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Conserved domains on  [gi|446685534|ref|WP_000762880|]
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MULTISPECIES: antitermination protein [Enterobacteriaceae]

Protein Classification

antitermination protein( domain architecture ID 10507976)

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 6.61e-30

Antitermination protein;


:

Pssm-ID: 427381  Cd Length: 85  Bit Score: 107.84  E-value: 6.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685534   25 SKDALSITDVMAAQGMTQNRAEMGFSAFLGKMGISMNDRARATELLADYALSRCDRVAAlrKLPAEIKPVVMRIMASYAF 104
Cdd:pfam03589   1 VSDACRCTDVMAALGMAQSKARFGVPVFCGKRGYSRLDSTEAIEALLQLAPDLTQKTVA--KLWEETYKPFLDALVTYAF 78


                  ....*..
gi 446685534  105 EDYARSA 111
Cdd:pfam03589  79 KEYSRSA 85
Antiterm super family cl04175
Antitermination protein;
180-265 1.19e-17

Antitermination protein;


The actual alignment was detected with superfamily member pfam03589:

Pssm-ID: 427381  Cd Length: 85  Bit Score: 75.48  E-value: 1.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685534  180 VSTACKdCRGRGVAIHREESVKR-GMPVIrdcqrCGGRGCERLPSTEAFNAICKVTSAIT----LDTWKKSVKRFYDTLV 254
Cdd:pfam03589   1 VSDACR-CTDVMAALGMAQSKARfGVPVF-----CGKRGYSRLDSTEAIEALLQLAPDLTqktvAKLWEETYKPFLDALV 74

                          90
                  ....*....|.
gi 446685534  255 VRFDIEEAWAE 265
Cdd:pfam03589  75 TYAFKEYSRSA 85
DnaJ_zf super family cl21539
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 166-191 1.05e-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.


The actual alignment was detected with superfamily member cd10719:

Pssm-ID: 473904 [Multi-domain]  Cd Length: 65  Bit Score: 36.85  E-value: 1.05e-03
                         10        20
                 ....*....|....*....|....*..
gi 446685534 166 VVKVACPECGGKGEV-STACKDCRGRG 191
Cdd:cd10719   39 QTQTTCPTCGGTGKIiKDPCPKCKGKG 65
DnaJ_CXXCXGXG super family cl47586
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 108-191 1.97e-03

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.


The actual alignment was detected with superfamily member pfam00684:

Pssm-ID: 459904 [Multi-domain]  Cd Length: 65  Bit Score: 36.00  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685534  108 ARSAASKKQCPCCHGKKFIESEVFTNKIQYpdgkppvwakctkgvypsyweewkkvreVVKVACPECGGKGEV-STACKD 186
Cdd:pfam00684   9 AKPGTKPTTCPTCGGTGQVRRVQQTGPGFF----------------------------QMQSTCPTCGGTGKIiKDPCKK 60


                  ....*
gi 446685534  187 CRGRG 191
Cdd:pfam00684  61 CKGKG 65
 
Name Accession Description Interval E-value
Antiterm pfam03589
Antitermination protein;
25-111 6.61e-30

Antitermination protein;


Pssm-ID: 427381  Cd Length: 85  Bit Score: 107.84  E-value: 6.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685534   25 SKDALSITDVMAAQGMTQNRAEMGFSAFLGKMGISMNDRARATELLADYALSRCDRVAAlrKLPAEIKPVVMRIMASYAF 104
Cdd:pfam03589   1 VSDACRCTDVMAALGMAQSKARFGVPVFCGKRGYSRLDSTEAIEALLQLAPDLTQKTVA--KLWEETYKPFLDALVTYAF 78


                  ....*..
gi 446685534  105 EDYARSA 111
Cdd:pfam03589  79 KEYSRSA 85
Antiterm pfam03589
Antitermination protein;
180-265 1.19e-17

Antitermination protein;


Pssm-ID: 427381  Cd Length: 85  Bit Score: 75.48  E-value: 1.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685534  180 VSTACKdCRGRGVAIHREESVKR-GMPVIrdcqrCGGRGCERLPSTEAFNAICKVTSAIT----LDTWKKSVKRFYDTLV 254
Cdd:pfam03589   1 VSDACR-CTDVMAALGMAQSKARfGVPVF-----CGKRGYSRLDSTEAIEALLQLAPDLTqktvAKLWEETYKPFLDALV 74

                          90
                  ....*....|.
gi 446685534  255 VRFDIEEAWAE 265
Cdd:pfam03589  75 TYAFKEYSRSA 85
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 171-217 6.08e-06

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: 43.01  E-value: 6.08e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446685534 171 CPECGGKG----EVSTACKDCRGRGVAIHREESVKRGMPVIRDCQRCGGRG 217
Cdd:cd10719    1 CPTCNGSGakpgTKPKTCPTCGGSGQVRQVQGTGFGFFQTQTTCPTCGGTG 51
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 155-240 5.98e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 40.68  E-value: 5.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685534 155 SYWEEWKKVREVVKVACPECGGKG---EVSTACKDCRGRGvaihrEESVKRG-----MPVIRDCQRCGGRGceRLPSTEA 226
Cdd:PRK14290 136 AYYGTEKRIKYRRNAMCPDCSGTGaknGKLITCPTCHGTG-----QQRIVRGqgffrMVTVTTCRTCGGRG--RIPEEKC 208

                         90
                 ....*....|....
gi 446685534 227 fnAICKVTSAITLD 240
Cdd:PRK14290 209 --PRCNGTGTVVVN 220
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 166-191 1.05e-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: 36.85  E-value: 1.05e-03
                         10        20
                 ....*....|....*....|....*..
gi 446685534 166 VVKVACPECGGKGEV-STACKDCRGRG 191
Cdd:cd10719   39 QTQTTCPTCGGTGKIiKDPCPKCKGKG 65
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 108-191 1.97e-03

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: 36.00  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685534  108 ARSAASKKQCPCCHGKKFIESEVFTNKIQYpdgkppvwakctkgvypsyweewkkvreVVKVACPECGGKGEV-STACKD 186
Cdd:pfam00684   9 AKPGTKPTTCPTCGGTGQVRRVQQTGPGFF----------------------------QMQSTCPTCGGTGKIiKDPCKK 60


                  ....*
gi 446685534  187 CRGRG 191
Cdd:pfam00684  61 CKGKG 65
 
Name Accession Description Interval E-value
Antiterm pfam03589
Antitermination protein;
25-111 6.61e-30

Antitermination protein;


Pssm-ID: 427381  Cd Length: 85  Bit Score: 107.84  E-value: 6.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685534   25 SKDALSITDVMAAQGMTQNRAEMGFSAFLGKMGISMNDRARATELLADYALSRCDRVAAlrKLPAEIKPVVMRIMASYAF 104
Cdd:pfam03589   1 VSDACRCTDVMAALGMAQSKARFGVPVFCGKRGYSRLDSTEAIEALLQLAPDLTQKTVA--KLWEETYKPFLDALVTYAF 78


                  ....*..
gi 446685534  105 EDYARSA 111
Cdd:pfam03589  79 KEYSRSA 85
Antiterm pfam03589
Antitermination protein;
180-265 1.19e-17

Antitermination protein;


Pssm-ID: 427381  Cd Length: 85  Bit Score: 75.48  E-value: 1.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685534  180 VSTACKdCRGRGVAIHREESVKR-GMPVIrdcqrCGGRGCERLPSTEAFNAICKVTSAIT----LDTWKKSVKRFYDTLV 254
Cdd:pfam03589   1 VSDACR-CTDVMAALGMAQSKARfGVPVF-----CGKRGYSRLDSTEAIEALLQLAPDLTqktvAKLWEETYKPFLDALV 74

                          90
                  ....*....|.
gi 446685534  255 VRFDIEEAWAE 265
Cdd:pfam03589  75 TYAFKEYSRSA 85
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 171-217 6.08e-06

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: 43.01  E-value: 6.08e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446685534 171 CPECGGKG----EVSTACKDCRGRGVAIHREESVKRGMPVIRDCQRCGGRG 217
Cdd:cd10719    1 CPTCNGSGakpgTKPKTCPTCGGSGQVRQVQGTGFGFFQTQTTCPTCGGTG 51
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 171-217 1.93e-04

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: 38.69  E-value: 1.93e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446685534  171 CPECGGKG----EVSTACKDCRGRGVAIHREESVKRGMPVIRDCQRCGGRG 217
Cdd:pfam00684   1 CPTCNGSGakpgTKPTTCPTCGGTGQVRRVQQTGPGFFQMQSTCPTCGGTG 51
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 155-240 5.98e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 40.68  E-value: 5.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685534 155 SYWEEWKKVREVVKVACPECGGKG---EVSTACKDCRGRGvaihrEESVKRG-----MPVIRDCQRCGGRGceRLPSTEA 226
Cdd:PRK14290 136 AYYGTEKRIKYRRNAMCPDCSGTGaknGKLITCPTCHGTG-----QQRIVRGqgffrMVTVTTCRTCGGRG--RIPEEKC 208

                         90
                 ....*....|....
gi 446685534 227 fnAICKVTSAITLD 240
Cdd:PRK14290 209 --PRCNGTGTVVVN 220
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 171-198 6.32e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 40.52  E-value: 6.32e-04
                         10        20
                 ....*....|....*....|....*...
gi 446685534 171 CPECGGKGEVSTACKDCRGRGVAIHREE 198
Cdd:PRK14291 198 CPTCGGEGVLREPCSKCNGRGLVIKKET 225
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 166-191 1.05e-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: 36.85  E-value: 1.05e-03
                         10        20
                 ....*....|....*....|....*..
gi 446685534 166 VVKVACPECGGKGEV-STACKDCRGRG 191
Cdd:cd10719   39 QTQTTCPTCGGTGKIiKDPCPKCKGKG 65
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 167-257 1.49e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 39.59  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685534 167 VKVACPECGGKGEV-STACKDCRGRGvAIHREESVKRGMPV-IRDCQRCGGRGCERL-PSTEAFNAICKVTSAITLDTWK 243
Cdd:PRK14285 184 VTTTCPKCYGNGKIiSNPCKSCKGKG-SLKKKETIELKIPAgIDDNQQIKMRGKGSVnPDNQQYGDLYIKILIKPHKIFK 262

                         90
                 ....*....|....
gi 446685534 244 KSVKRFYDTLVVRF 257
Cdd:PRK14285 263 RNGKDLYATLPISF 276
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 171-217 1.85e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 39.37  E-value: 1.85e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446685534 171 CPECGGKGEV---------STACKDCRGRGvaihreesvkrgmpVIRD-CQRCGGRG 217
Cdd:PRK14291 176 CPTCGGSGEIyqrggffriSQTCPTCGGEG--------------VLREpCSKCNGRG 218
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 108-191 1.97e-03

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: 36.00  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685534  108 ARSAASKKQCPCCHGKKFIESEVFTNKIQYpdgkppvwakctkgvypsyweewkkvreVVKVACPECGGKGEV-STACKD 186
Cdd:pfam00684   9 AKPGTKPTTCPTCGGTGQVRRVQQTGPGFF----------------------------QMQSTCPTCGGTGKIiKDPCKK 60


                  ....*
gi 446685534  187 CRGRG 191
Cdd:pfam00684  61 CKGKG 65
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 170-205 2.31e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 39.06  E-value: 2.31e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 446685534 170 ACPECGGKGEVST-ACKDCRGRGvAIHREESVKRGMP 205
Cdd:PRK14284 199 TCPECGGEGRVITdPCSVCRGQG-RIKDKRSVHVHIP 234
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 169-217 3.48e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 38.49  E-value: 3.48e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446685534 169 VACPECGGKGEVSTA-------------CKDCRGRGVaihreesvkrgmpVIRD-CQRCGGRG 217
Cdd:PRK14278 157 VTCDTCGGRGEVQTVqrsflgqvmtsrpCPTCRGVGE-------------VIPDpCHECAGDG 206
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 171-217 5.79e-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: 34.54  E-value: 5.79e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446685534 171 CPECGGKGEV-------------STACKDCRGRGVaihreesvkrgmpVIRD-CQRCGGRG 217
Cdd:cd10719   18 CPTCGGSGQVrqvqgtgfgffqtQTTCPTCGGTGK-------------IIKDpCPKCKGKG 65
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 165-222 7.16e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 37.44  E-value: 7.16e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446685534 165 EVVK-VACPECGGKGE----VSTACKDCRGRGvaihreESVKRG--MPVIRDCQRCGGRGCERLP 222
Cdd:PRK14291 152 EVPRyVPCEACGGTGYdpgsGEKVCPTCGGSG------EIYQRGgfFRISQTCPTCGGEGVLREP 210
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 171-217 7.54e-03

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: 34.46  E-value: 7.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446685534  171 CPECGGKGEV-------------STACKDCRGRGVaihreesvkrgmpVIRD-CQRCGGRG 217
Cdd:pfam00684  18 CPTCGGTGQVrrvqqtgpgffqmQSTCPTCGGTGK-------------IIKDpCKKCKGKG 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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