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Conserved domains on  [gi|124286805|ref|NP_031598|]
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complement C1q subcomponent subunit A precursor [Mus musculus]

Protein Classification

C1Q domain-containing protein( domain architecture ID 10638913)

C1Q domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 108-244 2.43e-64

Complement component C1q domain; Globular domain found in many collagens and eponymously in complement C1q. When part of full length proteins these domains form a 'bouquet' due to the multimerization of heterotrimers. The C1q fold is similar to that of tumour necrosis factor.


:

Pssm-ID: 128420  Cd Length: 135  Bit Score: 196.75  E-value: 2.43e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124286805   108 NIRDQPRPAFSAIRQN-PMTLGNVVIFDKVLTNQESPYQNHTGRFICAVPGFYYFNFQVISKWDLCLFIKSSSGGQPrds 186
Cdd:smart00110   1 NYKAQPRSAFSVIRSNrPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQV--- 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 124286805   187 LSFSNTNNKGLFQVLAGGTVLQLRRGDEVWIEKDPAKGRIYQGTEADSIFSGFLIFPS 244
Cdd:smart00110  78 MSTYDEYQKGLYDVASGGALLQLRQGDQVWLELPDEKNGLYAGEYVDSTFSGFLLFPD 135
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 27-107 1.64e-10

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 60.30  E-value: 1.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124286805  27 RAPNGKDGAPGNPGRPGRPGLKGERGEPGAAGIR-----TGIRGFKGDPGESGPPGKPGNV-----GLPGPSGPLGDSGP 96
Cdd:NF038329 173 QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQgpagpAGPDGEAGPAGEDGPAGPAGDGqqgpdGDPGPTGEDGPQGP 252

                         90
                 ....*....|.
gi 124286805  97 QGLKGVKGNPG 107
Cdd:NF038329 253 DGPAGKDGPRG 263
 
Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 108-244 2.43e-64

Complement component C1q domain; Globular domain found in many collagens and eponymously in complement C1q. When part of full length proteins these domains form a 'bouquet' due to the multimerization of heterotrimers. The C1q fold is similar to that of tumour necrosis factor.


Pssm-ID: 128420  Cd Length: 135  Bit Score: 196.75  E-value: 2.43e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124286805   108 NIRDQPRPAFSAIRQN-PMTLGNVVIFDKVLTNQESPYQNHTGRFICAVPGFYYFNFQVISKWDLCLFIKSSSGGQPrds 186
Cdd:smart00110   1 NYKAQPRSAFSVIRSNrPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQV--- 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 124286805   187 LSFSNTNNKGLFQVLAGGTVLQLRRGDEVWIEKDPAKGRIYQGTEADSIFSGFLIFPS 244
Cdd:smart00110  78 MSTYDEYQKGLYDVASGGALLQLRQGDQVWLELPDEKNGLYAGEYVDSTFSGFLLFPD 135
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 116-241 1.67e-51

C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement system.


Pssm-ID: 395310 [Multi-domain]  Cd Length: 126  Bit Score: 163.61  E-value: 1.67e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124286805  116 AFSAIRQNPMTLGN--VVIFDKVLTNQESPYQNHTGRFICAVPGFYYFNFQVIskWDLCLFIKSSSGGQPRDSLSFSNTN 193
Cdd:pfam00386   1 AFSAGRTTGLTAPNeqPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHIT--TVDGKSLYVSLVKNGQEVVSFYDQP 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 124286805  194 NKGLFQVLAGGTVLQLRRGDEVWIEKDPAKGRIYQGTEADSIFSGFLI 241
Cdd:pfam00386  79 QKGSLDVASGSVVLELQRGDEVWLQLTGYNGLYYDGSDTDSTFSGFLL 126
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 27-107 1.64e-10

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 60.30  E-value: 1.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124286805  27 RAPNGKDGAPGNPGRPGRPGLKGERGEPGAAGIR-----TGIRGFKGDPGESGPPGKPGNV-----GLPGPSGPLGDSGP 96
Cdd:NF038329 173 QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQgpagpAGPDGEAGPAGEDGPAGPAGDGqqgpdGDPGPTGEDGPQGP 252

                         90
                 ....*....|.
gi 124286805  97 QGLKGVKGNPG 107
Cdd:NF038329 253 DGPAGKDGPRG 263
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 40-96 3.71e-10

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 54.04  E-value: 3.71e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 124286805   40 GRPGRPGLKGERGEPGAAGIRtGIRGFKGDPGESGPPGKPGNVGLPGPSGPLGDSGP 96
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPP-GPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 47-107 1.38e-09

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 57.61  E-value: 1.38e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124286805  47 LKGERGEPGAAGIR--------TGIRGFKGDPGESGPPGKPGNVGLPGPSGPLGDSGPQGLKGVKGNPG 107
Cdd:NF038329 115 GDGEKGEPGPAGPAgpageqgpRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 28-128 2.52e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 38.45  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124286805  28 APNGkdGAPGNPGRPgRPGLKGERG--EPGAAGIRTGirGFKGDPGESGPPGKPGNVGLPGPSGPLGDSG-PQGLKGVKG 104
Cdd:PHA03264 269 APSG--GSPAPPGDD-RPEAKPEPGpvEDGAPGRETG--GEGEGPEPAGRDGAAGGEPKPGPPRPAPDADrPEGWPSLEA 343

                         90       100
                 ....*....|....*....|....*
gi 124286805 105 NPgniRDQPRPAFSAI-RQNPMTLG 128
Cdd:PHA03264 344 IT---FPPPTPATPAVpRARPVIVG 365
 
Name Accession Description Interval E-value
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 108-244 2.43e-64

Complement component C1q domain; Globular domain found in many collagens and eponymously in complement C1q. When part of full length proteins these domains form a 'bouquet' due to the multimerization of heterotrimers. The C1q fold is similar to that of tumour necrosis factor.


Pssm-ID: 128420  Cd Length: 135  Bit Score: 196.75  E-value: 2.43e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124286805   108 NIRDQPRPAFSAIRQN-PMTLGNVVIFDKVLTNQESPYQNHTGRFICAVPGFYYFNFQVISKWDLCLFIKSSSGGQPrds 186
Cdd:smart00110   1 NYKAQPRSAFSVIRSNrPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQV--- 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 124286805   187 LSFSNTNNKGLFQVLAGGTVLQLRRGDEVWIEKDPAKGRIYQGTEADSIFSGFLIFPS 244
Cdd:smart00110  78 MSTYDEYQKGLYDVASGGALLQLRQGDQVWLELPDEKNGLYAGEYVDSTFSGFLLFPD 135
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 116-241 1.67e-51

C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement system.


Pssm-ID: 395310 [Multi-domain]  Cd Length: 126  Bit Score: 163.61  E-value: 1.67e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124286805  116 AFSAIRQNPMTLGN--VVIFDKVLTNQESPYQNHTGRFICAVPGFYYFNFQVIskWDLCLFIKSSSGGQPRDSLSFSNTN 193
Cdd:pfam00386   1 AFSAGRTTGLTAPNeqPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHIT--TVDGKSLYVSLVKNGQEVVSFYDQP 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 124286805  194 NKGLFQVLAGGTVLQLRRGDEVWIEKDPAKGRIYQGTEADSIFSGFLI 241
Cdd:pfam00386  79 QKGSLDVASGSVVLELQRGDEVWLQLTGYNGLYYDGSDTDSTFSGFLL 126
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 27-107 1.64e-10

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 60.30  E-value: 1.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124286805  27 RAPNGKDGAPGNPGRPGRPGLKGERGEPGAAGIR-----TGIRGFKGDPGESGPPGKPGNV-----GLPGPSGPLGDSGP 96
Cdd:NF038329 173 QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQgpagpAGPDGEAGPAGEDGPAGPAGDGqqgpdGDPGPTGEDGPQGP 252

                         90
                 ....*....|.
gi 124286805  97 QGLKGVKGNPG 107
Cdd:NF038329 253 DGPAGKDGPRG 263
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 40-96 3.71e-10

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 54.04  E-value: 3.71e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 124286805   40 GRPGRPGLKGERGEPGAAGIRtGIRGFKGDPGESGPPGKPGNVGLPGPSGPLGDSGP 96
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPP-GPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 47-107 1.38e-09

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 57.61  E-value: 1.38e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124286805  47 LKGERGEPGAAGIR--------TGIRGFKGDPGESGPPGKPGNVGLPGPSGPLGDSGPQGLKGVKGNPG 107
Cdd:NF038329 115 GDGEKGEPGPAGPAgpageqgpRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAG 183
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 29-87 6.90e-09

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 50.57  E-value: 6.90e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 124286805   29 PNGKDGAPGNPGRPGRPGLKGERGEPGAAgirtGIRGFKGDPGESGPPGKPGNVGLPGP 87
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPP----GEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 29-79 4.10e-07

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 45.95  E-value: 4.10e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 124286805   29 PNGKDGAPGNPGRPGRPGLKGERGEPGAAgirtGIRGFKGDPGESGPPGKP 79
Cdd:pfam01391  11 PPGPPGPPGPPGPPGPPGPPGEPGPPGPP----GPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 62-108 1.36e-06

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.41  E-value: 1.36e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 124286805   62 GIRGFKGDPGESGPPGKPGNVGLPGPSGPLGDSGPQGLKGVKGNPGN 108
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP 47
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 62-109 8.33e-06

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 8.33e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 124286805   62 GIRGFKGDPGESGPPGKPGNVGLPGPSGPLGDSGPQGLKGVKGNPGNI 109
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 28-128 2.52e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 38.45  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124286805  28 APNGkdGAPGNPGRPgRPGLKGERG--EPGAAGIRTGirGFKGDPGESGPPGKPGNVGLPGPSGPLGDSG-PQGLKGVKG 104
Cdd:PHA03264 269 APSG--GSPAPPGDD-RPEAKPEPGpvEDGAPGRETG--GEGEGPEPAGRDGAAGGEPKPGPPRPAPDADrPEGWPSLEA 343

                         90       100
                 ....*....|....*....|....*
gi 124286805 105 NPgniRDQPRPAFSAI-RQNPMTLG 128
Cdd:PHA03264 344 IT---FPPPTPATPAVpRARPVIVG 365
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 27-58 6.02e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 34.01  E-value: 6.02e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 124286805   27 RAPNGKDGAPGNPGRPGRPGLKGERGEPGAAG 58
Cdd:pfam01391  24 PGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
 
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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