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Conserved domains on  [gi|1710358137|gb|TVO92747|]
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cobalamin 5'-phosphate synthase [Shewanella algae]

Protein Classification

co-chaperone HscB( domain architecture ID 11480322)

co-chaperone HscB is involved in the maturation of iron-sulfur cluster-containing proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hscB PRK05014
co-chaperone HscB; Provisional
 1-174 1.17e-92

co-chaperone HscB; Provisional


:

Pssm-ID: 179914 [Multi-domain]  Cd Length: 171  Bit Score: 266.77  E-value: 1.17e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358137   1 MNYFELFDLTPSFDVDTAELASRYRDLQRAVHPDKFANASEQQKLLAISRTAQINDAFQTLKDPIRRAEHMLALKGVDIS 80
Cdd:PRK05014    1 MDYFTLFGLPARYDIDTQLLASRYQELQRQFHPDKFANASERERLLAVQQAATINDAYQTLKHPLKRAEYLLSLHGFDLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358137  81 HETTTVKDTAFLMQQMEWREALEEIGQSGDAQSDIDELDVSFATYRKQVTELLRNQLHsskEADAIAAADQVRKLKFMAK 160
Cdd:PRK05014   81 HEQHTVRDTAFLMEQMELREELEDIEQSKDPEAALESFIKRVKKMFKTRLQQMVEQLD---NEAWDAAADTVRKLKFLDK 157

                         170
                  ....*....|....
gi 1710358137 161 LQDELQRAQDALFD 174
Cdd:PRK05014  158 LRSEVEQLEEKLLD 171
 
Name Accession Description Interval E-value
hscB PRK05014
co-chaperone HscB; Provisional
 1-174 1.17e-92

co-chaperone HscB; Provisional


Pssm-ID: 179914 [Multi-domain]  Cd Length: 171  Bit Score: 266.77  E-value: 1.17e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358137   1 MNYFELFDLTPSFDVDTAELASRYRDLQRAVHPDKFANASEQQKLLAISRTAQINDAFQTLKDPIRRAEHMLALKGVDIS 80
Cdd:PRK05014    1 MDYFTLFGLPARYDIDTQLLASRYQELQRQFHPDKFANASERERLLAVQQAATINDAYQTLKHPLKRAEYLLSLHGFDLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358137  81 HETTTVKDTAFLMQQMEWREALEEIGQSGDAQSDIDELDVSFATYRKQVTELLRNQLHsskEADAIAAADQVRKLKFMAK 160
Cdd:PRK05014   81 HEQHTVRDTAFLMEQMELREELEDIEQSKDPEAALESFIKRVKKMFKTRLQQMVEQLD---NEAWDAAADTVRKLKFLDK 157

                         170
                  ....*....|....
gi 1710358137 161 LQDELQRAQDALFD 174
Cdd:PRK05014  158 LRSEVEQLEEKLLD 171
hscB TIGR00714
Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K ...
 13-173 2.02e-30

Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K heat shock cognate protein) of a pair of proteins Hsc66-Hsc20, related to the DnaK-DnaJ heat shock proteins, which also serve as molecular chaperones. Hsc20, unlike DnaJ, appears not to have chaperone activity on its own, but to act solely as a regulatory subunit for Hsc66 (i.e., to be a co-chaperone). The gene for Hsc20 in E. coli, hscB, is not induced by heat shock. [Protein fate, Protein folding and stabilization]


Pssm-ID: 211601 [Multi-domain]  Cd Length: 155  Bit Score: 108.43  E-value: 2.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358137  13 FDVDTAELASRYRDLQRAVHPDKFANAseQQKLLAISRTAQINDAFQTLKDPIRRAEHMLALKGVDISHETTTVKDTAFL 92
Cdd:TIGR00714   1 WQLDQSRLRKRYRQLQAQYHPDASGMA--QEQLAASQQSTTLNQAYHTLKDPLRRAEYMLKLLNIDLTQEQTSERDTAFP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358137  93 MQQMEWREALEEIGQSGDaQSDIDeldvSFATYRKQVTELLRNQLHSS-KEADAIAAADQVRKLKFMAKLQDELQRAQDA 171
Cdd:TIGR00714  79 MELLKVRDELDEIEQMDD-EAGLE----LLEKQNKEMIQDIEAQLGQClNDQDWAAAVKYTVKLKYWYKLASAFEDWEEG 153


                  ..
gi 1710358137 172 LF 173
Cdd:TIGR00714 154 KQ 155
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
1-64 2.19e-20

DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 79.84  E-value: 2.19e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1710358137   1 MNYFELFDLTPsfDVDTAELASRYRDLQRAVHPDKFAN-ASEQQKLLAISRTAQINDAFQTLKDP 64
Cdd:COG1076     4 DDAFELLGLPP--DADDAELKRAYRKLQREHHPDRLAAgLPEEEQRLALQKAAAINEAYETLKDP 66
HSCB_C pfam07743
HSCB C-terminal oligomerization domain; This domain is the HSCB C-terminal oligomerization ...
 87-166 1.02e-12

HSCB C-terminal oligomerization domain; This domain is the HSCB C-terminal oligomerization domain and is found on co-chaperone proteins.


Pssm-ID: 462252  Cd Length: 75  Bit Score: 60.23  E-value: 1.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358137  87 KDTAFLMQQMEWREALEEIGQsgDAQSDIDELDVSFATYRKQVTELLRNQLhssKEADAIAAADQVRKLKFMAKLQDELQ 166
Cdd:pfam07743   1 MDPEFLMEQMEWREELEEAEA--RDEEELEELKAENKERIKELEAELEEAF---DEQDLEAAADLVRRLRYLEKIQEEIK 75
DnaJ smart00271
DnaJ molecular chaperone homology domain;
1-64 1.41e-08

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 48.77  E-value: 1.41e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1710358137    1 MNYFELFDLTPsfDVDTAELASRYRDLQRAVHPDKFANASEQqkllAISRTAQINDAFQTLKDP 64
Cdd:smart00271   1 TDYYEILGVPR--DASLDEIKKAYRKLALKYHPDKNPGDKEE----AEEKFKEINEAYEVLSDP 58
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 2-63 2.41e-08

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) 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 chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 48.31  E-value: 2.41e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1710358137   2 NYFELFDLTPsfDVDTAELASRYRDLQRAVHPDKFANASEQQKllaisRTAQINDAFQTLKD 63
Cdd:cd06257     1 DYYDILGVPP--DASDEEIKKAYRKLALKYHPDKNPDDPEAEE-----KFKEINEAYEVLSD 55
 
Name Accession Description Interval E-value
hscB PRK05014
co-chaperone HscB; Provisional
 1-174 1.17e-92

co-chaperone HscB; Provisional


Pssm-ID: 179914 [Multi-domain]  Cd Length: 171  Bit Score: 266.77  E-value: 1.17e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358137   1 MNYFELFDLTPSFDVDTAELASRYRDLQRAVHPDKFANASEQQKLLAISRTAQINDAFQTLKDPIRRAEHMLALKGVDIS 80
Cdd:PRK05014    1 MDYFTLFGLPARYDIDTQLLASRYQELQRQFHPDKFANASERERLLAVQQAATINDAYQTLKHPLKRAEYLLSLHGFDLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358137  81 HETTTVKDTAFLMQQMEWREALEEIGQSGDAQSDIDELDVSFATYRKQVTELLRNQLHsskEADAIAAADQVRKLKFMAK 160
Cdd:PRK05014   81 HEQHTVRDTAFLMEQMELREELEDIEQSKDPEAALESFIKRVKKMFKTRLQQMVEQLD---NEAWDAAADTVRKLKFLDK 157

                         170
                  ....*....|....
gi 1710358137 161 LQDELQRAQDALFD 174
Cdd:PRK05014  158 LRSEVEQLEEKLLD 171
hscB PRK01773
Fe-S protein assembly co-chaperone HscB;
1-174 5.14e-42

Fe-S protein assembly co-chaperone HscB;


Pssm-ID: 179335 [Multi-domain]  Cd Length: 173  Bit Score: 138.34  E-value: 5.14e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358137   1 MNYFELFDLTPSFDVDTAELASRYRDLQRAVHPDKFANASEQQKLLAISRTAQINDAFQTLKDPIRRAEHMLALK-GVDI 79
Cdd:PRK01773    2 NNPFALFDLPVDFQLDNALLSERYLALQKSLHPDNFANSSAQEQRLAMQKSAEVNDALQILKDPILRAEAIIALNtGEQQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358137  80 SHETTTVKDTAFLMQQMEWREALEEIGQsgdaQSDIDELdVSFATYRKQVTELLRNQLHSSKEADAIAAADQVR-KLKFM 158
Cdd:PRK01773   82 NLEEKSTQDMAFLMQQMEWREQLEEIEQ----QQDEDAL-TAFSKEIKQEQQAILTELSTALNSQQWQQASQINdRLRFI 156

                         170
                  ....*....|....*.
gi 1710358137 159 AKLQDELQRAQDALFD 174
Cdd:PRK01773  157 KKLIIEIERVEEKLFD 172
hscB PRK03578
Fe-S protein assembly co-chaperone HscB;
1-174 7.87e-42

Fe-S protein assembly co-chaperone HscB;


Pssm-ID: 235133 [Multi-domain]  Cd Length: 176  Bit Score: 137.84  E-value: 7.87e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358137   1 MNYFELFDLTPSFDVDTAELASRYRDLQRAVHPDKFANASEQQKLLAISRTAQINDAFQTLKDPIRRAEHMLALKGVDIS 80
Cdd:PRK03578    6 DDHFSLFGLPARFALDEAALDAAYRTVQAQVHPDRFAAAGDAEKRVAMQWATRANEAYQTLRDPLKRARYLLHLRGVDVQ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358137  81 HETTTVKDTAFLMQQMEWREALEEigqsGDAQSDIDELDVSFATYRKQVTEL---LRNQLHSSKEADaiAAADQVRKLKF 157
Cdd:PRK03578   86 AENNTAMPPAFLMQQMEWREAIED----ARAARDVDALDALLAELRDERRERyaeLGALLDSRGDDQ--AAAEAVRQLMF 159

                         170
                  ....*....|....*..
gi 1710358137 158 MAKLQDELQRAQDALFD 174
Cdd:PRK03578  160 IEKLAQEIGAAIERLED 176
hscB PRK00294
co-chaperone HscB; Provisional
 3-174 6.94e-36

co-chaperone HscB; Provisional


Pssm-ID: 166894 [Multi-domain]  Cd Length: 173  Bit Score: 122.65  E-value: 6.94e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358137   3 YFELFDLTPSFDVDTAELASRYRDLQRAVHPDKFANASEQQKLLAISRTAQINDAFQTLKDPIRRAEHMLALKGVDISHE 82
Cdd:PRK00294    6 HFALFDLQPSFRLDLDQLATRYRELAREVHPDRFADAPEREQRLALERSASLNEAYQTLKSPPRRARYLLALSGHEVPLE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358137  83 tTTVKDTAFLMQQMEWREALEEIGQSGDAQsdideldvSFATYRKQVtELLRNQLHSSKEA--DAIAAADQ----VRKLK 156
Cdd:PRK00294   86 -VTVHDPEFLLQQMQLREELEELQDEADLA--------GVATFKRRL-KAAQDELNESFAAcwDDAARREEaerlMRRMQ 155

                         170
                  ....*....|....*...
gi 1710358137 157 FMAKLQDELQRAQDALFD 174
Cdd:PRK00294  156 FLDKLAQEVRQLEERLDD 173
hscB TIGR00714
Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K ...
 13-173 2.02e-30

Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K heat shock cognate protein) of a pair of proteins Hsc66-Hsc20, related to the DnaK-DnaJ heat shock proteins, which also serve as molecular chaperones. Hsc20, unlike DnaJ, appears not to have chaperone activity on its own, but to act solely as a regulatory subunit for Hsc66 (i.e., to be a co-chaperone). The gene for Hsc20 in E. coli, hscB, is not induced by heat shock. [Protein fate, Protein folding and stabilization]


Pssm-ID: 211601 [Multi-domain]  Cd Length: 155  Bit Score: 108.43  E-value: 2.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358137  13 FDVDTAELASRYRDLQRAVHPDKFANAseQQKLLAISRTAQINDAFQTLKDPIRRAEHMLALKGVDISHETTTVKDTAFL 92
Cdd:TIGR00714   1 WQLDQSRLRKRYRQLQAQYHPDASGMA--QEQLAASQQSTTLNQAYHTLKDPLRRAEYMLKLLNIDLTQEQTSERDTAFP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358137  93 MQQMEWREALEEIGQSGDaQSDIDeldvSFATYRKQVTELLRNQLHSS-KEADAIAAADQVRKLKFMAKLQDELQRAQDA 171
Cdd:TIGR00714  79 MELLKVRDELDEIEQMDD-EAGLE----LLEKQNKEMIQDIEAQLGQClNDQDWAAAVKYTVKLKYWYKLASAFEDWEEG 153


                  ..
gi 1710358137 172 LF 173
Cdd:TIGR00714 154 KQ 155
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
1-64 2.19e-20

DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 79.84  E-value: 2.19e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1710358137   1 MNYFELFDLTPsfDVDTAELASRYRDLQRAVHPDKFAN-ASEQQKLLAISRTAQINDAFQTLKDP 64
Cdd:COG1076     4 DDAFELLGLPP--DADDAELKRAYRKLQREHHPDRLAAgLPEEEQRLALQKAAAINEAYETLKDP 66
hscB PRK01356
co-chaperone HscB; Provisional
 2-166 6.79e-18

co-chaperone HscB; Provisional


Pssm-ID: 167217 [Multi-domain]  Cd Length: 166  Bit Score: 76.07  E-value: 6.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358137   2 NYFELFDLTPSFDVDTAELASRYRDLQRAVHPDKFANASEQQKLLAISrtAQINDAFQTLKDPIRRAEHMLALKGVDISH 81
Cdd:PRK01356    3 NYFQLLGLPQEYNIDLKILEKQYFAMQVKYHPDKAKTLQEKEQNLIIA--SELNNAYSTLKDALKRAEYMLLLQNINLND 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358137  82 ETTTVKDTAFLMQQMeWREalEEIGQSGDAQSDIDELDVSFATYRKQVTELLRNQLhssKEADAIAAADQVRKLKFMAKL 161
Cdd:PRK01356   81 EKTRSLLSPLELSIF-WDE--MERIENTILFSDLEKIKNKYELMYKNEIDSLKQAF---EEQNLSDATIKTSKLKYIGTL 154


                  ....*
gi 1710358137 162 QDELQ 166
Cdd:PRK01356  155 LNKLQ 159
HSCB_C pfam07743
HSCB C-terminal oligomerization domain; This domain is the HSCB C-terminal oligomerization ...
 87-166 1.02e-12

HSCB C-terminal oligomerization domain; This domain is the HSCB C-terminal oligomerization domain and is found on co-chaperone proteins.


Pssm-ID: 462252  Cd Length: 75  Bit Score: 60.23  E-value: 1.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358137  87 KDTAFLMQQMEWREALEEIGQsgDAQSDIDELDVSFATYRKQVTELLRNQLhssKEADAIAAADQVRKLKFMAKLQDELQ 166
Cdd:pfam07743   1 MDPEFLMEQMEWREELEEAEA--RDEEELEELKAENKERIKELEAELEEAF---DEQDLEAAADLVRRLRYLEKIQEEIK 75
DnaJ smart00271
DnaJ molecular chaperone homology domain;
1-64 1.41e-08

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 48.77  E-value: 1.41e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1710358137    1 MNYFELFDLTPsfDVDTAELASRYRDLQRAVHPDKFANASEQqkllAISRTAQINDAFQTLKDP 64
Cdd:smart00271   1 TDYYEILGVPR--DASLDEIKKAYRKLALKYHPDKNPGDKEE----AEEKFKEINEAYEVLSDP 58
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 2-63 2.41e-08

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) 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 chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 48.31  E-value: 2.41e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1710358137   2 NYFELFDLTPsfDVDTAELASRYRDLQRAVHPDKFANASEQQKllaisRTAQINDAFQTLKD 63
Cdd:cd06257     1 DYYDILGVPP--DASDEEIKKAYRKLALKYHPDKNPDDPEAEE-----KFKEINEAYEVLSD 55
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
2-76 2.64e-08

Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 48.95  E-value: 2.64e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1710358137   2 NYFELFDLTPsfDVDTAELASRYRDLQRAVHPDKFAnaseQQKLLAISRTAQINDAFQTLKDPIRRAEHMLALKG 76
Cdd:COG2214     6 DHYAVLGVPP--DASLEEIRQAYRRLAKLLHPDRGG----ELKALAEELFQRLNEAYEVLSDPERRAEYDRELGQ 74
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 2-153 5.29e-07

DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440252 [Multi-domain]  Cd Length: 139  Bit Score: 46.62  E-value: 5.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358137   2 NYFELFDLTPsfDVDTAELASRYRDLQRAVHPDKFANASEqqkllAISRTAQINDAFQTLKDPIRRAEHMLAlkGVDISH 81
Cdd:COG0484     1 DYYEILGVSR--DASAEEIKKAYRKLAKKYHPDRNPGDPE-----AEEKFKEINEAYEVLSDPEKRAAYDRF--GHAAEL 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1710358137  82 ETTTVKDTAflmqqmEWREALEEIGQSGDAQSDIDELDVSFATYRKQVTELLRNQLHSSKEADAIAAADQVR 153
Cdd:COG0484    72 LLATELAES------AAAEAAAAEAKEEAAEAGASEYEAIAEEASQLRLASLLLLLALLELALAAVLGLLLA 137
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 1-70 8.10e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 44.88  E-value: 8.10e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358137   1 MNYFELFDLTPSFDVDtaELASRYRDLQRAVHPDKFANASEQQKLlaisrtAQINDAFQTLKDPIRRAEH 70
Cdd:PRK14292    2 MDYYELLGVSRTASAD--EIKSAYRKLALKYHPDRNKEKGAAEKF------AQINEAYAVLSDAEKRAHY 63
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 2-69 1.27e-04

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 38.22  E-value: 1.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1710358137   2 NYFELFDLTPsfDVDTAELASRYRDLQRAVHPDKfaNASEQQkllAISRTAQINDAFQTLKDPIRRAE 69
Cdd:pfam00226   1 DYYEILGVSP--DASDEEIKKAYRKLALKYHPDK--NPGDPE---AEEKFKEINEAYEVLSDPEKRAI 61
PRK10266 PRK10266
curved DNA-binding protein;
2-70 3.73e-04

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 39.80  E-value: 3.73e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1710358137   2 NYFELFDLTPSFDVDTAELAsrYRDLQRAVHPD--KFANASEQQKLLAisrtaqinDAFQTLKDPIRRAEH 70
Cdd:PRK10266    5 DYYAIMGVKPTDDLKTIKTA--YRRLARKYHPDvsKEPDAEARFKEVA--------EAWEVLSDEQRRAEY 65
PRK14295 PRK14295
molecular chaperone DnaJ;
14-70 4.27e-04

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 39.83  E-value: 4.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1710358137  14 DVDTAELASRYRDLQRAVHPDkfANASEQQkllAISRTAQINDAFQTLKDPIRRAEH 70
Cdd:PRK14295   20 DATEAEIKKAYRKLAREYHPD--ANKGDAK---AEERFKEISEAYDVLSDEKKRKEY 71
PRK14293 PRK14293
molecular chaperone DnaJ;
2-68 6.49e-04

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 39.20  E-value: 6.49e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1710358137   2 NYFELfdLTPSFDVDTAELASRYRDLQRAVHPD--KFANASEQQKllaisrtaQINDAFQTLKDPIRRA 68
Cdd:PRK14293    4 DYYEI--LGVSRDADKDELKRAYRRLARKYHPDvnKEPGAEDRFK--------EINRAYEVLSDPETRA 62
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 19-67 1.93e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 37.83  E-value: 1.93e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1710358137  19 ELASRYRDLQRAVHPDKFANASEQQKLlaisrtAQINDAFQTLKDPIRR 67
Cdd:PRK14291   19 EIKKAYRRLARKYHPDFNKNPEAEEKF------KEINEAYQVLSDPEKR 61
 
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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