|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14297 |
PRK14297 |
molecular chaperone DnaJ; |
34-126 |
5.13e-33 |
|
molecular chaperone DnaJ;
Pssm-ID: 184611 [Multi-domain] Cd Length: 380 Bit Score: 127.21 E-value: 5.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPSENQLD------- 106
Cdd:PRK14297 5 DYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKEAEEKFKEINEAYQVLSDPQKKAQYDQFGTADFNGAggfgsgg 84
|
90 100
....*....|....*....|
gi 392894610 107 FEGFDVSEMGGVGRVFGALF 126
Cdd:PRK14297 85 FGGFDFSDMGGFGDIFDSFF 104
|
|
| DnaJ |
pfam00226 |
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
34-96 |
1.78e-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: 116.42 E-value: 1.78e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYD 96
Cdd:pfam00226 1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
|
|
| DnaJ_bact |
TIGR02349 |
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
34-126 |
2.03e-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: 125.02 E-value: 2.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPnDAHAQEEFKKVSIAYSVLSDPNKRRQYDV-------SGPSENQLD 106
Cdd:TIGR02349 1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNK-DKEAEEKFKEINEAYEVLSDPEKRAQYDQfghagfnGGGGGGGGG 79
|
90 100
....*....|....*....|
gi 392894610 107 FEGFDVSEMGGVGRVFGALF 126
Cdd:TIGR02349 80 FNGFDIGFFGDFGDIFGDFF 99
|
|
| DnaJ |
COG0484 |
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
34-99 |
2.56e-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: 2.56e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSG 99
Cdd:COG0484 1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFG 66
|
|
| DnaJ |
cd06257 |
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
34-88 |
4.40e-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: 93.76 E-value: 4.40e-24
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSD 88
Cdd:cd06257 1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
|
|
| DnaJ |
smart00271 |
DnaJ molecular chaperone homology domain; |
33-91 |
1.06e-22 |
|
DnaJ molecular chaperone homology domain;
Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 90.37 E-value: 1.06e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 33 MDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAH-AQEEFKKVSIAYSVLSDPNK 91
Cdd:smart00271 1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEeAEEKFKEINEAYEVLSDPEK 60
|
|
| terminal_TopJ |
NF037946 |
terminal organelle assembly protein TopJ; |
34-112 |
3.62e-21 |
|
terminal organelle assembly protein TopJ;
Pssm-ID: 468284 [Multi-domain] Cd Length: 440 Bit Score: 94.50 E-value: 3.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNpNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSG----PSENQLDFEG 109
Cdd:NF037946 6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRN-KAPDAAEIFAEINEAYEVLSNPEKRANYDKYGhdgvDGEGGFGFDA 84
|
...
gi 392894610 110 FDV 112
Cdd:NF037946 85 FDV 87
|
|
| PLN02281 |
PLN02281 |
chlorophyllide a oxygenase |
297-370 |
3.65e-03 |
|
chlorophyllide a oxygenase
Pssm-ID: 177920 [Multi-domain] Cd Length: 536 Bit Score: 39.33 E-value: 3.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392894610 297 ITFLPVEPSAVEQLNEIQDTEKSISIIKKEMLDFQREFTEAKRKYDEAVAKLKvqddTILKALAHREELYNEVL 370
Cdd:PLN02281 100 LTIMILHDKVVDVLNPLAREYKSIGTVKKELAGLQEELSKAHQQVHISEARVS----TALDKLAHMEELVNDRL 169
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14297 |
PRK14297 |
molecular chaperone DnaJ; |
34-126 |
5.13e-33 |
|
molecular chaperone DnaJ;
Pssm-ID: 184611 [Multi-domain] Cd Length: 380 Bit Score: 127.21 E-value: 5.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPSENQLD------- 106
Cdd:PRK14297 5 DYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKEAEEKFKEINEAYQVLSDPQKKAQYDQFGTADFNGAggfgsgg 84
|
90 100
....*....|....*....|
gi 392894610 107 FEGFDVSEMGGVGRVFGALF 126
Cdd:PRK14297 85 FGGFDFSDMGGFGDIFDSFF 104
|
|
| PRK10767 |
PRK10767 |
chaperone protein DnaJ; Provisional |
31-127 |
1.13e-32 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 126.03 E-value: 1.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 31 SEMDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDvsgpsenQLDFEGF 110
Cdd:PRK10767 2 AKRDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYD-------QYGHAAF 74
|
90 100
....*....|....*....|....
gi 392894610 111 DVSEMGG-------VGRVFGALFS 127
Cdd:PRK10767 75 EQGGGGGgfgggggFGDIFGDIFG 98
|
|
| DnaJ |
pfam00226 |
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
34-96 |
1.78e-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: 116.42 E-value: 1.78e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYD 96
Cdd:pfam00226 1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
|
|
| DnaJ_bact |
TIGR02349 |
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
34-126 |
2.03e-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: 125.02 E-value: 2.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPnDAHAQEEFKKVSIAYSVLSDPNKRRQYDV-------SGPSENQLD 106
Cdd:TIGR02349 1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNK-DKEAEEKFKEINEAYEVLSDPEKRAQYDQfghagfnGGGGGGGGG 79
|
90 100
....*....|....*....|
gi 392894610 107 FEGFDVSEMGGVGRVFGALF 126
Cdd:TIGR02349 80 FNGFDIGFFGDFGDIFGDFF 99
|
|
| DnaJ |
COG0484 |
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
34-99 |
2.56e-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: 2.56e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSG 99
Cdd:COG0484 1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFG 66
|
|
| PRK14278 |
PRK14278 |
chaperone protein DnaJ; Provisional |
34-126 |
3.87e-28 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237654 [Multi-domain] Cd Length: 378 Bit Score: 113.61 E-value: 3.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAhAQEEFKKVSIAYSVLSDPNKRRQYDVSG-PSENQLDFEGFDV 112
Cdd:PRK14278 4 DYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDEE-AQEKFKEISVAYEVLSDPEKRRIVDLGGdPLESAGGGGGGFG 82
|
90
....*....|....
gi 392894610 113 SEMGGVGRVFGALF 126
Cdd:PRK14278 83 GGFGGLGDVFEAFF 96
|
|
| PRK14277 |
PRK14277 |
chaperone protein DnaJ; Provisional |
34-127 |
8.00e-28 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184599 [Multi-domain] Cd Length: 386 Bit Score: 112.97 E-value: 8.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPS------ENQLDF 107
Cdd:PRK14277 6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDKEAEQKFKEINEAYEILSDPQKRAQYDQFGHAafdpggFGQGGF 85
|
90 100
....*....|....*....|....*.
gi 392894610 108 ------EGFDVSEMGGVGRVFGALFS 127
Cdd:PRK14277 86 gqggfgGGGFDFDFGGFGDIFEDIFG 111
|
|
| SEC63 |
COG5407 |
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ... |
34-94 |
4.62e-27 |
|
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 444165 [Multi-domain] Cd Length: 61 Bit Score: 102.00 E-value: 4.62e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQ 94
Cdd:COG5407 1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDPKAEERFKEINEAYELLSDAEKRAR 61
|
|
| PRK14279 |
PRK14279 |
molecular chaperone DnaJ; |
27-130 |
6.77e-27 |
|
molecular chaperone DnaJ;
Pssm-ID: 237655 [Multi-domain] Cd Length: 392 Bit Score: 110.59 E-value: 6.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 27 QPKVSEMDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVS-------- 98
Cdd:PRK14279 3 QREWVEKDFYKELGVSSDASAEEIKKAYRKLARELHPDANPGDPAAEERFKAVSEAHDVLSDPAKRKEYDETrrlfaggg 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 392894610 99 ------------GPSENQLDFEGFDVSEM---------GGVGRVFGALFSKLG 130
Cdd:PRK14279 83 fggrrfdggggfGGFGTGGDGAEFNLNDLfdaagrgggGGIGDLFGGLFNRGG 135
|
|
| PRK14298 |
PRK14298 |
chaperone protein DnaJ; Provisional |
34-126 |
1.41e-26 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184612 [Multi-domain] Cd Length: 377 Bit Score: 109.55 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNpNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPS--ENQLDFEG-F 110
Cdd:PRK14298 6 DYYEILGLSKDASVEDIKKAYRKLAMKYHPDKN-KEPDAEEKFKEISEAYAVLSDAEKRAQYDRFGHAgiDNQYSAEDiF 84
|
90
....*....|....*.
gi 392894610 111 DVSEMGGVGRVFGALF 126
Cdd:PRK14298 85 RGADFGGFGDIFEMFF 100
|
|
| PRK14295 |
PRK14295 |
molecular chaperone DnaJ; |
32-130 |
5.45e-26 |
|
molecular chaperone DnaJ;
Pssm-ID: 237665 [Multi-domain] Cd Length: 389 Bit Score: 108.01 E-value: 5.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 32 EMDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVS-----------GP 100
Cdd:PRK14295 8 EKDYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDAKAEERFKEISEAYDVLSDEKKRKEYDEArslfgnggfrpGP 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 392894610 101 SENQLDFEGFDVSEM--------------GGVGRVFGALFSKLG 130
Cdd:PRK14295 88 GGGGGGGFNFDLGDLfgggaqggggagggGGLGDVFGGLFNRGG 131
|
|
| PRK14301 |
PRK14301 |
chaperone protein DnaJ; Provisional |
31-126 |
1.22e-25 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237668 [Multi-domain] Cd Length: 373 Bit Score: 106.75 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 31 SEMDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPS--ENQLDFE 108
Cdd:PRK14301 2 SQRDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNPEAEQKFKEAAEAYEVLRDAEKRARYDRFGHAgvNGNGGFG 81
|
90 100
....*....|....*....|
gi 392894610 109 GFDVSE--MGGVGRVFGALF 126
Cdd:PRK14301 82 GFSSAEdiFSHFSDIFGDLF 101
|
|
| PRK14284 |
PRK14284 |
chaperone protein DnaJ; Provisional |
33-130 |
1.60e-25 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237658 [Multi-domain] Cd Length: 391 Bit Score: 106.47 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 33 MDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYD-------------VSG 99
Cdd:PRK14284 1 MDYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDAEAEKRFKEVSEAYEVLSDAQKRESYDrygkdgpfagaggFGG 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 392894610 100 PSENQLD-----FEGFDVSEMGGVGRVFGALFSKLG 130
Cdd:PRK14284 81 AGMGNMEdalrtFMGAFGGEFGGGGSFFEGLFGGLG 116
|
|
| PRK14292 |
PRK14292 |
chaperone protein DnaJ; Provisional |
33-102 |
1.71e-25 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237662 [Multi-domain] Cd Length: 371 Bit Score: 106.13 E-value: 1.71e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 33 MDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPnDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPSE 102
Cdd:PRK14292 2 MDYYELLGVSRTASADEIKSAYRKLALKYHPDRNK-EKGAAEKFAQINEAYAVLSDAEKRAHYDRFGTAP 70
|
|
| PRK14294 |
PRK14294 |
chaperone protein DnaJ; Provisional |
34-126 |
1.14e-24 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237664 [Multi-domain] Cd Length: 366 Bit Score: 103.69 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPS--ENQ--LDFEG 109
Cdd:PRK14294 5 DYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDKEAEELFKEAAEAYEVLSDPKKRGIYDQYGHEglSGTgfSGFSG 84
|
90
....*....|....*..
gi 392894610 110 FDvSEMGGVGRVFGALF 126
Cdd:PRK14294 85 FD-DIFSSFGDIFEDFF 100
|
|
| PRK14276 |
PRK14276 |
chaperone protein DnaJ; Provisional |
32-126 |
2.76e-24 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237653 [Multi-domain] Cd Length: 380 Bit Score: 102.86 E-value: 2.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 32 EMDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNpNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPSENQLDF---- 107
Cdd:PRK14276 3 NTEYYDRLGVSKDASQDEIKKAYRKLSKKYHPDIN-KEPGAEEKYKEVQEAYETLSDPQKRAAYDQYGAAGANGGFggga 81
|
90 100
....*....|....*....|...
gi 392894610 108 ---EGFD-VSEMGGVGRVFGALF 126
Cdd:PRK14276 82 ggfGGFDgSGGFGGFEDIFSSFF 104
|
|
| PRK14289 |
PRK14289 |
molecular chaperone DnaJ; |
34-130 |
3.05e-24 |
|
molecular chaperone DnaJ;
Pssm-ID: 237660 [Multi-domain] Cd Length: 386 Bit Score: 102.99 E-value: 3.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYD------VSGPSENQlDF 107
Cdd:PRK14289 6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDKEAEEKFKEAAEAYDVLSDPDKRSRYDqfghagVGGAAGGG-GF 84
|
90 100
....*....|....*....|...
gi 392894610 108 EGFDVSeMGGVGRVFGALFSKLG 130
Cdd:PRK14289 85 SGEGMS-MEDIFSMFGDIFGGHG 106
|
|
| PRK14291 |
PRK14291 |
chaperone protein DnaJ; Provisional |
34-130 |
3.51e-24 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237661 [Multi-domain] Cd Length: 382 Bit Score: 102.54 E-value: 3.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNdAHAQEEFKKVSIAYSVLSDPNKRRQYD------VSGPSENQLDF 107
Cdd:PRK14291 4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKN-PEAEEKFKEINEAYQVLSDPEKRKLYDqfghaaFSGSGQQQQGQ 82
|
90 100
....*....|....*....|...
gi 392894610 108 EGFDVSEMGGVGRVFGALFSKLG 130
Cdd:PRK14291 83 EGFSDFGGGNIEDILEDVFDIFG 105
|
|
| DnaJ |
cd06257 |
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
34-88 |
4.40e-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: 93.76 E-value: 4.40e-24
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSD 88
Cdd:cd06257 1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
|
|
| PRK14281 |
PRK14281 |
chaperone protein DnaJ; Provisional |
34-124 |
1.87e-23 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237657 [Multi-domain] Cd Length: 397 Bit Score: 100.65 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDvsgpsenQLDFEGFDVS 113
Cdd:PRK14281 4 DYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKEAEEHFKEVNEAYEVLSNDDKRRRYD-------QFGHAGVGSS 76
|
90
....*....|.
gi 392894610 114 EMGGVGRVFGA 124
Cdd:PRK14281 77 AASGGGPGYGG 87
|
|
| PRK14293 |
PRK14293 |
molecular chaperone DnaJ; |
34-130 |
2.90e-23 |
|
molecular chaperone DnaJ;
Pssm-ID: 237663 [Multi-domain] Cd Length: 374 Bit Score: 100.06 E-value: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNpNDAHAQEEFKKVSIAYSVLSDPNKRRQYD------VSGPSenqldf 107
Cdd:PRK14293 4 DYYEILGVSRDADKDELKRAYRRLARKYHPDVN-KEPGAEDRFKEINRAYEVLSDPETRARYDqfgeagVSGAA------ 76
|
90 100
....*....|....*....|....
gi 392894610 108 eGF-DVSEMGGVGRVFGALFSKLG 130
Cdd:PRK14293 77 -GFpDMGDMGGFADIFETFFSGFG 99
|
|
| PRK14280 |
PRK14280 |
molecular chaperone DnaJ; |
30-126 |
3.17e-23 |
|
molecular chaperone DnaJ;
Pssm-ID: 237656 [Multi-domain] Cd Length: 376 Bit Score: 99.80 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 30 VSEMDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNpNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPSENQLDFEG 109
Cdd:PRK14280 1 MAKRDYYEVLGVSKSASKDEIKKAYRKLSKKYHPDIN-KEEGADEKFKEISEAYEVLSDDQKRAQYDQFGHAGPNQGFGG 79
|
90 100
....*....|....*....|..
gi 392894610 110 F-----DVSEMGGVGRVFGALF 126
Cdd:PRK14280 80 GgfgggDFGGGFGFEDIFSSFF 101
|
|
| PRK14286 |
PRK14286 |
chaperone protein DnaJ; Provisional |
30-126 |
4.24e-23 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172774 [Multi-domain] Cd Length: 372 Bit Score: 99.29 E-value: 4.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 30 VSEMDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPSENQLDFEG 109
Cdd:PRK14286 1 MSERSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYDQFGKAGVNAGAGG 80
|
90 100
....*....|....*....|....
gi 392894610 110 F------DVSEM-GGVGRVFGALF 126
Cdd:PRK14286 81 FgqgaytDFSDIfGDFGDIFGDFF 104
|
|
| DnaJ |
smart00271 |
DnaJ molecular chaperone homology domain; |
33-91 |
1.06e-22 |
|
DnaJ molecular chaperone homology domain;
Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 90.37 E-value: 1.06e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 33 MDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAH-AQEEFKKVSIAYSVLSDPNK 91
Cdd:smart00271 1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEeAEEKFKEINEAYEVLSDPEK 60
|
|
| PRK14299 |
PRK14299 |
chaperone protein DnaJ; Provisional |
34-130 |
5.88e-22 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237667 [Multi-domain] Cd Length: 291 Bit Score: 95.01 E-value: 5.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNpNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPSENQL-------- 105
Cdd:PRK14299 5 DYYAILGVPKNASQDEIKKAFKKLARKYHPDVN-KSPGAEEKFKEINEAYTVLSDPEKRRIYDTYGTTAASAgwqgpppg 83
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 392894610 106 -----DFEGFDVSEM-----------GGVGRvFGALFSKLG 130
Cdd:PRK14299 84 ppgggDFSGFNVGDFsdffqqlfggrGGFGG-FGDLFGSVG 123
|
|
| PRK14290 |
PRK14290 |
chaperone protein DnaJ; Provisional |
34-126 |
1.47e-21 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172778 [Multi-domain] Cd Length: 365 Bit Score: 95.00 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNP-NDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPSENQLDFEGF-- 110
Cdd:PRK14290 4 DYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPgNKAEAEEKFKEISEAYEVLSDPQKRRQYDQTGTVDFGAGGSNFnw 83
|
90
....*....|....*..
gi 392894610 111 -DVSEMGGVGRVFGALF 126
Cdd:PRK14290 84 dNFTHFSDINDIFNQIF 100
|
|
| terminal_TopJ |
NF037946 |
terminal organelle assembly protein TopJ; |
34-112 |
3.62e-21 |
|
terminal organelle assembly protein TopJ;
Pssm-ID: 468284 [Multi-domain] Cd Length: 440 Bit Score: 94.50 E-value: 3.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNpNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSG----PSENQLDFEG 109
Cdd:NF037946 6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRN-KAPDAAEIFAEINEAYEVLSNPEKRANYDKYGhdgvDGEGGFGFDA 84
|
...
gi 392894610 110 FDV 112
Cdd:NF037946 85 FDV 87
|
|
| PRK14283 |
PRK14283 |
chaperone protein DnaJ; Provisional |
34-130 |
4.89e-21 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184604 [Multi-domain] Cd Length: 378 Bit Score: 93.74 E-value: 4.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNpNDAHAQEEFKKVSIAYSVLSDPNKRRQYD------VSGPSE----N 103
Cdd:PRK14283 6 DYYEVLGVDRNADKKEIKKAYRKLARKYHPDVS-EEEGAEEKFKEISEAYAVLSDDEKRQRYDqfghagMDGFSQedifN 84
|
90 100
....*....|....*....|....*..
gi 392894610 104 QLDFEgfDVseMGGVGRVFGALFSKLG 130
Cdd:PRK14283 85 NINFE--DI--FQGFGFGIGNIFDMFG 107
|
|
| CbpA |
COG2214 |
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; |
34-98 |
3.00e-20 |
|
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
Pssm-ID: 441816 [Multi-domain] Cd Length: 91 Bit Score: 84.38 E-value: 3.00e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPND-AHAQEEFKKVSIAYSVLSDPNKRRQYDVS 98
Cdd:COG2214 6 DHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELkALAEELFQRLNEAYEVLSDPERRAEYDRE 71
|
|
| PRK14285 |
PRK14285 |
chaperone protein DnaJ; Provisional |
34-122 |
8.69e-20 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172773 [Multi-domain] Cd Length: 365 Bit Score: 89.67 E-value: 8.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPS--ENQLDFEGFD 111
Cdd:PRK14285 4 DYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKEAESIFKEATEAYEVLIDDNKRAQYDRFGHTafEGGGGFEGFS 83
|
90
....*....|.
gi 392894610 112 vSEMGGVGRVF 122
Cdd:PRK14285 84 -GGFSGFSDIF 93
|
|
| PRK14287 |
PRK14287 |
chaperone protein DnaJ; Provisional |
30-126 |
3.31e-19 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237659 [Multi-domain] Cd Length: 371 Bit Score: 88.14 E-value: 3.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 30 VSEMDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNpNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSGPSENQLDFEG 109
Cdd:PRK14287 1 MSKRDYYEVLGVDRNASVDEVKKAYRKLARKYHPDVN-KAPDAEDKFKEVKEAYDTLSDPQKKAHYDQFGHTDPNQGFGG 79
|
90
....*....|....*..
gi 392894610 110 FDVSEMGGVGRVFGALF 126
Cdd:PRK14287 80 GGAGDFGGFSDIFDMFF 96
|
|
| PRK14296 |
PRK14296 |
chaperone protein DnaJ; Provisional |
34-129 |
4.30e-19 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237666 [Multi-domain] Cd Length: 372 Bit Score: 87.69 E-value: 4.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNpNDAHAQEEFKKVSIAYSVLSDPNKRRQYD---------VSGPSENQ 104
Cdd:PRK14296 5 DYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLN-KSPDAHDKMVEINEAADVLLDKDKRKQYDqfghaafdgSSGFSSNF 83
|
90 100
....*....|....*....|....*.
gi 392894610 105 LDFEGFdVSEMGGVGRV-FGALFSKL 129
Cdd:PRK14296 84 GDFEDL-FSNMGSSGFSsFTNIFSDF 108
|
|
| PRK14282 |
PRK14282 |
chaperone protein DnaJ; Provisional |
34-99 |
2.99e-18 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184603 [Multi-domain] Cd Length: 369 Bit Score: 85.23 E-value: 2.99e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNP-NDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSG 99
Cdd:PRK14282 5 DYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPeNRKEAEQKFKEIQEAYEVLSDPQKRAMYDRFG 71
|
|
| PTZ00037 |
PTZ00037 |
DnaJ_C chaperone protein; Provisional |
35-99 |
7.20e-17 |
|
DnaJ_C chaperone protein; Provisional
Pssm-ID: 240236 [Multi-domain] Cd Length: 421 Bit Score: 81.79 E-value: 7.20e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392894610 35 FYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNdahaQEEFKKVSIAYSVLSDPNKRRQYDVSG 99
Cdd:PTZ00037 30 LYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGD----PEKFKEISRAYEVLSDPEKRKIYDEYG 90
|
|
| PRK14300 |
PRK14300 |
chaperone protein DnaJ; Provisional |
34-99 |
4.06e-15 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172788 [Multi-domain] Cd Length: 372 Bit Score: 76.21 E-value: 4.06e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDrNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSG 99
Cdd:PRK14300 4 DYYQILGVSKTASQADLKKAYLKLAKQYHPD-TTDAKDAEKKFKEINAAYDVLKDEQKRAAYDRFG 68
|
|
| PRK14288 |
PRK14288 |
molecular chaperone DnaJ; |
32-110 |
4.27e-15 |
|
molecular chaperone DnaJ;
Pssm-ID: 172776 [Multi-domain] Cd Length: 369 Bit Score: 75.88 E-value: 4.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 32 EMDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAHAQEEFKKVSIAYSVLSDPNKRRQYDVSG------PSENQL 105
Cdd:PRK14288 2 ELSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKEAEEKFKLINEAYGVLSDEKKRALYDRYGkkglnqAGASQS 81
|
....*
gi 392894610 106 DFEGF 110
Cdd:PRK14288 82 DFSDF 86
|
|
| PRK10266 |
PRK10266 |
curved DNA-binding protein; |
34-96 |
6.35e-14 |
|
curved DNA-binding protein;
Pssm-ID: 182347 [Multi-domain] Cd Length: 306 Bit Score: 71.78 E-value: 6.35e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNpNDAHAQEEFKKVSIAYSVLSDPNKRRQYD 96
Cdd:PRK10266 5 DYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVS-KEPDAEARFKEVAEAWEVLSDEQRRAEYD 66
|
|
| DjlA |
COG1076 |
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; |
31-100 |
2.90e-10 |
|
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440694 [Multi-domain] Cd Length: 75 Bit Score: 55.96 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 31 SEMDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRnpndaHAQ---EEFKKVSI--------AYSVLSDPnkrRQYDVSG 99
Cdd:COG1076 2 QLDDAFELLGLPPDADDAELKRAYRKLQREHHPDR-----LAAglpEEEQRLALqkaaaineAYETLKDP---RGIDLAA 73
|
.
gi 392894610 100 P 100
Cdd:COG1076 74 P 74
|
|
| ZUO1 |
COG5269 |
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ... |
34-96 |
3.14e-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: 55.04 E-value: 3.14e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392894610 34 DFYQLLGVEKM---ASEAEIKSAYRKLALKYHPDRNPNDAH--AQEEFKKVSIAYSVLSDPNKRRQYD 96
Cdd:COG5269 44 DLYALLGLSKYrtkAIPPQILKAHKKKVYKYHPDKTAAGGNkgCDEFFKLIQKAREVLGDRKLRLQYD 111
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
30-99 |
1.93e-06 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 50.17 E-value: 1.93e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 30 VSEMDFYQLLGVEKMASEAEIKSAYRKLALKYHPDRNPNDAhAQEEFKKVSIAYSVLSDPNKRRQYDVSG 99
Cdd:PTZ00341 570 IPDTLFYDILGVGVNADMKEISERYFKLAENYYPPKRSGNE-GFHKFKKINEAYQILGDIDKKKMYNKFG 638
|
|
| djlA |
PRK09430 |
co-chaperone DjlA; |
34-64 |
4.87e-06 |
|
co-chaperone DjlA;
Pssm-ID: 236512 [Multi-domain] Cd Length: 267 Bit Score: 47.50 E-value: 4.87e-06
10 20 30
....*....|....*....|....*....|.
gi 392894610 34 DFYQLLGVEKMASEAEIKSAYRKLALKYHPD 64
Cdd:PRK09430 201 DAYKVLGVSESDDDQEIKRAYRKLMSEHHPD 231
|
|
| PHA03102 |
PHA03102 |
Small T antigen; Reviewed |
37-127 |
1.77e-04 |
|
Small T antigen; Reviewed
Pssm-ID: 222986 [Multi-domain] Cd Length: 153 Bit Score: 41.58 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392894610 37 QLLGVEKMA--SEAEIKSAYRKLALKYHPDRNPNdahaQEEFKKVSIAYSVLsdpnkrRQYDvsgPSENQLDFEGFDVSE 114
Cdd:PHA03102 9 DLLGLPRSAwgNLPLMRKAYLRKCLEFHPDKGGD----EEKMKELNTLYKKF------RESV---KSLRDLDGEEDSSSE 75
|
90
....*....|....
gi 392894610 115 MGGVG-RVFGALFS 127
Cdd:PHA03102 76 EEDVPsGYVGATFG 89
|
|
| hscB |
PRK03578 |
Fe-S protein assembly co-chaperone HscB; |
33-95 |
4.57e-04 |
|
Fe-S protein assembly co-chaperone HscB;
Pssm-ID: 235133 [Multi-domain] Cd Length: 176 Bit Score: 40.77 E-value: 4.57e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392894610 33 MDFYQLLGVEKM--ASEAEIKSAYRKLALKYHPDRNpndAHAQEEFKKVSI--------AYSVLSDPNKRRQY 95
Cdd:PRK03578 6 DDHFSLFGLPARfaLDEAALDAAYRTVQAQVHPDRF---AAAGDAEKRVAMqwatraneAYQTLRDPLKRARY 75
|
|
| PLN02281 |
PLN02281 |
chlorophyllide a oxygenase |
297-370 |
3.65e-03 |
|
chlorophyllide a oxygenase
Pssm-ID: 177920 [Multi-domain] Cd Length: 536 Bit Score: 39.33 E-value: 3.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392894610 297 ITFLPVEPSAVEQLNEIQDTEKSISIIKKEMLDFQREFTEAKRKYDEAVAKLKvqddTILKALAHREELYNEVL 370
Cdd:PLN02281 100 LTIMILHDKVVDVLNPLAREYKSIGTVKKELAGLQEELSKAHQQVHISEARVS----TALDKLAHMEELVNDRL 169
|
|
|