|
Name |
Accession |
Description |
Interval |
E-value |
| DUF1977 |
pfam09320 |
Domain of unknown function (DUF1977); Members of this family of functionally uncharacterized ... |
186-284 |
7.04e-35 |
|
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: 121.96 E-value: 7.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 186 SNPPYSLYPRSGTGQTIKMQTENLGVVYYVNKDFKNEYKGMLLQKVEKSVEEDYVTNIRNNCWKERQQKTDMQYAAK--V 263
Cdd:pfam09320 8 SDPSYSFDPPPSPKYTVQRTTPNLKVPYYVNPNFVQKYSGRKLRRLEKEVEEDYVQNLRNECERERQQKERLIERAQgwF 87
|
90 100
....*....|....*....|.
gi 119626520 264 YRDDRLRRKADALSMDNCKEL 284
Cdd:pfam09320 88 FGDEEKLEKARAMPMPSCERL 108
|
|
| DnaJ_bact |
TIGR02349 |
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
24-129 |
1.63e-34 |
|
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: 128.10 E-value: 1.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 24 YYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGNE--EQACNHQNNGRF 101
Cdd:TIGR02349 2 YYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAgfNGGGGGGGGGFN 81
|
90 100
....*....|....*....|....*...
gi 119626520 102 NFHRGCEADItpEDLFNIFFGGGFPSGS 129
Cdd:TIGR02349 82 GFDIGFFGDF--GDIFGDFFGGGGGSGR 107
|
|
| PRK14298 |
PRK14298 |
chaperone protein DnaJ; Provisional |
22-128 |
1.02e-32 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184612 [Multi-domain] Cd Length: 377 Bit Score: 123.81 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGneeqacnHQN-NGR 100
Cdd:PRK14298 5 RDYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSDAEKRAQYDRFG-------HAGiDNQ 77
|
90 100 110
....*....|....*....|....*....|..
gi 119626520 101 F---NFHRGceADITP-EDLFNIFFGGGFPSG 128
Cdd:PRK14298 78 YsaeDIFRG--ADFGGfGDIFEMFFGGGGRRG 107
|
|
| DnaJ |
pfam00226 |
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
23-84 |
7.22e-32 |
|
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: 112.57 E-value: 7.22e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119626520 23 NYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKN-HAPGATDAFKKIGNAYAVLSNPEKRKQYD 84
Cdd:pfam00226 1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
|
|
| DnaJ |
COG0484 |
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
23-92 |
1.20e-30 |
|
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: 112.10 E-value: 1.20e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119626520 23 NYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHA-PGATDAFKKIGNAYAVLSNPEKRKQYDLTGNEEQA 92
Cdd:COG0484 1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGdPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAEL 71
|
|
| terminal_TopJ |
NF037946 |
terminal organelle assembly protein TopJ; |
22-165 |
5.89e-29 |
|
terminal organelle assembly protein TopJ;
Pssm-ID: 468284 [Multi-domain] Cd Length: 440 Bit Score: 114.53 E-value: 5.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGNEeqacNHQNNGRF 101
Cdd:NF037946 5 RDYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAEIFAEINEAYEVLSNPEKRANYDKYGHD----GVDGEGGF 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119626520 102 NFhrgceadiTPEDLFNIFFGGGFPSGSVHSFSNGRAGYSQQHQHRHSGHEREEERGDGGFSVF 165
Cdd:NF037946 81 GF--------DAFDVFSSFFETINKSGAFLDDSVDESVSADDDLDRLFDDSKEPSFTSGLDEIV 136
|
|
| DnaJ |
smart00271 |
DnaJ molecular chaperone homology domain; |
22-79 |
1.06e-23 |
|
DnaJ molecular chaperone homology domain;
Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 91.14 E-value: 1.06e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKN--HAPGATDAFKKIGNAYAVLSNPEK 79
Cdd:smart00271 1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNpgDKEEAEEKFKEINEAYEVLSDPEK 60
|
|
| DnaJ |
cd06257 |
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
23-76 |
1.37e-22 |
|
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: 88.37 E-value: 1.37e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 119626520 23 NYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKN-HAPGATDAFKKIGNAYAVLSN 76
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 ... |
186-284 |
7.04e-35 |
|
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: 121.96 E-value: 7.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 186 SNPPYSLYPRSGTGQTIKMQTENLGVVYYVNKDFKNEYKGMLLQKVEKSVEEDYVTNIRNNCWKERQQKTDMQYAAK--V 263
Cdd:pfam09320 8 SDPSYSFDPPPSPKYTVQRTTPNLKVPYYVNPNFVQKYSGRKLRRLEKEVEEDYVQNLRNECERERQQKERLIERAQgwF 87
|
90 100
....*....|....*....|.
gi 119626520 264 YRDDRLRRKADALSMDNCKEL 284
Cdd:pfam09320 88 FGDEEKLEKARAMPMPSCERL 108
|
|
| DnaJ_bact |
TIGR02349 |
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
24-129 |
1.63e-34 |
|
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: 128.10 E-value: 1.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 24 YYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGNE--EQACNHQNNGRF 101
Cdd:TIGR02349 2 YYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAgfNGGGGGGGGGFN 81
|
90 100
....*....|....*....|....*...
gi 119626520 102 NFHRGCEADItpEDLFNIFFGGGFPSGS 129
Cdd:TIGR02349 82 GFDIGFFGDF--GDIFGDFFGGGGGSGR 107
|
|
| PRK14298 |
PRK14298 |
chaperone protein DnaJ; Provisional |
22-128 |
1.02e-32 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184612 [Multi-domain] Cd Length: 377 Bit Score: 123.81 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGneeqacnHQN-NGR 100
Cdd:PRK14298 5 RDYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSDAEKRAQYDRFG-------HAGiDNQ 77
|
90 100 110
....*....|....*....|....*....|..
gi 119626520 101 F---NFHRGceADITP-EDLFNIFFGGGFPSG 128
Cdd:PRK14298 78 YsaeDIFRG--ADFGGfGDIFEMFFGGGGRRG 107
|
|
| DnaJ |
pfam00226 |
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
23-84 |
7.22e-32 |
|
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: 112.57 E-value: 7.22e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119626520 23 NYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKN-HAPGATDAFKKIGNAYAVLSNPEKRKQYD 84
Cdd:pfam00226 1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
|
|
| DnaJ |
COG0484 |
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
23-92 |
1.20e-30 |
|
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: 112.10 E-value: 1.20e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119626520 23 NYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHA-PGATDAFKKIGNAYAVLSNPEKRKQYDLTGNEEQA 92
Cdd:COG0484 1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGdPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAEL 71
|
|
| PRK10767 |
PRK10767 |
chaperone protein DnaJ; Provisional |
22-129 |
4.47e-29 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 113.70 E-value: 4.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNhaPGATDA---FKKIGNAYAVLSNPEKRKQYDLTGNE--EQACNHQ 96
Cdd:PRK10767 4 RDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRN--PGDKEAeekFKEIKEAYEVLSDPQKRAAYDQYGHAafEQGGGGG 81
|
90 100 110
....*....|....*....|....*....|....
gi 119626520 97 NNGRF-NFhrgceADITpEDLFNIFFGGGFPSGS 129
Cdd:PRK10767 82 GFGGGgGF-----GDIF-GDIFGDIFGGGRGGGR 109
|
|
| terminal_TopJ |
NF037946 |
terminal organelle assembly protein TopJ; |
22-165 |
5.89e-29 |
|
terminal organelle assembly protein TopJ;
Pssm-ID: 468284 [Multi-domain] Cd Length: 440 Bit Score: 114.53 E-value: 5.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGNEeqacNHQNNGRF 101
Cdd:NF037946 5 RDYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAEIFAEINEAYEVLSNPEKRANYDKYGHD----GVDGEGGF 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119626520 102 NFhrgceadiTPEDLFNIFFGGGFPSGSVHSFSNGRAGYSQQHQHRHSGHEREEERGDGGFSVF 165
Cdd:NF037946 81 GF--------DAFDVFSSFFETINKSGAFLDDSVDESVSADDDLDRLFDDSKEPSFTSGLDEIV 136
|
|
| PRK14280 |
PRK14280 |
molecular chaperone DnaJ; |
22-124 |
3.39e-27 |
|
molecular chaperone DnaJ;
Pssm-ID: 237656 [Multi-domain] Cd Length: 376 Bit Score: 108.66 E-value: 3.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGNEEQacnhqnNGRF 101
Cdd:PRK14280 4 RDYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDQKRAQYDQFGHAGP------NQGF 77
|
90 100
....*....|....*....|....*..
gi 119626520 102 NFHRGCEADITP----EDLFNIFFGGG 124
Cdd:PRK14280 78 GGGGFGGGDFGGgfgfEDIFSSFFGGG 104
|
|
| PRK14291 |
PRK14291 |
chaperone protein DnaJ; Provisional |
22-143 |
2.30e-26 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237661 [Multi-domain] Cd Length: 382 Bit Score: 106.78 E-value: 2.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGNEE---QACNHQNN 98
Cdd:PRK14291 3 KDYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAEEKFKEINEAYQVLSDPEKRKLYDQFGHAAfsgSGQQQQGQ 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 119626520 99 GRFNFHRGCEADITPEDLFNIF-FGGGFpsGSVHSFSNGRAGYSQQ 143
Cdd:PRK14291 83 EGFSDFGGGNIEDILEDVFDIFgFGDIF--GRRRATRERRKTYQRP 126
|
|
| PRK14297 |
PRK14297 |
molecular chaperone DnaJ; |
22-129 |
3.98e-26 |
|
molecular chaperone DnaJ;
Pssm-ID: 184611 [Multi-domain] Cd Length: 380 Bit Score: 106.02 E-value: 3.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNhaPGATDA---FKKIGNAYAVLSNPEKRKQYDLTGneeqACNHQNN 98
Cdd:PRK14297 4 KDYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKN--KGNKEAeekFKEINEAYQVLSDPQKKAQYDQFG----TADFNGA 77
|
90 100 110
....*....|....*....|....*....|....*
gi 119626520 99 GRFNFHRGCEADITP----EDLFNIFFGGGFPSGS 129
Cdd:PRK14297 78 GGFGSGGFGGFDFSDmggfGDIFDSFFGGGFGSSS 112
|
|
| PRK14277 |
PRK14277 |
chaperone protein DnaJ; Provisional |
22-124 |
5.72e-26 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184599 [Multi-domain] Cd Length: 386 Bit Score: 105.65 E-value: 5.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNhaPGATDA---FKKIGNAYAVLSNPEKRKQYDLTGNE--EQACNHQ 96
Cdd:PRK14277 5 KDYYEILGVDRNATEEEIKKAYRRLAKKYHPDLN--PGDKEAeqkFKEINEAYEILSDPQKRAQYDQFGHAafDPGGFGQ 82
|
90 100 110
....*....|....*....|....*....|....*.
gi 119626520 97 NN--------GRFNFHRGCEADITpEDLFNIFFGGG 124
Cdd:PRK14277 83 GGfgqggfggGGFDFDFGGFGDIF-EDIFGDFFGTG 117
|
|
| PRK14276 |
PRK14276 |
chaperone protein DnaJ; Provisional |
22-124 |
6.42e-26 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237653 [Multi-domain] Cd Length: 380 Bit Score: 105.17 E-value: 6.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTG----NEEQACNHQN 97
Cdd:PRK14276 4 TEYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAEEKYKEVQEAYETLSDPQKRAAYDQYGaagaNGGFGGGAGG 83
|
90 100
....*....|....*....|....*..
gi 119626520 98 NGRFNfhrGCEADITPEDLFNIFFGGG 124
Cdd:PRK14276 84 FGGFD---GSGGFGGFEDIFSSFFGGG 107
|
|
| PRK14278 |
PRK14278 |
chaperone protein DnaJ; Provisional |
22-124 |
1.13e-25 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237654 [Multi-domain] Cd Length: 378 Bit Score: 104.75 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGNEEQACNHQNNGrF 101
Cdd:PRK14278 3 RDYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDEEAQEKFKEISVAYEVLSDPEKRRIVDLGGDPLESAGGGGGG-F 81
|
90 100
....*....|....*....|...
gi 119626520 102 NFHRGCEADItpedlFNIFFGGG 124
Cdd:PRK14278 82 GGGFGGLGDV-----FEAFFGGG 99
|
|
| PRK14283 |
PRK14283 |
chaperone protein DnaJ; Provisional |
22-145 |
1.24e-25 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184604 [Multi-domain] Cd Length: 378 Bit Score: 104.52 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGneeqacnhqnngrf 101
Cdd:PRK14283 5 RDYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEGAEEKFKEISEAYAVLSDDEKRQRYDQFG-------------- 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 119626520 102 nfHRGCEAdITPEDLFN------IFFGGGFPSGSVH---SFSNGRAGYSQQHQ 145
Cdd:PRK14283 71 --HAGMDG-FSQEDIFNninfedIFQGFGFGIGNIFdmfGFGGGSRHGPQRGA 120
|
|
| PRK14294 |
PRK14294 |
chaperone protein DnaJ; Provisional |
22-139 |
2.38e-25 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237664 [Multi-domain] Cd Length: 366 Bit Score: 103.69 E-value: 2.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNhaPG---ATDAFKKIGNAYAVLSNPEKRKQYDLTGNEeqACNHQNN 98
Cdd:PRK14294 4 RDYYEILGVTRDASEEEIKKSYRKLAMKYHPDRN--PGdkeAEELFKEAAEAYEVLSDPKKRGIYDQYGHE--GLSGTGF 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 119626520 99 GRFnfhRGCEaDITPE--DLFNIFFGGGFPSGSvHSFSNGRAG 139
Cdd:PRK14294 80 SGF---SGFD-DIFSSfgDIFEDFFGFGGGRRG-RSRTAVRAG 117
|
|
| PRK14293 |
PRK14293 |
molecular chaperone DnaJ; |
23-84 |
5.01e-25 |
|
molecular chaperone DnaJ;
Pssm-ID: 237663 [Multi-domain] Cd Length: 374 Bit Score: 102.76 E-value: 5.01e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119626520 23 NYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYD 84
Cdd:PRK14293 4 DYYEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAEDRFKEINRAYEVLSDPETRARYD 65
|
|
| PRK14289 |
PRK14289 |
molecular chaperone DnaJ; |
22-149 |
1.74e-24 |
|
molecular chaperone DnaJ;
Pssm-ID: 237660 [Multi-domain] Cd Length: 386 Bit Score: 101.45 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNhaPGATDA---FKKIGNAYAVLSNPEKRKQYDLTGNEEQAcNHQNN 98
Cdd:PRK14289 5 RDYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKN--PGDKEAeekFKEAAEAYDVLSDPDKRSRYDQFGHAGVG-GAAGG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 119626520 99 GRFNfhrgcEADITPEDLFNIF------FGGGFpsGSVHSFSNGRagySQQHQHRHS 149
Cdd:PRK14289 82 GGFS-----GEGMSMEDIFSMFgdifggHGGGF--GGFGGFGGGG---SQQRVFRGS 128
|
|
| PRK14295 |
PRK14295 |
molecular chaperone DnaJ; |
22-136 |
2.99e-24 |
|
molecular chaperone DnaJ;
Pssm-ID: 237665 [Multi-domain] Cd Length: 389 Bit Score: 100.69 E-value: 2.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHA-PGATDAFKKIGNAYAVLSNPEKRKQYD----LTGNE--EQACN 94
Cdd:PRK14295 9 KDYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGdAKAEERFKEISEAYDVLSDEKKRKEYDearsLFGNGgfRPGPG 88
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 119626520 95 HQNNGRFNFHRGceaditpeDLfnifFGGGFPSGSVHSFSNG 136
Cdd:PRK14295 89 GGGGGGFNFDLG--------DL----FGGGAQGGGGAGGGGG 118
|
|
| PRK14299 |
PRK14299 |
chaperone protein DnaJ; Provisional |
22-123 |
4.21e-24 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237667 [Multi-domain] Cd Length: 291 Bit Score: 98.86 E-value: 4.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGNEEQACNHQN---- 97
Cdd:PRK14299 4 KDYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGAEEKFKEINEAYTVLSDPEKRRIYDTYGTTAASAGWQGpppg 83
|
90 100
....*....|....*....|....*..
gi 119626520 98 -NGRFNFHRGCEADITpeDLFNIFFGG 123
Cdd:PRK14299 84 pPGGGDFSGFNVGDFS--DFFQQLFGG 108
|
|
| termin_org_DnaJ |
TIGR03835 |
terminal organelle assembly protein TopJ; This model describes TopJ (MG_200, CbpA), a DnaJ ... |
22-121 |
5.69e-24 |
|
terminal organelle assembly protein TopJ; This model describes TopJ (MG_200, CbpA), a DnaJ homolog and probable assembly protein of the Mycoplasma terminal organelle. The terminal organelle is involved in both cytadherence and gliding motility. [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274808 [Multi-domain] Cd Length: 871 Bit Score: 101.81 E-value: 5.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGNEeqacNHQNNGRF 101
Cdd:TIGR03835 2 RDYYEVLGIDRDADEQEIKKAFRKLAKKYHPDRNKAPDAASIFAEINEANDVLSNPKKRANYDKYGHD----GVDREDDF 77
|
90 100
....*....|....*....|
gi 119626520 102 NFHrgceaditpEDLFNIFF 121
Cdd:TIGR03835 78 DFQ---------ADVFNSFF 88
|
|
| DnaJ |
smart00271 |
DnaJ molecular chaperone homology domain; |
22-79 |
1.06e-23 |
|
DnaJ molecular chaperone homology domain;
Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 91.14 E-value: 1.06e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKN--HAPGATDAFKKIGNAYAVLSNPEK 79
Cdd:smart00271 1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNpgDKEEAEEKFKEINEAYEVLSDPEK 60
|
|
| SEC63 |
COG5407 |
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ... |
23-82 |
1.78e-23 |
|
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 444165 [Multi-domain] Cd Length: 61 Bit Score: 90.83 E-value: 1.78e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119626520 23 NYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHA-PGATDAFKKIGNAYAVLSNPEKRKQ 82
Cdd:COG5407 1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGdPKAEERFKEINEAYELLSDAEKRAR 61
|
|
| PRK14290 |
PRK14290 |
chaperone protein DnaJ; Provisional |
22-136 |
2.64e-23 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172778 [Multi-domain] Cd Length: 365 Bit Score: 98.08 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNhaPG----ATDAFKKIGNAYAVLSNPEKRKQYDLTGNEEQACNHQN 97
Cdd:PRK14290 3 KDYYKILGVDRNASQEDIKKAFRELAKKWHPDLH--PGnkaeAEEKFKEISEAYEVLSDPQKRRQYDQTGTVDFGAGGSN 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 119626520 98 NGRFNFHRgcEADITpeDLFNIFFGGGFPSGSVHSFSNG 136
Cdd:PRK14290 81 FNWDNFTH--FSDIN--DIFNQIFGGNFGSDFFSGFGNQ 115
|
|
| PRK14301 |
PRK14301 |
chaperone protein DnaJ; Provisional |
22-139 |
3.16e-23 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237668 [Multi-domain] Cd Length: 373 Bit Score: 97.89 E-value: 3.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKN-HAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGNEeqacNHQNNGR 100
Cdd:PRK14301 4 RDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNpDNPEAEQKFKEAAEAYEVLRDAEKRARYDRFGHA----GVNGNGG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 119626520 101 F-NFHrgceadiTPEDLFNIF---FGG--GFPSGSVHSFSNGRAG 139
Cdd:PRK14301 80 FgGFS-------SAEDIFSHFsdiFGDlfGFSGGGSRRGPRPQAG 117
|
|
| PRK14292 |
PRK14292 |
chaperone protein DnaJ; Provisional |
23-128 |
3.81e-23 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237662 [Multi-domain] Cd Length: 371 Bit Score: 97.65 E-value: 3.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 23 NYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGNEEQACNHQNN--GR 100
Cdd:PRK14292 3 DYYELLGVSRTASADEIKSAYRKLALKYHPDRNKEKGAAEKFAQINEAYAVLSDAEKRAHYDRFGTAPGAGMPGGDpfGG 82
|
90 100
....*....|....*....|....*...
gi 119626520 101 FNFhrgceadiTPEDLFNIFFGGGFPSG 128
Cdd:PRK14292 83 MGF--------DPMDIFEQLFGGAGFGG 102
|
|
| DnaJ |
cd06257 |
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
23-76 |
1.37e-22 |
|
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: 88.37 E-value: 1.37e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 119626520 23 NYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKN-HAPGATDAFKKIGNAYAVLSN 76
Cdd:cd06257 1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNpDDPEAEEKFKEINEAYEVLSD 55
|
|
| PRK14286 |
PRK14286 |
chaperone protein DnaJ; Provisional |
22-129 |
4.43e-22 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172774 [Multi-domain] Cd Length: 372 Bit Score: 94.67 E-value: 4.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHA-PGATDAFKKIGNAYAVLSNPEKRKQYDLTGNEeqacnHQNNGR 100
Cdd:PRK14286 4 RSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGnKESEEKFKEATEAYEILRDPKKRQAYDQFGKA-----GVNAGA 78
|
90 100 110
....*....|....*....|....*....|....
gi 119626520 101 FNFHRGCEADITP-----EDLFNIFFGGGFPSGS 129
Cdd:PRK14286 79 GGFGQGAYTDFSDifgdfGDIFGDFFGGGRGGGS 112
|
|
| PRK14281 |
PRK14281 |
chaperone protein DnaJ; Provisional |
22-136 |
4.92e-22 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237657 [Multi-domain] Cd Length: 397 Bit Score: 94.87 E-value: 4.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNhaPGATDA---FKKIGNAYAVLSNPEKRKQYDLTGNEEQACNHQNN 98
Cdd:PRK14281 3 RDYYEVLGVSRSADKDEIKKAYRKLALKYHPDKN--PDNKEAeehFKEVNEAYEVLSNDDKRRRYDQFGHAGVGSSAASG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 119626520 99 GRfNFHRGCEADITpeDLFNIF---------FGGGFPSGSVHSFSNG 136
Cdd:PRK14281 81 GG-PGYGGGGGDFN--DIFSAFndmfgggarRGGGSPFGFEDVFGGG 124
|
|
| PTZ00037 |
PTZ00037 |
DnaJ_C chaperone protein; Provisional |
22-128 |
6.86e-21 |
|
DnaJ_C chaperone protein; Provisional
Pssm-ID: 240236 [Multi-domain] Cd Length: 421 Bit Score: 91.81 E-value: 6.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNhapGATDAFKKIGNAYAVLSNPEKRKQYDLTGNEEQACNHQNngrf 101
Cdd:PTZ00037 28 EKLYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKG---GDPEKFKEISRAYEVLSDPEKRKIYDEYGEEGLEGGEQP---- 100
|
90 100
....*....|....*....|....*..
gi 119626520 102 nfhrgceADitPEDLFNIFFGGGFPSG 128
Cdd:PTZ00037 101 -------AD--ASDLFDLIFGGGRKPG 118
|
|
| PRK14287 |
PRK14287 |
chaperone protein DnaJ; Provisional |
22-124 |
7.07e-21 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237659 [Multi-domain] Cd Length: 371 Bit Score: 91.22 E-value: 7.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGNEEqacnhQNNGrf 101
Cdd:PRK14287 4 RDYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAPDAEDKFKEVKEAYDTLSDPQKKAHYDQFGHTD-----PNQG-- 76
|
90 100
....*....|....*....|....
gi 119626520 102 nFHRGCEADITP-EDLFNIFFGGG 124
Cdd:PRK14287 77 -FGGGGAGDFGGfSDIFDMFFGGG 99
|
|
| CbpA |
COG2214 |
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; |
22-86 |
1.60e-20 |
|
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
Pssm-ID: 441816 [Multi-domain] Cd Length: 91 Bit Score: 84.00 E-value: 1.60e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKN--HAPGATDAFKKIGNAYAVLSNPEKRKQYDLT 86
Cdd:COG2214 5 KDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGgeLKALAEELFQRLNEAYEVLSDPERRAEYDRE 71
|
|
| PRK14282 |
PRK14282 |
chaperone protein DnaJ; Provisional |
22-122 |
1.93e-20 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184603 [Multi-domain] Cd Length: 369 Bit Score: 89.85 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHA--PGATDAFKKIGNAYAVLSNPEKRKQYDLTG--NEEQACNHQN 97
Cdd:PRK14282 4 KDYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPEnrKEAEQKFKEIQEAYEVLSDPQKRAMYDRFGyvGEQPPYQETE 83
|
90 100
....*....|....*....|....*...
gi 119626520 98 NGRFNFH---RGCEaDITPEDLFNIFFG 122
Cdd:PRK14282 84 SGGGFFEdifKDFE-NIFNRDIFDIFFG 110
|
|
| PRK14279 |
PRK14279 |
molecular chaperone DnaJ; |
22-86 |
2.70e-20 |
|
molecular chaperone DnaJ;
Pssm-ID: 237655 [Multi-domain] Cd Length: 392 Bit Score: 89.79 E-value: 2.70e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHA-PGATDAFKKIGNAYAVLSNPEKRKQYDLT 86
Cdd:PRK14279 9 KDFYKELGVSSDASAEEIKKAYRKLARELHPDANPGdPAAEERFKAVSEAHDVLSDPAKRKEYDET 74
|
|
| PRK14284 |
PRK14284 |
chaperone protein DnaJ; Provisional |
23-89 |
7.08e-19 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237658 [Multi-domain] Cd Length: 391 Bit Score: 85.66 E-value: 7.08e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 23 NYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNhaPGATDA---FKKIGNAYAVLSNPEKRKQYDLTGNE 89
Cdd:PRK14284 2 DYYTILGVSKTASPEEIKKAYRKLAVKYHPDKN--PGDAEAekrFKEVSEAYEVLSDAQKRESYDRYGKD 69
|
|
| PRK10266 |
PRK10266 |
curved DNA-binding protein; |
22-156 |
5.95e-18 |
|
curved DNA-binding protein;
Pssm-ID: 182347 [Multi-domain] Cd Length: 306 Bit Score: 82.18 E-value: 5.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDltgneeQACNHQNNGRF 101
Cdd:PRK10266 4 KDYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEARFKEVAEAWEVLSDEQRRAEYD------QLWQHRNDPQF 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 119626520 102 N--FHRGCEADITPEDLFNIFfgggfpsgsvHSFSNGRAGYSQQHqHRHSGHEREEE 156
Cdd:PRK10266 78 NrqFQHGDGQSFNAEDFDDIF----------SSIFGQHARQSRQR-PAARGHDIEIE 123
|
|
| PRK14300 |
PRK14300 |
chaperone protein DnaJ; Provisional |
22-124 |
5.99e-18 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172788 [Multi-domain] Cd Length: 372 Bit Score: 82.75 E-value: 5.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGNEEQAcNHQNNGRF 101
Cdd:PRK14300 3 QDYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEKKFKEINAAYDVLKDEQKRAAYDRFGHDAFQ-NQQSRGGG 81
|
90 100
....*....|....*....|....*
gi 119626520 102 NFHRGCEADITP--EDLFNIFFGGG 124
Cdd:PRK14300 82 GNHGGFHPDINDifGDFFSDFMGGS 106
|
|
| PRK14296 |
PRK14296 |
chaperone protein DnaJ; Provisional |
20-140 |
1.40e-17 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237666 [Multi-domain] Cd Length: 372 Bit Score: 81.92 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 20 KCKNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGneeqacNHQNNG 99
Cdd:PRK14296 2 KKKDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAHDKMVEINEAADVLLDKDKRKQYDQFG------HAAFDG 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 119626520 100 RFNFHRGCeADItpEDLF-NIFFGGGFPSGSVHS--FSNGRAGY 140
Cdd:PRK14296 76 SSGFSSNF-GDF--EDLFsNMGSSGFSSFTNIFSdfFGSNKSDY 116
|
|
| PRK14285 |
PRK14285 |
chaperone protein DnaJ; Provisional |
22-123 |
2.16e-15 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172773 [Multi-domain] Cd Length: 365 Bit Score: 75.41 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 22 KNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHA-PGATDAFKKIGNAYAVLSNPEKRKQYDLTGNEEqacnHQNNGR 100
Cdd:PRK14285 3 RDYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGnKEAESIFKEATEAYEVLIDDNKRAQYDRFGHTA----FEGGGG 78
|
90 100
....*....|....*....|....*...
gi 119626520 101 FN-FHRGCE--ADITPE--DLFNIFFGG 123
Cdd:PRK14285 79 FEgFSGGFSgfSDIFEDfgDIFDSFFTG 106
|
|
| DjlA |
COG1076 |
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; |
23-77 |
2.01e-14 |
|
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440694 [Multi-domain] Cd Length: 75 Bit Score: 66.74 E-value: 2.01e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119626520 23 NYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKnHAPGATDAFKK--------IGNAYAVLSNP 77
Cdd:COG1076 5 DAFELLGLPPDADDAELKRAYRKLQREHHPDR-LAAGLPEEEQRlalqkaaaINEAYETLKDP 66
|
|
| PRK14288 |
PRK14288 |
molecular chaperone DnaJ; |
23-89 |
1.68e-11 |
|
molecular chaperone DnaJ;
Pssm-ID: 172776 [Multi-domain] Cd Length: 369 Bit Score: 63.94 E-value: 1.68e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119626520 23 NYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPG-ATDAFKKIGNAYAVLSNPEKRKQYDLTGNE 89
Cdd:PRK14288 4 SYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKeAEEKFKLINEAYGVLSDEKKRALYDRYGKK 71
|
|
| ZUO1 |
COG5269 |
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ... |
2-84 |
4.75e-08 |
|
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227594 [Multi-domain] Cd Length: 379 Bit Score: 53.50 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626520 2 DIGTLIWDGGPVPNTHIN------KCKNYYEVLGVTK---DAGDEDLKKAYRKLALKFHPDKNHAPGATD---AFKKIGN 69
Cdd:COG5269 17 RIHSEYFKGRNVLNLYTRedfknwKKVDLYALLGLSKyrtKAIPPQILKAHKKKVYKYHPDKTAAGGNKGcdeFFKLIQK 96
|
90
....*....|....*
gi 119626520 70 AYAVLSNPEKRKQYD 84
Cdd:COG5269 97 AREVLGDRKLRLQYD 111
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
13-87 |
9.33e-07 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 50.17 E-value: 9.33e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119626520 13 VPNTHinkcknYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTG 87
Cdd:PTZ00341 570 IPDTL------FYDILGVGVNADMKEISERYFKLAENYYPPKRSGNEGFHKFKKINEAYQILGDIDKKKMYNKFG 638
|
|
| djlA |
PRK09430 |
co-chaperone DjlA; |
25-71 |
1.00e-06 |
|
co-chaperone DjlA;
Pssm-ID: 236512 [Multi-domain] Cd Length: 267 Bit Score: 49.04 E-value: 1.00e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 119626520 25 YEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPG--------ATDAFKKIGNAY 71
Cdd:PRK09430 203 YKVLGVSESDDDQEIKRAYRKLMSEHHPDKLVAKGlppemmemAKEKAQEIQAAY 257
|
|
| PHA03102 |
PHA03102 |
Small T antigen; Reviewed |
26-54 |
3.37e-03 |
|
Small T antigen; Reviewed
Pssm-ID: 222986 [Multi-domain] Cd Length: 153 Bit Score: 37.34 E-value: 3.37e-03
10 20 30
....*....|....*....|....*....|.
gi 119626520 26 EVLGVTKDA-GD-EDLKKAYRKLALKFHPDK 54
Cdd:PHA03102 9 DLLGLPRSAwGNlPLMRKAYLRKCLEFHPDK 39
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