|
Name |
Accession |
Description |
Interval |
E-value |
| DUF1977 |
pfam09320 |
Domain of unknown function (DUF1977); Members of this family of functionally uncharacterized ... |
249-347 |
2.80e-32 |
|
Domain of unknown function (DUF1977); Members of this family of functionally uncharacterized domains are predominantly found in dnaj-like proteins.
Pssm-ID: 462754 Cd Length: 108 Bit Score: 116.57 E-value: 2.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 249 ANPPYSLFYKSTLGYTISRETQNLQVPYFVDKNFDKAYRGASLRDLEKTIEKDYIDYIQTSCWKEKQQKSELTNLA--GL 326
Cdd:pfam09320 8 SDPSYSFDPPPSPKYTVQRTTPNLKVPYYVNPNFVQKYSGRKLRRLEKEVEEDYVQNLRNECERERQQKERLIERAqgWF 87
|
90 100
....*....|....*....|.
gi 569004710 327 YRDERLRQKAESLKLENCAKL 347
Cdd:pfam09320 88 FGDEEKLEKARAMPMPSCERL 108
|
|
| PRK14298 |
PRK14298 |
chaperone protein DnaJ; Provisional |
81-182 |
2.91e-18 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184612 [Multi-domain] Cd Length: 377 Bit Score: 84.90 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNCAPGATEAFKAIGNAFAVLSNPDKRLRYDEYG----DEQVTftvpr 156
Cdd:PRK14298 5 RDYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSDAEKRAQYDRFGhagiDNQYS----- 79
|
90 100
....*....|....*....|....*.
gi 569004710 157 ARSYHYYKDFeADIspEELFNVFFGG 182
Cdd:PRK14298 80 AEDIFRGADF-GGF--GDIFEMFFGG 102
|
|
| DnaJ_bact |
TIGR02349 |
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
83-187 |
1.45e-17 |
|
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.
Pssm-ID: 274090 [Multi-domain] Cd Length: 354 Bit Score: 82.65 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 83 YYDILGVSHNASDEELKKAYKKLALKFHPDKNCAPGATEAFKAIGNAFAVLSNPDKRLRYDEYGDEqvTFTVPRARSYHY 162
Cdd:TIGR02349 2 YYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQFGHA--GFNGGGGGGGGG 79
|
90 100
....*....|....*....|....*..
gi 569004710 163 YKDFEADISP--EELFNVFFGGHFPSG 187
Cdd:TIGR02349 80 FNGFDIGFFGdfGDIFGDFFGGGGGSG 106
|
|
| terminal_TopJ |
NF037946 |
terminal organelle assembly protein TopJ; |
81-182 |
1.43e-16 |
|
terminal organelle assembly protein TopJ;
Pssm-ID: 468284 [Multi-domain] Cd Length: 440 Bit Score: 80.25 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNCAPGATEAFKAIGNAFAVLSNPDKRLRYDEYGDEQVTftvprarsy 160
Cdd:NF037946 5 RDYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAEIFAEINEAYEVLSNPEKRANYDKYGHDGVD--------- 75
|
90 100
....*....|....*....|..
gi 569004710 161 hyyKDFEADISPEELFNVFFGG 182
Cdd:NF037946 76 ---GEGGFGFDAFDVFSSFFET 94
|
|
| DnaJ |
pfam00226 |
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
82-143 |
9.64e-16 |
|
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: 70.96 E-value: 9.64e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569004710 82 NYYDILGVSHNASDEELKKAYKKLALKFHPDKNC-APGATEAFKAIGNAFAVLSNPDKRLRYD 143
Cdd:pfam00226 1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPgDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
|
|
| DnaJ |
COG0484 |
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
82-159 |
2.21e-14 |
|
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: 69.35 E-value: 2.21e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569004710 82 NYYDILGVSHNASDEELKKAYKKLALKFHPDKN-CAPGATEAFKAIGNAFAVLSNPDKRLRYDEYGDEQVTFTVPRARS 159
Cdd:COG0484 1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNpGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAE 79
|
|
| DnaJ |
smart00271 |
DnaJ molecular chaperone homology domain; |
81-138 |
6.62e-10 |
|
DnaJ molecular chaperone homology domain;
Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 54.55 E-value: 6.62e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKN--CAPGATEAFKAIGNAFAVLSNPDK 138
Cdd:smart00271 1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNpgDKEEAEEKFKEINEAYEVLSDPEK 60
|
|
| DnaJ |
cd06257 |
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
82-135 |
1.89e-09 |
|
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: 52.93 E-value: 1.89e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 569004710 82 NYYDILGVSHNASDEELKKAYKKLALKFHPDKN-CAPGATEAFKAIGNAFAVLSN 135
Cdd:cd06257 1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNpDDPEAEEKFKEINEAYEVLSD 55
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| DUF1977 |
pfam09320 |
Domain of unknown function (DUF1977); Members of this family of functionally uncharacterized ... |
249-347 |
2.80e-32 |
|
Domain of unknown function (DUF1977); Members of this family of functionally uncharacterized domains are predominantly found in dnaj-like proteins.
Pssm-ID: 462754 Cd Length: 108 Bit Score: 116.57 E-value: 2.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 249 ANPPYSLFYKSTLGYTISRETQNLQVPYFVDKNFDKAYRGASLRDLEKTIEKDYIDYIQTSCWKEKQQKSELTNLA--GL 326
Cdd:pfam09320 8 SDPSYSFDPPPSPKYTVQRTTPNLKVPYYVNPNFVQKYSGRKLRRLEKEVEEDYVQNLRNECERERQQKERLIERAqgWF 87
|
90 100
....*....|....*....|.
gi 569004710 327 YRDERLRQKAESLKLENCAKL 347
Cdd:pfam09320 88 FGDEEKLEKARAMPMPSCERL 108
|
|
| PRK14298 |
PRK14298 |
chaperone protein DnaJ; Provisional |
81-182 |
2.91e-18 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184612 [Multi-domain] Cd Length: 377 Bit Score: 84.90 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNCAPGATEAFKAIGNAFAVLSNPDKRLRYDEYG----DEQVTftvpr 156
Cdd:PRK14298 5 RDYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSDAEKRAQYDRFGhagiDNQYS----- 79
|
90 100
....*....|....*....|....*.
gi 569004710 157 ARSYHYYKDFeADIspEELFNVFFGG 182
Cdd:PRK14298 80 AEDIFRGADF-GGF--GDIFEMFFGG 102
|
|
| DnaJ_bact |
TIGR02349 |
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
83-187 |
1.45e-17 |
|
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.
Pssm-ID: 274090 [Multi-domain] Cd Length: 354 Bit Score: 82.65 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 83 YYDILGVSHNASDEELKKAYKKLALKFHPDKNCAPGATEAFKAIGNAFAVLSNPDKRLRYDEYGDEqvTFTVPRARSYHY 162
Cdd:TIGR02349 2 YYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQFGHA--GFNGGGGGGGGG 79
|
90 100
....*....|....*....|....*..
gi 569004710 163 YKDFEADISP--EELFNVFFGGHFPSG 187
Cdd:TIGR02349 80 FNGFDIGFFGdfGDIFGDFFGGGGGSG 106
|
|
| PRK14293 |
PRK14293 |
molecular chaperone DnaJ; |
81-182 |
5.09e-17 |
|
molecular chaperone DnaJ;
Pssm-ID: 237663 [Multi-domain] Cd Length: 374 Bit Score: 81.19 E-value: 5.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNCAPGATEAFKAIGNAFAVLSNPDKRLRYDEYGDEQVTftvpRARSY 160
Cdd:PRK14293 3 ADYYEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAEDRFKEINRAYEVLSDPETRARYDQFGEAGVS----GAAGF 78
|
90 100
....*....|....*....|....
gi 569004710 161 HYYKDFE--ADIspeelFNVFFGG 182
Cdd:PRK14293 79 PDMGDMGgfADI-----FETFFSG 97
|
|
| terminal_TopJ |
NF037946 |
terminal organelle assembly protein TopJ; |
81-182 |
1.43e-16 |
|
terminal organelle assembly protein TopJ;
Pssm-ID: 468284 [Multi-domain] Cd Length: 440 Bit Score: 80.25 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNCAPGATEAFKAIGNAFAVLSNPDKRLRYDEYGDEQVTftvprarsy 160
Cdd:NF037946 5 RDYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAEIFAEINEAYEVLSNPEKRANYDKYGHDGVD--------- 75
|
90 100
....*....|....*....|..
gi 569004710 161 hyyKDFEADISPEELFNVFFGG 182
Cdd:NF037946 76 ---GEGGFGFDAFDVFSSFFET 94
|
|
| PRK14299 |
PRK14299 |
chaperone protein DnaJ; Provisional |
81-148 |
1.52e-16 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237667 [Multi-domain] Cd Length: 291 Bit Score: 78.83 E-value: 1.52e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNCAPGATEAFKAIGNAFAVLSNPDKRLRYDEYGDE 148
Cdd:PRK14299 4 KDYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGAEEKFKEINEAYTVLSDPEKRRIYDTYGTT 71
|
|
| PRK14291 |
PRK14291 |
chaperone protein DnaJ; Provisional |
81-184 |
3.11e-16 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237661 [Multi-domain] Cd Length: 382 Bit Score: 79.04 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNCAPGATEAFKAIGNAFAVLSNPDKRLRYDEYGDEQVTFTVPRARSY 160
Cdd:PRK14291 3 KDYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAEEKFKEINEAYQVLSDPEKRKLYDQFGHAAFSGSGQQQQGQ 82
|
90 100
....*....|....*....|....*....
gi 569004710 161 HYYKDFEA----DISpEELFNVF-FGGHF 184
Cdd:PRK14291 83 EGFSDFGGgnieDIL-EDVFDIFgFGDIF 110
|
|
| PRK14289 |
PRK14289 |
molecular chaperone DnaJ; |
81-146 |
5.81e-16 |
|
molecular chaperone DnaJ;
Pssm-ID: 237660 [Multi-domain] Cd Length: 386 Bit Score: 78.33 E-value: 5.81e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNcaPG---ATEAFKAIGNAFAVLSNPDKRLRYDEYG 146
Cdd:PRK14289 5 RDYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKN--PGdkeAEEKFKEAAEAYDVLSDPDKRSRYDQFG 71
|
|
| PRK14280 |
PRK14280 |
molecular chaperone DnaJ; |
81-182 |
6.85e-16 |
|
molecular chaperone DnaJ;
Pssm-ID: 237656 [Multi-domain] Cd Length: 376 Bit Score: 77.84 E-value: 6.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNCAPGATEAFKAIGNAFAVLSNPDKRLRYDEYG--DEQVTFtvprAR 158
Cdd:PRK14280 4 RDYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDQKRAQYDQFGhaGPNQGF----GG 79
|
90 100
....*....|....*....|....
gi 569004710 159 SYHYYKDFEADISPEELFNVFFGG 182
Cdd:PRK14280 80 GGFGGGDFGGGFGFEDIFSSFFGG 103
|
|
| DnaJ |
pfam00226 |
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
82-143 |
9.64e-16 |
|
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: 70.96 E-value: 9.64e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569004710 82 NYYDILGVSHNASDEELKKAYKKLALKFHPDKNC-APGATEAFKAIGNAFAVLSNPDKRLRYD 143
Cdd:pfam00226 1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPgDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
|
|
| PRK14282 |
PRK14282 |
chaperone protein DnaJ; Provisional |
81-181 |
1.54e-15 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184603 [Multi-domain] Cd Length: 369 Bit Score: 76.76 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNcaPG----ATEAFKAIGNAFAVLSNPDKRLRYDEYG--DEQVTFTV 154
Cdd:PRK14282 4 KDYYEILGVSRNATQEEIKRAYKRLVKEWHPDRH--PEnrkeAEQKFKEIQEAYEVLSDPQKRAMYDRFGyvGEQPPYQE 81
|
90 100 110
....*....|....*....|....*....|
gi 569004710 155 PRARSYHY---YKDFEaDISPEELFNVFFG 181
Cdd:PRK14282 82 TESGGGFFediFKDFE-NIFNRDIFDIFFG 110
|
|
| PRK14276 |
PRK14276 |
chaperone protein DnaJ; Provisional |
81-146 |
4.76e-15 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237653 [Multi-domain] Cd Length: 380 Bit Score: 75.51 E-value: 4.76e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNCAPGATEAFKAIGNAFAVLSNPDKRLRYDEYG 146
Cdd:PRK14276 4 TEYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAEEKYKEVQEAYETLSDPQKRAAYDQYG 69
|
|
| PRK14277 |
PRK14277 |
chaperone protein DnaJ; Provisional |
81-147 |
1.14e-14 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184599 [Multi-domain] Cd Length: 386 Bit Score: 74.45 E-value: 1.14e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNcaPGATEA---FKAIGNAFAVLSNPDKRLRYDEYGD 147
Cdd:PRK14277 5 KDYYEILGVDRNATEEEIKKAYRRLAKKYHPDLN--PGDKEAeqkFKEINEAYEILSDPQKRAQYDQFGH 72
|
|
| PRK10767 |
PRK10767 |
chaperone protein DnaJ; Provisional |
81-146 |
1.31e-14 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 74.03 E-value: 1.31e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNcaPG---ATEAFKAIGNAFAVLSNPDKRLRYDEYG 146
Cdd:PRK10767 4 RDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRN--PGdkeAEEKFKEIKEAYEVLSDPQKRAAYDQYG 70
|
|
| DnaJ |
COG0484 |
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
82-159 |
2.21e-14 |
|
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: 69.35 E-value: 2.21e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569004710 82 NYYDILGVSHNASDEELKKAYKKLALKFHPDKN-CAPGATEAFKAIGNAFAVLSNPDKRLRYDEYGDEQVTFTVPRARS 159
Cdd:COG0484 1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNpGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAE 79
|
|
| PRK14283 |
PRK14283 |
chaperone protein DnaJ; Provisional |
81-189 |
2.43e-14 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184604 [Multi-domain] Cd Length: 378 Bit Score: 73.32 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNCAPGATEAFKAIGNAFAVLSNPDKRLRYDEYGDEQVT-FTvprars 159
Cdd:PRK14283 5 RDYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEGAEEKFKEISEAYAVLSDDEKRQRYDQFGHAGMDgFS------ 78
|
90 100 110
....*....|....*....|....*....|
gi 569004710 160 yhyYKDFEADISPEELFNvFFGGHFpsGNI 189
Cdd:PRK14283 79 ---QEDIFNNINFEDIFQ-GFGFGI--GNI 102
|
|
| PRK14286 |
PRK14286 |
chaperone protein DnaJ; Provisional |
81-187 |
1.58e-13 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172774 [Multi-domain] Cd Length: 372 Bit Score: 70.79 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNCA-PGATEAFKAIGNAFAVLSNPDKRLRYDEYGDEQVTFTVP--RA 157
Cdd:PRK14286 4 RSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGnKESEEKFKEATEAYEILRDPKKRQAYDQFGKAGVNAGAGgfGQ 83
|
90 100 110
....*....|....*....|....*....|
gi 569004710 158 RSYHYYKDFEADISpeELFNVFFGGHFPSG 187
Cdd:PRK14286 84 GAYTDFSDIFGDFG--DIFGDFFGGGRGGG 111
|
|
| PRK14292 |
PRK14292 |
chaperone protein DnaJ; Provisional |
82-146 |
2.46e-13 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237662 [Multi-domain] Cd Length: 371 Bit Score: 70.30 E-value: 2.46e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569004710 82 NYYDILGVSHNASDEELKKAYKKLALKFHPDKNCAPGATEAFKAIGNAFAVLSNPDKRLRYDEYG 146
Cdd:PRK14292 3 DYYELLGVSRTASADEIKSAYRKLALKYHPDRNKEKGAAEKFAQINEAYAVLSDAEKRAHYDRFG 67
|
|
| PRK14281 |
PRK14281 |
chaperone protein DnaJ; Provisional |
81-146 |
3.29e-13 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237657 [Multi-domain] Cd Length: 397 Bit Score: 70.22 E-value: 3.29e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNcaPGATEA---FKAIGNAFAVLSNPDKRLRYDEYG 146
Cdd:PRK14281 3 RDYYEVLGVSRSADKDEIKKAYRKLALKYHPDKN--PDNKEAeehFKEVNEAYEVLSNDDKRRRYDQFG 69
|
|
| PRK14287 |
PRK14287 |
chaperone protein DnaJ; Provisional |
81-182 |
3.49e-13 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237659 [Multi-domain] Cd Length: 371 Bit Score: 70.04 E-value: 3.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNCAPGATEAFKAIGNAFAVLSNPDKRLRYDEYG--DEQVTFTVPRAR 158
Cdd:PRK14287 4 RDYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAPDAEDKFKEVKEAYDTLSDPQKKAHYDQFGhtDPNQGFGGGGAG 83
|
90 100
....*....|....*....|....
gi 569004710 159 SYHYYKDfeadispeeLFNVFFGG 182
Cdd:PRK14287 84 DFGGFSD---------IFDMFFGG 98
|
|
| PRK14294 |
PRK14294 |
chaperone protein DnaJ; Provisional |
81-181 |
4.51e-13 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237664 [Multi-domain] Cd Length: 366 Bit Score: 69.41 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNcaPG---ATEAFKAIGNAFAVLSNPDKRLRYDEYGDEQVtftvpRA 157
Cdd:PRK14294 4 RDYYEILGVTRDASEEEIKKSYRKLAMKYHPDRN--PGdkeAEELFKEAAEAYEVLSDPKKRGIYDQYGHEGL-----SG 76
|
90 100
....*....|....*....|....*.
gi 569004710 158 RSYHYYKDFEaDI--SPEELFNVFFG 181
Cdd:PRK14294 77 TGFSGFSGFD-DIfsSFGDIFEDFFG 101
|
|
| PRK14297 |
PRK14297 |
molecular chaperone DnaJ; |
81-187 |
5.46e-13 |
|
molecular chaperone DnaJ;
Pssm-ID: 184611 [Multi-domain] Cd Length: 380 Bit Score: 69.43 E-value: 5.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNcaPGATEA---FKAIGNAFAVLSNPDKRLRYDEYGDEQVTFTVPRA 157
Cdd:PRK14297 4 KDYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKN--KGNKEAeekFKEINEAYQVLSDPQKKAQYDQFGTADFNGAGGFG 81
|
90 100 110
....*....|....*....|....*....|
gi 569004710 158 RSYHYYKDFEADISPEELFNVFFGGHFPSG 187
Cdd:PRK14297 82 SGGFGGFDFSDMGGFGDIFDSFFGGGFGSS 111
|
|
| PRK14290 |
PRK14290 |
chaperone protein DnaJ; Provisional |
81-194 |
6.51e-13 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172778 [Multi-domain] Cd Length: 365 Bit Score: 69.19 E-value: 6.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNcaPG----ATEAFKAIGNAFAVLSNPDKRLRYDEYGdeqvTFTVPR 156
Cdd:PRK14290 3 KDYYKILGVDRNASQEDIKKAFRELAKKWHPDLH--PGnkaeAEEKFKEISEAYEVLSDPQKRRQYDQTG----TVDFGA 76
|
90 100 110
....*....|....*....|....*....|....*...
gi 569004710 157 ARSYHYYKDFEADISPEELFNVFFGGHFPSGNIHMFSN 194
Cdd:PRK14290 77 GGSNFNWDNFTHFSDINDIFNQIFGGNFGSDFFSGFGN 114
|
|
| PRK14301 |
PRK14301 |
chaperone protein DnaJ; Provisional |
81-150 |
9.97e-13 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237668 [Multi-domain] Cd Length: 373 Bit Score: 68.62 E-value: 9.97e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNcaPGATEA---FKAIGNAFAVLSNPDKRLRYDEYGDEQV 150
Cdd:PRK14301 4 RDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRN--PDNPEAeqkFKEAAEAYEVLRDAEKRARYDRFGHAGV 74
|
|
| PRK14278 |
PRK14278 |
chaperone protein DnaJ; Provisional |
81-147 |
1.27e-12 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237654 [Multi-domain] Cd Length: 378 Bit Score: 68.16 E-value: 1.27e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNCAPGATEAFKAIGNAFAVLSNPDKRLRYDEYGD 147
Cdd:PRK14278 3 RDYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDEEAQEKFKEISVAYEVLSDPEKRRIVDLGGD 69
|
|
| PRK14284 |
PRK14284 |
chaperone protein DnaJ; Provisional |
82-148 |
5.52e-12 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237658 [Multi-domain] Cd Length: 391 Bit Score: 66.40 E-value: 5.52e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 82 NYYDILGVSHNASDEELKKAYKKLALKFHPDKNcaPGATEA---FKAIGNAFAVLSNPDKRLRYDEYGDE 148
Cdd:PRK14284 2 DYYTILGVSKTASPEEIKKAYRKLAVKYHPDKN--PGDAEAekrFKEVSEAYEVLSDAQKRESYDRYGKD 69
|
|
| PTZ00037 |
PTZ00037 |
DnaJ_C chaperone protein; Provisional |
83-182 |
4.19e-11 |
|
DnaJ_C chaperone protein; Provisional
Pssm-ID: 240236 [Multi-domain] Cd Length: 421 Bit Score: 63.69 E-value: 4.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 83 YYDILGVSHNASDEELKKAYKKLALKFHPDKNcapGATEAFKAIGNAFAVLSNPDKRLRYDEYGDEQVTFTVPRArsyhy 162
Cdd:PTZ00037 30 LYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKG---GDPEKFKEISRAYEVLSDPEKRKIYDEYGEEGLEGGEQPA----- 101
|
90 100
....*....|....*....|
gi 569004710 163 ykdfeadiSPEELFNVFFGG 182
Cdd:PTZ00037 102 --------DASDLFDLIFGG 113
|
|
| PRK14296 |
PRK14296 |
chaperone protein DnaJ; Provisional |
79-181 |
6.27e-11 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237666 [Multi-domain] Cd Length: 372 Bit Score: 63.04 E-value: 6.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 79 KCRNYYDILGVSHNASDEELKKAYKKLALKFHPDKNCAPGATEAFKAIGNAFAVLSNPDKRLRYDEYGDEQVTFTVPRAR 158
Cdd:PRK14296 2 KKKDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAHDKMVEINEAADVLLDKDKRKQYDQFGHAAFDGSSGFSS 81
|
90 100
....*....|....*....|....*....
gi 569004710 159 SYHYYKDFEADISPE------ELFNVFFG 181
Cdd:PRK14296 82 NFGDFEDLFSNMGSSgfssftNIFSDFFG 110
|
|
| CbpA |
COG2214 |
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; |
81-160 |
1.43e-10 |
|
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
Pssm-ID: 441816 [Multi-domain] Cd Length: 91 Bit Score: 57.42 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKN--CAPGATEAFKAIGNAFAVLSNPDKRLRYDEYGDEQVTFTVPRAR 158
Cdd:COG2214 5 KDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGgeLKALAEELFQRLNEAYEVLSDPERRAEYDRELGQSGKGSASQPS 84
|
..
gi 569004710 159 SY 160
Cdd:COG2214 85 AA 86
|
|
| SEC63 |
COG5407 |
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ... |
82-139 |
1.66e-10 |
|
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 444165 [Multi-domain] Cd Length: 61 Bit Score: 56.16 E-value: 1.66e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 569004710 82 NYYDILGVSHNASDEELKKAYKKLALKFHPDKNCA-PGATEAFKAIGNAFAVLSNPDKR 139
Cdd:COG5407 1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGdPKAEERFKEINEAYELLSDAEKR 59
|
|
| PRK14295 |
PRK14295 |
molecular chaperone DnaJ; |
81-144 |
4.15e-10 |
|
molecular chaperone DnaJ;
Pssm-ID: 237665 [Multi-domain] Cd Length: 389 Bit Score: 60.63 E-value: 4.15e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNCA-PGATEAFKAIGNAFAVLSNPDKRLRYDE 144
Cdd:PRK14295 9 KDYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGdAKAEERFKEISEAYDVLSDEKKRKEYDE 73
|
|
| PRK14279 |
PRK14279 |
molecular chaperone DnaJ; |
81-144 |
4.83e-10 |
|
molecular chaperone DnaJ;
Pssm-ID: 237655 [Multi-domain] Cd Length: 392 Bit Score: 60.52 E-value: 4.83e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNCA-PGATEAFKAIGNAFAVLSNPDKRLRYDE 144
Cdd:PRK14279 9 KDFYKELGVSSDASAEEIKKAYRKLARELHPDANPGdPAAEERFKAVSEAHDVLSDPAKRKEYDE 73
|
|
| DnaJ |
smart00271 |
DnaJ molecular chaperone homology domain; |
81-138 |
6.62e-10 |
|
DnaJ molecular chaperone homology domain;
Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 54.55 E-value: 6.62e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKN--CAPGATEAFKAIGNAFAVLSNPDK 138
Cdd:smart00271 1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNpgDKEEAEEKFKEINEAYEVLSDPEK 60
|
|
| DnaJ |
cd06257 |
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
82-135 |
1.89e-09 |
|
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: 52.93 E-value: 1.89e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 569004710 82 NYYDILGVSHNASDEELKKAYKKLALKFHPDKN-CAPGATEAFKAIGNAFAVLSN 135
Cdd:cd06257 1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNpDDPEAEEKFKEINEAYEVLSD 55
|
|
| PRK14300 |
PRK14300 |
chaperone protein DnaJ; Provisional |
81-182 |
7.94e-09 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172788 [Multi-domain] Cd Length: 372 Bit Score: 56.56 E-value: 7.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNCAPGATEAFKAIGNAFAVLSNPDKRLRYDEYGDEqvTFTVPRAR-S 159
Cdd:PRK14300 3 QDYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEKKFKEINAAYDVLKDEQKRAAYDRFGHD--AFQNQQSRgG 80
|
90 100
....*....|....*....|....*
gi 569004710 160 YHYYKDFEADISP--EELFNVFFGG 182
Cdd:PRK14300 81 GGNHGGFHPDINDifGDFFSDFMGG 105
|
|
| PRK14285 |
PRK14285 |
chaperone protein DnaJ; Provisional |
81-146 |
2.25e-07 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172773 [Multi-domain] Cd Length: 365 Bit Score: 51.92 E-value: 2.25e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNCAPGATEA-FKAIGNAFAVLSNPDKRLRYDEYG 146
Cdd:PRK14285 3 RDYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKEAESiFKEATEAYEVLIDDNKRAQYDRFG 69
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
83-180 |
9.18e-06 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 47.86 E-value: 9.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 83 YYDILGVSHNASDEELKKAYKKLALKFHPDKNCAPGATEAFKAIGNAFAVLSNPDKRLRYDEYGDE---QVTFTVPRA-- 157
Cdd:PTZ00341 575 FYDILGVGVNADMKEISERYFKLAENYYPPKRSGNEGFHKFKKINEAYQILGDIDKKKMYNKFGYDgikGVNFIHPSIfy 654
|
90 100
....*....|....*....|....*
gi 569004710 158 --RSYHYYKDFEADISPEELFNVFF 180
Cdd:PTZ00341 655 llASLEKFADFTGSPQIVTLLKFFF 679
|
|
| PRK10266 |
PRK10266 |
curved DNA-binding protein; |
81-183 |
1.23e-05 |
|
curved DNA-binding protein;
Pssm-ID: 182347 [Multi-domain] Cd Length: 306 Bit Score: 46.35 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKNCAPGATEAFKAIGNAFAVLSNPDKRLRYDEYGDEQVTFTVPRARSY 160
Cdd:PRK10266 4 KDYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEARFKEVAEAWEVLSDEQRRAEYDQLWQHRNDPQFNRQFQH 83
|
90 100
....*....|....*....|....
gi 569004710 161 HYYKDFEA-DISpeELFNVFFGGH 183
Cdd:PRK10266 84 GDGQSFNAeDFD--DIFSSIFGQH 105
|
|
| PRK14288 |
PRK14288 |
molecular chaperone DnaJ; |
82-148 |
4.76e-05 |
|
molecular chaperone DnaJ;
Pssm-ID: 172776 [Multi-domain] Cd Length: 369 Bit Score: 44.68 E-value: 4.76e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569004710 82 NYYDILGVSHNASDEELKKAYKKLALKFHPDKNCAPG-ATEAFKAIGNAFAVLSNPDKRLRYDEYGDE 148
Cdd:PRK14288 4 SYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKeAEEKFKLINEAYGVLSDEKKRALYDRYGKK 71
|
|
| ZUO1 |
COG5269 |
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ... |
109-168 |
1.86e-03 |
|
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227594 [Multi-domain] Cd Length: 379 Bit Score: 40.02 E-value: 1.86e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569004710 109 FHPDKNCAPGAT---EAFKAIGNAFAVLSNPDKRLRYDEYGDEQvtfTVPRARSYHYYKDFEA 168
Cdd:COG5269 74 YHPDKTAAGGNKgcdEFFKLIQKAREVLGDRKLRLQYDSNDFDA---DVPPPRIYTPDEFFEV 133
|
|
| DjlA |
COG1076 |
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; |
81-136 |
8.78e-03 |
|
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440694 [Multi-domain] Cd Length: 75 Bit Score: 34.77 E-value: 8.78e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569004710 81 RNYYDILGVSHNASDEELKKAYKKLALKFHPDKnCAPGATEAFK--------AIGNAFAVLSNP 136
Cdd:COG1076 4 DDAFELLGLPPDADDAELKRAYRKLQREHHPDR-LAAGLPEEEQrlalqkaaAINEAYETLKDP 66
|
|
|