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Conserved domains on  [gi|38045928|ref|NP_116034.2|]
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43 kDa receptor-associated protein of the synapse isoform 2 [Homo sapiens]

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List of domain hits

Name Accession Description Interval E-value
SNAP super family cl24038
Soluble N-ethylmaleimide-sensitive factor (NSF) Attachment Protein family; Members of the ...
1-80 1.08e-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: 305195  Cd Length: 80  Bit Score: 134.27  E-value: 1.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045928     1 MGQDQTKQQIEKGLQLYQSNQTEKALQVWTKVLEKSSDLMGRFRVLGCLVTAHSEMGRYKEMLKFAVVQIDTARELEDAD 80
Cdd:pfam10579   1 MGQDQTKQQIEKGLRLYQSNNTEKALRTWRKVLKKTCDREGCFRVLGCLITAHSEMGKYKEMLEFGHQQIGTARELEDPD 80
zf-RING_2 pfam13639
Ring finger domain;
304-344 2.25e-04

Ring finger domain;


:

Pssm-ID: 290367  Cd Length: 44  Bit Score: 38.61  E-value: 2.25e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 38045928   304 CGLCGESIgEKNSRLQALPCSHIFHLRCLQN--NGTRSCPNCR 344
Cdd:pfam13639   3 CAICLDEF-EPGSKVRLLPCGHCFHRECLDKwlRSHGTCPLCR 44
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
9-239 2.32e-06

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


:

Pssm-ID: 223533 [Multi-domain]  Cd Length: 291  Bit Score: 47.15  E-value: 2.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045928   9 QIEKGLQLYQSNQTEKALQVWTKVLEKSSDLmGRFRVLGCLVTAHSEMGRYKEMLKFAVVQIDTARELEDADFLLESYLN 88
Cdd:COG0457  62 LLLLALALLKLGRLEEALELLEKALELELLP-NLAEALLNLGLLLEALGKYEEALELLEKALALDPDPDLAEALLALGAL 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045928  89 LarsneKLCEFHKTISYCKTCLGLPGTRAGAqlgGQVSLSMGNAFLGLSVFQKALESFEKALRYAHNNDDAMLEcrvccS 168
Cdd:COG0457 141 Y-----ELGDYEEALELYEKALELDPELNEL---AEALLALGALLEALGRYEEALELLEKALKLNPDDDAEALL-----N 207
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38045928 169 LGSFYAQVKDYEKALFFPCKAAELVNNYgkgwslkyrAMSQYHMAVAYRLLGRLGSAMECCEESMKIALQH 239
Cdd:COG0457 208 LGLLYLKLGKYEEALEYYEKALELDPDN---------AEALYNLALLLLELGRYEEALEALEKALELDPDL 269
 
Name Accession Description Interval E-value
Rapsyn_N pfam10579
Rapsyn N-terminal myristoylation and linker region; Neuromuscular junction formation relies ...
1-80 1.08e-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: 287540  Cd Length: 80  Bit Score: 134.27  E-value: 1.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045928     1 MGQDQTKQQIEKGLQLYQSNQTEKALQVWTKVLEKSSDLMGRFRVLGCLVTAHSEMGRYKEMLKFAVVQIDTARELEDAD 80
Cdd:pfam10579   1 MGQDQTKQQIEKGLRLYQSNNTEKALRTWRKVLKKTCDREGCFRVLGCLITAHSEMGKYKEMLEFGHQQIGTARELEDPD 80
zf-RING_2 pfam13639
Ring finger domain;
304-344 2.25e-04

Ring finger domain;


Pssm-ID: 290367  Cd Length: 44  Bit Score: 38.61  E-value: 2.25e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 38045928   304 CGLCGESIgEKNSRLQALPCSHIFHLRCLQN--NGTRSCPNCR 344
Cdd:pfam13639   3 CAICLDEF-EPGSKVRLLPCGHCFHRECLDKwlRSHGTCPLCR 44
RING cd00162
RING-finger (Really Interesting New Gene) domain, a specialized type of Zn-finger of 40 to 60 ...
304-346 4.96e-04

RING-finger (Really Interesting New Gene) domain, a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc; defined by the 'cross-brace' motif C-X2-C-X(9-39)-C-X(1-3)- H-X(2-3)-(N/C/H)-X2-C-X(4-48)C-X2-C; probably involved in mediating protein-protein interactions; identified in a proteins with a wide range of functions such as viral replication, signal transduction, and development; has two variants, the C3HC4-type and a C3H2C3-type (RING-H2 finger), which have different cysteine/histidine pattern; a subset of RINGs are associated with B-Boxes (C-X2-H-X7-C-X7-C-X2-C-H-X2-H)


Pssm-ID: 238093  Cd Length: 45  Bit Score: 37.43  E-value: 4.96e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 38045928 304 CGLCGESIGEKnsrLQALPCSHIFHLRCLQ---NNGTRSCPNCRRS 346
Cdd:cd00162   2 CPICLEEFREP---VVLLPCGHVFCRSCIDkwlKSGKNTCPLCRTP 44
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
9-239 2.32e-06

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


Pssm-ID: 223533 [Multi-domain]  Cd Length: 291  Bit Score: 47.15  E-value: 2.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045928   9 QIEKGLQLYQSNQTEKALQVWTKVLEKSSDLmGRFRVLGCLVTAHSEMGRYKEMLKFAVVQIDTARELEDADFLLESYLN 88
Cdd:COG0457  62 LLLLALALLKLGRLEEALELLEKALELELLP-NLAEALLNLGLLLEALGKYEEALELLEKALALDPDPDLAEALLALGAL 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045928  89 LarsneKLCEFHKTISYCKTCLGLPGTRAGAqlgGQVSLSMGNAFLGLSVFQKALESFEKALRYAHNNDDAMLEcrvccS 168
Cdd:COG0457 141 Y-----ELGDYEEALELYEKALELDPELNEL---AEALLALGALLEALGRYEEALELLEKALKLNPDDDAEALL-----N 207
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38045928 169 LGSFYAQVKDYEKALFFPCKAAELVNNYgkgwslkyrAMSQYHMAVAYRLLGRLGSAMECCEESMKIALQH 239
Cdd:COG0457 208 LGLLYLKLGKYEEALEYYEKALELDPDN---------AEALYNLALLLLELGRYEEALEALEKALELDPDL 269
TPR_12 pfam13424
Tetratricopeptide repeat;
204-263 2.13e-05

Tetratricopeptide repeat;


Pssm-ID: 290160 [Multi-domain]  Cd Length: 79  Bit Score: 42.02  E-value: 2.13e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38045928   204 YRAMSQYHMAVAYRLLGRLGSAMECCEESMKIALQH--GDRPLQALCLLCFADIHRSRGDLE 263
Cdd:pfam13424   3 DTATALNNLALVLRALGDYDEALELLEKALEIAERVlgPDHPLTATALNNLARLYLALGDYE 64
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
304-344 2.93e-05

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


Pssm-ID: 227827 [Multi-domain]  Cd Length: 374  Bit Score: 44.22  E-value: 2.93e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 38045928 304 CGLCGESIgEKNSRLQALPCSHIFHLRCLQN--NGTR-SCPNCR 344
Cdd:COG5540 326 CAICMSNF-IKNDRLRVLPCDHRFHVGCVDKwlLGYSnKCPVCR 368
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
62-285 3.16e-03

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 38.14  E-value: 3.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045928    62 MLKFAVVQIDTARELEDADFL----------LESYLNLARSNEKLCEFHKTISYCKTCLglpgtrAGAQLGGQVSLSMGN 131
Cdd:TIGR02917 536 ILALAGLYLRTGNEEEAVAWLekaaelnpqeIEPALALAQYYLGKGQLKKALAILNEAA------DAAPDSPEAWLMLGR 609
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045928   132 AFLGLSVFQKALESFEKALRYAHNNDDAMLEcrvccsLGSFYAQVKDYEKALffpckaaelvnnygkgWSLKyRAMSQY- 210
Cdd:TIGR02917 610 AQLAAGDLNKAVSSFKKLLALQPDSALALLL------LADAYAVMKNYAKAI----------------TSLK-RALELKp 666
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38045928   211 HMAVAYRLLGRLGSAMECCEESMKIALQ-HGDRPLQALCLLCFADIHRSRGDLELSQLKLHclsesiyrsKGLQRE 285
Cdd:TIGR02917 667 DNTEAQIGLAQLLLAAKRTESAKKIAKSlQKQHPKAALGFELEGDLYLRQKDYPAAIQAYR---------KALKRA 733
TPR_11 pfam13414
TPR repeat;
127-192 3.56e-03

TPR repeat;


Pssm-ID: 290150 [Multi-domain]  Cd Length: 67  Bit Score: 35.00  E-value: 3.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38045928   127 LSMGNAFLGLSVFQKALESFEKALRYAHNNDDAMLecrvccSLGSFYAQVKDYEKALFFPCKAAEL 192
Cdd:pfam13414   6 KNLGNALLKKGKYEEAIEAYEKALELDPDAAELYL------NLALALLKLGDYEEALEDLEKALEL 65
 
Name Accession Description Interval E-value
Rapsyn_N pfam10579
Rapsyn N-terminal myristoylation and linker region; Neuromuscular junction formation relies ...
1-80 1.08e-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: 287540  Cd Length: 80  Bit Score: 134.27  E-value: 1.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045928     1 MGQDQTKQQIEKGLQLYQSNQTEKALQVWTKVLEKSSDLMGRFRVLGCLVTAHSEMGRYKEMLKFAVVQIDTARELEDAD 80
Cdd:pfam10579   1 MGQDQTKQQIEKGLRLYQSNNTEKALRTWRKVLKKTCDREGCFRVLGCLITAHSEMGKYKEMLEFGHQQIGTARELEDPD 80
zf-RING_2 pfam13639
Ring finger domain;
304-344 2.25e-04

Ring finger domain;


Pssm-ID: 290367  Cd Length: 44  Bit Score: 38.61  E-value: 2.25e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 38045928   304 CGLCGESIgEKNSRLQALPCSHIFHLRCLQN--NGTRSCPNCR 344
Cdd:pfam13639   3 CAICLDEF-EPGSKVRLLPCGHCFHRECLDKwlRSHGTCPLCR 44
RING cd00162
RING-finger (Really Interesting New Gene) domain, a specialized type of Zn-finger of 40 to 60 ...
304-346 4.96e-04

RING-finger (Really Interesting New Gene) domain, a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc; defined by the 'cross-brace' motif C-X2-C-X(9-39)-C-X(1-3)- H-X(2-3)-(N/C/H)-X2-C-X(4-48)C-X2-C; probably involved in mediating protein-protein interactions; identified in a proteins with a wide range of functions such as viral replication, signal transduction, and development; has two variants, the C3HC4-type and a C3H2C3-type (RING-H2 finger), which have different cysteine/histidine pattern; a subset of RINGs are associated with B-Boxes (C-X2-H-X7-C-X7-C-X2-C-H-X2-H)


Pssm-ID: 238093  Cd Length: 45  Bit Score: 37.43  E-value: 4.96e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 38045928 304 CGLCGESIGEKnsrLQALPCSHIFHLRCLQ---NNGTRSCPNCRRS 346
Cdd:cd00162   2 CPICLEEFREP---VVLLPCGHVFCRSCIDkwlKSGKNTCPLCRTP 44
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
9-239 2.32e-06

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


Pssm-ID: 223533 [Multi-domain]  Cd Length: 291  Bit Score: 47.15  E-value: 2.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045928   9 QIEKGLQLYQSNQTEKALQVWTKVLEKSSDLmGRFRVLGCLVTAHSEMGRYKEMLKFAVVQIDTARELEDADFLLESYLN 88
Cdd:COG0457  62 LLLLALALLKLGRLEEALELLEKALELELLP-NLAEALLNLGLLLEALGKYEEALELLEKALALDPDPDLAEALLALGAL 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045928  89 LarsneKLCEFHKTISYCKTCLGLPGTRAGAqlgGQVSLSMGNAFLGLSVFQKALESFEKALRYAHNNDDAMLEcrvccS 168
Cdd:COG0457 141 Y-----ELGDYEEALELYEKALELDPELNEL---AEALLALGALLEALGRYEEALELLEKALKLNPDDDAEALL-----N 207
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38045928 169 LGSFYAQVKDYEKALFFPCKAAELVNNYgkgwslkyrAMSQYHMAVAYRLLGRLGSAMECCEESMKIALQH 239
Cdd:COG0457 208 LGLLYLKLGKYEEALEYYEKALELDPDN---------AEALYNLALLLLELGRYEEALEALEKALELDPDL 269
TPR_12 pfam13424
Tetratricopeptide repeat;
204-263 2.13e-05

Tetratricopeptide repeat;


Pssm-ID: 290160 [Multi-domain]  Cd Length: 79  Bit Score: 42.02  E-value: 2.13e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38045928   204 YRAMSQYHMAVAYRLLGRLGSAMECCEESMKIALQH--GDRPLQALCLLCFADIHRSRGDLE 263
Cdd:pfam13424   3 DTATALNNLALVLRALGDYDEALELLEKALEIAERVlgPDHPLTATALNNLARLYLALGDYE 64
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
304-344 2.93e-05

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


Pssm-ID: 227827 [Multi-domain]  Cd Length: 374  Bit Score: 44.22  E-value: 2.93e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 38045928 304 CGLCGESIgEKNSRLQALPCSHIFHLRCLQN--NGTR-SCPNCR 344
Cdd:COG5540 326 CAICMSNF-IKNDRLRVLPCDHRFHVGCVDKwlLGYSnKCPVCR 368
HRD1 COG5243
HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein ...
314-346 7.37e-05

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: 7.37e-05
                        10        20        30
                ....*....|....*....|....*....|....*
gi 38045928 314 KNSRLQALPCSHIFHLRCLQNNGTRS--CPNCRRS 346
Cdd:COG5243 309 LDMTPKRLPCGHILHLHCLKNWLERQqtCPICRRP 343
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
62-285 3.16e-03

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 38.14  E-value: 3.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045928    62 MLKFAVVQIDTARELEDADFL----------LESYLNLARSNEKLCEFHKTISYCKTCLglpgtrAGAQLGGQVSLSMGN 131
Cdd:TIGR02917 536 ILALAGLYLRTGNEEEAVAWLekaaelnpqeIEPALALAQYYLGKGQLKKALAILNEAA------DAAPDSPEAWLMLGR 609
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38045928   132 AFLGLSVFQKALESFEKALRYAHNNDDAMLEcrvccsLGSFYAQVKDYEKALffpckaaelvnnygkgWSLKyRAMSQY- 210
Cdd:TIGR02917 610 AQLAAGDLNKAVSSFKKLLALQPDSALALLL------LADAYAVMKNYAKAI----------------TSLK-RALELKp 666
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38045928   211 HMAVAYRLLGRLGSAMECCEESMKIALQ-HGDRPLQALCLLCFADIHRSRGDLELSQLKLHclsesiyrsKGLQRE 285
Cdd:TIGR02917 667 DNTEAQIGLAQLLLAAKRTESAKKIAKSlQKQHPKAALGFELEGDLYLRQKDYPAAIQAYR---------KALKRA 733
TPR_11 pfam13414
TPR repeat;
127-192 3.56e-03

TPR repeat;


Pssm-ID: 290150 [Multi-domain]  Cd Length: 67  Bit Score: 35.00  E-value: 3.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38045928   127 LSMGNAFLGLSVFQKALESFEKALRYAHNNDDAMLecrvccSLGSFYAQVKDYEKALFFPCKAAEL 192
Cdd:pfam13414   6 KNLGNALLKKGKYEEAIEAYEKALELDPDAAELYL------NLALALLKLGDYEEALEDLEKALEL 65
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • 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 et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • 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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