35.46  E-value: 2.43e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 224967081 363 CGLCGESIGERNsRLQALPCSHIFHLRCLQ---NNGTRSCPNCRR 404
Cdd:cd16665    3 CAICLDDYEEGD-KLRILPCSHAYHCKCIDpwlTQNRRTCPVCKR 46
RING-HC_TRIM56_C-V cd16584
RING finger, HC subclass, found in tripartite motif-containing protein 56 (TRIM56) and similar ...
361-403 3.95e-03

RING finger, HC subclass, found in tripartite motif-containing protein 56 (TRIM56) and similar proteins; TRIM56, also known as RING finger protein 109 (RNF109), is a virus-inducible E3 ubiquitin ligase that restricts pestivirus infection. It positively regulates the Toll-like receptor 3 (TLR3) antiviral signaling pathway, and possesses antiviral activity against bovine viral diarrhea virus (BVDV), a ruminant pestivirus classified within the family Flaviviridae shared by tick-borne encephalitis virus (TBEV). It also possesses antiviral activity against two classical flaviviruses, yellow fever virus (YFV) and dengue virus (DENV), as well as a human coronavirus, HCoV-OC43, which is responsible for a significant share of common cold cases. It may do not act on positive-strand RNA viruses indiscriminately. Moreover, TRIM56 is an interferon-inducible E3 ubiquitin ligase that modulates STING to confer double-stranded DNA-mediated innate immune responses. TRIM56 belongs to the C-V subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain.


Pssm-ID: 319498 [Multi-domain]  Cd Length: 44  Bit Score: 34.68  E-value: 3.95e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 224967081 361 LYCGLCGESIGernsRLQALPCSHIFHLRCLQ-----NNGTRSCPNCR 403
Cdd:cd16584    1 LNCPICLEHYT----KPKSLPCLHTFCEDCLEqlidhNSRRFSCPICR 44
RING-HC_TRIM9 cd16755
RING finger, HC subclass, found in tripartite motif-containing protein 9 (TRIM9) and similar ...
358-405 5.79e-03

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


Pssm-ID: 319669 [Multi-domain]  Cd Length: 52  Bit Score: 34.64  E-value: 5.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 224967081 358 ETELYCGLCGESIGERnsrlQALPCSHIFHLRCLQN--------NGTRSCPNCRRS 405
Cdd:cd16755    1 EEELKCPVCGSFYREP----IILPCSHNLCLACARNilvqtperNSCLTCPQCHRS 52
RING-H2_TRAIP cd16480
RING finger, H2 subclass, found in TRAF-interacting protein (TRAIP) and similar proteins; ...
362-403 6.40e-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: 319394 [Multi-domain]  Cd Length: 45  Bit Score: 34.45  E-value: 6.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 224967081 362 YCGLCGESIGerNSR-LQALPCSHIFHLRCL----QNNGTRSCPNCR 403
Cdd:cd16480    1 YCTICSDFFD--NSRdVAAIHCGHTFHYECLlqwfETAPSRTCPQCR 45
RING-H2_RNF181 cd16669
RING finger, H2 subclass, found in RING finger protein 181 (RNF181) and similar proteins; ...
372-403 6.61e-03

RING finger, H2 subclass, found in RING finger protein 181 (RNF181) and similar proteins; RNF181, also known as HSPC238, is a platelet E3 ubiquitin-protein ligase containing a C3H2C3-type RING-H2 finger. It interacts with the KVGFFKR motif of platelet integrin alpha(IIb)beta3, suggesting a role for RNF181-mediated ubiquitination in integrin and platelet signaling. It also suppresses the tumorigenesis of hepatocellular carcinoma (HCC) through the inhibition of extracellular signal-regulated kinase/mitogen-activated protein kinase (ERK/MAPK) signaling in the liver.


Pssm-ID: 319583 [Multi-domain]  Cd Length: 46  Bit Score: 34.27  E-value: 6.61e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 224967081 372 ERNSRLQALPCSHIFHLRCLQN--NGTRSCPNCR 403
Cdd:cd16669   10 EEGEEVKEMPCKHSFHSGCILPwlKKTNSCPLCR 43
RING-HC_TIF1alpha cd16764
RING finger, HC subclass, found in transcription inknown asiary factor 1-alpha (TIF1-alpha); ...
363-391 6.61e-03

RING finger, HC subclass, found in transcription inknown asiary factor 1-alpha (TIF1-alpha); TIF1-alpha, also known as tripartite motif-containing protein 24 (TRIM24), E3 ubiquitin-protein ligase TRIM24, or RING finger protein 82, belongs to the C-VI subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. It interacts specifically and in a ligand-dependent manner with the ligand binding domain (LBD) of several nuclear receptors (NRs), including retinoid X (RXR), retinoic acid (RAR), vitamin D3 (VDR), estrogen (ER), and progesterone (PR) receptors. It also associates with heterochromatin-associated factors HP1alpha, MOD1 (HP1beta), and MOD2 (HP1gamma), as well as the vertebrate Kruppel-type (C2H2) zinc finger proteins that contains transcriptional silencing domain KRAB. TIF1-alpha is a ligand-dependent co-repressor of retinoic acid receptor (RAR) that interacts with multiple nuclear receptors in vitro via an LXXLL motif and further acts as a gatekeeper of liver carcinogenesis. It also functions as an E3-ubiquitin ligase targeting p53, and is broadly associated with chromatin silencing. Moreover, it is a chromatin regulator that recognizes specific, combinatorial histone modifications through its C-terminal PHD-Bromo region. In addition, it interacts with chromatin and estrogen receptor to activate estrogen-dependent genes associated with cellular proliferation and tumor development.


Pssm-ID: 319678  Cd Length: 77  Bit Score: 35.37  E-value: 6.61e-03
                         10        20
                 ....*....|....*....|....*....
gi 224967081 363 CGLCGESIGERNSRLqaLPCSHIFHLRCL 391
Cdd:cd16764    4 CGVCRQHIQSRSPKL--LPCLHSFCQRCL 30
 
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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