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Conserved domains on  [gi|6679100|ref|NP_032744|]
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Protein Classification

HLH and PAS domain-containing protein (domain architecture ID 11512610)

HLH and PAS domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
316-387 4.96e-13

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


:

Pssm-ID: 337058 [Multi-domain]  Cd Length: 89  Bit Score: 64.67  E-value: 4.96e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6679100    316 ILACESRVSDHMDMGPSELVGR--SCYQFVHGQDATRIRQSHLDLLDKGQVVTGYYRWLQRAGGFVWLQSVATV 387
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARP 74
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
141-198 1.48e-12

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


:

Pssm-ID: 214512  Cd Length: 67  Bit Score: 62.80  E-value: 1.48e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 6679100     141 HILQSLDGFVFALNQEGKFLYISETVSIYLGLSQVELTGSSVFDYIHPGDHSEVLEQL 198
Cdd:smart00091   5 AILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEAL 62
HLH cd00083
Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription ...
45-96 1.76e-10

Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription factors; 60-100 amino acids long. A DNA-binding basic region is followed by two alpha-helices separated by a variable loop region; HLH forms homo- and heterodimers, dimerization creates a parallel, left-handed, four helix bundle; the basic region N-terminal to the first amphipathic helix mediates high-affinity DNA-binding; there are several groups of HLH proteins: those (E12/E47) which bind specific hexanucleotide sequences such as E-box (5-CANNTG-3) or StRE 5-ATCACCCCAC-3), those lacking the basic domain (Emc, Id) function as negative regulators since they fail to bind DNA, those (hairy, E(spl), deadpan) which repress transcription although they can bind specific hexanucleotide sequences such as N-box (5-CACGc/aG-3), those which have a COE domain (Collier/Olf-1/EBF) which is involved in both in dimerization and in DNA binding, and those which bind pentanucleotides ACGTG or GCGTG and have a PAS domain which allows the dimerization between PAS proteins, the binding of small molecules (e.g., dioxin), and interactions with non-PAS proteins.


:

Pssm-ID: 238036  Cd Length: 60  Bit Score: 56.45  E-value: 1.76e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 6679100   45 QRKEKSRNAARWRRGKENLEFFELAKLLPLPgAISSQLDKASIVRLSVTYLR 96
Cdd:cd00083   3 SRREAHNLRERRRRERINDAFDELRSLLPTL-PPSKKLSKAEILRKAVDYIK 53
 
Name Accession Description Interval E-value
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
316-387 4.96e-13

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 337058 [Multi-domain]  Cd Length: 89  Bit Score: 64.67  E-value: 4.96e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6679100    316 ILACESRVSDHMDMGPSELVGR--SCYQFVHGQDATRIRQSHLDLLDKGQVVTGYYRWLQRAGGFVWLQSVATV 387
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARP 74
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
141-198 1.48e-12

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 62.80  E-value: 1.48e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 6679100     141 HILQSLDGFVFALNQEGKFLYISETVSIYLGLSQVELTGSSVFDYIHPGDHSEVLEQL 198
Cdd:smart00091   5 AILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEAL 62
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
304-405 4.44e-12

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 62.65  E-value: 4.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679100  304 HMIVFRLSLGLTILACESRVSDHMDMGPSELVGRSCYQFVHGQDATRIRQSHLDLLDKGQVVTGYYRWLQRAGGFVWLQS 383
Cdd:cd00130   2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLV 81
                        90       100
                ....*....|....*....|..
gi 6679100  384 VATVAGNGKSTGEHHVLWVSHV 405
Cdd:cd00130  82 SLTPIRDEGGEVIGLLGVVRDI 103
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
146-198 3.24e-11

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 59.95  E-value: 3.24e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 6679100  146 LDGFVFALNQEGKFLYISETVSIYLGLSQVELTGSSVFDYIHPGDHSEVLEQL 198
Cdd:cd00130   1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERL 53
HLH cd00083
Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription ...
45-96 1.76e-10

Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription factors; 60-100 amino acids long. A DNA-binding basic region is followed by two alpha-helices separated by a variable loop region; HLH forms homo- and heterodimers, dimerization creates a parallel, left-handed, four helix bundle; the basic region N-terminal to the first amphipathic helix mediates high-affinity DNA-binding; there are several groups of HLH proteins: those (E12/E47) which bind specific hexanucleotide sequences such as E-box (5-CANNTG-3) or StRE 5-ATCACCCCAC-3), those lacking the basic domain (Emc, Id) function as negative regulators since they fail to bind DNA, those (hairy, E(spl), deadpan) which repress transcription although they can bind specific hexanucleotide sequences such as N-box (5-CACGc/aG-3), those which have a COE domain (Collier/Olf-1/EBF) which is involved in both in dimerization and in DNA binding, and those which bind pentanucleotides ACGTG or GCGTG and have a PAS domain which allows the dimerization between PAS proteins, the binding of small molecules (e.g., dioxin), and interactions with non-PAS proteins.


Pssm-ID: 238036  Cd Length: 60  Bit Score: 56.45  E-value: 1.76e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 6679100   45 QRKEKSRNAARWRRGKENLEFFELAKLLPLPgAISSQLDKASIVRLSVTYLR 96
Cdd:cd00083   3 SRREAHNLRERRRRERINDAFDELRSLLPTL-PPSKKLSKAEILRKAVDYIK 53
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
141-198 2.99e-10

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 334337 [Multi-domain]  Cd Length: 112  Bit Score: 57.42  E-value: 2.99e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 6679100    141 HILQSLDGFVFALNQEGKFLYISETVSIYLGLSQVELTGSSVFDYIHPGDHSEVLEQL 198
Cdd:pfam00989   5 AILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEDDDAEVVELL 62
HLH smart00353
helix loop helix domain;
53-96 1.02e-08

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 51.45  E-value: 1.02e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 6679100      53 AARWRRGKENLEFFELAKLLPlPGAISSQLDKASIVRLSVTYLR 96
Cdd:smart00353   3 RERRRRRKINEAFDELRSLLP-TLPKNKKLSKAEILRLAIEYIK 45
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
296-360 2.28e-06

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 45.08  E-value: 2.28e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6679100     296 LAELPLHGHMIVFRLSLGLTILACESRVSDHMDMGPSELVGRSCYQFVHGQDATRIRQSHLDLLD 360
Cdd:smart00091   3 LRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
HLH pfam00010
Helix-loop-helix DNA-binding domain;
47-96 3.04e-04

Helix-loop-helix DNA-binding domain;


Pssm-ID: 333763  Cd Length: 52  Bit Score: 38.67  E-value: 3.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 6679100     47 KEKSRNAA-RWRRGKENLEFFELAKLLPLPGaiSSQLDKASIVRLSVTYLR 96
Cdd:pfam00010   1 RRRAHNEReRRRRDRINDAFDELRELLPTPP--SKKLSKAEILRLAIEYIK 49
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
142-201 3.13e-04

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 40.74  E-value: 3.13e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679100    142 ILQSLDGFVFALNQEGKFLYISETVSIYLGLSQVELTGSSVFDYIHPGDHSEVLEQLGLR 201
Cdd:TIGR00229   8 IFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERR 67
 
Name Accession Description Interval E-value
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
316-387 4.96e-13

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 337058 [Multi-domain]  Cd Length: 89  Bit Score: 64.67  E-value: 4.96e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6679100    316 ILACESRVSDHMDMGPSELVGR--SCYQFVHGQDATRIRQSHLDLLDKGQVVTGYYRWLQRAGGFVWLQSVATV 387
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARP 74
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
141-198 1.48e-12

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 62.80  E-value: 1.48e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 6679100     141 HILQSLDGFVFALNQEGKFLYISETVSIYLGLSQVELTGSSVFDYIHPGDHSEVLEQL 198
Cdd:smart00091   5 AILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEAL 62
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
304-405 4.44e-12

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 62.65  E-value: 4.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679100  304 HMIVFRLSLGLTILACESRVSDHMDMGPSELVGRSCYQFVHGQDATRIRQSHLDLLDKGQVVTGYYRWLQRAGGFVWLQS 383
Cdd:cd00130   2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLV 81
                        90       100
                ....*....|....*....|..
gi 6679100  384 VATVAGNGKSTGEHHVLWVSHV 405
Cdd:cd00130  82 SLTPIRDEGGEVIGLLGVVRDI 103
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
146-198 3.24e-11

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 59.95  E-value: 3.24e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 6679100  146 LDGFVFALNQEGKFLYISETVSIYLGLSQVELTGSSVFDYIHPGDHSEVLEQL 198
Cdd:cd00130   1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERL 53
HLH cd00083
Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription ...
45-96 1.76e-10

Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription factors; 60-100 amino acids long. A DNA-binding basic region is followed by two alpha-helices separated by a variable loop region; HLH forms homo- and heterodimers, dimerization creates a parallel, left-handed, four helix bundle; the basic region N-terminal to the first amphipathic helix mediates high-affinity DNA-binding; there are several groups of HLH proteins: those (E12/E47) which bind specific hexanucleotide sequences such as E-box (5-CANNTG-3) or StRE 5-ATCACCCCAC-3), those lacking the basic domain (Emc, Id) function as negative regulators since they fail to bind DNA, those (hairy, E(spl), deadpan) which repress transcription although they can bind specific hexanucleotide sequences such as N-box (5-CACGc/aG-3), those which have a COE domain (Collier/Olf-1/EBF) which is involved in both in dimerization and in DNA binding, and those which bind pentanucleotides ACGTG or GCGTG and have a PAS domain which allows the dimerization between PAS proteins, the binding of small molecules (e.g., dioxin), and interactions with non-PAS proteins.


Pssm-ID: 238036  Cd Length: 60  Bit Score: 56.45  E-value: 1.76e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 6679100   45 QRKEKSRNAARWRRGKENLEFFELAKLLPLPgAISSQLDKASIVRLSVTYLR 96
Cdd:cd00083   3 SRREAHNLRERRRRERINDAFDELRSLLPTL-PPSKKLSKAEILRKAVDYIK 53
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
141-198 2.99e-10

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 334337 [Multi-domain]  Cd Length: 112  Bit Score: 57.42  E-value: 2.99e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 6679100    141 HILQSLDGFVFALNQEGKFLYISETVSIYLGLSQVELTGSSVFDYIHPGDHSEVLEQL 198
Cdd:pfam00989   5 AILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEDDDAEVVELL 62
HLH smart00353
helix loop helix domain;
53-96 1.02e-08

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 51.45  E-value: 1.02e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 6679100      53 AARWRRGKENLEFFELAKLLPlPGAISSQLDKASIVRLSVTYLR 96
Cdd:smart00353   3 RERRRRRKINEAFDELRSLLP-TLPKNKKLSKAEILRLAIEYIK 45
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
296-360 2.28e-06

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 45.08  E-value: 2.28e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6679100     296 LAELPLHGHMIVFRLSLGLTILACESRVSDHMDMGPSELVGRSCYQFVHGQDATRIRQSHLDLLD 360
Cdd:smart00091   3 LRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAS_11 pfam14598
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ...
308-411 1.69e-04

PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), which binds to an LXXLL motif in the C-terminal region of STAT6 (Signal transducer and activator of transcription 6).


Pssm-ID: 317051 [Multi-domain]  Cd Length: 112  Bit Score: 41.12  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679100    308 FRLSLGLTILACES---RVSDHMDMGPSELVGRSCYQFVHGQDATRIRQSHLDLLDK-GQVVTGYYRWLQRAGGFVWLQS 383
Cdd:pfam14598   5 TRHDMDGKIISIDTsslRASFSLGLEKDELVGRSIYDLCHPQDLRTAKSHLREVIDSnGRATSSSYRLRLRDGDFVYVHT 84
                          90       100
                  ....*....|....*....|....*...
gi 6679100    384 VATVAGNGKSTGEHHVLWVSHVLSNAEG 411
Cdd:pfam14598  85 KSKLFRNQKTNEQDFIMCTHTILREEEG 112
HLH pfam00010
Helix-loop-helix DNA-binding domain;
47-96 3.04e-04

Helix-loop-helix DNA-binding domain;


Pssm-ID: 333763  Cd Length: 52  Bit Score: 38.67  E-value: 3.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 6679100     47 KEKSRNAA-RWRRGKENLEFFELAKLLPLPGaiSSQLDKASIVRLSVTYLR 96
Cdd:pfam00010   1 RRRAHNEReRRRRDRINDAFDELRELLPTPP--SKKLSKAEILRLAIEYIK 49
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
142-201 3.13e-04

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 40.74  E-value: 3.13e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679100    142 ILQSLDGFVFALNQEGKFLYISETVSIYLGLSQVELTGSSVFDYIHPGDHSEVLEQLGLR 201
Cdd:TIGR00229   8 IFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERR 67
 
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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