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Conserved domains on  [gi|442616464|ref|NP_001259579|]
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magnetic receptor, isoform B [Drosophila melanogaster]

Protein Classification

HesB/IscA family protein( domain architecture ID 10001059)

HesB/IscA family protein is a scaffold protein upon which 2Fe-2S clusters are assembled and subsequently transferred to acceptor proteins; similar to iron-sulfur assembly protein IscA that is involved in the maturation of mitochondrial 4Fe-4S proteins functioning late in the iron-sulfur cluster assembly pathway

Gene Ontology:  GO:0016226|GO:0051536
PubMed:  32108236

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IscA COG0316
Fe-S cluster assembly iron-binding protein IscA [Posttranslational modification, protein ...
 25-131 6.24e-47

Fe-S cluster assembly iron-binding protein IscA [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440085 [Multi-domain]  Cd Length: 107  Bit Score: 146.84  E-value: 6.24e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616464  25 ALTLTPAAVLRIKTLL-QDKPDMVGLKVGVRQRGCNGLSYTLDYASQKADKlDEEVVQDGVKVFIDKKAQLSLLGTEMDF 103
Cdd:COG0316    1 PITLTDAAAKRIKRLLaKEGNPGLGLRVGVKGGGCSGFSYGLDFDDEPNED-DLVFEQDGVKVVVDPKSLPYLDGTEIDY 79

                         90       100
                 ....*....|....*....|....*...
gi 442616464 104 VESKLSSEFVFNNPNIKGTCGCGESFSM 131
Cdd:COG0316   80 VEELLGSGFKFNNPNAKSSCGCGESFSV 107
 
Name Accession Description Interval E-value
IscA COG0316
Fe-S cluster assembly iron-binding protein IscA [Posttranslational modification, protein ...
 25-131 6.24e-47

Fe-S cluster assembly iron-binding protein IscA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440085 [Multi-domain]  Cd Length: 107  Bit Score: 146.84  E-value: 6.24e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616464  25 ALTLTPAAVLRIKTLL-QDKPDMVGLKVGVRQRGCNGLSYTLDYASQKADKlDEEVVQDGVKVFIDKKAQLSLLGTEMDF 103
Cdd:COG0316    1 PITLTDAAAKRIKRLLaKEGNPGLGLRVGVKGGGCSGFSYGLDFDDEPNED-DLVFEQDGVKVVVDPKSLPYLDGTEIDY 79

                         90       100
                 ....*....|....*....|....*...
gi 442616464 104 VESKLSSEFVFNNPNIKGTCGCGESFSM 131
Cdd:COG0316   80 VEELLGSGFKFNNPNAKSSCGCGESFSV 107
TIGR00049 TIGR00049
Iron-sulfur cluster assembly accessory protein; Proteins in this subfamily appear to be ...
 27-130 1.61e-46

Iron-sulfur cluster assembly accessory protein; Proteins in this subfamily appear to be associated with the process of FeS-cluster assembly. The HesB proteins are associated with the nif gene cluster and the Rhizobium gene IscN has been shown to be required for nitrogen fixation. Nitrogenase includes multiple FeS clusters and many genes for their assembly. The E. coli SufA protein is associated with SufS, a NifS homolog and SufD which are involved in the FeS cluster assembly of the FhnF protein. The Azotobacter protein IscA (homologs of which are also found in E.coli) is associated which IscS, another NifS homolog and IscU, a nifU homolog as well as other factors consistent with a role in FeS cluster chemistry. A homolog from Geobacter contains a selenocysteine in place of an otherwise invariant cysteine, further suggesting a role in redox chemistry. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 272875 [Multi-domain]  Cd Length: 105  Bit Score: 145.80  E-value: 1.61e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616464   27 TLTPAAVLRIKTLLQDKPDMV-GLKVGVRQRGCNGLSYTLDYASqKADKLDEEVVQDGVKVFIDKKAQLSLLGTEMDFVE 105
Cdd:TIGR00049   1 TLTDSAAKRIKALLAGEGEPNlGLRVGVKGGGCSGLQYGLEFDD-EPNEDDEVFEQDGVKVVVDPKSLPYLDGSEIDYVE 79

                          90       100
                  ....*....|....*....|....*
gi 442616464  106 SKLSSEFVFNNPNIKGTCGCGESFS 130
Cdd:TIGR00049  80 ELLGSGFTFTNPNAKGTCGCGKSFS 104
sufA PRK09504
iron-sulfur cluster assembly scaffold protein; Provisional
 26-129 3.08e-30

iron-sulfur cluster assembly scaffold protein; Provisional


Pssm-ID: 181915  Cd Length: 122  Bit Score: 105.20  E-value: 3.08e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616464  26 LTLTPAAVLRIKTLLQDKPDMVGLKVGVRQRGCNGLSYTLDYASQKADklDEEVV-QDGVKVFIDKKAQLSLLGTEMDFV 104
Cdd:PRK09504  18 LTLTPAAAAHIRELMAKQPGMKGVRLGVKQTGCAGFGYVLDSVSEPDK--DDLVFeHDGAKLFVPLQAMPFIDGTEVDYV 95

                         90       100
                 ....*....|....*....|....*
gi 442616464 105 ESKLSSEFVFNNPNIKGTCGCGESF 129
Cdd:PRK09504  96 REGLNQIFKFHNPKAQNECGCGESF 120
Fe-S_biosyn pfam01521
Iron-sulphur cluster biosynthesis; This family is involved in iron-sulphur cluster ...
 26-127 2.48e-19

Iron-sulphur cluster biosynthesis; This family is involved in iron-sulphur cluster biosynthesis. Its members include proteins that are involved in nitrogen fixation such as the HesB and HesB-like proteins.


Pssm-ID: 426304  Cd Length: 111  Bit Score: 76.92  E-value: 2.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616464   26 LTLTPAAVLRIKTLLQDKPDMVGLKV----GVRQRGC--NGLSYTLDYASQKADKLDEEVVQDGVKVFIDKKAQLSLL-G 98
Cdd:pfam01521   3 ITITDAAAERLKKLLAGDKKELRLDVddggGPYSKGGcsIGGKFSLVLVDEPDPDYDEVIESNGGPIYVDSYSLPFLDeG 82

                          90       100
                  ....*....|....*....|....*....
gi 442616464   99 TEMDFVESKLSSEFVFNNPNIKGTCGCGE 127
Cdd:pfam01521  83 LTLDFVEDLGTLGLKSDNGNLDGNVGCGD 111
IscA_HesB_Se NF038090
IscA/HesB family protein; Members of this family, a large fraction of which are selenoproteins, ...
 26-125 1.38e-04

IscA/HesB family protein; Members of this family, a large fraction of which are selenoproteins, are homologous to proteins of iron-sulfur cluster biosynthesis such as IscA, and belong to the broader set of HesB-related proteins.


Pssm-ID: 411672  Cd Length: 99  Bit Score: 38.46  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616464  26 LTLTPAAVLRIKTLLQDKPDMVGLKVGVRQRGCNGLSYTLDYASQKADklDEEVVQDGVKVFIDKkaqlSLLGT----EM 101
Cdd:NF038090   2 LEVTDLASRKLKEYFADKKIDSPIRVFLNQGGUAGPSLGLALDEPKEN--DEVFEQDGLTFVIDK----ELLEQcgpiKV 75

                         90       100
                 ....*....|....*....|....
gi 442616464 102 DFVESKLSSEFVFNNPNIKGTCGC 125
Cdd:NF038090  76 DFIDCRSGFSITSSMPLGGGGCGS 99
PBP2_iGluR_Kainate_GluR6 cd13721
GluR6 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
 17-116 2.78e-03

GluR6 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group contains glutamate receptor domain GluR. These domains are found in the GluR proteins that have been shown to function as L-glutamate activated potassium channels, also known ionotropic glutamate receptors or iGluRs. In addition to two ligand binding core domains, iGluRs typically have a channel-like domain inserted in the middle of the GluR-like domain. Animal iGluRs mediate the ion flux in the synapses of the CNS and can be subdivided into several classes depending on the neurotransmitter specificity and ion conductance properties. Their plant homologs have been shown to function in light signal transduction and calcium homeostasis. The GluR proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270439 [Multi-domain]  Cd Length: 251  Bit Score: 36.15  E-value: 2.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616464  17 RKLIPTRAALTLTPAAVLRIKTLLQD--KPDMVgLKVGVRQRGCNGLSYTLDYASQKadKLDEEVVQDGVKVFIDKKAQL 94
Cdd:cd13721   74 RELIDHKADLAVAPLAITYVREKVIDfsKPFMT-LGISILYRKGTPIDSADDLAKQT--KIEYGAVEDGATMTFFKKSKI 150

                         90       100
                 ....*....|....*....|..
gi 442616464  95 SLLGTEMDFVESKLSSEFVFNN 116
Cdd:cd13721  151 STYDKMWAFMSSRRQSVLVKSN 172
 
Name Accession Description Interval E-value
IscA COG0316
Fe-S cluster assembly iron-binding protein IscA [Posttranslational modification, protein ...
 25-131 6.24e-47

Fe-S cluster assembly iron-binding protein IscA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440085 [Multi-domain]  Cd Length: 107  Bit Score: 146.84  E-value: 6.24e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616464  25 ALTLTPAAVLRIKTLL-QDKPDMVGLKVGVRQRGCNGLSYTLDYASQKADKlDEEVVQDGVKVFIDKKAQLSLLGTEMDF 103
Cdd:COG0316    1 PITLTDAAAKRIKRLLaKEGNPGLGLRVGVKGGGCSGFSYGLDFDDEPNED-DLVFEQDGVKVVVDPKSLPYLDGTEIDY 79

                         90       100
                 ....*....|....*....|....*...
gi 442616464 104 VESKLSSEFVFNNPNIKGTCGCGESFSM 131
Cdd:COG0316   80 VEELLGSGFKFNNPNAKSSCGCGESFSV 107
TIGR00049 TIGR00049
Iron-sulfur cluster assembly accessory protein; Proteins in this subfamily appear to be ...
 27-130 1.61e-46

Iron-sulfur cluster assembly accessory protein; Proteins in this subfamily appear to be associated with the process of FeS-cluster assembly. The HesB proteins are associated with the nif gene cluster and the Rhizobium gene IscN has been shown to be required for nitrogen fixation. Nitrogenase includes multiple FeS clusters and many genes for their assembly. The E. coli SufA protein is associated with SufS, a NifS homolog and SufD which are involved in the FeS cluster assembly of the FhnF protein. The Azotobacter protein IscA (homologs of which are also found in E.coli) is associated which IscS, another NifS homolog and IscU, a nifU homolog as well as other factors consistent with a role in FeS cluster chemistry. A homolog from Geobacter contains a selenocysteine in place of an otherwise invariant cysteine, further suggesting a role in redox chemistry. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 272875 [Multi-domain]  Cd Length: 105  Bit Score: 145.80  E-value: 1.61e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616464   27 TLTPAAVLRIKTLLQDKPDMV-GLKVGVRQRGCNGLSYTLDYASqKADKLDEEVVQDGVKVFIDKKAQLSLLGTEMDFVE 105
Cdd:TIGR00049   1 TLTDSAAKRIKALLAGEGEPNlGLRVGVKGGGCSGLQYGLEFDD-EPNEDDEVFEQDGVKVVVDPKSLPYLDGSEIDYVE 79

                          90       100
                  ....*....|....*....|....*
gi 442616464  106 SKLSSEFVFNNPNIKGTCGCGESFS 130
Cdd:TIGR00049  80 ELLGSGFTFTNPNAKGTCGCGKSFS 104
sufA_proteo TIGR01997
FeS assembly scaffold SufA; This model represents the SufA protein of the SUF system of ...
 24-131 2.41e-36

FeS assembly scaffold SufA; This model represents the SufA protein of the SUF system of iron-sulfur cluster biosynthesis. This system performs FeS biosynthesis even during oxidative stress and tends to be absent in obligate anaerobic and microaerophilic bacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 131052  Cd Length: 107  Bit Score: 120.32  E-value: 2.41e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616464   24 AALTLTPAAVLRIKTLLQDKPDMVGLKVGVRQRGCNGLSYTLDYASQkADKLDEEVVQDGVKVFIDKKAQLSLLGTEMDF 103
Cdd:TIGR01997   1 AVITLTDAAAIHIRELVAKRPEAVGIRLGVKKTGCAGMEYVLDLVSE-PKKDDDLIEHDGAKVFVAPEAVLFILGTQVDF 79

                          90       100
                  ....*....|....*....|....*...
gi 442616464  104 VESKLSSEFVFNNPNIKGTCGCGESFSM 131
Cdd:TIGR01997  80 VRTTLRQGFKFNNPNATSACGCGESFEL 107
sufA PRK09504
iron-sulfur cluster assembly scaffold protein; Provisional
 26-129 3.08e-30

iron-sulfur cluster assembly scaffold protein; Provisional


Pssm-ID: 181915  Cd Length: 122  Bit Score: 105.20  E-value: 3.08e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616464  26 LTLTPAAVLRIKTLLQDKPDMVGLKVGVRQRGCNGLSYTLDYASQKADklDEEVV-QDGVKVFIDKKAQLSLLGTEMDFV 104
Cdd:PRK09504  18 LTLTPAAAAHIRELMAKQPGMKGVRLGVKQTGCAGFGYVLDSVSEPDK--DDLVFeHDGAKLFVPLQAMPFIDGTEVDYV 95

                         90       100
                 ....*....|....*....|....*
gi 442616464 105 ESKLSSEFVFNNPNIKGTCGCGESF 129
Cdd:PRK09504  96 REGLNQIFKFHNPKAQNECGCGESF 120
IscA TIGR02011
iron-sulfur cluster assembly protein IscA; This model represents the IscA component of the ISC ...
 26-131 1.86e-28

iron-sulfur cluster assembly protein IscA; This model represents the IscA component of the ISC system for iron-sulfur cluster assembly. The ISC system consists of IscRASU, HscAB and an Isc-specific ferredoxin. IscA previously was believed to act as a scaffold and now is seen as an iron donor protein. This clade is limited to the proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 213674  Cd Length: 105  Bit Score: 99.90  E-value: 1.86e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616464   26 LTLTPAAVLRIKTLLQDKPDMVGLKVGVRQRGCNGLSYTLDYASQKADklDEEVVQ-DGVKVFIDKKAQLSLLGTEMDFV 104
Cdd:TIGR02011   1 ITLTDSAAARVNTFLANRGKGFGLRLGVKTSGCSGMAYVLEFVDEPTP--DDIVFEdKGVKIVIDGKSLQYLDGTQLDFV 78

                          90       100
                  ....*....|....*....|....*..
gi 442616464  105 ESKLSSEFVFNNPNIKGTCGCGESFSM 131
Cdd:TIGR02011  79 KEGLNEGFKFTNPNVKDECGCGESFHV 105
iscA PRK09502
iron-sulfur cluster assembly protein IscA;
25-131 5.24e-28

iron-sulfur cluster assembly protein IscA;


Pssm-ID: 181914 [Multi-domain]  Cd Length: 107  Bit Score: 99.17  E-value: 5.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616464  25 ALTLTPAAVLRIKTLLQDKPDMVGLKVGVRQRGCNGLSYTLDYASQKADklDEEVVQD-GVKVFIDKKAQLSLLGTEMDF 103
Cdd:PRK09502   2 SITLSDSAAARVNTFLANRGKGFGLRLGVRTSGCSGMAYVLEFVDEPTP--EDIVFEDkGVKVVVDGKSLQFLDGTQLDF 79

                         90       100
                 ....*....|....*....|....*...
gi 442616464 104 VESKLSSEFVFNNPNIKGTCGCGESFSM 131
Cdd:PRK09502  80 VKEGLNEGFKFTNPNVKDECGCGESFHV 107
PRK13623 PRK13623
iron-sulfur cluster insertion protein ErpA; Provisional
 24-131 8.42e-20

iron-sulfur cluster insertion protein ErpA; Provisional


Pssm-ID: 184186  Cd Length: 115  Bit Score: 78.43  E-value: 8.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616464  24 AALTLTPAAVLRIKTLL--QDKPDmVGLKVGVRQRGCNGLSYTLDYASQKADKlDEEVVQDGVKVFIDKKAQLSLLGTEM 101
Cdd:PRK13623   8 LPLVFTDAAAAKVKELIeeEGNPD-LKLRVYITGGGCSGFQYGFTFDEQVNED-DTTIEKQGVTLVVDPMSLQYLVGAEV 85

                         90       100       110
                 ....*....|....*....|....*....|
gi 442616464 102 DFVESKLSSEFVFNNPNIKGTCGCGESFSM 131
Cdd:PRK13623  86 DYTEGLEGSRFVIKNPNAKTTCGCGSSFSI 115
Fe-S_biosyn pfam01521
Iron-sulphur cluster biosynthesis; This family is involved in iron-sulphur cluster ...
 26-127 2.48e-19

Iron-sulphur cluster biosynthesis; This family is involved in iron-sulphur cluster biosynthesis. Its members include proteins that are involved in nitrogen fixation such as the HesB and HesB-like proteins.


Pssm-ID: 426304  Cd Length: 111  Bit Score: 76.92  E-value: 2.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616464   26 LTLTPAAVLRIKTLLQDKPDMVGLKV----GVRQRGC--NGLSYTLDYASQKADKLDEEVVQDGVKVFIDKKAQLSLL-G 98
Cdd:pfam01521   3 ITITDAAAERLKKLLAGDKKELRLDVddggGPYSKGGcsIGGKFSLVLVDEPDPDYDEVIESNGGPIYVDSYSLPFLDeG 82

                          90       100
                  ....*....|....*....|....*....
gi 442616464   99 TEMDFVESKLSSEFVFNNPNIKGTCGCGE 127
Cdd:pfam01521  83 LTLDFVEDLGTLGLKSDNGNLDGNVGCGD 111
PLN03082 PLN03082
Iron-sulfur cluster assembly; Provisional
 25-129 3.75e-10

Iron-sulfur cluster assembly; Provisional


Pssm-ID: 215564  Cd Length: 163  Bit Score: 54.55  E-value: 3.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616464  25 ALTLTPAAVLRIKTLLQDKPDMVG--LKVGVRQRGCNGLSYT--LDYASQKADKLDEevvQDGVKVFIDKKAQLSLLGTE 100
Cdd:PLN03082  54 AVHMTDNCIRRLKELQTSEPSAEDkmLRLSVETGGCSGFQYVfeLDDKTNSDDRVFE---KDGVKLVVDNISYDFVKGAT 130

                         90       100       110
                 ....*....|....*....|....*....|
gi 442616464 101 MDFVESKLSSEFVFN-NPNIKGTCGCGESF 129
Cdd:PLN03082 131 VDYVEELIRSAFVVStNPSAVGGCSCKSSF 160
IscA_HesB_Se NF038090
IscA/HesB family protein; Members of this family, a large fraction of which are selenoproteins, ...
 26-125 1.38e-04

IscA/HesB family protein; Members of this family, a large fraction of which are selenoproteins, are homologous to proteins of iron-sulfur cluster biosynthesis such as IscA, and belong to the broader set of HesB-related proteins.


Pssm-ID: 411672  Cd Length: 99  Bit Score: 38.46  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616464  26 LTLTPAAVLRIKTLLQDKPDMVGLKVGVRQRGCNGLSYTLDYASQKADklDEEVVQDGVKVFIDKkaqlSLLGT----EM 101
Cdd:NF038090   2 LEVTDLASRKLKEYFADKKIDSPIRVFLNQGGUAGPSLGLALDEPKEN--DEVFEQDGLTFVIDK----ELLEQcgpiKV 75

                         90       100
                 ....*....|....*....|....
gi 442616464 102 DFVESKLSSEFVFNNPNIKGTCGC 125
Cdd:NF038090  76 DFIDCRSGFSITSSMPLGGGGCGS 99
PBP2_iGluR_Kainate_GluR6 cd13721
GluR6 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
 17-116 2.78e-03

GluR6 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group contains glutamate receptor domain GluR. These domains are found in the GluR proteins that have been shown to function as L-glutamate activated potassium channels, also known ionotropic glutamate receptors or iGluRs. In addition to two ligand binding core domains, iGluRs typically have a channel-like domain inserted in the middle of the GluR-like domain. Animal iGluRs mediate the ion flux in the synapses of the CNS and can be subdivided into several classes depending on the neurotransmitter specificity and ion conductance properties. Their plant homologs have been shown to function in light signal transduction and calcium homeostasis. The GluR proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270439 [Multi-domain]  Cd Length: 251  Bit Score: 36.15  E-value: 2.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616464  17 RKLIPTRAALTLTPAAVLRIKTLLQD--KPDMVgLKVGVRQRGCNGLSYTLDYASQKadKLDEEVVQDGVKVFIDKKAQL 94
Cdd:cd13721   74 RELIDHKADLAVAPLAITYVREKVIDfsKPFMT-LGISILYRKGTPIDSADDLAKQT--KIEYGAVEDGATMTFFKKSKI 150

                         90       100
                 ....*....|....*....|..
gi 442616464  95 SLLGTEMDFVESKLSSEFVFNN 116
Cdd:cd13721  151 STYDKMWAFMSSRRQSVLVKSN 172
 
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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