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Conserved domains on  [gi|15600447|ref|NP_253941|]
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FkbP-type peptidyl-prolyl cis-trans isomerase [Pseudomonas aeruginosa PAO1]

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 ...
115-208 1.38e-31

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


:

Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 110.66  E-value: 1.38e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600447 115 LRRGQGNGIGAATQVHVRYRGLLADGQVFDQSESAE---WFALDS--VIEGWRTALRAMPVGARWRVVIPSAQAYGHEGA 189
Cdd:COG0545   6 LKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGepaTFPLGVgqVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGA 85
                        90
                ....*....|....*....
gi 15600447 190 GDLIPPDAPLVFEIDLLGF 208
Cdd:COG0545  86 GGVIPPNSTLVFEVELLDV 104
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
115-208 1.38e-31

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 110.66  E-value: 1.38e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600447 115 LRRGQGNGIGAATQVHVRYRGLLADGQVFDQSESAE---WFALDS--VIEGWRTALRAMPVGARWRVVIPSAQAYGHEGA 189
Cdd:COG0545   6 LKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGepaTFPLGVgqVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGA 85
                        90
                ....*....|....*....
gi 15600447 190 GDLIPPDAPLVFEIDLLGF 208
Cdd:COG0545  86 GGVIPPNSTLVFEVELLDV 104
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
128-206 2.28e-25

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 94.57  E-value: 2.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600447   128 QVHVRYRGLLADGQVFDQSESAE---WFALDS--VIEGWRTALRAMPVGARWRVVIPSAQAYGHEG-AGDLIPPDAPLVF 201
Cdd:pfam00254  10 RVTVHYTGTLEDGTVFDSSYDRGkpfEFTLGSgqVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPVIPPNATLVF 89

                  ....*
gi 15600447   202 EIDLL 206
Cdd:pfam00254  90 EVELL 94
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
26-206 1.26e-24

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 96.02  E-value: 1.26e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600447   26 AYAVGARLGMRLQQE-MPGLELSELLLGLRQAYRGEALEIPPERIEQLLLQ-HENATT---ETPRTTPAEA-RFLANEKA 99
Cdd:PRK11570  14 SYGIGLQVGQQLSESgLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREiHERADAvrrERQQAMAAEGvKFLEENAK 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600447  100 RFGVRELTGGVLVSELRRGQGNGIGAATQVHVRYRGLLADGQVFDQS----ESAEwFALDSVIEGWRTALRAMPVGARWR 175
Cdd:PRK11570  94 KEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSvargEPAE-FPVNGVIPGWIEALTLMPVGSKWE 172
                        170       180       190
                 ....*....|....*....|....*....|.
gi 15600447  176 VVIPSAQAYGHEGAGDLIPPDAPLVFEIDLL 206
Cdd:PRK11570 173 LTIPHELAYGERGAGASIPPFSTLVFEVELL 203
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
115-208 1.38e-31

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 110.66  E-value: 1.38e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600447 115 LRRGQGNGIGAATQVHVRYRGLLADGQVFDQSESAE---WFALDS--VIEGWRTALRAMPVGARWRVVIPSAQAYGHEGA 189
Cdd:COG0545   6 LKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGepaTFPLGVgqVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGA 85
                        90
                ....*....|....*....
gi 15600447 190 GDLIPPDAPLVFEIDLLGF 208
Cdd:COG0545  86 GGVIPPNSTLVFEVELLDV 104
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
128-206 2.28e-25

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 94.57  E-value: 2.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600447   128 QVHVRYRGLLADGQVFDQSESAE---WFALDS--VIEGWRTALRAMPVGARWRVVIPSAQAYGHEG-AGDLIPPDAPLVF 201
Cdd:pfam00254  10 RVTVHYTGTLEDGTVFDSSYDRGkpfEFTLGSgqVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPVIPPNATLVF 89

                  ....*
gi 15600447   202 EIDLL 206
Cdd:pfam00254  90 EVELL 94
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
26-206 1.26e-24

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 96.02  E-value: 1.26e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600447   26 AYAVGARLGMRLQQE-MPGLELSELLLGLRQAYRGEALEIPPERIEQLLLQ-HENATT---ETPRTTPAEA-RFLANEKA 99
Cdd:PRK11570  14 SYGIGLQVGQQLSESgLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREiHERADAvrrERQQAMAAEGvKFLEENAK 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600447  100 RFGVRELTGGVLVSELRRGQGNGIGAATQVHVRYRGLLADGQVFDQS----ESAEwFALDSVIEGWRTALRAMPVGARWR 175
Cdd:PRK11570  94 KEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSvargEPAE-FPVNGVIPGWIEALTLMPVGSKWE 172
                        170       180       190
                 ....*....|....*....|....*....|.
gi 15600447  176 VVIPSAQAYGHEGAGDLIPPDAPLVFEIDLL 206
Cdd:PRK11570 173 LTIPHELAYGERGAGASIPPFSTLVFEVELL 203
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
95-206 5.32e-16

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 74.03  E-value: 5.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600447   95 ANEKarfGVRELTGGVLVSELRRGQGNGIGAATQVHVRYRGLLADGQVFDQS-ESAE--WFALDSVIEGWRTALRAMPVG 171
Cdd:PRK10902 136 AKEK---GVKTTSTGLLYKVEKEGTGEAPKDSDTVVVNYKGTLIDGKEFDNSyTRGEplSFRLDGVIPGWTEGLKNIKKG 212
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 15600447  172 ARWRVVIPSAQAYGHEGAGDlIPPDAPLVFEIDLL 206
Cdd:PRK10902 213 GKIKLVIPPELAYGKAGVPG-IPANSTLVFDVELL 246
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
123-205 2.00e-06

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 45.48  E-value: 2.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600447 123 IGAATQVHVRYRGLLADGQVFDQSESAEWFAL----DSVIEGWRTALRAMPVGARWRVVIPSAQAYGhegagdliPPDAP 198
Cdd:COG1047   1 IEKGDVVTLHYTLKLEDGEVFDSTFEGEPLEFlhgaGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG--------ERDPE 72

                ....*..
gi 15600447 199 LVFEIDL 205
Cdd:COG1047  73 LVQTVPR 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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