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Conserved domains on  [gi|564383957|ref|XP_006251135|]
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complement C1q tumor necrosis factor-related protein 7 isoform X1 [Rattus norvegicus]

Protein Classification

complement C1q domain-containing protein( domain architecture ID 10448922)

complement C1q domain-containing protein may be involved in the regulation of the inflammatory network

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 156-280 7.19e-55

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: 174.01  E-value: 7.19e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564383957  156 AFSVGITTS-YPEERLPIIFNKVLFNEGEHYNPATGKFICAFPGIYYFSYDITLAN-KHLAIGLVHNGQYRIRTFDANT- 232
Cdd:pfam00386   1 AFSAGRTTGlTAPNEQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTVDgKSLYVSLVKNGQEVVSFYDQPQk 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 564383957  233 GNHDVASGSTVIYLQPEDEVWLEIFfnDQNGLFSDPGWADSLFSGFLL 280
Cdd:pfam00386  81 GSLDVASGSVVLELQRGDEVWLQLT--GYNGLYYDGSDTDSTFSGFLL 126
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 63-144 2.91e-13

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: 69.55  E-value: 2.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564383957  63 GRIGLPGRDGRDGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGKKGPIGPEGEKGEVGPAGPPGPKGDRGDQGDPGL 142
Cdd:NF038329 141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP 220


                 ..
gi 564383957 143 PG 144
Cdd:NF038329 221 AG 222
 
Name Accession Description Interval E-value
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 156-280 7.19e-55

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: 174.01  E-value: 7.19e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564383957  156 AFSVGITTS-YPEERLPIIFNKVLFNEGEHYNPATGKFICAFPGIYYFSYDITLAN-KHLAIGLVHNGQYRIRTFDANT- 232
Cdd:pfam00386   1 AFSAGRTTGlTAPNEQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTVDgKSLYVSLVKNGQEVVSFYDQPQk 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 564383957  233 GNHDVASGSTVIYLQPEDEVWLEIFfnDQNGLFSDPGWADSLFSGFLL 280
Cdd:pfam00386  81 GSLDVASGSVVLELQRGDEVWLQLT--GYNGLYYDGSDTDSTFSGFLL 126
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 154-283 3.24e-47

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: 154.77  E-value: 3.24e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564383957   154 KSAFSVGITTSYPEERLPIIFNKVLFNEGEHYNPATGKFICAFPGIYYFSYDITLANKHLAIGLVHNGQYRIRTFDANT- 232
Cdd:smart00110   7 RSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVMSTYDEYQk 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 564383957   233 GNHDVASGSTVIYLQPEDEVWLEIfFNDQNGLFSDpGWADSLFSGFLLYVD 283
Cdd:smart00110  87 GLYDVASGGALLQLRQGDQVWLEL-PDEKNGLYAG-EYVDSTFSGFLLFPD 135
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 63-144 2.91e-13

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: 69.55  E-value: 2.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564383957  63 GRIGLPGRDGRDGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGKKGPIGPEGEKGEVGPAGPPGPKGDRGDQGDPGL 142
Cdd:NF038329 141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP 220


                 ..
gi 564383957 143 PG 144
Cdd:NF038329 221 AG 222
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 63-144 7.36e-11

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: 62.23  E-value: 7.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564383957  63 GRIGLPGRDGR--DGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGK---------KGPIGPEGEKGEVGPAGPPGPK 131
Cdd:NF038329 222 GEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPdgpdgkdgeRGPVGPAGKDGQNGKDGLPGKD 301

                         90
                 ....*....|...
gi 564383957 132 GDRGDQGDPGLPG 144
Cdd:NF038329 302 GKDGQNGKDGLPG 314
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 57-144 2.90e-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: 2.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564383957  57 GSPgphGRIGLPGRDGRDGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGKKGPIGPEGEKGEvgpagppGPKGDRGD 136
Cdd:NF038329 168 GEA---GPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP-------AGDGQQGP 237


                 ....*...
gi 564383957 137 QGDPGLPG 144
Cdd:NF038329 238 DGDPGPTG 245
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 63-116 1.56e-07

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: 52.21  E-value: 1.56e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564383957  63 GRIGLPGRDGRDGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGKKGPIGPE 116
Cdd:NF038329 293 GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPE 346
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 66-115 2.58e-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: 46.72  E-value: 2.58e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 564383957   66 GLPGRDGRDGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGKKGPIGP 115
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PHA03169 PHA03169
hypothetical protein; Provisional
 66-144 3.63e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 38.41  E-value: 3.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564383957  66 GLPGRDGRDGRKGEKGEKGTAGLKGKTGPLGLA-GEKGDQGETGKKGPIGPEGEKGEVGPAGPPGPKGDRGDQGDPGLPG 144
Cdd:PHA03169  90 GGPSGSGSESVGSPTPSPSGSAEELASGLSPENtSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQP 169
 
Name Accession Description Interval E-value
C1q pfam00386
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ...
 156-280 7.19e-55

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: 174.01  E-value: 7.19e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564383957  156 AFSVGITTS-YPEERLPIIFNKVLFNEGEHYNPATGKFICAFPGIYYFSYDITLAN-KHLAIGLVHNGQYRIRTFDANT- 232
Cdd:pfam00386   1 AFSAGRTTGlTAPNEQPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTVDgKSLYVSLVKNGQEVVSFYDQPQk 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 564383957  233 GNHDVASGSTVIYLQPEDEVWLEIFfnDQNGLFSDPGWADSLFSGFLL 280
Cdd:pfam00386  81 GSLDVASGSVVLELQRGDEVWLQLT--GYNGLYYDGSDTDSTFSGFLL 126
C1Q smart00110
Complement component C1q domain; Globular domain found in many collagens and eponymously in ...
 154-283 3.24e-47

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: 154.77  E-value: 3.24e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564383957   154 KSAFSVGITTSYPEERLPIIFNKVLFNEGEHYNPATGKFICAFPGIYYFSYDITLANKHLAIGLVHNGQYRIRTFDANT- 232
Cdd:smart00110   7 RSAFSVIRSNRPPPPGQPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVMSTYDEYQk 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 564383957   233 GNHDVASGSTVIYLQPEDEVWLEIfFNDQNGLFSDpGWADSLFSGFLLYVD 283
Cdd:smart00110  87 GLYDVASGGALLQLRQGDQVWLEL-PDEKNGLYAG-EYVDSTFSGFLLFPD 135
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 63-144 2.91e-13

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: 69.55  E-value: 2.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564383957  63 GRIGLPGRDGRDGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGKKGPIGPEGEKGEVGPAGPPGPKGDRGDQGDPGL 142
Cdd:NF038329 141 GETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGP 220


                 ..
gi 564383957 143 PG 144
Cdd:NF038329 221 AG 222
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 63-144 7.36e-11

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: 62.23  E-value: 7.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564383957  63 GRIGLPGRDGR--DGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGK---------KGPIGPEGEKGEVGPAGPPGPK 131
Cdd:NF038329 222 GEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPdgpdgkdgeRGPVGPAGKDGQNGKDGLPGKD 301

                         90
                 ....*....|...
gi 564383957 132 GDRGDQGDPGLPG 144
Cdd:NF038329 302 GKDGQNGKDGLPG 314
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 57-144 2.90e-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: 2.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564383957  57 GSPgphGRIGLPGRDGRDGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGKKGPIGPEGEKGEvgpagppGPKGDRGD 136
Cdd:NF038329 168 GEA---GPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGP-------AGDGQQGP 237


                 ....*...
gi 564383957 137 QGDPGLPG 144
Cdd:NF038329 238 DGDPGPTG 245
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 63-116 1.56e-07

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: 52.21  E-value: 1.56e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564383957  63 GRIGLPGRDGRDGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGKKGPIGPE 116
Cdd:NF038329 293 GKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPE 346
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 66-115 2.58e-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: 46.72  E-value: 2.58e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 564383957   66 GLPGRDGRDGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGKKGPIGP 115
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 72-125 1.26e-04

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: 39.01  E-value: 1.26e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564383957   72 GRDGRKGEKGEKGTAGLKGKTGPLGLAGEKGDQGETGKKGPIGPEGEKGEvgpA 125
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA---P 51
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 81-144 1.81e-04

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: 38.63  E-value: 1.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564383957   81 GEKGTAGLKGKTGPLGLAGEKGDQGETGKKGPIGPEGEKGEvgpagppgpKGDRGDQGDPGLPG 144
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGP---------PGPPGPPGAPGAPG 55
PHA03169 PHA03169
hypothetical protein; Provisional
 66-144 3.63e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 38.41  E-value: 3.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564383957  66 GLPGRDGRDGRKGEKGEKGTAGLKGKTGPLGLA-GEKGDQGETGKKGPIGPEGEKGEVGPAGPPGPKGDRGDQGDPGLPG 144
Cdd:PHA03169  90 GGPSGSGSESVGSPTPSPSGSAEELASGLSPENtSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQP 169
 
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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