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Conserved domains on  [gi|1503143917|ref|XP_026806720|]
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dnaJ homolog subfamily B member 6-like isoform X2 [Rhopalosiphum maidis]

Protein Classification

J domain-containing protein( domain architecture ID 1000550)

J domain-containing protein similar to molecular chaperone DnaJ, a protein that plays crucial roles in protein translation, folding, unfolding, translocation, and degradation, primarily by stimulating the ATPase activity of Hsp70

CATH:  1.10.287.110
Gene Ontology:  GO:0006457
PubMed:  35729039|9644977|8016869|15170475
SCOP:  4000605

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10767 super family cl35946
chaperone protein DnaJ; Provisional
 4-74 7.04e-35

chaperone protein DnaJ; Provisional


The actual alignment was detected with superfamily member PRK10767:

Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 127.57  E-value: 7.04e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDDKKRKAYNQYGKDGL 74
Cdd:PRK10767    5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKE-AEEKFKEIKEAYEVLSDPQKRAAYDQYGHAAF 74
terminal_TopJ super family cl41578
terminal organelle assembly protein TopJ;
4-178 9.80e-23

terminal organelle assembly protein TopJ;


The actual alignment was detected with superfamily member NF037946:

Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 95.66  E-value: 9.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNpeNQEQANRMFKEISEAYEVLSDDKKRKAYNQYGKDGLINGgsgngg 83
Cdd:NF037946    6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRN--KAPDAAEIFAEINEAYEVLSNPEKRANYDKYGHDGVDGE------ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503143917  84 rrrsnqrhpghfDPFGqdfgpgffsfsfRDPEDVFKEFFNTSDVTDLLFPGQRFSNGHQEIS-SMMNPFGFGGFGGGFGS 162
Cdd:NF037946   78 ------------GGFG------------FDAFDVFSSFFETINKSGAFLDDSVDESVSADDDlDRLFDDSKEPSFTSGLD 133

                         170
                  ....*....|....*..
gi 1503143917 163 GFDNMFS-MANNGYSGH 178
Cdd:NF037946  134 EIVQFWEaFIGNPDYGY 150
 
Name Accession Description Interval E-value
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 4-74 7.04e-35

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 127.57  E-value: 7.04e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDDKKRKAYNQYGKDGL 74
Cdd:PRK10767    5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKE-AEEKFKEIKEAYEVLSDPQKRAAYDQYGHAAF 74
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 4-74 3.92e-34

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: 119.42  E-value: 3.92e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDDKKRKAYNQYGKDGL 74
Cdd:COG0484     1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPE-AEEKFKEINEAYEVLSDPEKRAAYDRFGHAAE 70
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 4-67 4.69e-33

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: 114.11  E-value: 4.69e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDDKKRKAYN 67
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPE-AEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 4-74 4.44e-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: 120.01  E-value: 4.44e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPEnqEQANRMFKEISEAYEVLSDDKKRKAYNQYGKDGL 74
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKD--KEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGF 69
DnaJ smart00271
DnaJ molecular chaperone homology domain;
4-62 1.55e-28

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 102.31  E-value: 1.55e-28
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1503143917    4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEQANRMFKEISEAYEVLSDDKK 62
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEKFKEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 4-59 1.37e-25

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: 94.53  E-value: 1.37e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENqEQANRMFKEISEAYEVLSD 59
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD-PEAEEKFKEINEAYEVLSD 55
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
4-178 9.80e-23

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 95.66  E-value: 9.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNpeNQEQANRMFKEISEAYEVLSDDKKRKAYNQYGKDGLINGgsgngg 83
Cdd:NF037946    6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRN--KAPDAAEIFAEINEAYEVLSNPEKRANYDKYGHDGVDGE------ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503143917  84 rrrsnqrhpghfDPFGqdfgpgffsfsfRDPEDVFKEFFNTSDVTDLLFPGQRFSNGHQEIS-SMMNPFGFGGFGGGFGS 162
Cdd:NF037946   78 ------------GGFG------------FDAFDVFSSFFETINKSGAFLDDSVDESVSADDDlDRLFDDSKEPSFTSGLD 133

                         170
                  ....*....|....*..
gi 1503143917 163 GFDNMFS-MANNGYSGH 178
Cdd:NF037946  134 EIVQFWEaFIGNPDYGY 150
PRK14289 PRK14289
molecular chaperone DnaJ;
4-147 4.21e-19

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 84.88  E-value: 4.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDDKKRKAYNQYGKDGLINGGSGngg 83
Cdd:PRK14289    6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDKE-AEEKFKEAAEAYDVLSDPDKRSRYDQFGHAGVGGAAGG--- 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1503143917  84 rrrsnqrhpGHFDPFGQDFgpgffsfsfrdpEDVFKEFFNtsdvtdlLFPGqrFSNGHQEISSM 147
Cdd:PRK14289   82 ---------GGFSGEGMSM------------EDIFSMFGD-------IFGG--HGGGFGGFGGF 115
 
Name Accession Description Interval E-value
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 4-74 7.04e-35

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 127.57  E-value: 7.04e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDDKKRKAYNQYGKDGL 74
Cdd:PRK10767    5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKE-AEEKFKEIKEAYEVLSDPQKRAAYDQYGHAAF 74
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 4-74 3.92e-34

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: 119.42  E-value: 3.92e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDDKKRKAYNQYGKDGL 74
Cdd:COG0484     1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPE-AEEKFKEINEAYEVLSDPEKRAAYDRFGHAAE 70
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 4-67 4.69e-33

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: 114.11  E-value: 4.69e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDDKKRKAYN 67
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPE-AEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 4-74 4.44e-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: 120.01  E-value: 4.44e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPEnqEQANRMFKEISEAYEVLSDDKKRKAYNQYGKDGL 74
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKD--KEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGF 69
DnaJ smart00271
DnaJ molecular chaperone homology domain;
4-62 1.55e-28

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 102.31  E-value: 1.55e-28
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1503143917    4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEQANRMFKEISEAYEVLSDDKK 62
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEKFKEINEAYEVLSDPEK 60
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 4-74 3.02e-28

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 109.85  E-value: 3.02e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDDKKRKAYNQYGKDGL 74
Cdd:PRK14294    5 DYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDKE-AEELFKEAAEAYEVLSDPKKRGIYDQYGHEGL 74
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 4-74 5.79e-28

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 109.55  E-value: 5.79e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDDKKRKAYNQYGKDGL 74
Cdd:PRK14284    2 DYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDAE-AEKRFKEVSEAYEVLSDAQKRESYDRYGKDGP 71
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 1-74 4.16e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 104.50  E-value: 4.16e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1503143917   1 MSGDYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDDKKRKAYNQYGKDGL 74
Cdd:PRK14281    1 MKRDYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKE-AEEHFKEVNEAYEVLSNDDKRRRYDQFGHAGV 73
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 4-59 1.37e-25

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: 94.53  E-value: 1.37e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENqEQANRMFKEISEAYEVLSD 59
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD-PEAEEKFKEINEAYEVLSD 55
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 4-74 2.26e-25

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 102.16  E-value: 2.26e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPD--KNPENQEQanrmFKEISEAYEVLSDDKKRKAYNQYGKDGL 74
Cdd:PRK14291    4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDfnKNPEAEEK----FKEINEAYQVLSDPEKRKLYDQFGHAAF 72
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
4-66 8.18e-25

Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 94.01  E-value: 8.18e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEQANRMFKEISEAYEVLSDDKKRKAY 66
Cdd:COG2214     6 DHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALAEELFQRLNEAYEVLSDPERRAEY 68
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 1-70 1.93e-24

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 99.62  E-value: 1.93e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503143917   1 MSGDYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEQANRMFKEISEAYEVLSDDKKRKAYNQYG 70
Cdd:PRK14290    1 MAKDYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNKAEAEEKFKEISEAYEVLSDPQKRRQYDQTG 70
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 4-74 1.93e-24

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 99.43  E-value: 1.93e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDDKKRKAYNQYGKDGL 74
Cdd:PRK14301    5 DYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNPE-AEQKFKEAAEAYEVLRDAEKRARYDRFGHAGV 74
PRK14280 PRK14280
molecular chaperone DnaJ;
4-73 2.07e-24

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 99.41  E-value: 2.07e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPEnqEQANRMFKEISEAYEVLSDDKKRKAYNQYGKDG 73
Cdd:PRK14280    5 DYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKE--EGADEKFKEISEAYEVLSDDQKRAQYDQFGHAG 72
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 4-65 2.25e-24

Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 91.60  E-value: 2.25e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQeQANRMFKEISEAYEVLSDDKKRKA 65
Cdd:COG5407     1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDP-KAEERFKEINEAYELLSDAEKRAR 61
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 4-74 3.51e-24

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 99.15  E-value: 3.51e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPEnqEQANRMFKEISEAYEVLSDDKKRKAYNQYGKDGL 74
Cdd:PRK14298    6 DYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKE--PDAEEKFKEISEAYAVLSDAEKRAQYDRFGHAGI 74
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 4-143 4.08e-24

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 98.71  E-value: 4.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEQANRMFKEISEAYEVLSDDKKRKAYNQYGKDGLInggsgngg 83
Cdd:PRK14282    5 DYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRKEAEQKFKEIQEAYEVLSDPQKRAMYDRFGYVGEQ-------- 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1503143917  84 rrrsnqrhpghfdPFGQDFGPGFFSFsfrdpEDVFKEF--FNTSDVTDLLFPGQRFSNGHQE 143
Cdd:PRK14282   77 -------------PPYQETESGGGFF-----EDIFKDFenIFNRDIFDIFFGERRTQEEQRE 120
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 4-70 4.37e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 96.02  E-value: 4.37e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDDKKRKAYNQYG 70
Cdd:PRK14277    6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDKE-AEQKFKEINEAYEILSDPQKRAQYDQFG 71
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 4-74 5.99e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 95.66  E-value: 5.99e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPEnqEQANRMFKEISEAYEVLSDDKKRKAYNQYGKDGL 74
Cdd:PRK14283    6 DYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEE--EGAEEKFKEISEAYAVLSDDEKRQRYDQFGHAGM 74
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
4-178 9.80e-23

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 95.66  E-value: 9.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNpeNQEQANRMFKEISEAYEVLSDDKKRKAYNQYGKDGLINGgsgngg 83
Cdd:NF037946    6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRN--KAPDAAEIFAEINEAYEVLSNPEKRANYDKYGHDGVDGE------ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503143917  84 rrrsnqrhpghfDPFGqdfgpgffsfsfRDPEDVFKEFFNTSDVTDLLFPGQRFSNGHQEIS-SMMNPFGFGGFGGGFGS 162
Cdd:NF037946   78 ------------GGFG------------FDAFDVFSSFFETINKSGAFLDDSVDESVSADDDlDRLFDDSKEPSFTSGLD 133

                         170
                  ....*....|....*..
gi 1503143917 163 GFDNMFS-MANNGYSGH 178
Cdd:NF037946  134 EIVQFWEaFIGNPDYGY 150
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 4-73 2.50e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 94.00  E-value: 2.50e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPEnqEQANRMFKEISEAYEVLSDDKKRKAYNQYGKDG 73
Cdd:PRK14276    5 EYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKE--PGAEEKYKEVQEAYETLSDPQKRAAYDQYGAAG 72
PRK14293 PRK14293
molecular chaperone DnaJ;
1-74 2.55e-22

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 93.90  E-value: 2.55e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1503143917   1 MSGDYYSILEVTPNASINDIKKSYRKLALKWHPDKNPEnqEQANRMFKEISEAYEVLSDDKKRKAYNQYGKDGL 74
Cdd:PRK14293    1 MAADYYEILGVSRDADKDELKRAYRRLARKYHPDVNKE--PGAEDRFKEINRAYEVLSDPETRARYDQFGEAGV 72
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 5-74 7.87e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 92.36  E-value: 7.87e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503143917   5 YYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDDKKRKAYNQYGKDGL 74
Cdd:PRK14286    6 YYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKE-SEEKFKEATEAYEILRDPKKRQAYDQFGKAGV 74
PRK14295 PRK14295
molecular chaperone DnaJ;
4-68 1.03e-21

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 92.22  E-value: 1.03e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEQANRmFKEISEAYEVLSDDKKRKAYNQ 68
Cdd:PRK14295   10 DYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDAKAEER-FKEISEAYDVLSDEKKRKEYDE 73
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 1-67 2.07e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 91.27  E-value: 2.07e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1503143917   1 MSGDYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEQANrmFKEISEAYEVLSDDKKRKAYN 67
Cdd:PRK14278    1 MARDYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDEEAQEK--FKEISVAYEVLSDPEKRRIVD 65
PRK14297 PRK14297
molecular chaperone DnaJ;
2-70 4.77e-21

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 90.23  E-value: 4.77e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1503143917   2 SGDYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDDKKRKAYNQYG 70
Cdd:PRK14297    3 SKDYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKE-AEEKFKEINEAYQVLSDPQKKAQYDQFG 70
PRK14279 PRK14279
molecular chaperone DnaJ;
4-68 1.86e-20

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 88.64  E-value: 1.86e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEQANRmFKEISEAYEVLSDDKKRKAYNQ 68
Cdd:PRK14279   10 DFYKELGVSSDASAEEIKKAYRKLARELHPDANPGDPAAEER-FKAVSEAHDVLSDPAKRKEYDE 73
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 5-74 2.42e-20

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 88.72  E-value: 2.42e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1503143917   5 YYSILEVTPNASINDIKKSYRKLALKWHPDK--NPEnqeqanrMFKEISEAYEVLSDDKKRKAYNQYGKDGL 74
Cdd:PTZ00037   30 LYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKggDPE-------KFKEISRAYEVLSDPEKRKIYDEYGEEGL 94
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 4-70 5.28e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 86.15  E-value: 5.28e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPD--KNPENQEQanrmFKEISEAYEVLSDDKKRKAYNQYG 70
Cdd:PRK14299    5 DYYAILGVPKNASQDEIKKAFKKLARKYHPDvnKSPGAEEK----FKEINEAYTVLSDPEKRRIYDTYG 69
termin_org_DnaJ TIGR03835
terminal organelle assembly protein TopJ; This model describes TopJ (MG_200, CbpA), a DnaJ ...
 4-74 5.43e-20

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: 88.33  E-value: 5.43e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNpeNQEQANRMFKEISEAYEVLSDDKKRKAYNQYGKDGL 74
Cdd:TIGR03835   3 DYYEVLGIDRDADEQEIKKAFRKLAKKYHPDRN--KAPDAASIFAEINEANDVLSNPKKRANYDKYGHDGV 71
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 4-122 2.07e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 85.71  E-value: 2.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPEnqEQANRMFKEISEAYEVLSDDKKRKAYNQYGkdglinggsgngg 83
Cdd:PRK14292    3 DYYELLGVSRTASADEIKSAYRKLALKYHPDRNKE--KGAAEKFAQINEAYAVLSDAEKRAHYDRFG------------- 67

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1503143917  84 rRRSNQRHPGHfDPFGqdfgpgffsFSFRDPEDVFKEFF 122
Cdd:PRK14292   68 -TAPGAGMPGG-DPFG---------GMGFDPMDIFEQLF 95
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 1-70 2.15e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 85.43  E-value: 2.15e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503143917   1 MSGDYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDDKKRKAYNQYG 70
Cdd:PRK14285    1 MKRDYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKE-AESIFKEATEAYEVLIDDNKRAQYDRFG 69
PRK14289 PRK14289
molecular chaperone DnaJ;
4-147 4.21e-19

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 84.88  E-value: 4.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDDKKRKAYNQYGKDGLINGGSGngg 83
Cdd:PRK14289    6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDKE-AEEKFKEAAEAYDVLSDPDKRSRYDQFGHAGVGGAAGG--- 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1503143917  84 rrrsnqrhpGHFDPFGQDFgpgffsfsfrdpEDVFKEFFNtsdvtdlLFPGqrFSNGHQEISSM 147
Cdd:PRK14289   82 ---------GGFSGEGMSM------------EDIFSMFGD-------IFGG--HGGGFGGFGGF 115
PRK10266 PRK10266
curved DNA-binding protein;
4-68 2.80e-18

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 81.79  E-value: 2.80e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEQANrmFKEISEAYEVLSDDKKRKAYNQ 68
Cdd:PRK10266    5 DYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEAR--FKEVAEAWEVLSDEQRRAEYDQ 67
PRK14288 PRK14288
molecular chaperone DnaJ;
1-74 2.16e-17

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 80.12  E-value: 2.16e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1503143917   1 MSGDYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEQANRmFKEISEAYEVLSDDKKRKAYNQYGKDGL 74
Cdd:PRK14288    1 MELSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKEAEEK-FKLINEAYGVLSDEKKRALYDRYGKKGL 73
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 1-72 2.30e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 76.98  E-value: 2.30e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1503143917   1 MSGDYYSILEVTPNASINDIKKSYRKLALKWHPDKNpeNQEQANRMFKEISEAYEVLSDDKKRKAYNQYGKD 72
Cdd:PRK14300    1 MSQDYYQILGVSKTASQADLKKAYLKLAKQYHPDTT--DAKDAEKKFKEINAAYDVLKDEQKRAAYDRFGHD 70
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 4-70 3.05e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 76.59  E-value: 3.05e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPEnqEQANRMFKEISEAYEVLSDDKKRKAYNQYG 70
Cdd:PRK14287    5 DYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKA--PDAEDKFKEVKEAYDTLSDPQKKAHYDQFG 69
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
4-65 2.83e-14

DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 65.59  E-value: 2.83e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDK-----NPENQEQANRMFKEISEAYEVLSDDKKRKA 65
Cdd:COG1076     5 DAFELLGLPPDADDAELKRAYRKLQREHHPDRlaaglPEEEQRLALQKAAAINEAYETLKDPRGIDL 71
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 5-74 4.27e-13

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 68.27  E-value: 4.27e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503143917    5 YYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEQANrmFKEISEAYEVLSDDKKRKAYNQYGKDGL 74
Cdd:PTZ00341   575 FYDILGVGVNADMKEISERYFKLAENYYPPKRSGNEGFHK--FKKINEAYQILGDIDKKKMYNKFGYDGI 642
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 4-70 1.83e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 65.74  E-value: 1.83e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENqeQANRMFKEISEAYEVLSDDKKRKAYNQYG 70
Cdd:PRK14296    5 DYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSP--DAHDKMVEINEAADVLLDKDKRKQYDQFG 69
djlA PRK09430
co-chaperone DjlA;
4-64 7.80e-09

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 54.43  E-value: 7.80e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1503143917   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDK------NPENQEQANRMFKEISEAYEVLSDDKKRK 64
Cdd:PRK09430  201 DAYKVLGVSESDDDQEIKRAYRKLMSEHHPDKlvakglPPEMMEMAKEKAQEIQAAYELIKKQKGFK 267
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 4-67 1.95e-04

Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 41.94  E-value: 1.95e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1503143917   4 DYYSILEVTP---NASINDIKKSYRKLALKWHPDKNPENQEQANR-MFKEISEAYEVLSDDKKRKAYN 67
Cdd:COG5269    44 DLYALLGLSKyrtKAIPPQILKAHKKKVYKYHPDKTAAGGNKGCDeFFKLIQKAREVLGDRKLRLQYD 111
PHA03102 PHA03102
Small T antigen; Reviewed
 7-60 6.61e-04

Small T antigen; Reviewed


Pssm-ID: 222986 [Multi-domain]  Cd Length: 153  Bit Score: 38.88  E-value: 6.61e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1503143917   7 SILEVTPNASIN--DIKKSYRKLALKWHPDK--NPENQEQANRMFKEISEAYEVLSDD 60
Cdd:PHA03102    9 DLLGLPRSAWGNlpLMRKAYLRKCLEFHPDKggDEEKMKELNTLYKKFRESVKSLRDL 66
hscB PRK01356
co-chaperone HscB; Provisional
 4-66 2.04e-03

co-chaperone HscB; Provisional


Pssm-ID: 167217 [Multi-domain]  Cd Length: 166  Bit Score: 37.93  E-value: 2.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1503143917   4 DYYSILEVTPNASIN--DIKKSYRKLALKWHPD--KNPENQEQANRMFKEISEAYEVLSDDKKRKAY 66
Cdd:PRK01356    3 NYFQLLGLPQEYNIDlkILEKQYFAMQVKYHPDkaKTLQEKEQNLIIASELNNAYSTLKDALKRAEY 69
hscB TIGR00714
Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K ...
 20-66 2.11e-03

Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K heat shock cognate protein) of a pair of proteins Hsc66-Hsc20, related to the DnaK-DnaJ heat shock proteins, which also serve as molecular chaperones. Hsc20, unlike DnaJ, appears not to have chaperone activity on its own, but to act solely as a regulatory subunit for Hsc66 (i.e., to be a co-chaperone). The gene for Hsc20 in E. coli, hscB, is not induced by heat shock. [Protein fate, Protein folding and stabilization]


Pssm-ID: 211601 [Multi-domain]  Cd Length: 155  Bit Score: 37.56  E-value: 2.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1503143917  20 IKKSYRKLALKWHPDKNPENQEQANRMFK--EISEAYEVLSDDKKRKAY 66
Cdd:TIGR00714   8 LRKRYRQLQAQYHPDASGMAQEQLAASQQstTLNQAYHTLKDPLRRAEY 56
Ubl_TECR_like cd01801
ubiquitin-like (Ubl) domain found in trans-2,3-enoyl-CoA reductase (TECR) and similar proteins; ...
 8-75 6.93e-03

ubiquitin-like (Ubl) domain found in trans-2,3-enoyl-CoA reductase (TECR) and similar proteins; This family includes TECR and many TECR-like proteins, such as TECRL. TECR, also termed very-long-chain enoyl-CoA reductase, or synaptic glycoprotein SC2, or TER, or GPSN2, is a synaptic glycoprotein that catalyzes the fourth reaction in the synthesis of very long-chain fatty acids (VLCFA) which is the reduction step of the microsomal fatty acyl-elongation process. Diseases involving perturbations to normal synthesis and degradation of VLCFA (e.g. adrenoleukodystrophy and Zellweger syndrome) have significant neurological consequences. The mammalian TECR P182L mutation causes nonsyndromic mental retardation. Deletion of the yeast TECR (TSC13) homolog is lethal. TECR contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions, as well as a C-terminal catalytic domain. TECRL, also termed steroid 5-alpha-reductase 2-like 2 protein (SRD5A2L2), is associated with life-threatening inherited arrhythmias displaying features of both long QT syndrome (LQTS) and catecholaminergic polymorphic ventricular tachycardia (CPVT). Both TECR and TECRL contain an N-terminal Ubl domain with a beta-grasp Ubl fold, and a C-terminal catalytic domain.


Pssm-ID: 340499 [Multi-domain]  Cd Length: 77  Bit Score: 34.57  E-value: 6.93e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1503143917   8 ILEVTPNASINDIKKSYRKLALKWHPDKnpenqeQAnrmFKEISEAYEVLSDDKKRKAYNqyGKDGLI 75
Cdd:cd01801    15 TLEVSSSATVADLKKAIHKKKKKLYPER------QR---LRLEVPKGKVLKDDKTLSSYG--VKDGST 71
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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