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Conserved domains on  [gi|2770159087|ref|WP_366547534|]
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antitermination protein [Salmonella enterica]

Protein Classification

antitermination protein( domain architecture ID 10507972)

antitermination protein positively regulates expression of some phage genes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Antiterm pfam03589
Antitermination protein;
25-111 7.09e-28

Antitermination protein;


:

Pssm-ID: 427381  Cd Length: 85  Bit Score: 102.45  E-value: 7.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770159087  25 SSEALTITDVMAAQGMTQNRAKFGFSAFLGKMGISRNDREAAIGLLTKYALSRCDEVAAlrKLDPSLKPGVMQILATYAF 104
Cdd:pfam03589   1 VSDACRCTDVMAALGMAQSKARFGVPVFCGKRGYSRLDSTEAIEALLQLAPDLTQKTVA--KLWEETYKPFLDALVTYAF 78


                  ....*..
gi 2770159087 105 EDYSRSA 111
Cdd:pfam03589  79 KEYSRSA 85
Antiterm super family cl04175
Antitermination protein;
180-265 6.43e-13

Antitermination protein;


The actual alignment was detected with superfamily member pfam03589:

Pssm-ID: 427381  Cd Length: 85  Bit Score: 62.77  E-value: 6.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770159087 180 VSAACNdCHGRGKAVKKKISEEQ-GVPVIgdcerCAGRGYERIPSTEAYKAICE----ITDAISLDTWKKSVKRFYGDLI 254
Cdd:pfam03589   1 VSDACR-CTDVMAALGMAQSKARfGVPVF-----CGKRGYSRLDSTEAIEALLQlapdLTQKTVAKLWEETYKPFLDALV 74

                          90
                  ....*....|.
gi 2770159087 255 AKFEVEESWAE 265
Cdd:pfam03589  75 TYAFKEYSRSA 85
PRK14292 super family cl36360
chaperone protein DnaJ; Provisional
 116-195 2.04e-04

chaperone protein DnaJ; Provisional


The actual alignment was detected with superfamily member PRK14292:

Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 42.18  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770159087 116 ICPCCHGKKfisvsvftnkvQYPDGKPPKWVKVT--SGVYPSYWEEWKSVQETQKViCPECKGKGEV-SAACNDCHGRGK 192
Cdd:PRK14292  141 ECEHCHGSR-----------TEPGGKPPKTCPTCrgAGAVRAQARTIFGVVETQQP-CPTCRGEGQIiTDPCTVCRGRGR 208


                  ...
gi 2770159087 193 AVK 195
Cdd:PRK14292  209 TLK 211
 
Name Accession Description Interval E-value
Antiterm pfam03589
Antitermination protein;
25-111 7.09e-28

Antitermination protein;


Pssm-ID: 427381  Cd Length: 85  Bit Score: 102.45  E-value: 7.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770159087  25 SSEALTITDVMAAQGMTQNRAKFGFSAFLGKMGISRNDREAAIGLLTKYALSRCDEVAAlrKLDPSLKPGVMQILATYAF 104
Cdd:pfam03589   1 VSDACRCTDVMAALGMAQSKARFGVPVFCGKRGYSRLDSTEAIEALLQLAPDLTQKTVA--KLWEETYKPFLDALVTYAF 78


                  ....*..
gi 2770159087 105 EDYSRSA 111
Cdd:pfam03589  79 KEYSRSA 85
Antiterm pfam03589
Antitermination protein;
180-265 6.43e-13

Antitermination protein;


Pssm-ID: 427381  Cd Length: 85  Bit Score: 62.77  E-value: 6.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770159087 180 VSAACNdCHGRGKAVKKKISEEQ-GVPVIgdcerCAGRGYERIPSTEAYKAICE----ITDAISLDTWKKSVKRFYGDLI 254
Cdd:pfam03589   1 VSDACR-CTDVMAALGMAQSKARfGVPVF-----CGKRGYSRLDSTEAIEALLQlapdLTQKTVAKLWEETYKPFLDALV 74

                          90
                  ....*....|.
gi 2770159087 255 AKFEVEESWAE 265
Cdd:pfam03589  75 TYAFKEYSRSA 85
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 166-217 1.06e-05

Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of DnaJ/Hsp40 (heat shock protein 40). DnaJ proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonin family. Hsp40 proteins are characterized by the presence of an N-terminal J domain, which mediates the interaction with Hsp70. This central domain contains four repeats of a CxxCxGxG motif and binds to two Zinc ions. It has been implicated in substrate binding.


Pssm-ID: 199908 [Multi-domain]  Cd Length: 65  Bit Score: 42.24  E-value: 1.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2770159087 166 TQKVICPECKGKGEV-------------SAACNDCHGRGKAVKKKiseeqgvpvigdCERCAGRG 217
Cdd:cd10719    13 TKPKTCPTCGGSGQVrqvqgtgfgffqtQTTCPTCGGTGKIIKDP------------CPKCKGKG 65
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 155-240 4.59e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 44.15  E-value: 4.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770159087 155 SYWEEWKSVQETQKVICPECKGKG---EVSAACNDCHGRGkavKKKISEEQG---VPVIGDCERCAGRGyeRIPSTEAyk 228
Cdd:PRK14290  136 AYYGTEKRIKYRRNAMCPDCSGTGaknGKLITCPTCHGTG---QQRIVRGQGffrMVTVTTCRTCGGRG--RIPEEKC-- 208

                          90
                  ....*....|..
gi 2770159087 229 AICEITDAISLD 240
Cdd:PRK14290  209 PRCNGTGTVVVN 220
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 116-195 2.04e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 42.18  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770159087 116 ICPCCHGKKfisvsvftnkvQYPDGKPPKWVKVT--SGVYPSYWEEWKSVQETQKViCPECKGKGEV-SAACNDCHGRGK 192
Cdd:PRK14292  141 ECEHCHGSR-----------TEPGGKPPKTCPTCrgAGAVRAQARTIFGVVETQQP-CPTCRGEGQIiTDPCTVCRGRGR 208


                  ...
gi 2770159087 193 AVK 195
Cdd:PRK14292  209 TLK 211
 
Name Accession Description Interval E-value
Antiterm pfam03589
Antitermination protein;
25-111 7.09e-28

Antitermination protein;


Pssm-ID: 427381  Cd Length: 85  Bit Score: 102.45  E-value: 7.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770159087  25 SSEALTITDVMAAQGMTQNRAKFGFSAFLGKMGISRNDREAAIGLLTKYALSRCDEVAAlrKLDPSLKPGVMQILATYAF 104
Cdd:pfam03589   1 VSDACRCTDVMAALGMAQSKARFGVPVFCGKRGYSRLDSTEAIEALLQLAPDLTQKTVA--KLWEETYKPFLDALVTYAF 78


                  ....*..
gi 2770159087 105 EDYSRSA 111
Cdd:pfam03589  79 KEYSRSA 85
Antiterm pfam03589
Antitermination protein;
180-265 6.43e-13

Antitermination protein;


Pssm-ID: 427381  Cd Length: 85  Bit Score: 62.77  E-value: 6.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770159087 180 VSAACNdCHGRGKAVKKKISEEQ-GVPVIgdcerCAGRGYERIPSTEAYKAICE----ITDAISLDTWKKSVKRFYGDLI 254
Cdd:pfam03589   1 VSDACR-CTDVMAALGMAQSKARfGVPVF-----CGKRGYSRLDSTEAIEALLQlapdLTQKTVAKLWEETYKPFLDALV 74

                          90
                  ....*....|.
gi 2770159087 255 AKFEVEESWAE 265
Cdd:pfam03589  75 TYAFKEYSRSA 85
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 166-217 1.06e-05

Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of DnaJ/Hsp40 (heat shock protein 40). DnaJ proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonin family. Hsp40 proteins are characterized by the presence of an N-terminal J domain, which mediates the interaction with Hsp70. This central domain contains four repeats of a CxxCxGxG motif and binds to two Zinc ions. It has been implicated in substrate binding.


Pssm-ID: 199908 [Multi-domain]  Cd Length: 65  Bit Score: 42.24  E-value: 1.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2770159087 166 TQKVICPECKGKGEV-------------SAACNDCHGRGKAVKKKiseeqgvpvigdCERCAGRG 217
Cdd:cd10719    13 TKPKTCPTCGGSGQVrqvqgtgfgffqtQTTCPTCGGTGKIIKDP------------CPKCKGKG 65
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 155-240 4.59e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 44.15  E-value: 4.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770159087 155 SYWEEWKSVQETQKVICPECKGKG---EVSAACNDCHGRGkavKKKISEEQG---VPVIGDCERCAGRGyeRIPSTEAyk 228
Cdd:PRK14290  136 AYYGTEKRIKYRRNAMCPDCSGTGaknGKLITCPTCHGTG---QQRIVRGQGffrMVTVTTCRTCGGRG--RIPEEKC-- 208

                          90
                  ....*....|..
gi 2770159087 229 AICEITDAISLD 240
Cdd:PRK14290  209 PRCNGTGTVVVN 220
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 166-217 7.65e-05

DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four repeats of the motif CXXCXGXG where X is any amino acid. The isolated cysteine rich domain folds in zinc dependent fashion. Each set of two repeats binds one unit of zinc. Although this domain has been implicated in substrate binding, no evidence of specific interaction between the isolated DNAJ cysteine rich domain and various hydrophobic peptides has been found.


Pssm-ID: 459904 [Multi-domain]  Cd Length: 65  Bit Score: 39.85  E-value: 7.65e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2770159087 166 TQKVICPECKGKGEV-------------SAACNDCHGRGKAVKKKiseeqgvpvigdCERCAGRG 217
Cdd:pfam00684  13 TKPTTCPTCGGTGQVrrvqqtgpgffqmQSTCPTCGGTGKIIKDP------------CKKCKGKG 65
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 166-220 1.29e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 42.82  E-value: 1.29e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2770159087 166 TQKVICPECKGKGEVSAA---------CNDCHGRGKAVKKKiseeqgvpvigdCERCAGRGYER 220
Cdd:PRK10767  157 TSPKTCPTCHGAGQVRMQqgfftvqqtCPTCHGRGKIIKDP------------CKKCHGQGRVE 208
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 116-195 2.04e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 42.18  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770159087 116 ICPCCHGKKfisvsvftnkvQYPDGKPPKWVKVT--SGVYPSYWEEWKSVQETQKViCPECKGKGEV-SAACNDCHGRGK 192
Cdd:PRK14292  141 ECEHCHGSR-----------TEPGGKPPKTCPTCrgAGAVRAQARTIFGVVETQQP-CPTCRGEGQIiTDPCTVCRGRGR 208


                  ...
gi 2770159087 193 AVK 195
Cdd:PRK14292  209 TLK 211
PRK14293 PRK14293
molecular chaperone DnaJ;
166-198 1.48e-03

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 39.59  E-value: 1.48e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2770159087 166 TQKVICPECKGKGEV-SAACNDCHGRG-KAVKKKI 198
Cdd:PRK14293  184 TQVSECPTCNGTGQViEDPCDACGGQGvKQVTKKL 218
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 171-217 1.88e-03

Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of DnaJ/Hsp40 (heat shock protein 40). DnaJ proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonin family. Hsp40 proteins are characterized by the presence of an N-terminal J domain, which mediates the interaction with Hsp70. This central domain contains four repeats of a CxxCxGxG motif and binds to two Zinc ions. It has been implicated in substrate binding.


Pssm-ID: 199908 [Multi-domain]  Cd Length: 65  Bit Score: 36.08  E-value: 1.88e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2770159087 171 CPECKGKGEVSAA----CNDCHGRGKAVKKKISEEQGVPVIGDCERCAGRG 217
Cdd:cd10719     1 CPTCNGSGAKPGTkpktCPTCGGSGQVRQVQGTGFGFFQTQTTCPTCGGTG 51
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 166-224 1.94e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 38.98  E-value: 1.94e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2770159087 166 TQKVICPECKGKGE---------VSAACNDCHGRGKAVKKKiseeqgvpvigdCERCAGRGYERIPST 224
Cdd:PRK14294  159 TSPTTCPQCGGSGQvtqsqgffsIRTTCPRCRGMGKVIVSP------------CKTCHGQGRVRVSKT 214
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 169-228 2.63e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 38.60  E-value: 2.63e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770159087 169 VICPECKGKGEV---------SAACNDCHGRGkavkkkiseeqgvpVIGD-CERCAGRGYerIPSTEAYK 228
Cdd:PRK14291  174 KVCPTCGGSGEIyqrggffriSQTCPTCGGEG--------------VLREpCSKCNGRGL--VIKKETIK 227
 
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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