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Conserved domains on  [gi|15242478|ref|NP_199383|]
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winged-helix DNA-binding transcription factor family protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HSF smart00415
heat shock factor;
10-103 1.91e-40

heat shock factor;


:

Pssm-ID: 214654  Cd Length: 105  Bit Score: 137.80  E-value: 1.91e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242478     10 SLPPFLTKTYEMVDDSSSDSVVAWSENNKSFIVKNPAEFSRDLLPRFFKHKNFSSFIRQLNTYGFRKVDP---------- 79
Cdd:smart00415   1 QPPPFLTKLYLLVEDPSTDKIISWSPSGKSFVIWDPEEFAKNLLPRYFKHNNFSSFVRQLNMYGFRKVDPefqgilynft 80
                           90       100
                   ....*....|....*....|....*
gi 15242478     80 -EKWEFLNDDFVRGRPYLMKNIHRR 103
Cdd:smart00415  81 sDQWEFANPDFVRGQPELLRNIKRK 105
HSF1 super family cl47090
Heat shock transcription factor [Transcription];
8-208 1.20e-24

Heat shock transcription factor [Transcription];


The actual alignment was detected with superfamily member COG5169:

Pssm-ID: 227497 [Multi-domain]  Cd Length: 282  Bit Score: 101.35  E-value: 1.20e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242478   8 SSSLPPFLTKTYEMVDDSSSDSVVAWSENNKSFIVKNPAEFSRDLLPRFFKHKNFSSFIRQLNTYGFRKV---------- 77
Cdd:COG5169   7 WSQPKEFVHKLYQILEEPEYYKLIQWSPDGRSFVILDPEEFTKVILPRYFKHGNFASFVRQLNKYGFHKVshksgqrsyy 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242478  78 DPEKWEFLNDDFVRGRPYLMKNIHRRKPVHSHSLVNLQAQNPLTESERRSMEDQIERLKNEKEGLLAELQNQEQERKEfe 157
Cdd:COG5169  87 NENVWEFGNKNFQLGMIELLKKIKRKKAPSNRVDSNNESKDAMMNIEVENIILPQSELYNSLSSLSNVNQTLLLYLNE-- 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15242478 158 lqvttlkdrLQHMEQHQKSIVAYVSQVLGKPglSLNLENHERRKRRFQENS 208
Cdd:COG5169 165 ---------LKEYNYRNLRTIDDINAMLADL--SMSPFADEHLKSFLQELF 204
 
Name Accession Description Interval E-value
HSF smart00415
heat shock factor;
10-103 1.91e-40

heat shock factor;


Pssm-ID: 214654  Cd Length: 105  Bit Score: 137.80  E-value: 1.91e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242478     10 SLPPFLTKTYEMVDDSSSDSVVAWSENNKSFIVKNPAEFSRDLLPRFFKHKNFSSFIRQLNTYGFRKVDP---------- 79
Cdd:smart00415   1 QPPPFLTKLYLLVEDPSTDKIISWSPSGKSFVIWDPEEFAKNLLPRYFKHNNFSSFVRQLNMYGFRKVDPefqgilynft 80
                           90       100
                   ....*....|....*....|....*
gi 15242478     80 -EKWEFLNDDFVRGRPYLMKNIHRR 103
Cdd:smart00415  81 sDQWEFANPDFVRGQPELLRNIKRK 105
HSF_DNA-bind pfam00447
HSF-type DNA-binding;
14-103 6.27e-36

HSF-type DNA-binding;


Pssm-ID: 459813  Cd Length: 98  Bit Score: 125.76  E-value: 6.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242478    14 FLTKTYEMVDDSSSDSVVAWSENNKSFIVKNPAEFSRDLLPRFFKHKNFSSFIRQLNTYGFRKVDP--------EKWEFL 85
Cdd:pfam00447   1 FLRKLYRMLEDPETDDIISWSDDGDSFVILDPEEFAKEVLPKYFKHSNFSSFVRQLNMYGFHKVKDlsssksmgDSWEFR 80
                          90
                  ....*....|....*...
gi 15242478    86 NDDFVRGRPYLMKNIHRR 103
Cdd:pfam00447  81 HPNFRRGRPDLLKNIKRK 98
HSF1 COG5169
Heat shock transcription factor [Transcription];
8-208 1.20e-24

Heat shock transcription factor [Transcription];


Pssm-ID: 227497 [Multi-domain]  Cd Length: 282  Bit Score: 101.35  E-value: 1.20e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242478   8 SSSLPPFLTKTYEMVDDSSSDSVVAWSENNKSFIVKNPAEFSRDLLPRFFKHKNFSSFIRQLNTYGFRKV---------- 77
Cdd:COG5169   7 WSQPKEFVHKLYQILEEPEYYKLIQWSPDGRSFVILDPEEFTKVILPRYFKHGNFASFVRQLNKYGFHKVshksgqrsyy 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242478  78 DPEKWEFLNDDFVRGRPYLMKNIHRRKPVHSHSLVNLQAQNPLTESERRSMEDQIERLKNEKEGLLAELQNQEQERKEfe 157
Cdd:COG5169  87 NENVWEFGNKNFQLGMIELLKKIKRKKAPSNRVDSNNESKDAMMNIEVENIILPQSELYNSLSSLSNVNQTLLLYLNE-- 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15242478 158 lqvttlkdrLQHMEQHQKSIVAYVSQVLGKPglSLNLENHERRKRRFQENS 208
Cdd:COG5169 165 ---------LKEYNYRNLRTIDDINAMLADL--SMSPFADEHLKSFLQELF 204
Flagellar_rod pfam05149
Paraflagellar rod protein; This family consists of several eukaryotic paraflagellar rod ...
107-239 4.34e-03

Paraflagellar rod protein; This family consists of several eukaryotic paraflagellar rod component proteins. The eukaryotic flagellum represents one of the most complex macromolecular structures found in any organizm and contains more than 250 proteins. In addition to its locomotive role, the flagellum is probably involved in nutrient uptake since receptors for host low-density lipoproteins are localized on the flagellar membrane as well as on the flagellar pocket membrane.


Pssm-ID: 368306 [Multi-domain]  Cd Length: 287  Bit Score: 38.50  E-value: 4.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242478   107 HSHSLVNLQAQNPLTESERRSMEDQIERLKNEKEGLLAELQNQEQERKEFelqvttLKDRLQHMEQHQKSIVAYVSQVLG 186
Cdd:pfam05149  35 DAKQRKRFKTQRRESDKFLQQNVEQQQKLWREIEELERELQKLAEERREE------VEDRIEAVEREAQRRTDHESFLNF 108
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15242478   187 KpglslnlENHERRKRRFQENslppssshIEQVEKLESSLtfwENLVSESCEK 239
Cdd:pfam05149 109 A-------DQHKQRLRRTLEN--------CDGALDCARSL---EEYVQEGCDH 143
 
Name Accession Description Interval E-value
HSF smart00415
heat shock factor;
10-103 1.91e-40

heat shock factor;


Pssm-ID: 214654  Cd Length: 105  Bit Score: 137.80  E-value: 1.91e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242478     10 SLPPFLTKTYEMVDDSSSDSVVAWSENNKSFIVKNPAEFSRDLLPRFFKHKNFSSFIRQLNTYGFRKVDP---------- 79
Cdd:smart00415   1 QPPPFLTKLYLLVEDPSTDKIISWSPSGKSFVIWDPEEFAKNLLPRYFKHNNFSSFVRQLNMYGFRKVDPefqgilynft 80
                           90       100
                   ....*....|....*....|....*
gi 15242478     80 -EKWEFLNDDFVRGRPYLMKNIHRR 103
Cdd:smart00415  81 sDQWEFANPDFVRGQPELLRNIKRK 105
HSF_DNA-bind pfam00447
HSF-type DNA-binding;
14-103 6.27e-36

HSF-type DNA-binding;


Pssm-ID: 459813  Cd Length: 98  Bit Score: 125.76  E-value: 6.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242478    14 FLTKTYEMVDDSSSDSVVAWSENNKSFIVKNPAEFSRDLLPRFFKHKNFSSFIRQLNTYGFRKVDP--------EKWEFL 85
Cdd:pfam00447   1 FLRKLYRMLEDPETDDIISWSDDGDSFVILDPEEFAKEVLPKYFKHSNFSSFVRQLNMYGFHKVKDlsssksmgDSWEFR 80
                          90
                  ....*....|....*...
gi 15242478    86 NDDFVRGRPYLMKNIHRR 103
Cdd:pfam00447  81 HPNFRRGRPDLLKNIKRK 98
HSF1 COG5169
Heat shock transcription factor [Transcription];
8-208 1.20e-24

Heat shock transcription factor [Transcription];


Pssm-ID: 227497 [Multi-domain]  Cd Length: 282  Bit Score: 101.35  E-value: 1.20e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242478   8 SSSLPPFLTKTYEMVDDSSSDSVVAWSENNKSFIVKNPAEFSRDLLPRFFKHKNFSSFIRQLNTYGFRKV---------- 77
Cdd:COG5169   7 WSQPKEFVHKLYQILEEPEYYKLIQWSPDGRSFVILDPEEFTKVILPRYFKHGNFASFVRQLNKYGFHKVshksgqrsyy 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242478  78 DPEKWEFLNDDFVRGRPYLMKNIHRRKPVHSHSLVNLQAQNPLTESERRSMEDQIERLKNEKEGLLAELQNQEQERKEfe 157
Cdd:COG5169  87 NENVWEFGNKNFQLGMIELLKKIKRKKAPSNRVDSNNESKDAMMNIEVENIILPQSELYNSLSSLSNVNQTLLLYLNE-- 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15242478 158 lqvttlkdrLQHMEQHQKSIVAYVSQVLGKPglSLNLENHERRKRRFQENS 208
Cdd:COG5169 165 ---------LKEYNYRNLRTIDDINAMLADL--SMSPFADEHLKSFLQELF 204
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
113-186 1.38e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 1.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242478 113 NLQAQNPLTESERRSMEDQIERLKNEKEGLLAELQNQEQERKEFELQVTT-----------LKDRLQHMeQHQKSIVAYV 181
Cdd:COG3883  27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEaeaeieerreeLGERARAL-YRSGGSVSYL 105

                ....*
gi 15242478 182 SQVLG 186
Cdd:COG3883 106 DVLLG 110
Flagellar_rod pfam05149
Paraflagellar rod protein; This family consists of several eukaryotic paraflagellar rod ...
107-239 4.34e-03

Paraflagellar rod protein; This family consists of several eukaryotic paraflagellar rod component proteins. The eukaryotic flagellum represents one of the most complex macromolecular structures found in any organizm and contains more than 250 proteins. In addition to its locomotive role, the flagellum is probably involved in nutrient uptake since receptors for host low-density lipoproteins are localized on the flagellar membrane as well as on the flagellar pocket membrane.


Pssm-ID: 368306 [Multi-domain]  Cd Length: 287  Bit Score: 38.50  E-value: 4.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242478   107 HSHSLVNLQAQNPLTESERRSMEDQIERLKNEKEGLLAELQNQEQERKEFelqvttLKDRLQHMEQHQKSIVAYVSQVLG 186
Cdd:pfam05149  35 DAKQRKRFKTQRRESDKFLQQNVEQQQKLWREIEELERELQKLAEERREE------VEDRIEAVEREAQRRTDHESFLNF 108
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15242478   187 KpglslnlENHERRKRRFQENslppssshIEQVEKLESSLtfwENLVSESCEK 239
Cdd:pfam05149 109 A-------DQHKQRLRRTLEN--------CDGALDCARSL---EEYVQEGCDH 143
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
111-172 7.90e-03

Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.


Pssm-ID: 465452 [Multi-domain]  Cd Length: 127  Bit Score: 36.03  E-value: 7.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15242478   111 LVNLQAQnplTESERRSMEDQIERLKNEKEGLLAELQNQEQERKEFELQVTTLKDRLQHMEQ 172
Cdd:pfam17675  32 LKKLEKE---TPEELEELEKELEKLEKEEEELLQELEELEKEREELDAELEALEEELEALDE 90
 
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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