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Conserved domains on  [gi|242091189|ref|XP_002441427|]
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uncharacterized protein LOC8084439 [Sorghum bicolor]

Protein Classification

J domain-containing protein( domain architecture ID 11088423)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 75-137 1.54e-23

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: 91.77  E-value: 1.54e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242091189   75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTNFCMFINEVYSVLSDPAQRAVYD 137
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
Fer4_13 pfam13370
4Fe-4S single cluster domain of Ferredoxin I; Fer4_13 is a ferredoxin I from sulfate-reducing ...
 162-216 3.40e-18

4Fe-4S single cluster domain of Ferredoxin I; Fer4_13 is a ferredoxin I from sulfate-reducing bacteria. Chemical sequence analysis suggests that this characteriztic [4Fe-4S] cluster sulfur environment is widely distributed among ferredoxins.


:

Pssm-ID: 433153 [Multi-domain]  Cd Length: 58  Bit Score: 77.35  E-value: 3.40e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 242091189  162 VDEFTCIGCKNCANICPGVFEIEEDFGRSRVYSQSGSTELI---QDAIDSCPVDCIHW 216
Cdd:pfam13370   1 VDEDTCIDCGTCRELAPEVFKYDDDGGASFVHDQPVNEEEEdlaEEALDSCPVEAIGT 58
PRK11749 super family cl46914
dihydropyrimidine dehydrogenase subunit A; Provisional
 158-299 1.10e-03

dihydropyrimidine dehydrogenase subunit A; Provisional


The actual alignment was detected with superfamily member PRK12809:

Pssm-ID: 481254 [Multi-domain]  Cd Length: 639  Bit Score: 40.78  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242091189 158 DHVFVDEFTCIGCKNCANICP-GVFEIEEDFG-RSRVYSQSGSTEliQDAIDSCPVDCIHWTSAAQLslleNEMRRVERV 235
Cdd:PRK12809  78 DSVQLDEQKCIGCKRCAIACPfGVVEMVDTIAqKCDLCNQRSSGT--QACIEVCPTQALRLMDDKGL----QQIKVARQR 151

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242091189 236 NvglmlAGMGASVDvfrmaSARWEKRQAKVLGKVRTRMVKQENSDTRSSWSDIW-GSPPQDQSNE 299
Cdd:PRK12809 152 K-----TAAGKASS-----DAQPSRSAALLPVNSRKGADKISASERKTHFGEIYcGLDPQQATYE 206
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 75-137 1.54e-23

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: 91.77  E-value: 1.54e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242091189   75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTNFCMFINEVYSVLSDPAQRAVYD 137
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 75-138 4.28e-21

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: 87.84  E-value: 4.28e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTNFCMFINEVYSVLSDPAQRAVYDE 138
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDR 64
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 75-129 6.58e-20

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: 81.82  E-value: 6.58e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTNFCMFINEVYSVLSD 129
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
Fer4_13 pfam13370
4Fe-4S single cluster domain of Ferredoxin I; Fer4_13 is a ferredoxin I from sulfate-reducing ...
 162-216 3.40e-18

4Fe-4S single cluster domain of Ferredoxin I; Fer4_13 is a ferredoxin I from sulfate-reducing bacteria. Chemical sequence analysis suggests that this characteriztic [4Fe-4S] cluster sulfur environment is widely distributed among ferredoxins.


Pssm-ID: 433153 [Multi-domain]  Cd Length: 58  Bit Score: 77.35  E-value: 3.40e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 242091189  162 VDEFTCIGCKNCANICPGVFEIEEDFGRSRVYSQSGSTELI---QDAIDSCPVDCIHW 216
Cdd:pfam13370   1 VDEDTCIDCGTCRELAPEVFKYDDDGGASFVHDQPVNEEEEdlaEEALDSCPVEAIGT 58
DnaJ smart00271
DnaJ molecular chaperone homology domain;
75-130 1.50e-15

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 69.96  E-value: 1.50e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 242091189    75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPD-LSGNDPDVTNFCMFINEVYSVLSDP 130
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDkNPGDKEEAEEKFKEINEAYEVLSDP 58
Fer COG1141
Ferredoxin [Energy production and conversion];
159-216 1.71e-14

Ferredoxin [Energy production and conversion];


Pssm-ID: 440756 [Multi-domain]  Cd Length: 63  Bit Score: 67.21  E-value: 1.71e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242091189 159 HVFVDEFTCIGCKNCANICPGVFEIEEDfGRSRVYSQ---SGSTELIQDAIDSCPVDCIHW 216
Cdd:COG1141    2 KVTVDRDTCIGCGLCVALAPEVFELDDD-GKAVVLDEevpEELEEDVREAADACPVGAITV 61
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 75-138 2.11e-14

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: 73.02  E-value: 2.11e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242091189   75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSgNDPDVTNFCMFINEVYSVLSDPAQRAVYDE 138
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRN-KDKEAEEKFKEINEAYEVLSDPEKRAQYDQ 63
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 75-150 7.30e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 71.76  E-value: 7.30e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTNFCMFINEVYSVLSDPAQRAVYDEIhGYTATAINPF 150
Cdd:PRK14277   6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDKEAEQKFKEINEAYEILSDPQKRAQYDQF-GHAAFDPGGF 80
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
75-166 2.74e-13

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 70.23  E-value: 2.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDlSGNDPDVTNFCMFINEVYSVLSDPAQRAVYDEI-H---------GYTA 144
Cdd:NF037946   6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPD-RNKAPDAAEIFAEINEAYEVLSNPEKRANYDKYgHdgvdgeggfGFDA 84

                         90       100
                 ....*....|....*....|...
gi 242091189 145 TAI-NPFFDDSApKDHVFVDEFT 166
Cdd:NF037946  85 FDVfSSFFETIN-KSGAFLDDSV 106
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 152-215 1.55e-04

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 40.84  E-value: 1.55e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 242091189 152 DDSAPKDHVFVDEFTCIGCKNCANICP-GVFEIEEDFGRSRVysQSGSTELIQDA-------IDSCPVDCIH 215
Cdd:cd10549   27 PNGAIARGPEIDEDKCVFCGACVEVCPtGAIELTPEGKEYVP--KEKEAEIDEEKcigcglcVKVCPVDAIT 96
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 166-218 1.09e-03

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 38.28  E-value: 1.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 242091189 166 TCIGCKNCANICP-GVFEIEEDFGRSRVYsqSGSTELIQDAIDSCPVDCIHWTS 218
Cdd:PRK08348  43 KCVGCRMCVTVCPaGVFVYLPEIRKVALW--TGRCVFCGQCVDVCPTGALQMSD 94
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 158-299 1.10e-03

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 40.78  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242091189 158 DHVFVDEFTCIGCKNCANICP-GVFEIEEDFG-RSRVYSQSGSTEliQDAIDSCPVDCIHWTSAAQLslleNEMRRVERV 235
Cdd:PRK12809  78 DSVQLDEQKCIGCKRCAIACPfGVVEMVDTIAqKCDLCNQRSSGT--QACIEVCPTQALRLMDDKGL----QQIKVARQR 151

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242091189 236 NvglmlAGMGASVDvfrmaSARWEKRQAKVLGKVRTRMVKQENSDTRSSWSDIW-GSPPQDQSNE 299
Cdd:PRK12809 152 K-----TAAGKASS-----DAQPSRSAALLPVNSRKGADKISASERKTHFGEIYcGLDPQQATYE 206
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 147-178 7.75e-03

EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 37.53  E-value: 7.75e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 242091189 147 INPFFDDSAPKDHVF-VDEfTCIGCKNCANICP 178
Cdd:NF038196 167 VNPLFYKFKVKDKKFhVTD-KCIGCGICAKVCP 198
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 75-137 1.54e-23

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: 91.77  E-value: 1.54e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242091189   75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTNFCMFINEVYSVLSDPAQRAVYD 137
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 75-138 4.28e-21

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: 87.84  E-value: 4.28e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTNFCMFINEVYSVLSDPAQRAVYDE 138
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDR 64
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 75-129 6.58e-20

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: 81.82  E-value: 6.58e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTNFCMFINEVYSVLSD 129
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
Fer4_13 pfam13370
4Fe-4S single cluster domain of Ferredoxin I; Fer4_13 is a ferredoxin I from sulfate-reducing ...
 162-216 3.40e-18

4Fe-4S single cluster domain of Ferredoxin I; Fer4_13 is a ferredoxin I from sulfate-reducing bacteria. Chemical sequence analysis suggests that this characteriztic [4Fe-4S] cluster sulfur environment is widely distributed among ferredoxins.


Pssm-ID: 433153 [Multi-domain]  Cd Length: 58  Bit Score: 77.35  E-value: 3.40e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 242091189  162 VDEFTCIGCKNCANICPGVFEIEEDFGRSRVYSQSGSTELI---QDAIDSCPVDCIHW 216
Cdd:pfam13370   1 VDEDTCIDCGTCRELAPEVFKYDDDGGASFVHDQPVNEEEEdlaEEALDSCPVEAIGT 58
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
73-146 1.37e-15

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 71.29  E-value: 1.37e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242091189  73 ADDYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTN--FCMfINEVYSVLSDPAQRAVYDEIHGYTATA 146
Cdd:COG2214    4 LKDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALAEelFQR-LNEAYEVLSDPERRAEYDRELGQSGKG 78
DnaJ smart00271
DnaJ molecular chaperone homology domain;
75-130 1.50e-15

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 69.96  E-value: 1.50e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 242091189    75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPD-LSGNDPDVTNFCMFINEVYSVLSDP 130
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDkNPGDKEEAEEKFKEINEAYEVLSDP 58
Fer COG1141
Ferredoxin [Energy production and conversion];
159-216 1.71e-14

Ferredoxin [Energy production and conversion];


Pssm-ID: 440756 [Multi-domain]  Cd Length: 63  Bit Score: 67.21  E-value: 1.71e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242091189 159 HVFVDEFTCIGCKNCANICPGVFEIEEDfGRSRVYSQ---SGSTELIQDAIDSCPVDCIHW 216
Cdd:COG1141    2 KVTVDRDTCIGCGLCVALAPEVFELDDD-GKAVVLDEevpEELEEDVREAADACPVGAITV 61
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 75-138 2.11e-14

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: 73.02  E-value: 2.11e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242091189   75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSgNDPDVTNFCMFINEVYSVLSDPAQRAVYDE 138
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRN-KDKEAEEKFKEINEAYEVLSDPEKRAQYDQ 63
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 75-150 7.30e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 71.76  E-value: 7.30e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTNFCMFINEVYSVLSDPAQRAVYDEIhGYTATAINPF 150
Cdd:PRK14277   6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDKEAEQKFKEINEAYEILSDPQKRAQYDQF-GHAAFDPGGF 80
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 75-134 8.47e-14

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 65.41  E-value: 8.47e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTNFCMFINEVYSVLSDPAQRA 134
Cdd:COG5407    1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDPKAEERFKEINEAYELLSDAEKRA 60
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 75-153 9.62e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 71.36  E-value: 9.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLS-GNDPDVTNFCMFINEVYSVLSDPAQRAVYDEIhGY--------TAT 145
Cdd:PRK14282   5 DYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHpENRKEAEQKFKEIQEAYEVLSDPQKRAMYDRF-GYvgeqppyqETE 83


                 ....*...
gi 242091189 146 AINPFFDD 153
Cdd:PRK14282  84 SGGGFFED 91
PRK14279 PRK14279
molecular chaperone DnaJ;
70-138 2.16e-13

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 70.53  E-value: 2.16e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 242091189  70 EDVADDYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTNFCMFINEVYSVLSDPAQRAVYDE 138
Cdd:PRK14279   5 EWVEKDFYKELGVSSDASAEEIKKAYRKLARELHPDANPGDPAAEERFKAVSEAHDVLSDPAKRKEYDE 73
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
75-166 2.74e-13

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 70.23  E-value: 2.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDlSGNDPDVTNFCMFINEVYSVLSDPAQRAVYDEI-H---------GYTA 144
Cdd:NF037946   6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPD-RNKAPDAAEIFAEINEAYEVLSNPEKRANYDKYgHdgvdgeggfGFDA 84

                         90       100
                 ....*....|....*....|...
gi 242091189 145 TAI-NPFFDDSApKDHVFVDEFT 166
Cdd:NF037946  85 FDVfSSFFETIN-KSGAFLDDSV 106
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 75-138 2.85e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 69.80  E-value: 2.85e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNdPDVTNFCMFINEVYSVLSDPAQRAVYDE 138
Cdd:PRK14291   4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKN-PEAEEKFKEINEAYQVLSDPEKRKLYDQ 66
PRK14295 PRK14295
molecular chaperone DnaJ;
72-138 3.52e-13

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 69.88  E-value: 3.52e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 242091189  72 VADDYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTNFCMFINEVYSVLSDPAQRAVYDE 138
Cdd:PRK14295   7 IEKDYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDAKAEERFKEISEAYDVLSDEKKRKEYDE 73
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 75-137 1.03e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 68.25  E-value: 1.03e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTNfcMF--INEVYSVLSDPAQRAVYD 137
Cdd:PRK10767   5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKEAEE--KFkeIKEAYEVLSDPQKRAAYD 67
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 75-151 1.24e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 68.19  E-value: 1.24e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSgNDPDVTNFCMFINEVYSVLSDPAQRAVYDEihgYTATAINPFF 151
Cdd:PRK14276   5 EYYDRLGVSKDASQDEIKKAYRKLSKKYHPDIN-KEPGAEEKYKEVQEAYETLSDPQKRAAYDQ---YGAAGANGGF 77
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 75-156 1.45e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 67.27  E-value: 1.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSgNDPDVTNFCMFINEVYSVLSDPAQRAVYDEihgYTATAINPFFDDS 154
Cdd:PRK14299   5 DYYAILGVPKNASQDEIKKAFKKLARKYHPDVN-KSPGAEEKFKEINEAYTVLSDPEKRRIYDT---YGTTAASAGWQGP 80


                 ..
gi 242091189 155 AP 156
Cdd:PRK14299  81 PP 82
termin_org_DnaJ TIGR03835
terminal organelle assembly protein TopJ; This model describes TopJ (MG_200, CbpA), a DnaJ ...
 75-138 1.54e-12

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: 68.69  E-value: 1.54e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242091189   75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDlSGNDPDVTNFCMFINEVYSVLSDPAQRAVYDE 138
Cdd:TIGR03835   3 DYYEVLGIDRDADEQEIKKAFRKLAKKYHPD-RNKAPDAASIFAEINEANDVLSNPKKRANYDK 65
PRK14280 PRK14280
molecular chaperone DnaJ;
75-138 2.81e-12

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 67.05  E-value: 2.81e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSgNDPDVTNFCMFINEVYSVLSDPAQRAVYDE 138
Cdd:PRK14280   5 DYYEVLGVSKSASKDEIKKAYRKLSKKYHPDIN-KEEGADEKFKEISEAYEVLSDDQKRAQYDQ 67
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 75-137 9.58e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 65.26  E-value: 9.58e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSgNDPDVTNFCMFINEVYSVLSDPAQRAVYD 137
Cdd:PRK14298   6 DYYEILGLSKDASVEDIKKAYRKLAMKYHPDKN-KEPDAEEKFKEISEAYAVLSDAEKRAQYD 67
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 72-138 1.17e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 64.95  E-value: 1.17e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 242091189  72 VADDYYSVLGVMPDATPEEIKKAYYGCMKECHPDLS-GNDPDVTNFCMFINEVYSVLSDPAQRAVYDE 138
Cdd:PRK14290   1 MAKDYYKILGVDRNASQEDIKKAFRELAKKWHPDLHpGNKAEAEEKFKEISEAYEVLSDPQKRRQYDQ 68
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 75-137 1.55e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 64.86  E-value: 1.55e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTNFCMFINEVYSVLSDPAQRAVYD 137
Cdd:PRK14284   2 DYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDAEAEKRFKEVSEAYEVLSDAQKRESYD 64
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 75-161 2.42e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 63.99  E-value: 2.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTNFCMFINEVYSVLSDPAQRAVYDEIhGYTATAINPFFDDS 154
Cdd:PRK14301   5 DYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNPEAEQKFKEAAEAYEVLRDAEKRARYDRF-GHAGVNGNGGFGGF 83


                 ....*..
gi 242091189 155 APKDHVF 161
Cdd:PRK14301  84 SSAEDIF 90
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 73-137 4.06e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 63.53  E-value: 4.06e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242091189  73 ADDYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTNFcMFINEVYSVLSDPAQRAVYD 137
Cdd:PRK14278   2 ARDYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDEEAQEKF-KEISVAYEVLSDPEKRRIVD 65
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 75-138 2.15e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 61.32  E-value: 2.15e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTNFCMFINEVYSVLSDPAQRAVYDE 138
Cdd:PRK14294   5 DYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDKEAEELFKEAAEAYEVLSDPKKRGIYDQ 68
PRK14297 PRK14297
molecular chaperone DnaJ;
75-138 3.53e-10

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 60.57  E-value: 3.53e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTNFCMFINEVYSVLSDPAQRAVYDE 138
Cdd:PRK14297   5 DYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKEAEEKFKEINEAYQVLSDPQKKAQYDQ 68
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 75-138 4.56e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 60.22  E-value: 4.56e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSgNDPDVTNFCMFINEVYSVLSDPAQRAVYDE 138
Cdd:PRK14283   6 DYYEVLGVDRNADKKEIKKAYRKLARKYHPDVS-EEEGAEEKFKEISEAYAVLSDDEKRQRYDQ 68
PRK14293 PRK14293
molecular chaperone DnaJ;
73-137 4.66e-10

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 60.00  E-value: 4.66e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242091189  73 ADDYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSgNDPDVTNFCMFINEVYSVLSDPAQRAVYD 137
Cdd:PRK14293   2 AADYYEILGVSRDADKDELKRAYRRLARKYHPDVN-KEPGAEDRFKEINRAYEVLSDPETRARYD 65
PRK14289 PRK14289
molecular chaperone DnaJ;
75-138 6.86e-10

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 59.84  E-value: 6.86e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTNFCMFINEVYSVLSDPAQRAVYDE 138
Cdd:PRK14289   6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDKEAEEKFKEAAEAYDVLSDPDKRSRYDQ 69
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 75-138 1.05e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 59.05  E-value: 1.05e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTNFCMFINEVYSVLSDPAQRAVYDE 138
Cdd:PRK14281   4 DYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKEAEEHFKEVNEAYEVLSNDDKRRRYDQ 67
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 66-138 1.77e-09

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 58.68  E-value: 1.77e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242091189  66 HEREEDVADD-YYSVLGVMPDATPEEIKKAYYGCMKECHPDlSGNDPDvtnfcMF--INEVYSVLSDPAQRAVYDE 138
Cdd:PTZ00037  19 GRRKREVDNEkLYEVLNLSKDCTTSEIKKAYRKLAIKHHPD-KGGDPE-----KFkeISRAYEVLSDPEKRKIYDE 88
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 75-143 3.30e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 57.71  E-value: 3.30e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSgNDPDVTNFCMFINEVYSVLSDPAQRAVYDEIhGYT 143
Cdd:PRK14287   5 DYYEVLGVDRNASVDEVKKAYRKLARKYHPDVN-KAPDAEDKFKEVKEAYDTLSDPQKKAHYDQF-GHT 71
Fer4_15 pfam13459
4Fe-4S single cluster domain;
160-216 3.45e-09

4Fe-4S single cluster domain;


Pssm-ID: 404359 [Multi-domain]  Cd Length: 66  Bit Score: 52.36  E-value: 3.45e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 242091189  160 VFVDEFTCIGCKNCANICPGVFEIEEDfGRSRVYSQSGST----------ELIQDAIDSCPVDCIHW 216
Cdd:pfam13459   1 VEVDRDRCIGCGLCVALDPELFELDDD-GKASVLLDDGEIgegevpdddeEAAQEAARACPVDAIRV 66
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 75-155 4.45e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 57.26  E-value: 4.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSgNDPDVTNFCMFINEVYSVLSDPAQRAVYDEIhGYTAtainpfFDDS 154
Cdd:PRK14296   5 DYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLN-KSPDAHDKMVEINEAADVLLDKDKRKQYDQF-GHAA------FDGS 76


                 .
gi 242091189 155 A 155
Cdd:PRK14296  77 S 77
PRK10266 PRK10266
curved DNA-binding protein;
75-139 1.56e-08

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 55.21  E-value: 1.56e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSgNDPDVTNFCMFINEVYSVLSDPAQRAVYDEI 139
Cdd:PRK10266   5 DYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVS-KEPDAEARFKEVAEAWEVLSDEQRRAEYDQL 68
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
73-130 2.06e-08

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 50.57  E-value: 2.06e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 242091189  73 ADDYYSVLGVMPDATPEEIKKAYYGCMKECHPD-LSGNDPDvtnfcMF----------INEVYSVLSDP 130
Cdd:COG1076    3 LDDAFELLGLPPDADDAELKRAYRKLQREHHPDrLAAGLPE-----EEqrlalqkaaaINEAYETLKDP 66
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 72-137 3.14e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 54.64  E-value: 3.14e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242091189  72 VADDYYSVLGVMPDATPEEIKKAYYGCMKECHPDlSGNDPDVTNFCMFINEVYSVLSDPAQRAVYD 137
Cdd:PRK14300   1 MSQDYYQILGVSKTASQADLKKAYLKLAKQYHPD-TTDAKDAEKKFKEINAAYDVLKDEQKRAAYD 65
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 75-137 3.77e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 54.51  E-value: 3.77e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTNFCMfINEVYSVLSDPAQRAVYD 137
Cdd:PRK14292   3 DYYELLGVSRTASADEIKSAYRKLALKYHPDRNKEKGAAEKFAQ-INEAYAVLSDAEKRAHYD 64
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 75-144 1.08e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 53.07  E-value: 1.08e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242091189  75 DYYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTNFCMFINEVYSVLSDPAQRAVYDEIhGYTA 144
Cdd:PRK14285   4 DYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKEAESIFKEATEAYEVLIDDNKRAQYDRF-GHTA 72
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 76-165 2.52e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 51.91  E-value: 2.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242091189  76 YYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTNFCMFINEVYSVLSDPAQRAVYDEI---------HGYTATA 146
Cdd:PRK14286   6 YYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYDQFgkagvnagaGGFGQGA 85

                         90
                 ....*....|....*....
gi 242091189 147 INPFFDDSAPKDHVFVDEF 165
Cdd:PRK14286  86 YTDFSDIFGDFGDIFGDFF 104
PRK14288 PRK14288
molecular chaperone DnaJ;
76-153 1.94e-06

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 48.92  E-value: 1.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242091189  76 YYSVLGVMPDATPEEIKKAYYGCMKECHPDLSGNDPDVTNFCMFINEVYSVLSDPAQRAVYDEI-------HGYTATAIN 148
Cdd:PRK14288   5 YYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKEAEEKFKLINEAYGVLSDEKKRALYDRYgkkglnqAGASQSDFS 84


                 ....*
gi 242091189 149 PFFDD 153
Cdd:PRK14288  85 DFFED 89
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 159-214 5.21e-06

NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 43.54  E-value: 5.21e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 242091189 159 HVFVDEFTCIGCKNCANICP-GVFEIEEDFGRSRVYSQSGSTELiQDAIDSCPVDCI 214
Cdd:COG1146    2 MPVIDTDKCIGCGACVEVCPvDVLELDEEGKKALVINPEECIGC-GACELVCPVGAI 57
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 75-164 9.37e-06

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 46.95  E-value: 9.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242091189  75 DYYSVLGVMP---DATPEEIKKAYYGCMKECHPDL--SGNDPDVTNFCMFINEVYSVLSDPAQRAVYDEIhgytatainp 149
Cdd:COG5269   44 DLYALLGLSKyrtKAIPPQILKAHKKKVYKYHPDKtaAGGNKGCDEFFKLIQKAREVLGDRKLRLQYDSN---------- 113

                         90
                 ....*....|....*
gi 242091189 150 FFDDSAPKDHVFVDE 164
Cdd:COG5269  114 DFDADVPPPRIYTPD 128
djlA PRK09430
co-chaperone DjlA;
74-105 1.20e-04

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 42.88  E-value: 1.20e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 242091189  74 DDYYSVLGVMPDATPEEIKKAYYGCMKECHPD 105
Cdd:PRK09430 200 EDAYKVLGVSESDDDQEIKRAYRKLMSEHHPD 231
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 152-215 1.55e-04

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 40.84  E-value: 1.55e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 242091189 152 DDSAPKDHVFVDEFTCIGCKNCANICP-GVFEIEEDFGRSRVysQSGSTELIQDA-------IDSCPVDCIH 215
Cdd:cd10549   27 PNGAIARGPEIDEDKCVFCGACVEVCPtGAIELTPEGKEYVP--KEKEAEIDEEKcigcglcVKVCPVDAIT 96
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
158-193 4.54e-04

Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 40.03  E-value: 4.54e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 242091189 158 DHVFVDEFTCIGCKNCANICP-GVFEIEEDFGRSRVY 193
Cdd:COG1142   74 GAVVVDEEKCIGCGLCVLACPfGAITMVGEKSRAVAV 110
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 166-218 1.09e-03

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 38.28  E-value: 1.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 242091189 166 TCIGCKNCANICP-GVFEIEEDFGRSRVYsqSGSTELIQDAIDSCPVDCIHWTS 218
Cdd:PRK08348  43 KCVGCRMCVTVCPaGVFVYLPEIRKVALW--TGRCVFCGQCVDVCPTGALQMSD 94
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 158-299 1.10e-03

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 40.78  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242091189 158 DHVFVDEFTCIGCKNCANICP-GVFEIEEDFG-RSRVYSQSGSTEliQDAIDSCPVDCIHWTSAAQLslleNEMRRVERV 235
Cdd:PRK12809  78 DSVQLDEQKCIGCKRCAIACPfGVVEMVDTIAqKCDLCNQRSSGT--QACIEVCPTQALRLMDDKGL----QQIKVARQR 151

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242091189 236 NvglmlAGMGASVDvfrmaSARWEKRQAKVLGKVRTRMVKQENSDTRSSWSDIW-GSPPQDQSNE 299
Cdd:PRK12809 152 K-----TAAGKASS-----DAQPSRSAALLPVNSRKGADKISASERKTHFGEIYcGLDPQQATYE 206
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 155-191 1.92e-03

beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family contains beta FeS subunits of several dehydrogenases in the DMSO reductase superfamily, including formate dehydrogenase N (FDH-N), tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N is a major component of nitrate respiration of Escherichia coli; it catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate to a cytochrome. W-FDH contains a tungsten instead of molybdenum at the catalytic center and seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate.


Pssm-ID: 319888 [Multi-domain]  Cd Length: 156  Bit Score: 38.15  E-value: 1.92e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 242091189 155 APKDHVFVDEFTCIGCKNCANICP-GVFEIEEDFGRSR 191
Cdd:cd16366   90 TETGTVVVDPETCIGCGYCVNACPfDIPRFDEETGRVA 127
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 157-178 2.88e-03

HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 37.62  E-value: 2.88e-03
                         10        20
                 ....*....|....*....|..
gi 242091189 157 KDHVFVDEFTCIGCKNCANICP 178
Cdd:cd10554   77 DGVVQVDEERCIGCKLCVLACP 98
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 167-217 3.96e-03

Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 35.49  E-value: 3.96e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 242091189 167 CIGCKNCANICP-GVFEIEEDFGRSRVysqsgstELIQDA-------IDSCPVDCIHWT 217
Cdd:COG1143    4 CIGCGLCVRVCPvDAITIEDGEPGKVY-------VIDPDKcigcglcVEVCPTGAISMT 55
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 157-178 5.09e-03

TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 35.40  E-value: 5.09e-03
                         10        20
                 ....*....|....*....|..
gi 242091189 157 KDHVFVDEFTCIGCKNCANICP 178
Cdd:COG4231   43 DGKAVIDPDLCIGCGSCVQVCP 64
PRK06273 PRK06273
ferredoxin; Provisional
 162-178 5.31e-03

ferredoxin; Provisional


Pssm-ID: 235764 [Multi-domain]  Cd Length: 165  Bit Score: 37.00  E-value: 5.31e-03
                         10
                 ....*....|....*..
gi 242091189 162 VDEFTCIGCKNCANICP 178
Cdd:PRK06273  46 VFEELCIGCGGCANVCP 62
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 159-186 7.62e-03

TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 35.02  E-value: 7.62e-03
                         10        20
                 ....*....|....*....|....*....
gi 242091189 159 HVFVDEFTCIGCKNCANICP-GVFEIEED 186
Cdd:COG4231   16 RYVIDEDKCTGCGACVKVCPaDAIEEGDG 44
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 147-178 7.75e-03

EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 37.53  E-value: 7.75e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 242091189 147 INPFFDDSAPKDHVF-VDEfTCIGCKNCANICP 178
Cdd:NF038196 167 VNPLFYKFKVKDKKFhVTD-KCIGCGICAKVCP 198
 
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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