NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1519738687|gb|RPH07303|]
View 

FKBP-type peptidyl-prolyl cis-trans isomerase [bacterium TMED46]

Protein Classification

FKBP-type peptidyl-prolyl cis-trans isomerase( domain architecture ID 11425492)

FKBP-type peptidyl-prolyl cis-trans isomerase acts as a PPIase that accelerates the folding of proteins

CATH:  3.10.50.40
EC:  5.2.1.8
Gene Ontology:  GO:0003755
SCOP:  4001062

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
131-231 2.98e-55

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


:

Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 171.90  E-value: 2.98e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519738687 131 LQYRVLTEGNGESPKKTDRVKVHYVGKLMDGSEFDSSIERGEPTEFALN--QVIKGWTEGLQLMKVGSKYEFFIHPNIAY 208
Cdd:COG0545     1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80
                          90       100
                  ....*....|....*....|....
gi 1519738687 209 GQR-ARPKIPANSVLIFEVELLDI 231
Cdd:COG0545    81 GERgAGGVIPPNSTLVFEVELLDV 104
PRK10902 super family cl29493
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
23-231 1.44e-50

FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional


The actual alignment was detected with superfamily member PRK10902:

Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 165.71  E-value: 1.44e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519738687  23 PKSKSKSVSTLSTFMDSTSYSLGADLG---EN-LKRQQ---VEIDYDVFMAGLMDGMETEMvKLDQGQRRAVMASLQKNI 95
Cdd:PRK10902   31 PAATADSKAAFKNDDQQSAYALGASLGrymENsLKEQEklgIKLDKDQLIAGVQDAFADKS-KLSDQEIEQTLQAFEARV 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519738687  96 RD----KSKKEGEANLKLADEFLDNNVKENpDIKETPTGLQYRVLTEGNGESPKKTDRVKVHYVGKLMDGSEFDSSIERG 171
Cdd:PRK10902  110 KSaaqaKMEKDAADNEAKGKKYREKFAKEK-GVKTTSTGLLYKVEKEGTGEAPKDSDTVVVNYKGTLIDGKEFDNSYTRG 188
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519738687 172 EPTEFALNQVIKGWTEGLQLMKVGSKYEFFIHPNIAYGQRARPKIPANSVLIFEVELLDI 231
Cdd:PRK10902  189 EPLSFRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPANSTLVFDVELLDV 248
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
131-231 2.98e-55

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 171.90  E-value: 2.98e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519738687 131 LQYRVLTEGNGESPKKTDRVKVHYVGKLMDGSEFDSSIERGEPTEFALN--QVIKGWTEGLQLMKVGSKYEFFIHPNIAY 208
Cdd:COG0545     1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80
                          90       100
                  ....*....|....*....|....
gi 1519738687 209 GQR-ARPKIPANSVLIFEVELLDI 231
Cdd:COG0545    81 GERgAGGVIPPNSTLVFEVELLDV 104
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
41-232 1.97e-52

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 168.44  E-value: 1.97e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519738687  41 SYSLGADLGENLKRQQVE-IDYDVFMAGLMDGME--TEMVKLDQGQR--RAVMASLQKNIRDKSKKEGEANLKladeFLD 115
Cdd:PRK11570   14 SYGIGLQVGQQLSESGLEgLLPEALVAGLADALEgkHPAVPVDVVHRalREIHERADAVRRERQQAMAAEGVK----FLE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519738687 116 NNVKENpDIKETPTGLQYRVLTEGNGESPKKTDRVKVHYVGKLMDGSEFDSSIERGEPTEFALNQVIKGWTEGLQLMKVG 195
Cdd:PRK11570   90 ENAKKE-GVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIEALTLMPVG 168
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1519738687 196 SKYEFFIHPNIAYGQR-ARPKIPANSVLIFEVELLDII 232
Cdd:PRK11570  169 SKWELTIPHELAYGERgAGASIPPFSTLVFEVELLEIL 206
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
23-231 1.44e-50

FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 165.71  E-value: 1.44e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519738687  23 PKSKSKSVSTLSTFMDSTSYSLGADLG---EN-LKRQQ---VEIDYDVFMAGLMDGMETEMvKLDQGQRRAVMASLQKNI 95
Cdd:PRK10902   31 PAATADSKAAFKNDDQQSAYALGASLGrymENsLKEQEklgIKLDKDQLIAGVQDAFADKS-KLSDQEIEQTLQAFEARV 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519738687  96 RD----KSKKEGEANLKLADEFLDNNVKENpDIKETPTGLQYRVLTEGNGESPKKTDRVKVHYVGKLMDGSEFDSSIERG 171
Cdd:PRK10902  110 KSaaqaKMEKDAADNEAKGKKYREKFAKEK-GVKTTSTGLLYKVEKEGTGEAPKDSDTVVVNYKGTLIDGKEFDNSYTRG 188
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519738687 172 EPTEFALNQVIKGWTEGLQLMKVGSKYEFFIHPNIAYGQRARPKIPANSVLIFEVELLDI 231
Cdd:PRK10902  189 EPLSFRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPANSTLVFDVELLDV 248
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
142-229 1.17e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 126.93  E-value: 1.17e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519738687 142 ESPKKTDRVKVHYVGKLMDGSEFDSSIERGEPTEFAL--NQVIKGWTEGLQLMKVGSKYEFFIHPNIAYGQR--ARPKIP 217
Cdd:pfam00254   3 EKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLgsGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEglAGPVIP 82
                          90
                  ....*....|..
gi 1519738687 218 ANSVLIFEVELL 229
Cdd:pfam00254  83 PNATLVFEVELL 94
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
37-135 1.94e-24

Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the amino terminus of pfam00254. This entry represents the N-terminal domain found in FKBP-type peptidylprolyl isomerases (PPIase). The N-terminal domain forms the dimer interface by the mutual exchange of two beta-strands between monomers.


Pssm-ID: 460169  Cd Length: 97  Bit Score: 92.95  E-value: 1.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519738687  37 MDSTSYSLGADLGENLKRQQVEIDYDVFMAGLMDGMETEMVKLDQgQRRAVMASLQKNIRDKSKKEGEANLKLADEFLDN 116
Cdd:pfam01346   1 KDKVSYAIGLQIGQQLKQQGIELDLDAFLAGLKDALAGKPLLTDE-EAQEALQAFQEKLQAKQEEQAEKNKAEGEAFLAE 79
                          90
                  ....*....|....*....
gi 1519738687 117 NvKENPDIKETPTGLQYRV 135
Cdd:pfam01346  80 N-KKKEGVKTTESGLQYKV 97
ppisom_GldI TIGR03516
peptidyl-prolyl isomerase, gliding motility-associated; Members of this protein family are ...
99-231 1.44e-06

peptidyl-prolyl isomerase, gliding motility-associated; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldI is a FKBP-type peptidyl-prolyl cis-trans isomerase (pfam00254) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockout of this gene abolishes the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. This family is only found in Bacteroidetes containing the suite of genes proposed to confer the gliding motility phenotype.


Pssm-ID: 132555  Cd Length: 177  Bit Score: 47.06  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519738687  99 SKKEGEANLKL--ADE-FLDNNVKENPDIK-ETPT-GLQYRVLTEGNGE--SPKKTDRVKVHYVGKLMDGSEFDSSIERG 171
Cdd:TIGR03516  34 IKLSAERNKKLiaAEEaAIKRIISADSIVKyETSQnGFWYYYNQKDTGEgtTPEFGDLVTFEYDIRALDGDVIYSEEELG 113
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519738687 172 ePTEFALNQ--VIKGWTEGLQLMKVGSKYEFFIHPNIAYGQRA-RPKIPANSVLIFEVELLDI 231
Cdd:TIGR03516 114 -PQTYKVDQqdLFSGLRDGLKLMKEGETATFLFPSHKAYGYYGdQNKIGPNLPIISTVTLLNI 175
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
131-231 2.98e-55

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 171.90  E-value: 2.98e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519738687 131 LQYRVLTEGNGESPKKTDRVKVHYVGKLMDGSEFDSSIERGEPTEFALN--QVIKGWTEGLQLMKVGSKYEFFIHPNIAY 208
Cdd:COG0545     1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80
                          90       100
                  ....*....|....*....|....
gi 1519738687 209 GQR-ARPKIPANSVLIFEVELLDI 231
Cdd:COG0545    81 GERgAGGVIPPNSTLVFEVELLDV 104
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
41-232 1.97e-52

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 168.44  E-value: 1.97e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519738687  41 SYSLGADLGENLKRQQVE-IDYDVFMAGLMDGME--TEMVKLDQGQR--RAVMASLQKNIRDKSKKEGEANLKladeFLD 115
Cdd:PRK11570   14 SYGIGLQVGQQLSESGLEgLLPEALVAGLADALEgkHPAVPVDVVHRalREIHERADAVRRERQQAMAAEGVK----FLE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519738687 116 NNVKENpDIKETPTGLQYRVLTEGNGESPKKTDRVKVHYVGKLMDGSEFDSSIERGEPTEFALNQVIKGWTEGLQLMKVG 195
Cdd:PRK11570   90 ENAKKE-GVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIEALTLMPVG 168
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1519738687 196 SKYEFFIHPNIAYGQR-ARPKIPANSVLIFEVELLDII 232
Cdd:PRK11570  169 SKWELTIPHELAYGERgAGASIPPFSTLVFEVELLEIL 206
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
23-231 1.44e-50

FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 165.71  E-value: 1.44e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519738687  23 PKSKSKSVSTLSTFMDSTSYSLGADLG---EN-LKRQQ---VEIDYDVFMAGLMDGMETEMvKLDQGQRRAVMASLQKNI 95
Cdd:PRK10902   31 PAATADSKAAFKNDDQQSAYALGASLGrymENsLKEQEklgIKLDKDQLIAGVQDAFADKS-KLSDQEIEQTLQAFEARV 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519738687  96 RD----KSKKEGEANLKLADEFLDNNVKENpDIKETPTGLQYRVLTEGNGESPKKTDRVKVHYVGKLMDGSEFDSSIERG 171
Cdd:PRK10902  110 KSaaqaKMEKDAADNEAKGKKYREKFAKEK-GVKTTSTGLLYKVEKEGTGEAPKDSDTVVVNYKGTLIDGKEFDNSYTRG 188
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519738687 172 EPTEFALNQVIKGWTEGLQLMKVGSKYEFFIHPNIAYGQRARPKIPANSVLIFEVELLDI 231
Cdd:PRK10902  189 EPLSFRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPANSTLVFDVELLDV 248
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
142-229 1.17e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 126.93  E-value: 1.17e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519738687 142 ESPKKTDRVKVHYVGKLMDGSEFDSSIERGEPTEFAL--NQVIKGWTEGLQLMKVGSKYEFFIHPNIAYGQR--ARPKIP 217
Cdd:pfam00254   3 EKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLgsGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEglAGPVIP 82
                          90
                  ....*....|..
gi 1519738687 218 ANSVLIFEVELL 229
Cdd:pfam00254  83 PNATLVFEVELL 94
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
37-135 1.94e-24

Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the amino terminus of pfam00254. This entry represents the N-terminal domain found in FKBP-type peptidylprolyl isomerases (PPIase). The N-terminal domain forms the dimer interface by the mutual exchange of two beta-strands between monomers.


Pssm-ID: 460169  Cd Length: 97  Bit Score: 92.95  E-value: 1.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519738687  37 MDSTSYSLGADLGENLKRQQVEIDYDVFMAGLMDGMETEMVKLDQgQRRAVMASLQKNIRDKSKKEGEANLKLADEFLDN 116
Cdd:pfam01346   1 KDKVSYAIGLQIGQQLKQQGIELDLDAFLAGLKDALAGKPLLTDE-EAQEALQAFQEKLQAKQEEQAEKNKAEGEAFLAE 79
                          90
                  ....*....|....*....
gi 1519738687 117 NvKENPDIKETPTGLQYRV 135
Cdd:pfam01346  80 N-KKKEGVKTTESGLQYKV 97
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
145-228 6.22e-11

Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 58.19  E-value: 6.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519738687 145 KKTDRVKVHYVGKLMDGSEFDSSIERgEPTEFAL--NQVIKGWTEGLQLMKVGSKYEFFIHPNIAYGQRarpkipaNSVL 222
Cdd:COG1047     2 EKGDVVTLHYTLKLEDGEVFDSTFEG-EPLEFLHgaGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGER-------DPEL 73

                  ....*.
gi 1519738687 223 IFEVEL 228
Cdd:COG1047    74 VQTVPR 79
ppisom_GldI TIGR03516
peptidyl-prolyl isomerase, gliding motility-associated; Members of this protein family are ...
99-231 1.44e-06

peptidyl-prolyl isomerase, gliding motility-associated; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldI is a FKBP-type peptidyl-prolyl cis-trans isomerase (pfam00254) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockout of this gene abolishes the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. This family is only found in Bacteroidetes containing the suite of genes proposed to confer the gliding motility phenotype.


Pssm-ID: 132555  Cd Length: 177  Bit Score: 47.06  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519738687  99 SKKEGEANLKL--ADE-FLDNNVKENPDIK-ETPT-GLQYRVLTEGNGE--SPKKTDRVKVHYVGKLMDGSEFDSSIERG 171
Cdd:TIGR03516  34 IKLSAERNKKLiaAEEaAIKRIISADSIVKyETSQnGFWYYYNQKDTGEgtTPEFGDLVTFEYDIRALDGDVIYSEEELG 113
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519738687 172 ePTEFALNQ--VIKGWTEGLQLMKVGSKYEFFIHPNIAYGQRA-RPKIPANSVLIFEVELLDI 231
Cdd:TIGR03516 114 -PQTYKVDQqdLFSGLRDGLKLMKEGETATFLFPSHKAYGYYGdQNKIGPNLPIISTVTLLNI 175
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
150-211 3.90e-03

FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 36.61  E-value: 3.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519738687 150 VKVHYVGKLMDGSEFDSSIERGEPTEFALNQviKGWTEGL--QL--MKVGSKYEFFIHPNIAYGQR 211
Cdd:PRK15095   11 VLVHFTLKLDDGSTAESTRNNGKPALFRLGD--GSLSEGLeqQLlgLKVGDKKTFSLEPEAAFGVP 74
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH