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Conserved domains on  [gi|487977695|ref|WP_002050486|]
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MULTISPECIES: FKBP-type peptidyl-prolyl cis-trans isomerase [Acinetobacter]

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

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List of domain hits

Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
127-228 2.75e-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: 2.75e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487977695 127 LQYQVLKEGSGKTPKATSRVKVNYEGRLLDGTVFDSSIARNHPVDFQLN--QVIAGWTEGLQTMKEGGKTRFFIPAKLAY 204
Cdd:COG0545    1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80
                         90       100
                 ....*....|....*....|....
gi 487977695 205 GEVGAGDSIGPNSTLIFDIELLQV 228
Cdd:COG0545   81 GERGAGGVIPPNSTLVFEVELLDV 104
PRK10902 super family cl29493
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
1-230 3.66e-48

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: 159.54  E-value: 3.66e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487977695   1 MK---KISLVIAASTMSLSVIAATPVTNKSPAK------------DQFSYSYGYLMGRNNTDALTD-------LNLDIFY 58
Cdd:PRK10902   1 MKslfKVTLLATTMAVALNAPITFAADAAKPAAtadskaafknddQQSAYALGASLGRYMENSLKEqeklgikLDKDQLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487977695  59 QGLQEGAQKKTaRLTDEEMAKAINEYKKTLEAKQLVEFQKLAQQNAQAGAAFLAENAKKSGVITTKSGLQYQVLKEGSGK 138
Cdd:PRK10902  81 AGVQDAFADKS-KLSDQEIEQTLQAFEARVKSAAQAKMEKDAADNEAKGKKYREKFAKEKGVKTTSTGLLYKVEKEGTGE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487977695 139 TPKATSRVKVNYEGRLLDGTVFDSSIARNHPVDFQLNQVIAGWTEGLQTMKEGGKTRFFIPAKLAYGEVGAgDSIGPNST 218
Cdd:PRK10902 160 APKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGV-PGIPANST 238
                        250
                 ....*....|..
gi 487977695 219 LIFDIELLQVLP 230
Cdd:PRK10902 239 LVFDVELLDVKP 250
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
127-228 2.75e-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: 2.75e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487977695 127 LQYQVLKEGSGKTPKATSRVKVNYEGRLLDGTVFDSSIARNHPVDFQLN--QVIAGWTEGLQTMKEGGKTRFFIPAKLAY 204
Cdd:COG0545    1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80
                         90       100
                 ....*....|....*....|....
gi 487977695 205 GEVGAGDSIGPNSTLIFDIELLQV 228
Cdd:COG0545   81 GERGAGGVIPPNSTLVFEVELLDV 104
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
32-229 1.02e-51

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 166.51  E-value: 1.02e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487977695  32 QFSYSYGYLMGRN-NTDALTDLNLDIFYQGLQEGAQKKTARLTDEEMAKAINEYKKTLEAKQLVEFQKLAQQNAQagaaF 110
Cdd:PRK11570  12 QASYGIGLQVGQQlSESGLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAMAAEGVK----F 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487977695 111 LAENAKKSGVITTKSGLQYQVLKEGSGKTPKATSRVKVNYEGRLLDGTVFDSSIARNHPVDFQLNQVIAGWTEGLQTMKE 190
Cdd:PRK11570  88 LEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIEALTLMPV 167
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 487977695 191 GGKTRFFIPAKLAYGEVGAGDSIGPNSTLIFDIELLQVL 229
Cdd:PRK11570 168 GSKWELTIPHELAYGERGAGASIPPFSTLVFEVELLEIL 206
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
1-230 3.66e-48

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 159.54  E-value: 3.66e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487977695   1 MK---KISLVIAASTMSLSVIAATPVTNKSPAK------------DQFSYSYGYLMGRNNTDALTD-------LNLDIFY 58
Cdd:PRK10902   1 MKslfKVTLLATTMAVALNAPITFAADAAKPAAtadskaafknddQQSAYALGASLGRYMENSLKEqeklgikLDKDQLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487977695  59 QGLQEGAQKKTaRLTDEEMAKAINEYKKTLEAKQLVEFQKLAQQNAQAGAAFLAENAKKSGVITTKSGLQYQVLKEGSGK 138
Cdd:PRK10902  81 AGVQDAFADKS-KLSDQEIEQTLQAFEARVKSAAQAKMEKDAADNEAKGKKYREKFAKEKGVKTTSTGLLYKVEKEGTGE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487977695 139 TPKATSRVKVNYEGRLLDGTVFDSSIARNHPVDFQLNQVIAGWTEGLQTMKEGGKTRFFIPAKLAYGEVGAgDSIGPNST 218
Cdd:PRK10902 160 APKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGV-PGIPANST 238
                        250
                 ....*....|..
gi 487977695 219 LIFDIELLQVLP 230
Cdd:PRK10902 239 LVFDVELLDVKP 250
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
138-226 3.55e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 125.39  E-value: 3.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487977695  138 KTPKATSRVKVNYEGRLLDGTVFDSSIARNHPVDFQL--NQVIAGWTEGLQTMKEGGKTRFFIPAKLAYGEVG-AGDSIG 214
Cdd:pfam00254   3 EKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLgsGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPVIP 82
                          90
                  ....*....|..
gi 487977695  215 PNSTLIFDIELL 226
Cdd:pfam00254  83 PNATLVFEVELL 94
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
30-131 8.67e-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: 91.02  E-value: 8.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487977695   30 KDQFSYSYGYLMGRNNTDALTDLNLDIFYQGLQEGAQKKTArLTDEEMAKAINEYKKTLEAKQlvefQKLAQQNAQAGAA 109
Cdd:pfam01346   1 KDKVSYAIGLQIGQQLKQQGIELDLDAFLAGLKDALAGKPL-LTDEEAQEALQAFQEKLQAKQ----EEQAEKNKAEGEA 75
                          90       100
                  ....*....|....*....|..
gi 487977695  110 FLAENAKKSGVITTKSGLQYQV 131
Cdd:pfam01346  76 FLAENKKKEGVKTTESGLQYKV 97
ppisom_GldI TIGR03516
peptidyl-prolyl isomerase, gliding motility-associated; Members of this protein family are ...
122-230 1.49e-13

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: 66.32  E-value: 1.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487977695  122 TTKSGLQYQVLKE--GSGKTPKATSRVKVNYEGRLLDGTVFDSSiARNHPVDFQLNQ--VIAGWTEGLQTMKEGGKTRFF 197
Cdd:TIGR03516  66 TSQNGFWYYYNQKdtGEGTTPEFGDLVTFEYDIRALDGDVIYSE-EELGPQTYKVDQqdLFSGLRDGLKLMKEGETATFL 144
                          90       100       110
                  ....*....|....*....|....*....|...
gi 487977695  198 IPAKLAYGEVGAGDSIGPNSTLIFDIELLQVLP 230
Cdd:TIGR03516 145 FPSHKAYGYYGDQNKIGPNLPIISTVTLLNIKP 177
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
127-228 2.75e-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: 2.75e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487977695 127 LQYQVLKEGSGKTPKATSRVKVNYEGRLLDGTVFDSSIARNHPVDFQLN--QVIAGWTEGLQTMKEGGKTRFFIPAKLAY 204
Cdd:COG0545    1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80
                         90       100
                 ....*....|....*....|....
gi 487977695 205 GEVGAGDSIGPNSTLIFDIELLQV 228
Cdd:COG0545   81 GERGAGGVIPPNSTLVFEVELLDV 104
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
32-229 1.02e-51

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 166.51  E-value: 1.02e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487977695  32 QFSYSYGYLMGRN-NTDALTDLNLDIFYQGLQEGAQKKTARLTDEEMAKAINEYKKTLEAKQLVEFQKLAQQNAQagaaF 110
Cdd:PRK11570  12 QASYGIGLQVGQQlSESGLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAMAAEGVK----F 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487977695 111 LAENAKKSGVITTKSGLQYQVLKEGSGKTPKATSRVKVNYEGRLLDGTVFDSSIARNHPVDFQLNQVIAGWTEGLQTMKE 190
Cdd:PRK11570  88 LEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIEALTLMPV 167
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 487977695 191 GGKTRFFIPAKLAYGEVGAGDSIGPNSTLIFDIELLQVL 229
Cdd:PRK11570 168 GSKWELTIPHELAYGERGAGASIPPFSTLVFEVELLEIL 206
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
1-230 3.66e-48

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 159.54  E-value: 3.66e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487977695   1 MK---KISLVIAASTMSLSVIAATPVTNKSPAK------------DQFSYSYGYLMGRNNTDALTD-------LNLDIFY 58
Cdd:PRK10902   1 MKslfKVTLLATTMAVALNAPITFAADAAKPAAtadskaafknddQQSAYALGASLGRYMENSLKEqeklgikLDKDQLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487977695  59 QGLQEGAQKKTaRLTDEEMAKAINEYKKTLEAKQLVEFQKLAQQNAQAGAAFLAENAKKSGVITTKSGLQYQVLKEGSGK 138
Cdd:PRK10902  81 AGVQDAFADKS-KLSDQEIEQTLQAFEARVKSAAQAKMEKDAADNEAKGKKYREKFAKEKGVKTTSTGLLYKVEKEGTGE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487977695 139 TPKATSRVKVNYEGRLLDGTVFDSSIARNHPVDFQLNQVIAGWTEGLQTMKEGGKTRFFIPAKLAYGEVGAgDSIGPNST 218
Cdd:PRK10902 160 APKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGV-PGIPANST 238
                        250
                 ....*....|..
gi 487977695 219 LIFDIELLQVLP 230
Cdd:PRK10902 239 LVFDVELLDVKP 250
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
138-226 3.55e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 125.39  E-value: 3.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487977695  138 KTPKATSRVKVNYEGRLLDGTVFDSSIARNHPVDFQL--NQVIAGWTEGLQTMKEGGKTRFFIPAKLAYGEVG-AGDSIG 214
Cdd:pfam00254   3 EKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLgsGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPVIP 82
                          90
                  ....*....|..
gi 487977695  215 PNSTLIFDIELL 226
Cdd:pfam00254  83 PNATLVFEVELL 94
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
30-131 8.67e-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: 91.02  E-value: 8.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487977695   30 KDQFSYSYGYLMGRNNTDALTDLNLDIFYQGLQEGAQKKTArLTDEEMAKAINEYKKTLEAKQlvefQKLAQQNAQAGAA 109
Cdd:pfam01346   1 KDKVSYAIGLQIGQQLKQQGIELDLDAFLAGLKDALAGKPL-LTDEEAQEALQAFQEKLQAKQ----EEQAEKNKAEGEA 75
                          90       100
                  ....*....|....*....|..
gi 487977695  110 FLAENAKKSGVITTKSGLQYQV 131
Cdd:pfam01346  76 FLAENKKKEGVKTTESGLQYKV 97
ppisom_GldI TIGR03516
peptidyl-prolyl isomerase, gliding motility-associated; Members of this protein family are ...
122-230 1.49e-13

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: 66.32  E-value: 1.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487977695  122 TTKSGLQYQVLKE--GSGKTPKATSRVKVNYEGRLLDGTVFDSSiARNHPVDFQLNQ--VIAGWTEGLQTMKEGGKTRFF 197
Cdd:TIGR03516  66 TSQNGFWYYYNQKdtGEGTTPEFGDLVTFEYDIRALDGDVIYSE-EELGPQTYKVDQqdLFSGLRDGLKLMKEGETATFL 144
                          90       100       110
                  ....*....|....*....|....*....|...
gi 487977695  198 IPAKLAYGEVGAGDSIGPNSTLIFDIELLQVLP 230
Cdd:TIGR03516 145 FPSHKAYGYYGDQNKIGPNLPIISTVTLLNIKP 177
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
144-231 2.08e-10

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 57.03  E-value: 2.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487977695 144 SRVKVNYEGRLLDGTVFDSSIARNhPVDFQL--NQVIAGWTEGLQTMKEGGKTRFFIPAKLAYGEvgagdsigpnstliF 221
Cdd:COG1047    5 DVVTLHYTLKLEDGEVFDSTFEGE-PLEFLHgaGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGE--------------R 69
                         90
                 ....*....|
gi 487977695 222 DIELLQVLPK 231
Cdd:COG1047   70 DPELVQTVPR 79
 
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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