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Conserved domains on  [gi|6226230|sp|Q9ZCB7|]
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RecName: Full=Trigger factor; Short=TF; AltName: Full=PPIase

Protein Classification

trigger factor( domain architecture ID 11425490)

trigger factor functions as a peptidylprolyl isomerase that is involved in protein export and acts as a chaperone by maintaining the newly synthesized protein in an open conformation

EC:  5.2.1.8
Gene Ontology:  GO:0003755

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
1-436 2.22e-134

FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 223618 [Multi-domain]  Cd Length: 441  Bit Score: 393.57  E-value: 2.22e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230    1 MGIIVLKNEGLNFHARISTPLSEIDDDIQKELLDLTKKVKVAGFRAGKVPVSIVKKKYGTSVRHDIIEKRINNLVNHIIK 80
Cdd:COG0544   1 MKVTVEKLEGLEVRLTVEVPAEEIKKALDKALKKLAKKVKIPGFRKGKVPRKVIEQRYGEAVRQDVLNELLPEAFEEAIK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230   81 EYNLNIIGRPKIEELQNEPDKDLEFTVKIELLPKITIPDLKKISLDRPKLAVNSQDVEIQLEKLAALTKCYTkESKTKIK 160
Cdd:COG0544  81 EEGLKPAGQPEIEITEFEKGEDFEFTAEVEVYPEVELGDYKGIEVEKPVVEVTDEDVDEELEKLRKRFATLE-PVEGAAE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230  161 DGDQVTIDAIGYIKDRAFDGGKLNDFKVVIGSNTLIQGFEQQLIGSKTGNEVDVNVTFPENYHDKNLSGKDAHFVVQIKA 240
Cdd:COG0544 160 NGDRVTIDFEGSVDGEEFEGGKAENFSLELGSGRFIPGFEDQLVGMKAGEEKDIKVTFPEDYHAEELAGKEATFKVKVKE 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230  241 VHTAEPTIIDEEFAKKFQSN-SLEELRTHFAKQIENESEEAINTIMKMNLFDKLEKLLDFDVPESLLEQE-KNILKSETD 318
Cdd:COG0544 240 VKKRELPELDDEFAKKLGEEdTLEELKEKLRKNLERELKEATLEKRKEQLLDALVEANDFDLPESLVEAEiDNLLKQALQ 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230  319 KNKHDGSLLN---GKSSKEITEYYNKLALRRVRIGLLLAEYAKFKNLQLEPDDFKKIIMQQARNFPG-QENMIFDFYKNN 394
Cdd:COG0544 320 QLQQQGIDSLeasGESEEELREEFKEEAEKRVKLGLLLEEIAKEEKLEVTEEEIKAEIEELARQYGGeQPEEVIKLYYNN 399
                       410       420       430       440
                ....*....|....*....|....*....|....*....|..
gi 6226230  395 PRAIEGLKGPALEDKTVQYIFNNEIQLKEKRYTKEELEKYLE 436
Cdd:COG0544 400 QELLDALKADILEEKAVDLLLANKKKVTEKEVSFEELMNEAE 441
 
Name Accession Description Interval E-value
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
1-436 2.22e-134

FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 223618 [Multi-domain]  Cd Length: 441  Bit Score: 393.57  E-value: 2.22e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230    1 MGIIVLKNEGLNFHARISTPLSEIDDDIQKELLDLTKKVKVAGFRAGKVPVSIVKKKYGTSVRHDIIEKRINNLVNHIIK 80
Cdd:COG0544   1 MKVTVEKLEGLEVRLTVEVPAEEIKKALDKALKKLAKKVKIPGFRKGKVPRKVIEQRYGEAVRQDVLNELLPEAFEEAIK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230   81 EYNLNIIGRPKIEELQNEPDKDLEFTVKIELLPKITIPDLKKISLDRPKLAVNSQDVEIQLEKLAALTKCYTkESKTKIK 160
Cdd:COG0544  81 EEGLKPAGQPEIEITEFEKGEDFEFTAEVEVYPEVELGDYKGIEVEKPVVEVTDEDVDEELEKLRKRFATLE-PVEGAAE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230  161 DGDQVTIDAIGYIKDRAFDGGKLNDFKVVIGSNTLIQGFEQQLIGSKTGNEVDVNVTFPENYHDKNLSGKDAHFVVQIKA 240
Cdd:COG0544 160 NGDRVTIDFEGSVDGEEFEGGKAENFSLELGSGRFIPGFEDQLVGMKAGEEKDIKVTFPEDYHAEELAGKEATFKVKVKE 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230  241 VHTAEPTIIDEEFAKKFQSN-SLEELRTHFAKQIENESEEAINTIMKMNLFDKLEKLLDFDVPESLLEQE-KNILKSETD 318
Cdd:COG0544 240 VKKRELPELDDEFAKKLGEEdTLEELKEKLRKNLERELKEATLEKRKEQLLDALVEANDFDLPESLVEAEiDNLLKQALQ 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230  319 KNKHDGSLLN---GKSSKEITEYYNKLALRRVRIGLLLAEYAKFKNLQLEPDDFKKIIMQQARNFPG-QENMIFDFYKNN 394
Cdd:COG0544 320 QLQQQGIDSLeasGESEEELREEFKEEAEKRVKLGLLLEEIAKEEKLEVTEEEIKAEIEELARQYGGeQPEEVIKLYYNN 399
                       410       420       430       440
                ....*....|....*....|....*....|....*....|..
gi 6226230  395 PRAIEGLKGPALEDKTVQYIFNNEIQLKEKRYTKEELEKYLE 436
Cdd:COG0544 400 QELLDALKADILEEKAVDLLLANKKKVTEKEVSFEELMNEAE 441
tig TIGR00115
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first ...
17-415 1.05e-116

trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first chaperone to interact with nascent polypeptide. Trigger factor can bind at the same time as the signal recognition particle (SRP), but is excluded by the SRP receptor (FtsY). The central domain of trigger factor has peptidyl-prolyl cis/trans isomerase activity. This protein is found in a single copy in virtually every bacterial genome. [Protein fate, Protein folding and stabilization]


Pssm-ID: 272913 [Multi-domain]  Cd Length: 410  Bit Score: 347.62  E-value: 1.05e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230     17 ISTPLSEIDDDIQKELLDLTKKVKVAGFRAGKVPVSIVKKKYGTSVRHDIIEKRINNLVNHIIKEYNLNIIGRPKIEELQ 96
Cdd:TIGR00115   7 VEVPAEEVEEEVDKALKELAKTVKIPGFRKGKVPRSVVEKRYGESVLQEALNELLQEAFSEAVKEEKIRPLGQPEIEVKE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230     97 NEPDKDLEFTVKIELLPKITIPDLKKISLDRPKLAVNSQDVEIQLEKLAALTKCYTKESKTKIKDGDQVTIDAIGYIKDR 176
Cdd:TIGR00115  87 LEDGKDLEFTAEFEVYPEVELGDYKGIEVEKPEVEVTDEDVDEELERLREQNATLVPVERGAAEKGDRVTIDFEGFIDGE 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230    177 AFDGGKLNDFKVVIGSNTLIQGFEQQLIGSKTGNEVDVNVTFPENYHDKNLSGKDAHFVVQIKAVHTAEPTIIDEEFAKK 256
Cdd:TIGR00115 167 AFEGGKAENFSLELGSGQFIPGFEEQLVGMKAGEEKEIKVTFPEDYHAEELAGKEATFKVTVKEVKEKELPELDDEFAKS 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230    257 F--QSNSLEELRTHFAKQIENESEEAINTIMKMNLFDKLEKLLDFDVPESLLEQEKNILKSETDKN----KHDGSLLNGK 330
Cdd:TIGR00115 247 LgeEFETLEELKADIRKNLEEEKKERAKAKLKEQLLDKLVENNEFELPESLVEQEIDRLLEQAEQQlqqqGIDLEEYLKI 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230    331 SSKEITEYYNKLALRRVRIGLLLAEYAKFKNLQLEPDDFKKIIMQQARNFPGQENMIFDFYKnNPRAIEGLKGPALEDKT 410
Cdd:TIGR00115 327 TEEELREEFREEAERRVKLGLILEEIAKKEKIEVSEEEVEAEIEELAQQYGEDPEEVKKYYK-KPGLLEQLRNDLLEEKV 405

                  ....*
gi 6226230    411 VQYIF 415
Cdd:TIGR00115 406 LDFLL 410
Trigger_N pfam05697
Bacterial trigger factor protein (TF); In the E. coli cytosol, a fraction of the newly ...
1-144 3.49e-33

Bacterial trigger factor protein (TF); In the E. coli cytosol, a fraction of the newly synthesized proteins requires the activity of molecular chaperones for folding to the native state. The major chaperones implicated in this folding process are the ribosome-associated Trigger Factor (TF), and the DnaK and GroEL chaperones with their respective co-chaperones. Trigger Factor is an ATP-independent chaperone and displays chaperone and peptidyl-prolyl-cis-trans-isomerase (PPIase) activities in vitro. It is composed of at least three domains, an N-terminal domain which mediates association with the large ribosomal subunit, a central substrate binding and PPIase domain with homology to FKBP proteins, and a C-terminal domain of unknown function. The positioning of TF at the peptide exit channel, together with its ability to interact with nascent chains as short as 57 residues renders TF a prime candidate for being the first chaperone that binds to the nascent polypeptide chains. This family represents the N-terminal region of the protein.


Pssm-ID: 428591 [Multi-domain]  Cd Length: 144  Bit Score: 121.81  E-value: 3.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230      1 MGIIVLKNEGLNFHARISTPLSEIDDDIQKELLDLTKKVKVAGFRAGKVPVSIVKKKYGTSVRHDIIEKRINNLVNHIIK 80
Cdd:pfam05697   1 MKVTVEKLEGLKVKLTVEVPAEEVEKAVDKALKKLAKKVNIPGFRKGKVPRSVIEKRYGKEVYEEALNELLPEAYEEAIE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6226230     81 EYNLNIIGRPKIEELQNEPDKDLEFTVKIELLPKITIPDLKKISLDRPKLAVNSQDVEIQLEKL 144
Cdd:pfam05697  81 EEKLEPVGQPEIEVVEIEKGKDLEFTAEVEVKPEVELGDYKGLEVEKPEVEVTDEDVDEELERL 144
 
Name Accession Description Interval E-value
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
1-436 2.22e-134

FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 223618 [Multi-domain]  Cd Length: 441  Bit Score: 393.57  E-value: 2.22e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230    1 MGIIVLKNEGLNFHARISTPLSEIDDDIQKELLDLTKKVKVAGFRAGKVPVSIVKKKYGTSVRHDIIEKRINNLVNHIIK 80
Cdd:COG0544   1 MKVTVEKLEGLEVRLTVEVPAEEIKKALDKALKKLAKKVKIPGFRKGKVPRKVIEQRYGEAVRQDVLNELLPEAFEEAIK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230   81 EYNLNIIGRPKIEELQNEPDKDLEFTVKIELLPKITIPDLKKISLDRPKLAVNSQDVEIQLEKLAALTKCYTkESKTKIK 160
Cdd:COG0544  81 EEGLKPAGQPEIEITEFEKGEDFEFTAEVEVYPEVELGDYKGIEVEKPVVEVTDEDVDEELEKLRKRFATLE-PVEGAAE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230  161 DGDQVTIDAIGYIKDRAFDGGKLNDFKVVIGSNTLIQGFEQQLIGSKTGNEVDVNVTFPENYHDKNLSGKDAHFVVQIKA 240
Cdd:COG0544 160 NGDRVTIDFEGSVDGEEFEGGKAENFSLELGSGRFIPGFEDQLVGMKAGEEKDIKVTFPEDYHAEELAGKEATFKVKVKE 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230  241 VHTAEPTIIDEEFAKKFQSN-SLEELRTHFAKQIENESEEAINTIMKMNLFDKLEKLLDFDVPESLLEQE-KNILKSETD 318
Cdd:COG0544 240 VKKRELPELDDEFAKKLGEEdTLEELKEKLRKNLERELKEATLEKRKEQLLDALVEANDFDLPESLVEAEiDNLLKQALQ 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230  319 KNKHDGSLLN---GKSSKEITEYYNKLALRRVRIGLLLAEYAKFKNLQLEPDDFKKIIMQQARNFPG-QENMIFDFYKNN 394
Cdd:COG0544 320 QLQQQGIDSLeasGESEEELREEFKEEAEKRVKLGLLLEEIAKEEKLEVTEEEIKAEIEELARQYGGeQPEEVIKLYYNN 399
                       410       420       430       440
                ....*....|....*....|....*....|....*....|..
gi 6226230  395 PRAIEGLKGPALEDKTVQYIFNNEIQLKEKRYTKEELEKYLE 436
Cdd:COG0544 400 QELLDALKADILEEKAVDLLLANKKKVTEKEVSFEELMNEAE 441
tig TIGR00115
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first ...
17-415 1.05e-116

trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first chaperone to interact with nascent polypeptide. Trigger factor can bind at the same time as the signal recognition particle (SRP), but is excluded by the SRP receptor (FtsY). The central domain of trigger factor has peptidyl-prolyl cis/trans isomerase activity. This protein is found in a single copy in virtually every bacterial genome. [Protein fate, Protein folding and stabilization]


Pssm-ID: 272913 [Multi-domain]  Cd Length: 410  Bit Score: 347.62  E-value: 1.05e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230     17 ISTPLSEIDDDIQKELLDLTKKVKVAGFRAGKVPVSIVKKKYGTSVRHDIIEKRINNLVNHIIKEYNLNIIGRPKIEELQ 96
Cdd:TIGR00115   7 VEVPAEEVEEEVDKALKELAKTVKIPGFRKGKVPRSVVEKRYGESVLQEALNELLQEAFSEAVKEEKIRPLGQPEIEVKE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230     97 NEPDKDLEFTVKIELLPKITIPDLKKISLDRPKLAVNSQDVEIQLEKLAALTKCYTKESKTKIKDGDQVTIDAIGYIKDR 176
Cdd:TIGR00115  87 LEDGKDLEFTAEFEVYPEVELGDYKGIEVEKPEVEVTDEDVDEELERLREQNATLVPVERGAAEKGDRVTIDFEGFIDGE 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230    177 AFDGGKLNDFKVVIGSNTLIQGFEQQLIGSKTGNEVDVNVTFPENYHDKNLSGKDAHFVVQIKAVHTAEPTIIDEEFAKK 256
Cdd:TIGR00115 167 AFEGGKAENFSLELGSGQFIPGFEEQLVGMKAGEEKEIKVTFPEDYHAEELAGKEATFKVTVKEVKEKELPELDDEFAKS 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230    257 F--QSNSLEELRTHFAKQIENESEEAINTIMKMNLFDKLEKLLDFDVPESLLEQEKNILKSETDKN----KHDGSLLNGK 330
Cdd:TIGR00115 247 LgeEFETLEELKADIRKNLEEEKKERAKAKLKEQLLDKLVENNEFELPESLVEQEIDRLLEQAEQQlqqqGIDLEEYLKI 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230    331 SSKEITEYYNKLALRRVRIGLLLAEYAKFKNLQLEPDDFKKIIMQQARNFPGQENMIFDFYKnNPRAIEGLKGPALEDKT 410
Cdd:TIGR00115 327 TEEELREEFREEAERRVKLGLILEEIAKKEKIEVSEEEVEAEIEELAQQYGEDPEEVKKYYK-KPGLLEQLRNDLLEEKV 405

                  ....*
gi 6226230    411 VQYIF 415
Cdd:TIGR00115 406 LDFLL 410
Trigger_N pfam05697
Bacterial trigger factor protein (TF); In the E. coli cytosol, a fraction of the newly ...
1-144 3.49e-33

Bacterial trigger factor protein (TF); In the E. coli cytosol, a fraction of the newly synthesized proteins requires the activity of molecular chaperones for folding to the native state. The major chaperones implicated in this folding process are the ribosome-associated Trigger Factor (TF), and the DnaK and GroEL chaperones with their respective co-chaperones. Trigger Factor is an ATP-independent chaperone and displays chaperone and peptidyl-prolyl-cis-trans-isomerase (PPIase) activities in vitro. It is composed of at least three domains, an N-terminal domain which mediates association with the large ribosomal subunit, a central substrate binding and PPIase domain with homology to FKBP proteins, and a C-terminal domain of unknown function. The positioning of TF at the peptide exit channel, together with its ability to interact with nascent chains as short as 57 residues renders TF a prime candidate for being the first chaperone that binds to the nascent polypeptide chains. This family represents the N-terminal region of the protein.


Pssm-ID: 428591 [Multi-domain]  Cd Length: 144  Bit Score: 121.81  E-value: 3.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230      1 MGIIVLKNEGLNFHARISTPLSEIDDDIQKELLDLTKKVKVAGFRAGKVPVSIVKKKYGTSVRHDIIEKRINNLVNHIIK 80
Cdd:pfam05697   1 MKVTVEKLEGLKVKLTVEVPAEEVEKAVDKALKKLAKKVNIPGFRKGKVPRSVIEKRYGKEVYEEALNELLPEAYEEAIE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6226230     81 EYNLNIIGRPKIEELQNEPDKDLEFTVKIELLPKITIPDLKKISLDRPKLAVNSQDVEIQLEKL 144
Cdd:pfam05697  81 EEKLEPVGQPEIEVVEIEKGKDLEFTAEVEVKPEVELGDYKGLEVEKPEVEVTDEDVDEELERL 144
Trigger_C pfam05698
Bacterial trigger factor protein (TF) C-terminus; In the E. coli cytosol, a fraction of the ...
261-415 2.00e-21

Bacterial trigger factor protein (TF) C-terminus; In the E. coli cytosol, a fraction of the newly synthesized proteins requires the activity of molecular chaperones for folding to the native state. The major chaperones implicated in this folding process are the ribosome-associated Trigger Factor (TF), and the DnaK and GroEL chaperones with their respective co-chaperones. Trigger Factor is an ATP-independent chaperone and displays chaperone and peptidyl-prolyl-cis-trans-isomerase (PPIase) activities in vitro. It is composed of at least three domains, an N-terminal domain which mediates association with the large ribosomal subunit, a central substrate binding and PPIase domain with homology to FKBP proteins, and a C-terminal domain of unknown function. The positioning of TF at the peptide exit channel, together with its ability to interact with nascent chains as short as 57 residues renders TF a prime candidate for being the first chaperone that binds to the nascent polypeptide chains. This family represents the C-terminal region of the protein.


Pssm-ID: 428592 [Multi-domain]  Cd Length: 162  Bit Score: 90.38  E-value: 2.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230    261 SLEELRTHFAKQIENESEEAINTIMKMNLFDKLEKLLDFDVPESLLEQEKNILKSETDKN-KHDGSLLN------GKSSK 333
Cdd:pfam05698   1 TLEELKADLRKNLEEEKKEATKEELKEAILDKLVENAEIDIPESLVEEEIDRLLRQALQQlQQQGLDLEeylqlsGSSEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230    334 EITEYYNKLALRRVRIGLLLAEYAKFKNLQLEPDDFKKIIMQQARNFPGQENMIFDFYKNNPRaIEGLKGPALEDKTVQY 413
Cdd:pfam05698  81 EFREEFKEEAEKRVKLGLVLEEIAKEEKIEVTEEELKEELEELASQYGMEPEEVKEFYRKNGQ-LSALKEDILEEKVVDL 159

                  ..
gi 6226230    414 IF 415
Cdd:pfam05698 160 LL 161
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
156-239 2.56e-15

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 425560  Cd Length: 94  Bit Score: 71.07  E-value: 2.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226230    156 KTKIKDGDQVTIDAIGYIKD-RAFDGGKLN--DFKVVIGSNTLIQGFEQQLIGSKTGNEVDVNVTFPENYHDKNLSG--- 229
Cdd:pfam00254   2 PEKAKKGDRVTVHYTGTLEDgTVFDSSYDRgkPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpvi 81
                          90
                  ....*....|...
gi 6226230    230 ---KDAHFVVQIK 239
Cdd:pfam00254  82 ppnATLVFEVELL 94
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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