|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14297 |
PRK14297 |
molecular chaperone DnaJ; |
17-109 |
4.77e-33 |
|
molecular chaperone DnaJ;
Pssm-ID: 184611 [Multi-domain] Cd Length: 380 Bit Score: 126.82 E-value: 4.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPSENQLD------- 89
Cdd:PRK14297 5 DYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKEAEEKFKEINEAYQVLSDPQKKAQYDQFGTADFNGAggfgsgg 84
|
90 100
....*....|....*....|
gi 392894612 90 FEGFDVSEMGGVGRVFGALF 109
Cdd:PRK14297 85 FGGFDFSDMGGFGDIFDSFF 104
|
|
| DnaJ_bact |
TIGR02349 |
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
17-109 |
2.02e-32 |
|
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: 124.64 E-value: 2.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPnDAHAQEEFKKVSIAYSVLSDPNKRRQYDV-------SGPSENQLD 89
Cdd:TIGR02349 1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNK-DKEAEEKFKEINEAYEVLSDPEKRAQYDQfghagfnGGGGGGGGG 79
|
90 100
....*....|....*....|
gi 392894612 90 FEGFDVSEMGGVGRVFGALF 109
Cdd:TIGR02349 80 FNGFDIGFFGDFGDIFGDFF 99
|
|
| DnaJ |
pfam00226 |
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
17-79 |
2.63e-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: 115.65 E-value: 2.63e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYD 79
Cdd:pfam00226 1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
|
|
| DnaJ |
COG0484 |
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
17-82 |
2.52e-31 |
|
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: 115.96 E-value: 2.52e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSG 82
Cdd:COG0484 1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFG 66
|
|
| DnaJ |
cd06257 |
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
17-71 |
5.76e-24 |
|
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: 93.38 E-value: 5.76e-24
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSD 71
Cdd:cd06257 1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
|
|
| DnaJ |
smart00271 |
DnaJ molecular chaperone homology domain; |
16-74 |
1.41e-22 |
|
DnaJ molecular chaperone homology domain;
Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 89.60 E-value: 1.41e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 16 MDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAH-AQEEFKKVSIAYSVLSDPNK 74
Cdd:smart00271 1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEeAEEKFKEINEAYEVLSDPEK 60
|
|
| terminal_TopJ |
NF037946 |
terminal organelle assembly protein TopJ; |
17-95 |
5.62e-21 |
|
terminal organelle assembly protein TopJ;
Pssm-ID: 468284 [Multi-domain] Cd Length: 440 Bit Score: 93.73 E-value: 5.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNpNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSG----PSENQLDFEG 92
Cdd:NF037946 6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRN-KAPDAAEIFAEINEAYEVLSNPEKRANYDKYGhdgvDGEGGFGFDA 84
|
...
gi 392894612 93 FDV 95
Cdd:NF037946 85 FDV 87
|
|
| PLN02281 |
PLN02281 |
chlorophyllide a oxygenase |
280-353 |
3.62e-03 |
|
chlorophyllide a oxygenase
Pssm-ID: 177920 [Multi-domain] Cd Length: 536 Bit Score: 39.33 E-value: 3.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392894612 280 ITFLPVEPSAVEQLNEIQDTEKSISIIKKEMLDFQREFTEAKRKYDEAVAKLKvqddTILKALAHREELYNEVL 353
Cdd:PLN02281 100 LTIMILHDKVVDVLNPLAREYKSIGTVKKELAGLQEELSKAHQQVHISEARVS----TALDKLAHMEELVNDRL 169
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14297 |
PRK14297 |
molecular chaperone DnaJ; |
17-109 |
4.77e-33 |
|
molecular chaperone DnaJ;
Pssm-ID: 184611 [Multi-domain] Cd Length: 380 Bit Score: 126.82 E-value: 4.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPSENQLD------- 89
Cdd:PRK14297 5 DYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKEAEEKFKEINEAYQVLSDPQKKAQYDQFGTADFNGAggfgsgg 84
|
90 100
....*....|....*....|
gi 392894612 90 FEGFDVSEMGGVGRVFGALF 109
Cdd:PRK14297 85 FGGFDFSDMGGFGDIFDSFF 104
|
|
| PRK10767 |
PRK10767 |
chaperone protein DnaJ; Provisional |
14-110 |
8.30e-33 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 126.03 E-value: 8.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 14 SEMDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDvsgpsenQLDFEGF 93
Cdd:PRK10767 2 AKRDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYD-------QYGHAAF 74
|
90 100
....*....|....*....|....
gi 392894612 94 DVSEMGG-------VGRVFGALFS 110
Cdd:PRK10767 75 EQGGGGGgfgggggFGDIFGDIFG 98
|
|
| DnaJ_bact |
TIGR02349 |
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
17-109 |
2.02e-32 |
|
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: 124.64 E-value: 2.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPnDAHAQEEFKKVSIAYSVLSDPNKRRQYDV-------SGPSENQLD 89
Cdd:TIGR02349 1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNK-DKEAEEKFKEINEAYEVLSDPEKRAQYDQfghagfnGGGGGGGGG 79
|
90 100
....*....|....*....|
gi 392894612 90 FEGFDVSEMGGVGRVFGALF 109
Cdd:TIGR02349 80 FNGFDIGFFGDFGDIFGDFF 99
|
|
| DnaJ |
pfam00226 |
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
17-79 |
2.63e-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: 115.65 E-value: 2.63e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYD 79
Cdd:pfam00226 1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
|
|
| DnaJ |
COG0484 |
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
17-82 |
2.52e-31 |
|
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: 115.96 E-value: 2.52e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSG 82
Cdd:COG0484 1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFG 66
|
|
| PRK14278 |
PRK14278 |
chaperone protein DnaJ; Provisional |
17-109 |
2.91e-28 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237654 [Multi-domain] Cd Length: 378 Bit Score: 113.61 E-value: 2.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAhAQEEFKKVSIAYSVLSDPNKRRQYDVSG-PSENQLDFEGFDV 95
Cdd:PRK14278 4 DYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDEE-AQEKFKEISVAYEVLSDPEKRRIVDLGGdPLESAGGGGGGFG 82
|
90
....*....|....
gi 392894612 96 SEMGGVGRVFGALF 109
Cdd:PRK14278 83 GGFGGLGDVFEAFF 96
|
|
| PRK14277 |
PRK14277 |
chaperone protein DnaJ; Provisional |
17-110 |
8.23e-28 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184599 [Multi-domain] Cd Length: 386 Bit Score: 112.59 E-value: 8.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPS------ENQLDF 90
Cdd:PRK14277 6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDKEAEQKFKEINEAYEILSDPQKRAQYDQFGHAafdpggFGQGGF 85
|
90 100
....*....|....*....|....*.
gi 392894612 91 ------EGFDVSEMGGVGRVFGALFS 110
Cdd:PRK14277 86 gqggfgGGGFDFDFGGFGDIFEDIFG 111
|
|
| PRK14279 |
PRK14279 |
molecular chaperone DnaJ; |
10-113 |
5.16e-27 |
|
molecular chaperone DnaJ;
Pssm-ID: 237655 [Multi-domain] Cd Length: 392 Bit Score: 110.59 E-value: 5.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 10 QPKVSEMDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVS-------- 81
Cdd:PRK14279 3 QREWVEKDFYKELGVSSDASAEEIKKAYRKLARELHPDANPGDPAAEERFKAVSEAHDVLSDPAKRKEYDETrrlfaggg 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 392894612 82 ------------GPSENQLDFEGFDVSEM---------GGVGRVFGALFSKLG 113
Cdd:PRK14279 83 fggrrfdggggfGGFGTGGDGAEFNLNDLfdaagrgggGGIGDLFGGLFNRGG 135
|
|
| SEC63 |
COG5407 |
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ... |
17-77 |
5.80e-27 |
|
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 444165 [Multi-domain] Cd Length: 61 Bit Score: 101.61 E-value: 5.80e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQ 77
Cdd:COG5407 1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDPKAEERFKEINEAYELLSDAEKRAR 61
|
|
| PRK14298 |
PRK14298 |
chaperone protein DnaJ; Provisional |
17-109 |
1.08e-26 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184612 [Multi-domain] Cd Length: 377 Bit Score: 109.55 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNpNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPS--ENQLDFEG-F 93
Cdd:PRK14298 6 DYYEILGLSKDASVEDIKKAYRKLAMKYHPDKN-KEPDAEEKFKEISEAYAVLSDAEKRAQYDRFGHAgiDNQYSAEDiF 84
|
90
....*....|....*.
gi 392894612 94 DVSEMGGVGRVFGALF 109
Cdd:PRK14298 85 RGADFGGFGDIFEMFF 100
|
|
| PRK14295 |
PRK14295 |
molecular chaperone DnaJ; |
15-113 |
4.20e-26 |
|
molecular chaperone DnaJ;
Pssm-ID: 237665 [Multi-domain] Cd Length: 389 Bit Score: 108.01 E-value: 4.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 15 EMDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVS-----------GP 83
Cdd:PRK14295 8 EKDYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDAKAEERFKEISEAYDVLSDEKKRKEYDEArslfgnggfrpGP 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 392894612 84 SENQLDFEGFDVSEM--------------GGVGRVFGALFSKLG 113
Cdd:PRK14295 88 GGGGGGGFNFDLGDLfgggaqggggagggGGLGDVFGGLFNRGG 131
|
|
| PRK14301 |
PRK14301 |
chaperone protein DnaJ; Provisional |
14-109 |
1.11e-25 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237668 [Multi-domain] Cd Length: 373 Bit Score: 106.36 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 14 SEMDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPS--ENQLDFE 91
Cdd:PRK14301 2 SQRDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNPEAEQKFKEAAEAYEVLRDAEKRARYDRFGHAgvNGNGGFG 81
|
90 100
....*....|....*....|
gi 392894612 92 GFDVSE--MGGVGRVFGALF 109
Cdd:PRK14301 82 GFSSAEdiFSHFSDIFGDLF 101
|
|
| PRK14284 |
PRK14284 |
chaperone protein DnaJ; Provisional |
16-113 |
1.39e-25 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237658 [Multi-domain] Cd Length: 391 Bit Score: 106.47 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 16 MDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYD-------------VSG 82
Cdd:PRK14284 1 MDYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDAEAEKRFKEVSEAYEVLSDAQKRESYDrygkdgpfagaggFGG 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 392894612 83 PSENQLD-----FEGFDVSEMGGVGRVFGALFSKLG 113
Cdd:PRK14284 81 AGMGNMEdalrtFMGAFGGEFGGGGSFFEGLFGGLG 116
|
|
| PRK14292 |
PRK14292 |
chaperone protein DnaJ; Provisional |
16-85 |
1.46e-25 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237662 [Multi-domain] Cd Length: 371 Bit Score: 106.13 E-value: 1.46e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 16 MDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPnDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPSE 85
Cdd:PRK14292 2 MDYYELLGVSRTASADEIKSAYRKLALKYHPDRNK-EKGAAEKFAQINEAYAVLSDAEKRAHYDRFGTAP 70
|
|
| PRK14294 |
PRK14294 |
chaperone protein DnaJ; Provisional |
17-109 |
8.48e-25 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237664 [Multi-domain] Cd Length: 366 Bit Score: 103.69 E-value: 8.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPS--ENQ--LDFEG 92
Cdd:PRK14294 5 DYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDKEAEELFKEAAEAYEVLSDPKKRGIYDQYGHEglSGTgfSGFSG 84
|
90
....*....|....*..
gi 392894612 93 FDvSEMGGVGRVFGALF 109
Cdd:PRK14294 85 FD-DIFSSFGDIFEDFF 100
|
|
| PRK14276 |
PRK14276 |
chaperone protein DnaJ; Provisional |
15-109 |
2.58e-24 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237653 [Multi-domain] Cd Length: 380 Bit Score: 102.86 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 15 EMDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNpNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPSENQLDF---- 90
Cdd:PRK14276 3 NTEYYDRLGVSKDASQDEIKKAYRKLSKKYHPDIN-KEPGAEEKYKEVQEAYETLSDPQKRAAYDQYGAAGANGGFggga 81
|
90 100
....*....|....*....|...
gi 392894612 91 ---EGFD-VSEMGGVGRVFGALF 109
Cdd:PRK14276 82 ggfGGFDgSGGFGGFEDIFSSFF 104
|
|
| PRK14289 |
PRK14289 |
molecular chaperone DnaJ; |
17-113 |
3.24e-24 |
|
molecular chaperone DnaJ;
Pssm-ID: 237660 [Multi-domain] Cd Length: 386 Bit Score: 102.60 E-value: 3.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYD------VSGPSENQlDF 90
Cdd:PRK14289 6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDKEAEEKFKEAAEAYDVLSDPDKRSRYDqfghagVGGAAGGG-GF 84
|
90 100
....*....|....*....|...
gi 392894612 91 EGFDVSeMGGVGRVFGALFSKLG 113
Cdd:PRK14289 85 SGEGMS-MEDIFSMFGDIFGGHG 106
|
|
| PRK14291 |
PRK14291 |
chaperone protein DnaJ; Provisional |
17-113 |
3.85e-24 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237661 [Multi-domain] Cd Length: 382 Bit Score: 102.16 E-value: 3.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNdAHAQEEFKKVSIAYSVLSDPNKRRQYD------VSGPSENQLDF 90
Cdd:PRK14291 4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKN-PEAEEKFKEINEAYQVLSDPEKRKLYDqfghaaFSGSGQQQQGQ 82
|
90 100
....*....|....*....|...
gi 392894612 91 EGFDVSEMGGVGRVFGALFSKLG 113
Cdd:PRK14291 83 EGFSDFGGGNIEDILEDVFDIFG 105
|
|
| DnaJ |
cd06257 |
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
17-71 |
5.76e-24 |
|
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: 93.38 E-value: 5.76e-24
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSD 71
Cdd:cd06257 1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
|
|
| PRK14281 |
PRK14281 |
chaperone protein DnaJ; Provisional |
17-107 |
1.70e-23 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237657 [Multi-domain] Cd Length: 397 Bit Score: 100.65 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDvsgpsenQLDFEGFDVS 96
Cdd:PRK14281 4 DYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKEAEEHFKEVNEAYEVLSNDDKRRRYD-------QFGHAGVGSS 76
|
90
....*....|.
gi 392894612 97 EMGGVGRVFGA 107
Cdd:PRK14281 77 AASGGGPGYGG 87
|
|
| PRK14293 |
PRK14293 |
molecular chaperone DnaJ; |
17-113 |
2.30e-23 |
|
molecular chaperone DnaJ;
Pssm-ID: 237663 [Multi-domain] Cd Length: 374 Bit Score: 100.06 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNpNDAHAQEEFKKVSIAYSVLSDPNKRRQYD------VSGPSenqldf 90
Cdd:PRK14293 4 DYYEILGVSRDADKDELKRAYRRLARKYHPDVN-KEPGAEDRFKEINRAYEVLSDPETRARYDqfgeagVSGAA------ 76
|
90 100
....*....|....*....|....
gi 392894612 91 eGF-DVSEMGGVGRVFGALFSKLG 113
Cdd:PRK14293 77 -GFpDMGDMGGFADIFETFFSGFG 99
|
|
| PRK14286 |
PRK14286 |
chaperone protein DnaJ; Provisional |
13-109 |
3.38e-23 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172774 [Multi-domain] Cd Length: 372 Bit Score: 99.29 E-value: 3.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 13 VSEMDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPSENQLDFEG 92
Cdd:PRK14286 1 MSERSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYDQFGKAGVNAGAGG 80
|
90 100
....*....|....*....|....
gi 392894612 93 F------DVSEM-GGVGRVFGALF 109
Cdd:PRK14286 81 FgqgaytDFSDIfGDFGDIFGDFF 104
|
|
| PRK14280 |
PRK14280 |
molecular chaperone DnaJ; |
13-109 |
3.47e-23 |
|
molecular chaperone DnaJ;
Pssm-ID: 237656 [Multi-domain] Cd Length: 376 Bit Score: 99.41 E-value: 3.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 13 VSEMDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNpNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPSENQLDFEG 92
Cdd:PRK14280 1 MAKRDYYEVLGVSKSASKDEIKKAYRKLSKKYHPDIN-KEEGADEKFKEISEAYEVLSDDQKRAQYDQFGHAGPNQGFGG 79
|
90 100
....*....|....*....|..
gi 392894612 93 F-----DVSEMGGVGRVFGALF 109
Cdd:PRK14280 80 GgfgggDFGGGFGFEDIFSSFF 101
|
|
| DnaJ |
smart00271 |
DnaJ molecular chaperone homology domain; |
16-74 |
1.41e-22 |
|
DnaJ molecular chaperone homology domain;
Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 89.60 E-value: 1.41e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 16 MDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAH-AQEEFKKVSIAYSVLSDPNK 74
Cdd:smart00271 1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEeAEEKFKEINEAYEVLSDPEK 60
|
|
| PRK14299 |
PRK14299 |
chaperone protein DnaJ; Provisional |
17-113 |
6.02e-22 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237667 [Multi-domain] Cd Length: 291 Bit Score: 94.62 E-value: 6.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNpNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPSENQL-------- 88
Cdd:PRK14299 5 DYYAILGVPKNASQDEIKKAFKKLARKYHPDVN-KSPGAEEKFKEINEAYTVLSDPEKRRIYDTYGTTAASAgwqgpppg 83
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 392894612 89 -----DFEGFDVSEM-----------GGVGRvFGALFSKLG 113
Cdd:PRK14299 84 ppgggDFSGFNVGDFsdffqqlfggrGGFGG-FGDLFGSVG 123
|
|
| PRK14290 |
PRK14290 |
chaperone protein DnaJ; Provisional |
17-109 |
1.66e-21 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172778 [Multi-domain] Cd Length: 365 Bit Score: 94.61 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNP-NDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPSENQLDFEGF-- 93
Cdd:PRK14290 4 DYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPgNKAEAEEKFKEISEAYEVLSDPQKRRQYDQTGTVDFGAGGSNFnw 83
|
90
....*....|....*..
gi 392894612 94 -DVSEMGGVGRVFGALF 109
Cdd:PRK14290 84 dNFTHFSDINDIFNQIF 100
|
|
| PRK14283 |
PRK14283 |
chaperone protein DnaJ; Provisional |
17-113 |
5.22e-21 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184604 [Multi-domain] Cd Length: 378 Bit Score: 93.35 E-value: 5.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNpNDAHAQEEFKKVSIAYSVLSDPNKRRQYD------VSGPSE----N 86
Cdd:PRK14283 6 DYYEVLGVDRNADKKEIKKAYRKLARKYHPDVS-EEEGAEEKFKEISEAYAVLSDDEKRQRYDqfghagMDGFSQedifN 84
|
90 100
....*....|....*....|....*..
gi 392894612 87 QLDFEgfDVseMGGVGRVFGALFSKLG 113
Cdd:PRK14283 85 NINFE--DI--FQGFGFGIGNIFDMFG 107
|
|
| terminal_TopJ |
NF037946 |
terminal organelle assembly protein TopJ; |
17-95 |
5.62e-21 |
|
terminal organelle assembly protein TopJ;
Pssm-ID: 468284 [Multi-domain] Cd Length: 440 Bit Score: 93.73 E-value: 5.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNpNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSG----PSENQLDFEG 92
Cdd:NF037946 6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRN-KAPDAAEIFAEINEAYEVLSNPEKRANYDKYGhdgvDGEGGFGFDA 84
|
...
gi 392894612 93 FDV 95
Cdd:NF037946 85 FDV 87
|
|
| CbpA |
COG2214 |
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; |
17-81 |
2.36e-20 |
|
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
Pssm-ID: 441816 [Multi-domain] Cd Length: 91 Bit Score: 84.77 E-value: 2.36e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPND-AHAQEEFKKVSIAYSVLSDPNKRRQYDVS 81
Cdd:COG2214 6 DHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELkALAEELFQRLNEAYEVLSDPERRAEYDRE 71
|
|
| PRK14285 |
PRK14285 |
chaperone protein DnaJ; Provisional |
17-105 |
8.65e-20 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172773 [Multi-domain] Cd Length: 365 Bit Score: 89.67 E-value: 8.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPS--ENQLDFEGFD 94
Cdd:PRK14285 4 DYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKEAESIFKEATEAYEVLIDDNKRAQYDRFGHTafEGGGGFEGFS 83
|
90
....*....|.
gi 392894612 95 vSEMGGVGRVF 105
Cdd:PRK14285 84 -GGFSGFSDIF 93
|
|
| PRK14287 |
PRK14287 |
chaperone protein DnaJ; Provisional |
13-109 |
3.57e-19 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237659 [Multi-domain] Cd Length: 371 Bit Score: 87.76 E-value: 3.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 13 VSEMDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNpNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPSENQLDFEG 92
Cdd:PRK14287 1 MSKRDYYEVLGVDRNASVDEVKKAYRKLARKYHPDVN-KAPDAEDKFKEVKEAYDTLSDPQKKAHYDQFGHTDPNQGFGG 79
|
90
....*....|....*..
gi 392894612 93 FDVSEMGGVGRVFGALF 109
Cdd:PRK14287 80 GGAGDFGGFSDIFDMFF 96
|
|
| PRK14296 |
PRK14296 |
chaperone protein DnaJ; Provisional |
17-112 |
4.96e-19 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237666 [Multi-domain] Cd Length: 372 Bit Score: 87.31 E-value: 4.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNpNDAHAQEEFKKVSIAYSVLSDPNKRRQYD---------VSGPSENQ 87
Cdd:PRK14296 5 DYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLN-KSPDAHDKMVEINEAADVLLDKDKRKQYDqfghaafdgSSGFSSNF 83
|
90 100
....*....|....*....|....*.
gi 392894612 88 LDFEGFdVSEMGGVGRV-FGALFSKL 112
Cdd:PRK14296 84 GDFEDL-FSNMGSSGFSsFTNIFSDF 108
|
|
| PRK14282 |
PRK14282 |
chaperone protein DnaJ; Provisional |
17-82 |
3.20e-18 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184603 [Multi-domain] Cd Length: 369 Bit Score: 85.23 E-value: 3.20e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNP-NDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSG 82
Cdd:PRK14282 5 DYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPeNRKEAEQKFKEIQEAYEVLSDPQKRAMYDRFG 71
|
|
| PTZ00037 |
PTZ00037 |
DnaJ_C chaperone protein; Provisional |
18-82 |
8.47e-17 |
|
DnaJ_C chaperone protein; Provisional
Pssm-ID: 240236 [Multi-domain] Cd Length: 421 Bit Score: 81.41 E-value: 8.47e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392894612 18 FYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNdahaQEEFKKVSIAYSVLSDPNKRRQYDVSG 82
Cdd:PTZ00037 30 LYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGD----PEKFKEISRAYEVLSDPEKRKIYDEYG 90
|
|
| PRK14300 |
PRK14300 |
chaperone protein DnaJ; Provisional |
17-82 |
3.64e-15 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172788 [Multi-domain] Cd Length: 372 Bit Score: 76.21 E-value: 3.64e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDrNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSG 82
Cdd:PRK14300 4 DYYQILGVSKTASQADLKKAYLKLAKQYHPD-TTDAKDAEKKFKEINAAYDVLKDEQKRAAYDRFG 68
|
|
| PRK14288 |
PRK14288 |
molecular chaperone DnaJ; |
15-93 |
4.53e-15 |
|
molecular chaperone DnaJ;
Pssm-ID: 172776 [Multi-domain] Cd Length: 369 Bit Score: 75.88 E-value: 4.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 15 EMDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSG------PSENQL 88
Cdd:PRK14288 2 ELSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKEAEEKFKLINEAYGVLSDEKKRALYDRYGkkglnqAGASQS 81
|
....*
gi 392894612 89 DFEGF 93
Cdd:PRK14288 82 DFSDF 86
|
|
| PRK10266 |
PRK10266 |
curved DNA-binding protein; |
17-79 |
6.34e-14 |
|
curved DNA-binding protein;
Pssm-ID: 182347 [Multi-domain] Cd Length: 306 Bit Score: 71.78 E-value: 6.34e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNpNDAHAQEEFKKVSIAYSVLSDPNKRRQYD 79
Cdd:PRK10266 5 DYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVS-KEPDAEARFKEVAEAWEVLSDEQRRAEYD 66
|
|
| DjlA |
COG1076 |
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; |
14-83 |
2.73e-10 |
|
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440694 [Multi-domain] Cd Length: 75 Bit Score: 55.96 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 14 SEMDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRnpndaHAQ---EEFKKVSI--------AYSVLSDPnkrRQYDVSG 82
Cdd:COG1076 2 QLDDAFELLGLPPDADDAELKRAYRKLQREHHPDR-----LAAglpEEEQRLALqkaaaineAYETLKDP---RGIDLAA 73
|
.
gi 392894612 83 P 83
Cdd:COG1076 74 P 74
|
|
| ZUO1 |
COG5269 |
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ... |
17-79 |
3.35e-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: 54.65 E-value: 3.35e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392894612 17 DFYQLLGVEKM---ASEAEIKSAYRKLALKYHPDRNPNDAH--AQEEFKKVSIAYSVLSDPNKRRQYD 79
Cdd:COG5269 44 DLYALLGLSKYrtkAIPPQILKAHKKKVYKYHPDKTAAGGNkgCDEFFKLIQKAREVLGDRKLRLQYD 111
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
13-82 |
2.64e-06 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 49.40 E-value: 2.64e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 13 VSEMDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAhAQEEFKKVSIAYSVLSDPNKRRQYDVSG 82
Cdd:PTZ00341 570 IPDTLFYDILGVGVNADMKEISERYFKLAENYYPPKRSGNE-GFHKFKKINEAYQILGDIDKKKMYNKFG 638
|
|
| djlA |
PRK09430 |
co-chaperone DjlA; |
17-47 |
4.10e-06 |
|
co-chaperone DjlA;
Pssm-ID: 236512 [Multi-domain] Cd Length: 267 Bit Score: 47.88 E-value: 4.10e-06
10 20 30
....*....|....*....|....*....|.
gi 392894612 17 DFYQLLGVEKMASEAEIKSAYRKLALKYHPD 47
Cdd:PRK09430 201 DAYKVLGVSESDDDQEIKRAYRKLMSEHHPD 231
|
|
| PHA03102 |
PHA03102 |
Small T antigen; Reviewed |
20-110 |
1.90e-04 |
|
Small T antigen; Reviewed
Pssm-ID: 222986 [Multi-domain] Cd Length: 153 Bit Score: 41.58 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894612 20 QLLGVEKMA--SEAEIKSAYRKLALKYHPDRNPNdahaQEEFKKVSIAYSVLsdpnkrRQYDvsgPSENQLDFEGFDVSE 97
Cdd:PHA03102 9 DLLGLPRSAwgNLPLMRKAYLRKCLEFHPDKGGD----EEKMKELNTLYKKF------RESV---KSLRDLDGEEDSSSE 75
|
90
....*....|....
gi 392894612 98 MGGVG-RVFGALFS 110
Cdd:PHA03102 76 EEDVPsGYVGATFG 89
|
|
| hscB |
PRK03578 |
Fe-S protein assembly co-chaperone HscB; |
16-78 |
3.78e-04 |
|
Fe-S protein assembly co-chaperone HscB;
Pssm-ID: 235133 [Multi-domain] Cd Length: 176 Bit Score: 40.77 E-value: 3.78e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392894612 16 MDFYQLLGVEKM--ASEAEIKSAYRKLALKYHPDRNpndAHAQEEFKKVSI--------AYSVLSDPNKRRQY 78
Cdd:PRK03578 6 DDHFSLFGLPARfaLDEAALDAAYRTVQAQVHPDRF---AAAGDAEKRVAMqwatraneAYQTLRDPLKRARY 75
|
|
| PLN02281 |
PLN02281 |
chlorophyllide a oxygenase |
280-353 |
3.62e-03 |
|
chlorophyllide a oxygenase
Pssm-ID: 177920 [Multi-domain] Cd Length: 536 Bit Score: 39.33 E-value: 3.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392894612 280 ITFLPVEPSAVEQLNEIQDTEKSISIIKKEMLDFQREFTEAKRKYDEAVAKLKvqddTILKALAHREELYNEVL 353
Cdd:PLN02281 100 LTIMILHDKVVDVLNPLAREYKSIGTVKKELAGLQEELSKAHQQVHISEARVS----TALDKLAHMEELVNDRL 169
|
|
|