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Conserved domains on  [gi|1207164114|ref|XP_021325468|]
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NSFL1 cofactor p47 isoform X2 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UBA_p47 cd14348
UBA-like domain found in NSFL1 cofactor p47 and similar proteins; p47, also called UBX ...
5-44 1.69e-16

UBA-like domain found in NSFL1 cofactor p47 and similar proteins; p47, also called UBX domain-containing protein 2C, is a major cofactor of the cytosolic AAA ATPase p97. It is required for the p97-regulated membrane reassembly of the endoplasmic reticulum (ER), the nuclear envelope and the Golgi apparatus. p47, together with p97, forms the p97-p47 complex that plays an important role in regulation of membrane fusion events. p47 contains an N-terminal ubiquitin-associated (UBA)-like domain, a central SEP (named after shp1, eyc and p47) domain, and a ubiquitin-like (UBX) domain. UBA-like domain is responsible for forming a highly stable complex with ubiquitin. SEP domain and UBX domain may involve in p47 trimerization or forms a stable complex with the p97 N-terminal domain.


:

Pssm-ID: 270533  Cd Length: 40  Bit Score: 70.26  E-value: 1.69e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1207164114   5 EEAVRGFVAVTDVDEERARFFLESAGWDLQLALANFFEDG 44
Cdd:cd14348     1 DELIAQFVSVTGADEDRAKFFLESAGWDLEAALSSFFESG 40
SEP super family cl02662
SEP domain; The SEP domain is named after Saccharomyces cerevisiae Shp1, Drosophila ...
178-216 2.00e-16

SEP domain; The SEP domain is named after Saccharomyces cerevisiae Shp1, Drosophila melanogaster eyes closed gene (eyc), and vertebrate p47. In p47, the SEP domain has been shown to bind to and inhibit the cysteine protease cathepsin L. Most SEP domains are succeeded closely by a UBX domain.


The actual alignment was detected with superfamily member smart00553:

Pssm-ID: 470648  Cd Length: 93  Bit Score: 71.28  E-value: 2.00e-16
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1207164114  178 QDVHVVLKLWKTGFSLDEGELRTYSDPENALFLESIRRG 216
Cdd:smart00553   1 QKVIHTLTFWSNGFSVDDGPLRTYDDPENAEFLESIRRG 39
 
Name Accession Description Interval E-value
UBA_p47 cd14348
UBA-like domain found in NSFL1 cofactor p47 and similar proteins; p47, also called UBX ...
5-44 1.69e-16

UBA-like domain found in NSFL1 cofactor p47 and similar proteins; p47, also called UBX domain-containing protein 2C, is a major cofactor of the cytosolic AAA ATPase p97. It is required for the p97-regulated membrane reassembly of the endoplasmic reticulum (ER), the nuclear envelope and the Golgi apparatus. p47, together with p97, forms the p97-p47 complex that plays an important role in regulation of membrane fusion events. p47 contains an N-terminal ubiquitin-associated (UBA)-like domain, a central SEP (named after shp1, eyc and p47) domain, and a ubiquitin-like (UBX) domain. UBA-like domain is responsible for forming a highly stable complex with ubiquitin. SEP domain and UBX domain may involve in p47 trimerization or forms a stable complex with the p97 N-terminal domain.


Pssm-ID: 270533  Cd Length: 40  Bit Score: 70.26  E-value: 1.69e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1207164114   5 EEAVRGFVAVTDVDEERARFFLESAGWDLQLALANFFEDG 44
Cdd:cd14348     1 DELIAQFVSVTGADEDRAKFFLESAGWDLEAALSSFFESG 40
SEP smart00553
Domain present in Saccharomyces cerevisiae Shp1, Drosophila melanogaster eyes closed gene (eyc) ...
178-216 2.00e-16

Domain present in Saccharomyces cerevisiae Shp1, Drosophila melanogaster eyes closed gene (eyc), and vertebrate p47;


Pssm-ID: 197786  Cd Length: 93  Bit Score: 71.28  E-value: 2.00e-16
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1207164114  178 QDVHVVLKLWKTGFSLDEGELRTYSDPENALFLESIRRG 216
Cdd:smart00553   1 QKVIHTLTFWSNGFSVDDGPLRTYDDPENAEFLESIRRG 39
UBA_4 pfam14555
UBA-like domain;
5-47 9.47e-14

UBA-like domain;


Pssm-ID: 464207  Cd Length: 43  Bit Score: 62.85  E-value: 9.47e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1207164114   5 EEAVRGFVAVTDVDEERARFFLESAGWDLQLALANFFEDGGED 47
Cdd:pfam14555   1 DELIAQFQAITGADEEVARQYLEAHNWDLEAAVNAFFDDGEAS 43
SEP pfam08059
SEP domain; The SEP domain is named after Saccharomyces cerevisiae Shp1, Drosophila ...
184-216 1.82e-13

SEP domain; The SEP domain is named after Saccharomyces cerevisiae Shp1, Drosophila melanogaster eyes closed gene (eyc), and vertebrate p47. In p47, the SEP domain has been shown to bind to and inhibit the cysteine protease cathepsin L. Most SEP domains are succeeded closely by a UBX domain.


Pssm-ID: 462348  Cd Length: 75  Bit Score: 63.26  E-value: 1.82e-13
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1207164114 184 LKLWKTGFSLDEGELRTYSDPENALFLESIRRG 216
Cdd:pfam08059   1 LTFWRNGFSVDDGPLRRYDDPANAEFLEAINRG 33
 
Name Accession Description Interval E-value
UBA_p47 cd14348
UBA-like domain found in NSFL1 cofactor p47 and similar proteins; p47, also called UBX ...
5-44 1.69e-16

UBA-like domain found in NSFL1 cofactor p47 and similar proteins; p47, also called UBX domain-containing protein 2C, is a major cofactor of the cytosolic AAA ATPase p97. It is required for the p97-regulated membrane reassembly of the endoplasmic reticulum (ER), the nuclear envelope and the Golgi apparatus. p47, together with p97, forms the p97-p47 complex that plays an important role in regulation of membrane fusion events. p47 contains an N-terminal ubiquitin-associated (UBA)-like domain, a central SEP (named after shp1, eyc and p47) domain, and a ubiquitin-like (UBX) domain. UBA-like domain is responsible for forming a highly stable complex with ubiquitin. SEP domain and UBX domain may involve in p47 trimerization or forms a stable complex with the p97 N-terminal domain.


Pssm-ID: 270533  Cd Length: 40  Bit Score: 70.26  E-value: 1.69e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1207164114   5 EEAVRGFVAVTDVDEERARFFLESAGWDLQLALANFFEDG 44
Cdd:cd14348     1 DELIAQFVSVTGADEDRAKFFLESAGWDLEAALSSFFESG 40
SEP smart00553
Domain present in Saccharomyces cerevisiae Shp1, Drosophila melanogaster eyes closed gene (eyc) ...
178-216 2.00e-16

Domain present in Saccharomyces cerevisiae Shp1, Drosophila melanogaster eyes closed gene (eyc), and vertebrate p47;


Pssm-ID: 197786  Cd Length: 93  Bit Score: 71.28  E-value: 2.00e-16
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1207164114  178 QDVHVVLKLWKTGFSLDEGELRTYSDPENALFLESIRRG 216
Cdd:smart00553   1 QKVIHTLTFWSNGFSVDDGPLRTYDDPENAEFLESIRRG 39
UBA_4 pfam14555
UBA-like domain;
5-47 9.47e-14

UBA-like domain;


Pssm-ID: 464207  Cd Length: 43  Bit Score: 62.85  E-value: 9.47e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1207164114   5 EEAVRGFVAVTDVDEERARFFLESAGWDLQLALANFFEDGGED 47
Cdd:pfam14555   1 DELIAQFQAITGADEEVARQYLEAHNWDLEAAVNAFFDDGEAS 43
SEP pfam08059
SEP domain; The SEP domain is named after Saccharomyces cerevisiae Shp1, Drosophila ...
184-216 1.82e-13

SEP domain; The SEP domain is named after Saccharomyces cerevisiae Shp1, Drosophila melanogaster eyes closed gene (eyc), and vertebrate p47. In p47, the SEP domain has been shown to bind to and inhibit the cysteine protease cathepsin L. Most SEP domains are succeeded closely by a UBX domain.


Pssm-ID: 462348  Cd Length: 75  Bit Score: 63.26  E-value: 1.82e-13
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1207164114 184 LKLWKTGFSLDEGELRTYSDPENALFLESIRRG 216
Cdd:pfam08059   1 LTFWRNGFSVDDGPLRRYDDPANAEFLEAINRG 33
UBA_TAP-C_like cd14273
UBA-like domain found in the NXF family of mRNA nuclear export factors and similar proteins; ...
11-41 5.66e-09

UBA-like domain found in the NXF family of mRNA nuclear export factors and similar proteins; This family includes nuclear RNA export factors (NXF1/NXF2), FAS-associated factors (FAF1/2), tyrosyl-DNA phosphodiesterase 2 (TDP2), OTU domain-containing proteins (OTU7A/OTU7B), NSFL1 cofactor p47, defective in cullin neddylation protein 1 (DCN1)-like protein (DCNL1/DCNL2), yeast defective in cullin neddylation protein 1 (DCN1) and similar proteins. NXF proteins can stimulate nuclear export of mRNAs and facilitate the export of unspliced viral mRNA containing the constitutive transport element. FAF1 is an apoptotic signaling molecule that acts downstream in the Fas signal transduction pathway. It interacts with the cytoplasmic domain of Fas, but not to a Fas mutant that is deficient in signal transduction. FAF2 is the translation product of a highly expressed gene in the T-cells and eosinophils of atopic dermatitis patients compared with those of normal individuals. Its biological function remains unclear. TDP2 is a 5'-Tyr-DNA phosphodiesterase required for the efficient repair of topoisomerase II-induced DNA double strand breaks. OTU7A and OTU7B are zinc finger proteins that function as deubiquitinating enzymes. p47 is a major cofactor of the cytosolic AAA ATPase p97. It is required for the p97-regulated membrane reassembly of the endoplasmic reticulum (ER), the nuclear envelope and the Golgi apparatus. DCNL1 plays an essential role in the neddylation E3 complex and participates in the release of inhibitory effects of CAND1 on cullin-RING ligase E3 complex assembly and activity. The biological function of DCNL2 remains unclear. Yeast DCN1 is a scaffold-type E3 ligase for cullin neddylation. It can bind directly to cullins and the ubiquitin-like protein Nedd8-specific E2 (Ubc12), and regulate cullin neddylation and thus display ubiquitin ligase activity.


Pssm-ID: 270459  Cd Length: 31  Bit Score: 50.09  E-value: 5.66e-09
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1207164114  11 FVAVTDVDEERARFFLESAGWDLQLALANFF 41
Cdd:cd14273     1 FMEITGADPETARQYLESNNWDLEAAINLYF 31
UBA_CF106 cd14349
UBA-like domain found in uncharacterized protein C6orf106 and similar proteins; The family ...
4-42 3.52e-06

UBA-like domain found in uncharacterized protein C6orf106 and similar proteins; The family corresponds to a group of uncharacterized protein C6orf106 and its homologs mainly found in Metazoa. All family members contain a ubiquitin-associated (UBA)-like domain.


Pssm-ID: 270534  Cd Length: 41  Bit Score: 42.60  E-value: 3.52e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1207164114   4 REEAVRGFVAVT-DVDEERARFFLESAGWDLQLALANFFE 42
Cdd:cd14349     2 HEELISQFQSILgAQNESEAAFFLEMNNWNLQAAVGAYFD 41
UBA_ceTYDP2_like cd14672
UBA-like domain found in Caenorhabditis elegans tyrosyl-DNA phosphodiesterase 2 (TDP2) and ...
6-42 4.43e-06

UBA-like domain found in Caenorhabditis elegans tyrosyl-DNA phosphodiesterase 2 (TDP2) and similar proteins; The family includes C. elegans TDP2 and its homologs found in bilateria. TDP2 (also known as TTRAP or EAPII) belongs to the Mg(2+)/Mn(2+)-dependent family of phosphodiesterases which contains an N-terminal ubiquitin-associated (UBA)-like domain and a C-terminal phosphodiesterase domain. It required for the efficient repair of topoisomerase II-induced DNA double strand breaks. The topoisomerase is covalently linked by a phosphotyrosyl bond to the 5'-terminus of the break. TDP2 cleaves the DNA 5'-phosphodiester bond and restores 5'-phosphate termini needed for subsequent DNA ligation and hence repair of the break. Tyrosyl-DNA phosphodiesterase 1 (TDP1), an enzyme that cleaves 3'-phosphotyrosyl bonds, and TDP2 are complementary activities; together, they allow cells to remove trapped topoisomerase from both 3'- and 5'-DNA termini. TDP2 has been reported as being involved in apoptosis, embryonic development, and transcriptional regulation.


Pssm-ID: 270612  Cd Length: 37  Bit Score: 42.29  E-value: 4.43e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1207164114   6 EAVRGFVAVTDVDEERARFFLESAGWDLQLALANFFE 42
Cdd:cd14672     1 QLCEEFAEITGTDEALAQFYLQDRDWDLEKALDVYFG 37
UBA_DCNL cd14350
UBA-like domain found in DCN1-like protein DCNL1, DCNL2 and similar proteins; DCNL1 (defective ...
6-43 7.87e-06

UBA-like domain found in DCN1-like protein DCNL1, DCNL2 and similar proteins; DCNL1 (defective in cullin neddylation protein 1-like protein 1), also called DCUN1 domain-containing protein 1, is encoded by squamous cell carcinoma-related oncogene SCCRO (DCUN1D1). It interacts with known cullin isoforms as well as ROC1, Ubc12 and CAND1, the components of the neddylation pathway. It plays an essential role in the neddylation E3 complex and participates in the release of inhibitory effects of CAND1 on cullin-RING ligase E3 complex assembly and activity. DCNL1 contains an N-terminal ubiquitin-associated (UBA)-like domain and a C-terminal cullin binding domain that binds to cullins and Rbx-1, components of an E3 ubiquitin ligase complex for neddylation. DCNL2 (defective in cullin neddylation protein 1-like protein 2), also called DCUN1 domain-containing protein 2, is encoded by gene DCUN1D2. Although its biological function remains unclear, DCNL2 shows high sequence similarity with DCNL1 and may also contribute to neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. Like DCNL1, DCNL2 contains an N-terminal UBA-like domain and a C-terminal cullin binding domain.


Pssm-ID: 270535  Cd Length: 42  Bit Score: 41.47  E-value: 7.87e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1207164114   6 EAVRGFVAVTDVDEERARFFLESAGWDLQLALANFFED 43
Cdd:cd14350     4 DKVRQFMSITQANEKTAIQCLKDADWNLELAVDAYFQN 41
UBA_DCN1 cd14352
UBA-like domain found in yeast defective in cullin neddylation protein 1 (DCN1) and similar ...
6-41 9.29e-05

UBA-like domain found in yeast defective in cullin neddylation protein 1 (DCN1) and similar proteins; DCN1 is a scaffold-type E3 ligase for cullin neddylation. It can bind directly to cullins and the ubiquitin-like protein Nedd8-specific E2 (Ubc12), and regulate cullin neddylation and thus display ubiquitin ligase activity. It contains an N-terminal ubiquitin-associated (UBA)-like domain and a unique C-terminal PONY domain that is essential for the neddylation function of DCN1.


Pssm-ID: 270537  Cd Length: 36  Bit Score: 38.42  E-value: 9.29e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1207164114   6 EAVRGFVAVTDVDEERARFFLESAGWDLQLALANFF 41
Cdd:cd14352     1 ELIKQFREITATSPEVARDYLQRSNWNLNYAVDDFY 36
UBA_Ubx1_like cd14351
UBA-like domain found in yeast UBX domain-containing protein 1 (Ubx1) and similar proteins; ...
5-41 2.74e-04

UBA-like domain found in yeast UBX domain-containing protein 1 (Ubx1) and similar proteins; Ubx1, also called suppressor of high-copy PP1 protein (Shp1), is the substrate-recruiting cofactor of AAA-adenosine triphosphatase Cdc48 in Saccharomyces cerevisiae. In concert with ubiquitin-like Atg8, Cdc48 and Ubx1 are involved in the regulation of autophagosome biogenesis. Ubx1 also functions as a regulator of phosphoprotein phosphatase 1 (PP1) with differential effects on glycogen metabolism, meiotic differentiation, and mitotic cell cycle progression. All family members contain an N-terminal ubiquitin-associated (UBA)-like domain.


Pssm-ID: 270536  Cd Length: 37  Bit Score: 37.07  E-value: 2.74e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1207164114   5 EEAVRGFVAVTDVDEERARFFLESAGWDLQLALANFF 41
Cdd:cd14351     1 DEAIQQFMELTGASPEVAQQYLEEYGGDLNDAINAYF 37
UBA_Ubx5_like cd14346
UBA-like domain found in Saccharomyces cerevisiae UBX domain-containing protein 5 (Ubx5) and ...
5-42 4.95e-04

UBA-like domain found in Saccharomyces cerevisiae UBX domain-containing protein 5 (Ubx5) and similar proteins; Ubx5 is a ubiquitin regulatory X (UBX) domain-containing protein encoded by the open reading frame (ORF) YDR330W in yeast. As the yeast ortholog of mammalian UBXD7, Ubx5 functions as the cofactor of AAA+ ATPase p97, also known as VCP or Cdc48. It binds only to the active, NEDD8- or Rub1-modified form of cullins. Ubx5 contains the ubiquitin-associated (UBA), ubiquitin-associating (UAS), ubiquitin regulatory X (UBX) and ubiquitin-interacting motif (UIM) domains and its UIM domain is required to promote UV-dependent degradation of polyubiquitinated Rpb1.


Pssm-ID: 270531  Cd Length: 39  Bit Score: 36.50  E-value: 4.95e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1207164114   5 EEAVRGFVAVTDV-DEERARFFLESAGWDLQLALANFFE 42
Cdd:cd14346     1 DEQISTFLAITGSeDAAVARQFLEMAGGDLETAVSLFFE 39
UBA_TYDP2 cd14344
UBA-like domain found in tyrosyl-DNA phosphodiesterase 2 (TDP2) and similar proteins; TDP2, ...
11-42 1.76e-03

UBA-like domain found in tyrosyl-DNA phosphodiesterase 2 (TDP2) and similar proteins; TDP2, also called ETS1-associated protein II (EAPII) or TRAF and TNF receptor-associated protein (Ttrap), is a 5'-Tyr-DNA phosphodiesterase, a member of the Mg(2+)/Mn(2+)-dependent family of phosphodiesterases which contains an N-terminal ubiquitin-associated (UBA)-like domain and a C-terminal phosphodiesterase domain. TDP2 is required for the efficient repair of topoisomerase II-induced DNA double strand breaks. The topoisomerase is covalently linked by a phosphotyrosyl bond to the 5'-terminus of the break. TDP2 cleaves the DNA 5'-phosphodiester bond and restores 5'-phosphate termini needed for subsequent DNA ligation and hence repair of the break. Tyrosyl-DNA phosphodiesterase 1 (TDP1), an enzyme that cleaves 3'-phosphotyrosyl bonds, and TDP2 are complementary activities; together, they allow cells to remove trapped topoisomerase from both 3'- and 5'-DNA termini. TDP2 has been reported as being involved in apoptosis, embryonic development, and transcriptional regulation. It can associate with CD40, tumor necrosis factor receptor-75 (TNF-R75) and TNF receptor-associated factors (TRAFs) and may inhibit the activation of nuclear factor-kappa B (NF-kappaB).


Pssm-ID: 270529  Cd Length: 37  Bit Score: 35.14  E-value: 1.76e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1207164114  11 FVAVTDVDEERARFFLESAGWDLQLALANFFE 42
Cdd:cd14344     6 FANVTSCDEAVAQRYLAENGWHMERALNAYFE 37
UBA_like_SF cd00194
UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains ...
11-38 1.87e-03

UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains alpha-helical structural homology ubiquitin-binding domains, including UBA domains and coupling of ubiquitin conjugation to endoplasmic reticulum degradation (CUE) domains which share a common three-helical bundle architecture. UBA domains are commonly occurring sequence motifs found in proteins involved in ubiquitin-mediated proteolysis. They contribute to ubiquitin (Ub) binding or ubiquitin-like (UbL) domain binding. However, some kinds of UBA domains can only bind the UbL domain, but not the Ub domain. UBA domains are normally comprised of compact three-helix bundles which contain a conserved GF/Y-loop. They can bind polyubiquitin with high affinity. They also bind monoubiquitin and other proteins. Most UBA domain-containing proteins have one UBA domain, but some harbor two or three UBA domains. CUE domain containing proteins are characterized by an FP and a di-leucine-like sequence and bind to monoubiquitin with varying affinities. Some higher eukaryotic CUE domain proteins do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains. This superfamily also includes many UBA-like domains found in AMP-activated protein kinase (AMPK) related kinases, the NXF family of mRNA nuclear export factors, elongation factor Ts (EF-Ts), nascent polypeptide-associated complex subunit alpha (NACA) and similar proteins. Although many UBA-like domains may have a conserved TG but not GF/Y-loop, they still show a high level of structural and sequence similarity with three-helical ubiquitin binding domains.


Pssm-ID: 270455  Cd Length: 28  Bit Score: 34.69  E-value: 1.87e-03
                          10        20
                  ....*....|....*....|....*...
gi 1207164114  11 FVAVTDVDEERARFFLESAGWDLQLALA 38
Cdd:cd00194     1 LVDITGASQEEAQQALEACGGNLNIAAN 28
UBA_UBXD7 cd14345
UBA-like domain found in UBX domain-containing protein 7 (UBXD7) and similar proteins; UBXD7, ...
6-42 3.23e-03

UBA-like domain found in UBX domain-containing protein 7 (UBXD7) and similar proteins; UBXD7, also known as UBXN7, functions as a ubiquitin-binding adaptor that mediates the interaction between the AAA+ ATPase p97 (also known as VCP or Cdc48) and the transcription factor HIF1alpha. It binds only to the active, NEDD8- or Rub1-modified form of cullins. UBXD7 contains the ubiquitin-associated (UBA), ubiquitin-associating (UAS), ubiquitin regulatory X (UBX), and ubiquitin-interacting motif (UIM) domains. Either UBA or UIM could serve as a docking site for neddylated-cullins. Moreover, UBA-like domain is required for binding ubiquitylated-protein substrates, UIM motif is responsible for the binding to cullin RING ligases (CRLs), and UBX domain is essential for p97 binding.


Pssm-ID: 270530  Cd Length: 37  Bit Score: 34.15  E-value: 3.23e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1207164114   6 EAVRGFVAVTDVDEERARFFLESAGWDLQLALANFFE 42
Cdd:cd14345     1 ALIEQFTSITGADDTVARHMLEACNGNLEMAVNMHLD 37
 
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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