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Conserved domains on  [gi|446969854|ref|WP_001047110|]
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MULTISPECIES: antitermination protein [Enterobacteriaceae]

Protein Classification

antitermination protein( domain architecture ID 11143760)

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;
25-107 5.39e-31

Antitermination protein;


:

Pssm-ID: 427381  Cd Length: 85  Bit Score: 109.77  E-value: 5.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969854   25 GSGGLTITDVMAAQGMVQSKAPLGFALFLAKVGVQ--DPQFAIEGLLNYAMALDNPTLNKLSEETRLQIIPYLVNFAFAD 102
Cdd:pfam03589   1 VSDACRCTDVMAALGMAQSKARFGVPVFCGKRGYSrlDSTEAIEALLQLAPDLTQKTVAKLWEETYKPFLDALVTYAFKE 80


                  ....*
gi 446969854  103 YSRSA 107
Cdd:pfam03589  81 YSRSA 85
Antiterm pfam03589
Antitermination protein;
157-242 2.02e-23

Antitermination protein;


:

Pssm-ID: 427381  Cd Length: 85  Bit Score: 90.51  E-value: 2.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969854  157 VSTACRgCKGKGIVLDEKRTRLH-GTPVYkvcgrCNGNRFSRLPTTLARLHVQKLVPDLTDYQ----WYKGYADVIDKLV 231
Cdd:pfam03589   1 VSDACR-CTDVMAALGMAQSKARfGVPVF-----CGKRGYSRLDSTEAIEALLQLAPDLTQKTvaklWEETYKPFLDALV 74

                          90
                  ....*....|.
gi 446969854  232 TKCWQEEAYAE 242
Cdd:pfam03589  75 TYAFKEYSRSA 85
DnaJ_CXXCXGXG super family cl47586
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 113-194 2.38e-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.


The actual alignment was detected with superfamily member pfam00684:

Pssm-ID: 459904 [Multi-domain]  Cd Length: 65  Bit Score: 41.00  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969854  113 CEHCAGTGfhnvlrevvkhSRSGESVIKeewvkelCQHCHGKGEV-------------STACRGCKGKGIVLDEKrtrlh 179
Cdd:pfam00684   1 CPTCNGSG-----------AKPGTKPTT-------CPTCGGTGQVrrvqqtgpgffqmQSTCPTCGGTGKIIKDP----- 57

                          90
                  ....*....|....*
gi 446969854  180 gtpvykvCGRCNGNR 194
Cdd:pfam00684  58 -------CKKCKGKG 65
 
Name Accession Description Interval E-value
Antiterm pfam03589
Antitermination protein;
25-107 5.39e-31

Antitermination protein;


Pssm-ID: 427381  Cd Length: 85  Bit Score: 109.77  E-value: 5.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969854   25 GSGGLTITDVMAAQGMVQSKAPLGFALFLAKVGVQ--DPQFAIEGLLNYAMALDNPTLNKLSEETRLQIIPYLVNFAFAD 102
Cdd:pfam03589   1 VSDACRCTDVMAALGMAQSKARFGVPVFCGKRGYSrlDSTEAIEALLQLAPDLTQKTVAKLWEETYKPFLDALVTYAFKE 80


                  ....*
gi 446969854  103 YSRSA 107
Cdd:pfam03589  81 YSRSA 85
Antiterm pfam03589
Antitermination protein;
157-242 2.02e-23

Antitermination protein;


Pssm-ID: 427381  Cd Length: 85  Bit Score: 90.51  E-value: 2.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969854  157 VSTACRgCKGKGIVLDEKRTRLH-GTPVYkvcgrCNGNRFSRLPTTLARLHVQKLVPDLTDYQ----WYKGYADVIDKLV 231
Cdd:pfam03589   1 VSDACR-CTDVMAALGMAQSKARfGVPVF-----CGKRGYSRLDSTEAIEALLQLAPDLTQKTvaklWEETYKPFLDALV 74

                          90
                  ....*....|.
gi 446969854  232 TKCWQEEAYAE 242
Cdd:pfam03589  75 TYAFKEYSRSA 85
phage_xxxx TIGR02642
uncharacterized phage protein; This uncharacterized protein is found in prophage regions of ...
 3-159 6.19e-06

uncharacterized phage protein; This uncharacterized protein is found in prophage regions of Shewanella oneidensis MR-1, Vibrio vulnificus YJ016, Yersinia pseudotuberculosis IP 32953, and Aeromonas hydrophila ATCC7966. It appears to have regions of sequence similarity to phage lambda antitermination protein Q. [Mobile and extrachromosomal element functions, Prophage functions]


Pssm-ID: 274243 [Multi-domain]  Cd Length: 186  Bit Score: 45.63  E-value: 6.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969854    3 LEALPKYYSPKSPKLSDDAPATGSGGLTITDVMAAQGMVQSKAPLGFALFLAKVgVQDPQfAIEGLLnyamALDNPTLNK 82
Cdd:TIGR02642   5 IEMLTILSSPRGMSIEERTAKRGPNVLTKEQLLGAIALAQRDNPIGIAILMAKY-MRDAY-AIQKLY----AHICEQLLP 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446969854   83 LSEETRLQIIPYL-VNfafadysrSAASKARCEHCAGTGfhnvlrevVKHSRSGEsvikeewvkelCQHCHGKGEVST 159
Cdd:TIGR02642  79 LITPNAAEAASYLaVN--------EVLNSCKCPRCRGTG--------LIQRRQRE-----------CDTCAGTGRFRP 129
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 113-194 2.38e-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: 41.00  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969854  113 CEHCAGTGfhnvlrevvkhSRSGESVIKeewvkelCQHCHGKGEV-------------STACRGCKGKGIVLDEKrtrlh 179
Cdd:pfam00684   1 CPTCNGSG-----------AKPGTKPTT-------CPTCGGTGQVrrvqqtgpgffqmQSTCPTCGGTGKIIKDP----- 57

                          90
                  ....*....|....*
gi 446969854  180 gtpvykvCGRCNGNR 194
Cdd:pfam00684  58 -------CKKCKGKG 65
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 113-194 2.49e-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: 41.09  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969854 113 CEHCAGTGfhnvlrevvkhSRSGESVIKeewvkelCQHCHGKGEV-------------STACRGCKGKGIVLDEKrtrlh 179
Cdd:cd10719    1 CPTCNGSG-----------AKPGTKPKT-------CPTCGGSGQVrqvqgtgfgffqtQTTCPTCGGTGKIIKDP----- 57

                         90
                 ....*....|....*
gi 446969854 180 gtpvykvCGRCNGNR 194
Cdd:cd10719   58 -------CPKCKGKG 65
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 113-180 2.51e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 44.80  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969854 113 CEHCAGTGfhnvlrevvkhSRSGESvikeewvkELCQHCHGKGEVS-------------TACRGCKGKGIVLDEKRTRLH 179
Cdd:PRK14281 166 CKECNGTG-----------SKTGAT--------ETCPTCHGSGEVRqasktmfgqfvniTACPTCGGEGRVVKDRCPACY 226


                 .
gi 446969854 180 G 180
Cdd:PRK14281 227 G 227
PRK14289 PRK14289
molecular chaperone DnaJ;
148-192 1.92e-04

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 42.13  E-value: 1.92e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 446969854 148 CQHCHGKG----EVSTACRGCKGKGIVLDEKRTRLHGTPVYKVCGRCNG 192
Cdd:PRK14289 157 CSHCHGTGaegnNGSETCPTCKGSGSVTRVQNTILGTMQTQSTCPTCNG 205
 
Name Accession Description Interval E-value
Antiterm pfam03589
Antitermination protein;
25-107 5.39e-31

Antitermination protein;


Pssm-ID: 427381  Cd Length: 85  Bit Score: 109.77  E-value: 5.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969854   25 GSGGLTITDVMAAQGMVQSKAPLGFALFLAKVGVQ--DPQFAIEGLLNYAMALDNPTLNKLSEETRLQIIPYLVNFAFAD 102
Cdd:pfam03589   1 VSDACRCTDVMAALGMAQSKARFGVPVFCGKRGYSrlDSTEAIEALLQLAPDLTQKTVAKLWEETYKPFLDALVTYAFKE 80


                  ....*
gi 446969854  103 YSRSA 107
Cdd:pfam03589  81 YSRSA 85
Antiterm pfam03589
Antitermination protein;
157-242 2.02e-23

Antitermination protein;


Pssm-ID: 427381  Cd Length: 85  Bit Score: 90.51  E-value: 2.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969854  157 VSTACRgCKGKGIVLDEKRTRLH-GTPVYkvcgrCNGNRFSRLPTTLARLHVQKLVPDLTDYQ----WYKGYADVIDKLV 231
Cdd:pfam03589   1 VSDACR-CTDVMAALGMAQSKARfGVPVF-----CGKRGYSRLDSTEAIEALLQLAPDLTQKTvaklWEETYKPFLDALV 74

                          90
                  ....*....|.
gi 446969854  232 TKCWQEEAYAE 242
Cdd:pfam03589  75 TYAFKEYSRSA 85
phage_xxxx TIGR02642
uncharacterized phage protein; This uncharacterized protein is found in prophage regions of ...
 3-159 6.19e-06

uncharacterized phage protein; This uncharacterized protein is found in prophage regions of Shewanella oneidensis MR-1, Vibrio vulnificus YJ016, Yersinia pseudotuberculosis IP 32953, and Aeromonas hydrophila ATCC7966. It appears to have regions of sequence similarity to phage lambda antitermination protein Q. [Mobile and extrachromosomal element functions, Prophage functions]


Pssm-ID: 274243 [Multi-domain]  Cd Length: 186  Bit Score: 45.63  E-value: 6.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969854    3 LEALPKYYSPKSPKLSDDAPATGSGGLTITDVMAAQGMVQSKAPLGFALFLAKVgVQDPQfAIEGLLnyamALDNPTLNK 82
Cdd:TIGR02642   5 IEMLTILSSPRGMSIEERTAKRGPNVLTKEQLLGAIALAQRDNPIGIAILMAKY-MRDAY-AIQKLY----AHICEQLLP 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446969854   83 LSEETRLQIIPYL-VNfafadysrSAASKARCEHCAGTGfhnvlrevVKHSRSGEsvikeewvkelCQHCHGKGEVST 159
Cdd:TIGR02642  79 LITPNAAEAASYLaVN--------EVLNSCKCPRCRGTG--------LIQRRQRE-----------CDTCAGTGRFRP 129
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 113-194 2.38e-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: 41.00  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969854  113 CEHCAGTGfhnvlrevvkhSRSGESVIKeewvkelCQHCHGKGEV-------------STACRGCKGKGIVLDEKrtrlh 179
Cdd:pfam00684   1 CPTCNGSG-----------AKPGTKPTT-------CPTCGGTGQVrrvqqtgpgffqmQSTCPTCGGTGKIIKDP----- 57

                          90
                  ....*....|....*
gi 446969854  180 gtpvykvCGRCNGNR 194
Cdd:pfam00684  58 -------CKKCKGKG 65
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 113-194 2.49e-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: 41.09  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969854 113 CEHCAGTGfhnvlrevvkhSRSGESVIKeewvkelCQHCHGKGEV-------------STACRGCKGKGIVLDEKrtrlh 179
Cdd:cd10719    1 CPTCNGSG-----------AKPGTKPKT-------CPTCGGSGQVrqvqgtgfgffqtQTTCPTCGGTGKIIKDP----- 57

                         90
                 ....*....|....*
gi 446969854 180 gtpvykvCGRCNGNR 194
Cdd:cd10719   58 -------CPKCKGKG 65
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 113-180 2.51e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 44.80  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969854 113 CEHCAGTGfhnvlrevvkhSRSGESvikeewvkELCQHCHGKGEVS-------------TACRGCKGKGIVLDEKRTRLH 179
Cdd:PRK14281 166 CKECNGTG-----------SKTGAT--------ETCPTCHGSGEVRqasktmfgqfvniTACPTCGGEGRVVKDRCPACY 226


                 .
gi 446969854 180 G 180
Cdd:PRK14281 227 G 227
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 104-168 4.29e-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: 40.32  E-value: 4.29e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446969854 104 SRSAASKARCEHCAGTGFhnvlreVVKHSRSGESVIKeewVKELCQHCHGKGEV-STACRGCKGKG 168
Cdd:cd10719    9 AKPGTKPKTCPTCGGSGQ------VRQVQGTGFGFFQ---TQTTCPTCGGTGKIiKDPCPKCKGKG 65
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 61-179 5.57e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 43.82  E-value: 5.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969854  61 PQFAIEGLLNYAMALDNPTLNKlseETRLQIiPYLVnfAFADYSRSAASK----ARCEHCAGTGfhnvlreVVKHSRSGE 136
Cdd:PRK14286 120 PQRGSDLRYNLEVSLEDAALGR---EYKIEI-PRLE--SCVDCNGSGASKgsspTTCPDCGGSG-------QIRRTQGFF 186

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446969854 137 SVIKEewvkelCQHCHGKGEV-STACRGCKGKGivLDEKRTRLH 179
Cdd:PRK14286 187 SVATT------CPTCRGKGTViSNPCKTCGGQG--LQEKRRTIN 222
PRK14289 PRK14289
molecular chaperone DnaJ;
148-192 1.92e-04

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 42.13  E-value: 1.92e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 446969854 148 CQHCHGKG----EVSTACRGCKGKGIVLDEKRTRLHGTPVYKVCGRCNG 192
Cdd:PRK14289 157 CSHCHGTGaegnNGSETCPTCKGSGSVTRVQNTILGTMQTQSTCPTCNG 205
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 104-168 3.37e-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: 37.92  E-value: 3.37e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446969854  104 SRSAASKARCEHCAGTGFHNVLREVVKHSRSGESVikeewvkelCQHCHGKGEV-STACRGCKGKG 168
Cdd:pfam00684   9 AKPGTKPTTCPTCGGTGQVRRVQQTGPGFFQMQST---------CPTCGGTGKIiKDPCKKCKGKG 65
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 111-181 5.74e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 40.68  E-value: 5.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969854 111 ARCEHCAGTGFHNvlrevvkhsrsgesvikeewvKEL--CQHCHGKGE-------------VSTACRGCKGKGIVLDEKR 175
Cdd:PRK14290 150 AMCPDCSGTGAKN---------------------GKLitCPTCHGTGQqrivrgqgffrmvTVTTCRTCGGRGRIPEEKC 208


                 ....*.
gi 446969854 176 TRLHGT 181
Cdd:PRK14290 209 PRCNGT 214
PRK14289 PRK14289
molecular chaperone DnaJ;
86-174 6.04e-04

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 40.58  E-value: 6.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446969854  86 ETRLQIIPYLV-NFAFADYSRSAASKARCEHCAGTGfhnvlreVVkhSRSGESVIKEEWVKELCQHCHGKGEVST-ACRG 163
Cdd:PRK14289 146 EKKFKVKKYVPcSHCHGTGAEGNNGSETCPTCKGSG-------SV--TRVQNTILGTMQTQSTCPTCNGEGKIIKkKCKK 216

                         90
                 ....*....|.
gi 446969854 164 CKGKGIVLDEK 174
Cdd:PRK14289 217 CGGEGIVYGEE 227
PRK14280 PRK14280
molecular chaperone DnaJ;
109-179 3.24e-03

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 38.16  E-value: 3.24e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446969854 109 SKARCEHCAGTGFHNV-----LREVVKhsrsgesvikeewvKELCQHCHGKG-EVSTACRGCKGKGIVldEKRTRLH 179
Cdd:PRK14280 159 SKETCSHCGGSGQVSVeqntpFGRVVN--------------RQTCPHCNGTGqEIKEKCPTCHGKGKV--RKRKKIN 219
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 146-192 4.93e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 37.85  E-value: 4.93e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446969854 146 ELCQHCHGKGEVSTA----CRGCKGKGIVLDEKRTRLHGTPVYKVCGRCNG 192
Cdd:PRK14282 153 ETCPHCGGTGVEPGSgyvtCPKCHGTGRIREERRSFFGVFVSERTCERCGG 203
PRK14288 PRK14288
molecular chaperone DnaJ;
113-174 7.15e-03

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 37.36  E-value: 7.15e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446969854 113 CEHCAGTGFHNVLREVVKHSR-SGESVIKEEWVK--ELCQHCHGKGEV-STACRGCKGKGIVLDEK 174
Cdd:PRK14288 143 CESCDGTGAKDKALETCKQCNgQGQVFMRQGFMSfaQTCGACQGKGKIiKTPCQACKGKTYILKDE 208
 
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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