NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1109557811|ref|NP_463258|]
View 

FKBP-type 22KD peptidyl-prolyl cis-trans isomerase [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 11485412)

FKBP-type peptidylprolyl isomerase (PPIase) accelerates the folding of proteins; it catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
15-220 4.57e-151

peptidyl-prolyl cis-trans isomerase; Provisional


:

Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 417.66  E-value: 4.57e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557811  15 MATPTFDTIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGIADALEGKHPAVPVDVVHRALREIHERADAVRRERFKAM 94
Cdd:PRK11570    1 MTTPTFDSIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557811  95 AAEGVKYLEENREKDGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIAGWIE 174
Cdd:PRK11570   81 AAEGVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1109557811 175 ALTLMPVGSKWELTIPQELAYGERGAGASIPPFSTLVFEVELLEIL 220
Cdd:PRK11570  161 ALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVFEVELLEIL 206
 
Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
15-220 4.57e-151

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 417.66  E-value: 4.57e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557811  15 MATPTFDTIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGIADALEGKHPAVPVDVVHRALREIHERADAVRRERFKAM 94
Cdd:PRK11570    1 MTTPTFDSIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557811  95 AAEGVKYLEENREKDGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIAGWIE 174
Cdd:PRK11570   81 AAEGVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1109557811 175 ALTLMPVGSKWELTIPQELAYGERGAGASIPPFSTLVFEVELLEIL 220
Cdd:PRK11570  161 ALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVFEVELLEIL 206
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
118-219 1.67e-54

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 169.59  E-value: 1.67e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557811 118 LQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVN--GVIAGWIEALTLMPVGSKWELTIPQELAY 195
Cdd:COG0545     1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80
                          90       100
                  ....*....|....*....|....
gi 1109557811 196 GERGAGASIPPFSTLVFEVELLEI 219
Cdd:COG0545    81 GERGAGGVIPPNSTLVFEVELLDV 104
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
131-217 6.70e-39

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 129.62  E-value: 6.70e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557811 131 PARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPV--NGVIAGWIEALTLMPVGSKWELTIPQELAYGERG-AGASIPPF 207
Cdd:pfam00254   5 AKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLgsGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPVIPPN 84
                          90
                  ....*....|
gi 1109557811 208 STLVFEVELL 217
Cdd:pfam00254  85 ATLVFEVELL 94
 
Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
15-220 4.57e-151

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 417.66  E-value: 4.57e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557811  15 MATPTFDTIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGIADALEGKHPAVPVDVVHRALREIHERADAVRRERFKAM 94
Cdd:PRK11570    1 MTTPTFDSIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557811  95 AAEGVKYLEENREKDGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIAGWIE 174
Cdd:PRK11570   81 AAEGVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1109557811 175 ALTLMPVGSKWELTIPQELAYGERGAGASIPPFSTLVFEVELLEIL 220
Cdd:PRK11570  161 ALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVFEVELLEIL 206
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
118-219 1.67e-54

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 169.59  E-value: 1.67e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557811 118 LQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVN--GVIAGWIEALTLMPVGSKWELTIPQELAY 195
Cdd:COG0545     1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80
                          90       100
                  ....*....|....*....|....
gi 1109557811 196 GERGAGASIPPFSTLVFEVELLEI 219
Cdd:COG0545    81 GERGAGGVIPPNSTLVFEVELLDV 104
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
16-219 7.09e-42

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 142.59  E-value: 7.09e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557811  16 ATPTFDTIEAQASYGIGLQVGQQLSESGLE------GLLPEALVAGIADALEGKHPAVPVDVvHRALREIHERADAVRRE 89
Cdd:PRK10902   37 SKAAFKNDDQQSAYALGASLGRYMENSLKEqeklgiKLDKDQLIAGVQDAFADKSKLSDQEI-EQTLQAFEARVKSAAQA 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557811  90 RFKAMAAE----GVKYLEENREKDGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPV 165
Cdd:PRK10902  116 KMEKDAADneakGKKYREKFAKEKGVKTTSTGLLYKVEKEGTGEAPKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL 195
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1109557811 166 NGVIAGWIEALTLMPVGSKWELTIPQELAYGERGAgASIPPFSTLVFEVELLEI 219
Cdd:PRK10902  196 DGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGV-PGIPANSTLVFDVELLDV 248
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
131-217 6.70e-39

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 129.62  E-value: 6.70e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557811 131 PARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPV--NGVIAGWIEALTLMPVGSKWELTIPQELAYGERG-AGASIPPF 207
Cdd:pfam00254   5 AKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLgsGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPVIPPN 84
                          90
                  ....*....|
gi 1109557811 208 STLVFEVELL 217
Cdd:pfam00254  85 ATLVFEVELL 94
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
24-122 5.68e-26

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: 96.41  E-value: 5.68e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557811  24 EAQASYGIGLQVGQQLSESGLEgLLPEALVAGIADALEGKHPAVPvDVVHRALREIHERADAVRRERFKAMAAEGVKYLE 103
Cdd:pfam01346   1 KDKVSYAIGLQIGQQLKQQGIE-LDLDAFLAGLKDALAGKPLLTD-EEAQEALQAFQEKLQAKQEEQAEKNKAEGEAFLA 78
                          90
                  ....*....|....*....
gi 1109557811 104 ENREKDGVNSTESGLQFRV 122
Cdd:pfam01346  79 ENKKKEGVKTTESGLQYKV 97
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
135-198 1.02e-11

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 60.11  E-value: 1.02e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109557811 135 DRVRVHYTGKLIDGTVFDSSVaRGEPAEFPV--NGVIAGWIEALTLMPVGSKWELTIPQELAYGER 198
Cdd:COG1047     5 DVVTLHYTLKLEDGEVFDSTF-EGEPLEFLHgaGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGER 69
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
137-198 1.90e-04

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 40.46  E-value: 1.90e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109557811 137 VRVHYTGKLIDGTVFDSSVARGEPAEFPV-NGVIAGWIEA-LTLMPVGSKWELTIPQELAYGER 198
Cdd:PRK15095   11 VLVHFTLKLDDGSTAESTRNNGKPALFRLgDGSLSEGLEQqLLGLKVGDKKTFSLEPEAAFGVP 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