|
Name |
Accession |
Description |
Interval |
E-value |
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
1-201 |
6.33e-124 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 363.27 E-value: 6.33e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 1 SQVFSTAEDSQNAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATAKEQQIRIQ 80
Cdd:PRK00290 416 SQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDIDANGIVHVSAKDKGTGKEQSITIT 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 81 ASGGLSEADIDKMVKDAEANAAADKQRREAVDAKNHADALVHSTEKALAEHGSKVAETERRAIEDAVSDLKEALKGSDAE 160
Cdd:PRK00290 496 ASSGLSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKELGDKVPADEKEKIEAAIKELKEALKGEDKE 575
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 148791482 161 AIKAKTNTLAQASMKLGEAMYTQQAEADAKRDAAK--DDVVDA 201
Cdd:PRK00290 576 AIKAKTEELTQASQKLGEAMYQQAQAAQGAAGAAAkdDDVVDA 618
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
1-181 |
1.91e-93 |
|
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE chaperone system. All members of the seed alignment were taken from completely sequenced bacterial or archaeal genomes and (except for Mycoplasma sequence) found clustered with other genes of this systems. This model excludes DnaK homologs that are not DnaK itself, such as the heat shock cognate protein HscA (TIGR01991). However, it is not designed to distinguish among DnaK paralogs in eukaryotes. Note that a number of dnaK genes have shadow ORFs in the same reverse (relative to dnaK) reading frame, a few of which have been assigned glutamate dehydrogenase activity. The significance of this observation is unclear; lengths of such shadow ORFs are highly variable as if the presumptive protein product is not conserved. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274091 [Multi-domain] Cd Length: 595 Bit Score: 284.20 E-value: 1.91e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 1 SQVFSTAEDSQNAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATAKEQQIRIQ 80
Cdd:TIGR02350 414 SQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDANGILHVSAKDKGTGKEQSITIT 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 81 ASGGLSEADIDKMVKDAEANAAADKQRREAVDAKNHADALVHSTEKALAEHGSKVAETERRAIEDAVSDLKEALKGSDAE 160
Cdd:TIGR02350 494 ASSGLSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAGDKLPAEEKEKIEKAVAELKEALKGEDVE 573
|
170 180
....*....|....*....|.
gi 148791482 161 AIKAKTNTLAQASMKLGEAMY 181
Cdd:TIGR02350 574 EIKAKTEELQQALQKLAEAMY 594
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
1-181 |
3.13e-84 |
|
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region.
Pssm-ID: 394970 [Multi-domain] Cd Length: 598 Bit Score: 260.27 E-value: 3.13e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 1 SQVFSTAEDSQNAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATAKEQQIRIQ 80
Cdd:pfam00012 417 SQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDANGILTVSAKDKGTGKEQEITIE 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 81 ASGGLSEADIDKMVKDAEANAAADKQRREAVDAKNHADALVHSTEKALAEHGSKVAETERRAIEDAVSDLKEALKGSDAE 160
Cdd:pfam00012 497 ASEGLSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGDKVPEAEKSKVESAIEWLKDELEGDDKE 576
|
170 180
....*....|....*....|.
gi 148791482 161 AIKAKTNTLAQASMKLGEAMY 181
Cdd:pfam00012 577 EIEAKTEELAQVSQKIGERMY 597
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
1-94 |
4.41e-38 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 136.49 E-value: 4.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 1 SQVFSTAEDSQNAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATAKEQQIRIQ 80
Cdd:COG0443 387 SQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGILSVSAKDLGTGKEQSITIK 466
|
90
....*....|....
gi 148791482 81 asgglseADIDKMV 94
Cdd:COG0443 467 -------EEIERML 473
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
1-201 |
6.33e-124 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 363.27 E-value: 6.33e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 1 SQVFSTAEDSQNAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATAKEQQIRIQ 80
Cdd:PRK00290 416 SQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDIDANGIVHVSAKDKGTGKEQSITIT 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 81 ASGGLSEADIDKMVKDAEANAAADKQRREAVDAKNHADALVHSTEKALAEHGSKVAETERRAIEDAVSDLKEALKGSDAE 160
Cdd:PRK00290 496 ASSGLSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKELGDKVPADEKEKIEAAIKELKEALKGEDKE 575
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 148791482 161 AIKAKTNTLAQASMKLGEAMYTQQAEADAKRDAAK--DDVVDA 201
Cdd:PRK00290 576 AIKAKTEELTQASQKLGEAMYQQAQAAQGAAGAAAkdDDVVDA 618
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
1-181 |
1.91e-93 |
|
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE chaperone system. All members of the seed alignment were taken from completely sequenced bacterial or archaeal genomes and (except for Mycoplasma sequence) found clustered with other genes of this systems. This model excludes DnaK homologs that are not DnaK itself, such as the heat shock cognate protein HscA (TIGR01991). However, it is not designed to distinguish among DnaK paralogs in eukaryotes. Note that a number of dnaK genes have shadow ORFs in the same reverse (relative to dnaK) reading frame, a few of which have been assigned glutamate dehydrogenase activity. The significance of this observation is unclear; lengths of such shadow ORFs are highly variable as if the presumptive protein product is not conserved. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274091 [Multi-domain] Cd Length: 595 Bit Score: 284.20 E-value: 1.91e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 1 SQVFSTAEDSQNAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATAKEQQIRIQ 80
Cdd:TIGR02350 414 SQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDANGILHVSAKDKGTGKEQSITIT 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 81 ASGGLSEADIDKMVKDAEANAAADKQRREAVDAKNHADALVHSTEKALAEHGSKVAETERRAIEDAVSDLKEALKGSDAE 160
Cdd:TIGR02350 494 ASSGLSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAGDKLPAEEKEKIEKAVAELKEALKGEDVE 573
|
170 180
....*....|....*....|.
gi 148791482 161 AIKAKTNTLAQASMKLGEAMY 181
Cdd:TIGR02350 574 EIKAKTEELQQALQKLAEAMY 594
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
1-181 |
3.13e-84 |
|
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region.
Pssm-ID: 394970 [Multi-domain] Cd Length: 598 Bit Score: 260.27 E-value: 3.13e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 1 SQVFSTAEDSQNAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATAKEQQIRIQ 80
Cdd:pfam00012 417 SQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDANGILTVSAKDKGTGKEQEITIE 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 81 ASGGLSEADIDKMVKDAEANAAADKQRREAVDAKNHADALVHSTEKALAEHGSKVAETERRAIEDAVSDLKEALKGSDAE 160
Cdd:pfam00012 497 ASEGLSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGDKVPEAEKSKVESAIEWLKDELEGDDKE 576
|
170 180
....*....|....*....|.
gi 148791482 161 AIKAKTNTLAQASMKLGEAMY 181
Cdd:pfam00012 577 EIEAKTEELAQVSQKIGERMY 597
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
1-196 |
5.30e-77 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 243.19 E-value: 5.30e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 1 SQVFSTAEDSQNAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATAKEQQIRIQ 80
Cdd:PTZ00400 457 SQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTFDVDANGIMNISAVDKSTGKKQEITIQ 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 81 ASGGLSEADIDKMVKDAEANAAADKQRREAVDAKNHADALVHSTEKALAEHGSKVAETERRAIEDAVSDLKEALKGSDAE 160
Cdd:PTZ00400 537 SSGGLSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSDLKDKISDADKDELKQKITKLRSTLSSEDVD 616
|
170 180 190
....*....|....*....|....*....|....*.
gi 148791482 161 AIKAKTNTLAQASMKLGEAMYTQQAEADAKRDAAKD 196
Cdd:PTZ00400 617 SIKDKTKQLQEASWKISQQAYKQGNSDNQQSEQSTN 652
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
1-201 |
3.91e-70 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 224.22 E-value: 3.91e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 1 SQVFSTAEDSQNAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATAKEQQIRIQ 80
Cdd:CHL00094 418 SEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDIDANGILSVTAKDKGTGKEQSITIQ 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 81 ASGGLSEADIDKMVKDAEANAAADKQRREAVDAKNHADALVHSTEKALAEHGSKVAETERRAIEDAVSDLKEALKGSDAE 160
Cdd:CHL00094 498 GASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKELKDKISEEKKEKIENLIKKLRQALQNDNYE 577
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 148791482 161 AIKAKTNTLAQASMKLGEAMYTQQAEADAKRDaaKDDVVDA 201
Cdd:CHL00094 578 SIKSLLEELQKALMEIGKEVYSSTSTTDPASN--DDDVIDT 616
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
1-201 |
1.90e-65 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 212.79 E-value: 1.90e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 1 SQVFSTAEDSQNAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATAKEQQIRIQ 80
Cdd:PLN03184 455 SEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFDIDANGILSVSATDKGTGKKQDITIT 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 81 ASGGLSEADIDKMVKDAEANAAADKQRREAVDAKNHADALVHSTEKALAEHGSKVAETERRAIEDAVSDLKEALKGSDAE 160
Cdd:PLN03184 535 GASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKELGDKVPADVKEKVEAKLKELKDAIASGSTQ 614
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 148791482 161 AIKAKTNTLAQASMKLGEAMYTQQAEADA--------------KRDAAKDDVVDA 201
Cdd:PLN03184 615 KMKDAMAALNQEVMQIGQSLYNQPGAGGAgpapggeagsssssSSGGDGDDVIDA 669
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
1-183 |
4.48e-64 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 208.84 E-value: 4.48e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 1 SQVFSTAEDSQNAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATAKEQQIRIQ 80
Cdd:PRK13411 418 SQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSFEIDVNGILKVSAQDQGTGREQSIRIT 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 81 ASGGLSEADIDKMVKDAEANAAADKQRREAVDAKNHADALVHSTEKALAEHGSKVAETERRAIEDAVSDLKEALKGSD-- 158
Cdd:PRK13411 498 NTGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKENGELISEELKQRAEQKVEQLEAALTDPNis 577
|
170 180
....*....|....*....|....*
gi 148791482 159 AEAIKAKTNTLAQASMKLGEAMYTQ 183
Cdd:PRK13411 578 LEELKQQLEEFQQALLAIGAEVYQQ 602
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
1-201 |
4.58e-62 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 203.71 E-value: 4.58e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 1 SQVFSTAEDSQNAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATAKEQQIRIQ 80
Cdd:PRK13410 418 SDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFDIDANGILQVSATDRTTGREQSVTIQ 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 81 ASGGLSEADIDKMVKDAEANAAADKQRREAVDAKNHADALVHSTEKALA----EHGSKVAETERRAIEDAVSDLKEALKG 156
Cdd:PRK13410 498 GASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERRLRdaalEFGPYFAERQRRAVESAMRDVQDSLEQ 577
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 148791482 157 SDAEAIKaktntLAQASmkLGEAMYTQQAEADAKRDAAKDDVVDA 201
Cdd:PRK13410 578 DDDRELD-----LAVAD--LQEALYGLNREVRAEYKEEDEGPLQG 615
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
1-197 |
2.69e-58 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 193.75 E-value: 2.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 1 SQVFSTAEDSQNAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATAKEQQIRIQ 80
Cdd:PTZ00186 443 SQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDIDANGICHVTAKDKATGKTQNITIT 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 81 ASGGLSEADIDKMVKDAEANAAADKQRREAVDAKNHADALVHSTEKALAEHgSKVAETERRAIEDAVSDLKEALKGSDA- 159
Cdd:PTZ00186 523 ANGGLSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGEW-KYVSDAEKENVKTLVAELRKAMENPNVa 601
|
170 180 190
....*....|....*....|....*....|....*....
gi 148791482 160 -EAIKAKTNTLAQASMKLGEAMYTQQAEADAKRDAAKDD 197
Cdd:PTZ00186 602 kDDLAAATDKLQKAVMECGRTEYQQAAAANSGSSSNSGE 640
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
1-155 |
3.68e-47 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 163.43 E-value: 3.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 1 SQVFSTAEDSQNAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATAKEQQIRIQ 80
Cdd:PTZ00009 427 SQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTFDIDANGILNVSAEDKSTGKSNKITIT 506
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148791482 81 ASGG-LSEADIDKMVKDAEANAAADKQRREAVDAKNHADALVHSTEKALAEH--GSKVAETERRAIEDAVsdlKEALK 155
Cdd:PTZ00009 507 NDKGrLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDEkvKGKLSDSDKATIEKAI---DEALE 581
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
2-173 |
1.22e-45 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 158.80 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 2 QVFSTAEDSQNAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATAKEQQIRIQA 81
Cdd:PRK05183 421 QEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADGLLSVTAMEKSTGVEASIQVKP 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 82 SGGLSEADIDKMVKDAEANAAADKQRREAVDAKNHADALVHSTEKALAEHGSKVAETERRAIEDAVSDLKEALKGSDAEA 161
Cdd:PRK05183 501 SYGLTDDEIARMLKDSMSHAEEDMQARALAEQKVEAERVLEALQAALAADGDLLSAAERAAIDAAMAALREVAQGDDADA 580
|
170
....*....|..
gi 148791482 162 IKAKTNTLAQAS 173
Cdd:PRK05183 581 IEAAIKALDKAT 592
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
1-94 |
4.41e-38 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 136.49 E-value: 4.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 1 SQVFSTAEDSQNAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATAKEQQIRIQ 80
Cdd:COG0443 387 SQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGILSVSAKDLGTGKEQSITIK 466
|
90
....*....|....
gi 148791482 81 asgglseADIDKMV 94
Cdd:COG0443 467 -------EEIERML 473
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
4-163 |
3.30e-30 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 116.11 E-value: 3.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 4 FSTAEDSQNAVTIRVFQGEREMAADNKMLGQFDLMGIPPAPRGMPQIEVTFDIDANGIVNVSAKDKATAKEQQIRIQASG 83
Cdd:PRK01433 401 FTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDADGILSVSAYEKISNTSHAIEVKPNH 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 84 GLSEADIDKMVKDAEANAAADKQRREAVDAKNHADALVHSTEKALAEHGSKVAETERRAIEDAVSDLKEALKGSDAEAIK 163
Cdd:PRK01433 481 GIDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAIAELTTLLSESEISIINSLLDNIKEAVHARDIILIN 560
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
70-192 |
5.85e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 36.90 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148791482 70 ATAKEQQIRIQASggLSEADIDKMVKDAE-ANAAADKQRREAVDAKNHADALVHSTEKALAEHGSKVAETERRAIEDAVS 148
Cdd:pfam05262 211 DAKRAQQLKEELD--KKQIDADKAQQKADfAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 148791482 149 DLK----EALKGSDAEAIKAKTNTLAQASMKlgeamytQQAEADAKRD 192
Cdd:pfam05262 289 EIKkndeEALKAKDHKAFDLKQESKASEKEA-------EDKELEAQKK 329
|
|
|