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Conserved domains on  [gi|501066859|ref|WP_012118046|]
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MULTISPECIES: DinB family protein [Bacillus]

Protein Classification

DinB family protein( domain architecture ID 10524297)

DinB family protein adopts a four-helix bundle structure and is encoded by a DNA damage-inducible (din) gene

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DinB pfam05163
DinB family; DNA damage-inducible (din) genes in Bacillus subtilis are coordinately regulated ...
 2-157 7.75e-46

DinB family; DNA damage-inducible (din) genes in Bacillus subtilis are coordinately regulated and together compose a global regulatory network that has been termed the SOS-like or SOB regulon. This family includes DinB from B. subtilis.


:

Pssm-ID: 398707  Cd Length: 163  Bit Score: 147.54  E-value: 7.75e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066859    2 FQTLDHFLKSWEFEADATQKLLNHLTDESLKQEITSQHWTLGRIAWHTVAAIHIITSNTDLTFHAPAEDYPVPASARFIA 81
Cdd:pfam05163   1 SQKLLELLQYNQWARDVTLDLLEALPDEDLKAEIGEGFQSVAQLLNHIVDVEHLWLRRFKGKEGTPQPDQNTERKDLEGA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501066859   82 ESYHQASNAFVQALKTQWTD---DTLQECVNFIGQQLPNGSLLMFLIQHQNHHRGQMTVLMRQAGLPVPGIYGPAKEEW 157
Cdd:pfam05163  81 DALRRALDALTAAFLQQLTEeerEELLDNPDGGGGKMTPAELLMHVINHETHHRGQITVLLRQLGHTPPATDYLRFEGN 159
 
Name Accession Description Interval E-value
DinB pfam05163
DinB family; DNA damage-inducible (din) genes in Bacillus subtilis are coordinately regulated ...
 2-157 7.75e-46

DinB family; DNA damage-inducible (din) genes in Bacillus subtilis are coordinately regulated and together compose a global regulatory network that has been termed the SOS-like or SOB regulon. This family includes DinB from B. subtilis.


Pssm-ID: 398707  Cd Length: 163  Bit Score: 147.54  E-value: 7.75e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066859    2 FQTLDHFLKSWEFEADATQKLLNHLTDESLKQEITSQHWTLGRIAWHTVAAIHIITSNTDLTFHAPAEDYPVPASARFIA 81
Cdd:pfam05163   1 SQKLLELLQYNQWARDVTLDLLEALPDEDLKAEIGEGFQSVAQLLNHIVDVEHLWLRRFKGKEGTPQPDQNTERKDLEGA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501066859   82 ESYHQASNAFVQALKTQWTD---DTLQECVNFIGQQLPNGSLLMFLIQHQNHHRGQMTVLMRQAGLPVPGIYGPAKEEW 157
Cdd:pfam05163  81 DALRRALDALTAAFLQQLTEeerEELLDNPDGGGGKMTPAELLMHVINHETHHRGQITVLLRQLGHTPPATDYLRFEGN 159
DinB COG2318
Bacillithiol/mycothiol S-transferase BstA/DinB, DinB/YfiT family (unrelated to E. coli DinB) ...
 8-147 9.68e-23

Bacillithiol/mycothiol S-transferase BstA/DinB, DinB/YfiT family (unrelated to E. coli DinB) [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441892  Cd Length: 145  Bit Score: 87.80  E-value: 9.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066859   8 FLKSWEFEADATQKLLNHLTDESLKQEITSQHWTLGRIAWHTVAAIHI-ITSNTDLTFHAPAEDYPVPASARFIAESYHQ 86
Cdd:COG2318    1 LLRYNEWANRRLLKALEALPEEELDWKPGAGFRSIGELLNHILVVDRIwLARLTGEPPPPAALDAELFPTLAELLAALEE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501066859  87 ASNAFVQALKtQWTDDTLQECVNFIGQQ----LPNGSLLMFLIQHQNHHRGQMTVLMRQAGLPVP 147
Cdd:COG2318   81 ADARLLEFLA-SLTDEDLDETVTFFSGDgegeMTRGEILLHVFNHETHHRGQLTVYLRQLGIEPP 144
IgI_1_Neogenin_like cd05722
First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of ...
 96-132 1.71e-03

First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409387  Cd Length: 97  Bit Score: 35.92  E-value: 1.71e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 501066859  96 KTQWTDD--TLQECVNFIGQQLPNGSLLMFLIQHQNHHR 132
Cdd:cd05722   32 KIEWKKDgvLLNLVSDERRQQLPNGSLLITSVVHSKHNK 70
 
Name Accession Description Interval E-value
DinB pfam05163
DinB family; DNA damage-inducible (din) genes in Bacillus subtilis are coordinately regulated ...
 2-157 7.75e-46

DinB family; DNA damage-inducible (din) genes in Bacillus subtilis are coordinately regulated and together compose a global regulatory network that has been termed the SOS-like or SOB regulon. This family includes DinB from B. subtilis.


Pssm-ID: 398707  Cd Length: 163  Bit Score: 147.54  E-value: 7.75e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066859    2 FQTLDHFLKSWEFEADATQKLLNHLTDESLKQEITSQHWTLGRIAWHTVAAIHIITSNTDLTFHAPAEDYPVPASARFIA 81
Cdd:pfam05163   1 SQKLLELLQYNQWARDVTLDLLEALPDEDLKAEIGEGFQSVAQLLNHIVDVEHLWLRRFKGKEGTPQPDQNTERKDLEGA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501066859   82 ESYHQASNAFVQALKTQWTD---DTLQECVNFIGQQLPNGSLLMFLIQHQNHHRGQMTVLMRQAGLPVPGIYGPAKEEW 157
Cdd:pfam05163  81 DALRRALDALTAAFLQQLTEeerEELLDNPDGGGGKMTPAELLMHVINHETHHRGQITVLLRQLGHTPPATDYLRFEGN 159
DinB COG2318
Bacillithiol/mycothiol S-transferase BstA/DinB, DinB/YfiT family (unrelated to E. coli DinB) ...
 8-147 9.68e-23

Bacillithiol/mycothiol S-transferase BstA/DinB, DinB/YfiT family (unrelated to E. coli DinB) [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441892  Cd Length: 145  Bit Score: 87.80  E-value: 9.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066859   8 FLKSWEFEADATQKLLNHLTDESLKQEITSQHWTLGRIAWHTVAAIHI-ITSNTDLTFHAPAEDYPVPASARFIAESYHQ 86
Cdd:COG2318    1 LLRYNEWANRRLLKALEALPEEELDWKPGAGFRSIGELLNHILVVDRIwLARLTGEPPPPAALDAELFPTLAELLAALEE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501066859  87 ASNAFVQALKtQWTDDTLQECVNFIGQQ----LPNGSLLMFLIQHQNHHRGQMTVLMRQAGLPVP 147
Cdd:COG2318   81 ADARLLEFLA-SLTDEDLDETVTFFSGDgegeMTRGEILLHVFNHETHHRGQLTVYLRQLGIEPP 144
DinB_2 pfam12867
DinB superfamily; The DinB family are an uncharacterized family of potential enzymes. The ...
 12-135 1.71e-05

DinB superfamily; The DinB family are an uncharacterized family of potential enzymes. The structure of these proteins is composed of a four helix bundle.


Pssm-ID: 463733  Cd Length: 128  Bit Score: 42.06  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501066859   12 WEFEADATQKLLNHLTDESLKQEITSQHWTLGRIAWHTVAAIHIIT--SNTDLTFHAPAEDYPVPASARFIAEsYHQASN 89
Cdd:pfam12867   2 LERARARLLALLEGLPDEELNWRPAPGKWSIAWLLGHLADVEEVLLarLRLGEEAPRPAYDPGEPPSAAELLA-YLAAVR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 501066859   90 AFVQALKTQWTDDTLQECV--NFIGQQLPNGSLLMFLIQHQNHHRGQM 135
Cdd:pfam12867  81 ARLLALLAALTDADLARPVtaPPGLGKLTLGELLLFVAAHEAHHLGQI 128
IgI_1_Neogenin_like cd05722
First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of ...
 96-132 1.71e-03

First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409387  Cd Length: 97  Bit Score: 35.92  E-value: 1.71e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 501066859  96 KTQWTDD--TLQECVNFIGQQLPNGSLLMFLIQHQNHHR 132
Cdd:cd05722   32 KIEWKKDgvLLNLVSDERRQQLPNGSLLITSVVHSKHNK 70
 
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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