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Conserved domains on  [gi|1901933175|dbj|GGR87280|]
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hypothetical protein GCM10008960_13100 [Deinococcus sedimenti]

Protein Classification

PRK13918 family protein( domain architecture ID 11486949)

PRK13918 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK13918 PRK13918
CRP/FNR family transcriptional regulator; Provisional
8-194 5.58e-124

CRP/FNR family transcriptional regulator; Provisional


:

Pssm-ID: 237557 [Multi-domain]  Cd Length: 202  Bit Score: 348.35  E-value: 5.58e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933175   8 ARTFVDTVTYRPGAVILYPG---KSDMLYRVSTGLVRVHTMDDDGNGLTLRYVKPGEYFGEEALAGVNRAYFAEAVTDSS 84
Cdd:PRK13918    2 STTVVDTVTYRPGAVILYPGvpgPSDMLYRVRSGLVRLHTVDDEGNALTLRYVRPGEYFGEEALAGAERAYFAEAVTDSR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933175  85 IDVINPALMSAEDNLHVTTHLVRTLERAYESIYRLVGKRLRARIAGELLELKDTALATQLDSGETMIYATHDELAAAVGS 164
Cdd:PRK13918   82 IDVLNPALMSAEDNLVLTQHLVRTLARAYESIYRLVGQRLKNRIAAALLELSDTPLATQEDSGETMIYATHDELAAAVGS 161
                         170       180       190
                  ....*....|....*....|....*....|
gi 1901933175 165 VRETVTKVVGELSREGVISAGYGKITLKNE 194
Cdd:PRK13918  162 VRETVTKVIGELSREGYIRSGYGKIQLLDL 191
 
Name Accession Description Interval E-value
PRK13918 PRK13918
CRP/FNR family transcriptional regulator; Provisional
8-194 5.58e-124

CRP/FNR family transcriptional regulator; Provisional


Pssm-ID: 237557 [Multi-domain]  Cd Length: 202  Bit Score: 348.35  E-value: 5.58e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933175   8 ARTFVDTVTYRPGAVILYPG---KSDMLYRVSTGLVRVHTMDDDGNGLTLRYVKPGEYFGEEALAGVNRAYFAEAVTDSS 84
Cdd:PRK13918    2 STTVVDTVTYRPGAVILYPGvpgPSDMLYRVRSGLVRLHTVDDEGNALTLRYVRPGEYFGEEALAGAERAYFAEAVTDSR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933175  85 IDVINPALMSAEDNLHVTTHLVRTLERAYESIYRLVGKRLRARIAGELLELKDTALATQLDSGETMIYATHDELAAAVGS 164
Cdd:PRK13918   82 IDVLNPALMSAEDNLVLTQHLVRTLARAYESIYRLVGQRLKNRIAAALLELSDTPLATQEDSGETMIYATHDELAAAVGS 161
                         170       180       190
                  ....*....|....*....|....*....|
gi 1901933175 165 VRETVTKVVGELSREGVISAGYGKITLKNE 194
Cdd:PRK13918  162 VRETVTKVIGELSREGYIRSGYGKIQLLDL 191
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
14-193 3.88e-31

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 112.77  E-value: 3.88e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933175  14 TVTYRPGAVILYPG-KSDMLYRVSTGLVRVHTMDDDGNGLTLRYVKPGEYFGEEA-LAGVNRAYFAEAVTDSSIDVINPA 91
Cdd:COG0664    18 LRTLKKGEVLFREGdPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSlLGGEPSPATAEALEDSELLRIPRE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933175  92 LMSA--EDNLHVTTHLVRTLER----AYESIYRLVGKRLRARIAGELLELKDTAlatqldSGETMIYATHDELAAAVGSV 165
Cdd:COG0664    98 DLEEllERNPELARALLRLLARrlrqLQERLVSLAFLSAEERLARFLLELADRL------DGRIDLPLTQEEIASYLGLT 171
                         170       180
                  ....*....|....*....|....*...
gi 1901933175 166 RETVTKVVGELSREGVISAGYGKITLKN 193
Cdd:COG0664   172 RETVSRILKKLEKEGLIELERGRITILD 199
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
12-89 9.96e-14

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 64.65  E-value: 9.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933175  12 VDTVTYRPGAVILYPG-KSDMLYRVSTGLVRVHTMDDDGNGLTLRYVKPGEYFGEEALAGVN-RAYFAEAVTDSSIDVIN 89
Cdd:cd00038    17 LEERRFPAGEVIIRQGdPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGpRSATVRALTDSELLVLP 96
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
15-85 3.85e-11

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 57.23  E-value: 3.85e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1901933175  15 VTYRPGAVILYPG-KSDMLYRVSTGLVRVHTMDDDGNGLTLRYVKPGEYFGEEAL-AGVNRAYFAEAVTDSSI 85
Cdd:pfam00027   2 RSYKAGEVIFREGdPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALlGGEPRSATVVALTDSEL 74
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
12-88 1.95e-09

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 53.17  E-value: 1.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933175   12 VDTVTYRPGAVILYPG-KSDMLYRVSTGLVRVHTMDDDGNGLTLRYVKPGEYFGEEALAGVNRAYF---AEAVTDSSIDV 87
Cdd:smart00100  17 LEPVRYPAGEVIIRQGdVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRRAAsaaAVALELATLLR 96

                   .
gi 1901933175   88 I 88
Cdd:smart00100  97 I 97
 
Name Accession Description Interval E-value
PRK13918 PRK13918
CRP/FNR family transcriptional regulator; Provisional
8-194 5.58e-124

CRP/FNR family transcriptional regulator; Provisional


Pssm-ID: 237557 [Multi-domain]  Cd Length: 202  Bit Score: 348.35  E-value: 5.58e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933175   8 ARTFVDTVTYRPGAVILYPG---KSDMLYRVSTGLVRVHTMDDDGNGLTLRYVKPGEYFGEEALAGVNRAYFAEAVTDSS 84
Cdd:PRK13918    2 STTVVDTVTYRPGAVILYPGvpgPSDMLYRVRSGLVRLHTVDDEGNALTLRYVRPGEYFGEEALAGAERAYFAEAVTDSR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933175  85 IDVINPALMSAEDNLHVTTHLVRTLERAYESIYRLVGKRLRARIAGELLELKDTALATQLDSGETMIYATHDELAAAVGS 164
Cdd:PRK13918   82 IDVLNPALMSAEDNLVLTQHLVRTLARAYESIYRLVGQRLKNRIAAALLELSDTPLATQEDSGETMIYATHDELAAAVGS 161
                         170       180       190
                  ....*....|....*....|....*....|
gi 1901933175 165 VRETVTKVVGELSREGVISAGYGKITLKNE 194
Cdd:PRK13918  162 VRETVTKVIGELSREGYIRSGYGKIQLLDL 191
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
14-193 3.88e-31

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 112.77  E-value: 3.88e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933175  14 TVTYRPGAVILYPG-KSDMLYRVSTGLVRVHTMDDDGNGLTLRYVKPGEYFGEEA-LAGVNRAYFAEAVTDSSIDVINPA 91
Cdd:COG0664    18 LRTLKKGEVLFREGdPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSlLGGEPSPATAEALEDSELLRIPRE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933175  92 LMSA--EDNLHVTTHLVRTLER----AYESIYRLVGKRLRARIAGELLELKDTAlatqldSGETMIYATHDELAAAVGSV 165
Cdd:COG0664    98 DLEEllERNPELARALLRLLARrlrqLQERLVSLAFLSAEERLARFLLELADRL------DGRIDLPLTQEEIASYLGLT 171
                         170       180
                  ....*....|....*....|....*...
gi 1901933175 166 RETVTKVVGELSREGVISAGYGKITLKN 193
Cdd:COG0664   172 RETVSRILKKLEKEGLIELERGRITILD 199
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
12-89 9.96e-14

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 64.65  E-value: 9.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933175  12 VDTVTYRPGAVILYPG-KSDMLYRVSTGLVRVHTMDDDGNGLTLRYVKPGEYFGEEALAGVN-RAYFAEAVTDSSIDVIN 89
Cdd:cd00038    17 LEERRFPAGEVIIRQGdPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGpRSATVRALTDSELLVLP 96
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
15-85 3.85e-11

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 57.23  E-value: 3.85e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1901933175  15 VTYRPGAVILYPG-KSDMLYRVSTGLVRVHTMDDDGNGLTLRYVKPGEYFGEEAL-AGVNRAYFAEAVTDSSI 85
Cdd:pfam00027   2 RSYKAGEVIFREGdPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALlGGEPRSATVVALTDSEL 74
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
17-188 9.41e-11

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 58.84  E-value: 9.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933175  17 YRPGAVILYPG-KSDMLYRVSTGLVRVHTMDDDGNGLTLRYVKPGEYFGEEAL--AGVNRAYFAEAVTDSSIDVI----- 88
Cdd:PRK11753   25 YPAKSTLIHAGeKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLfeEGQERSAWVRAKTACEVAEIsykkf 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933175  89 ------NPALMSAednlhVTTHLVRTLERAYESIYRLVGKRLRARIAGELLELKDTALATQLDSGeTMIYATHDELAAAV 162
Cdd:PRK11753  105 rqliqvNPDILMA-----LSAQMARRLQNTSRKVGDLAFLDVTGRIAQTLLDLAKQPDAMTHPDG-MQIKITRQEIGRIV 178
                         170       180
                  ....*....|....*....|....*.
gi 1901933175 163 GSVRETVTKVVGELSREGVISAgYGK 188
Cdd:PRK11753  179 GCSREMVGRVLKMLEDQGLISA-HGK 203
HTH_Crp_2 pfam13545
Crp-like helix-turn-helix domain; This family represents a crp-like helix-turn-helix domain ...
126-194 1.53e-09

Crp-like helix-turn-helix domain; This family represents a crp-like helix-turn-helix domain that is likely to bind DNA.


Pssm-ID: 463917 [Multi-domain]  Cd Length: 68  Bit Score: 52.07  E-value: 1.53e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1901933175 126 ARIAGELLELkdtalATQLDSGETMIYATHDELAAAVGSVRETVTKVVGELSREGVISagYGKITLKNE 194
Cdd:pfam13545   1 QRLARFLLEL-----AARDGGGRIDLPLTQEDLADLLGTTRETVSRVLSELRREGLIE--RGRITILDP 62
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
12-88 1.95e-09

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 53.17  E-value: 1.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933175   12 VDTVTYRPGAVILYPG-KSDMLYRVSTGLVRVHTMDDDGNGLTLRYVKPGEYFGEEALAGVNRAYF---AEAVTDSSIDV 87
Cdd:smart00100  17 LEPVRYPAGEVIIRQGdVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRRAAsaaAVALELATLLR 96

                   .
gi 1901933175   88 I 88
Cdd:smart00100  97 I 97
fixK PRK09391
transcriptional regulator FixK; Provisional
5-182 1.18e-07

transcriptional regulator FixK; Provisional


Pssm-ID: 236494 [Multi-domain]  Cd Length: 230  Bit Score: 50.42  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933175   5 TRTARTFVDTVTYRPGAVILYPG-KSDMLYRVSTGLVRVHTMDDDGNGLTLRYVKPGEYFGEEalAGVNRAYFAEAVTDS 83
Cdd:PRK09391   31 SGHAGLVASEFSYKKGEEIYGEGePADYVYQVESGAVRTYRLLSDGRRQIGAFHLPGDVFGLE--SGSTHRFTAEAIVDT 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933175  84 SIDVIN-PAL-MSAEDNLHVTTHLVR----TLERAYESIYRLVGKRLRARIAGELLEL-KDTALATQLDsgetmIYATHD 156
Cdd:PRK09391  109 TVRLIKrRSLeQAAATDVDVARALLSltagGLRHAQDHMLLLGRKTAMERVAAFLLEMdERLGGAGMMA-----LPMSRR 183
                         170       180
                  ....*....|....*....|....*.
gi 1901933175 157 ELAAAVGSVRETVTKVVGELSREGVI 182
Cdd:PRK09391  184 DIADYLGLTIETVSRALSQLQDRGLI 209
HTH_CRP smart00419
helix_turn_helix, cAMP Regulatory protein;
145-191 1.15e-06

helix_turn_helix, cAMP Regulatory protein;


Pssm-ID: 128696 [Multi-domain]  Cd Length: 48  Bit Score: 43.97  E-value: 1.15e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1901933175  145 DSGETMIYATHDELAAAVGSVRETVTKVVGELSREGVISAGYGKITL 191
Cdd:smart00419   1 EGIRVRLPLTRQEIAELLGLTRETVSRTLKRLEKEGLISREGGRIVI 47
HTH_CRP cd00092
helix_turn_helix, cAMP Regulatory protein C-terminus; DNA binding domain of prokaryotic ...
127-191 1.30e-03

helix_turn_helix, cAMP Regulatory protein C-terminus; DNA binding domain of prokaryotic regulatory proteins belonging to the catabolite activator protein family.


Pssm-ID: 238044 [Multi-domain]  Cd Length: 67  Bit Score: 36.10  E-value: 1.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1901933175 127 RIAGELLELkdtalATQLDSGETM-IYATHDELAAAVGSVRETVTKVVGELSREGVISA-GYGKITL 191
Cdd:cd00092     4 RLASFLLNL-----SLRYGAGDLVqLPLTRQEIADYLGLTRETVSRTLKELEEEGLISRrGRGKYRV 65
 
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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