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Conserved domains on  [gi|516458042|ref|WP_017846882|]
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MULTISPECIES: FKBP-type peptidyl-prolyl cis-trans isomerase [Pseudomonas]

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
PRK11570 super family cl29491
peptidyl-prolyl cis-trans isomerase; Provisional
34-227 4.05e-66

peptidyl-prolyl cis-trans isomerase; Provisional


The actual alignment was detected with superfamily member PRK11570:

Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 203.49  E-value: 4.05e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458042  34 KASYGIGLNMGKSLAQEGMDDLDSKAVAQGIEDAVGKKEQKLKDDELVEAFAALQKRAEERMAKMSEESAAAGKKFLEDN 113
Cdd:PRK11570  12 QASYGIGLQVGQQLSESGLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAMAAEGVKFLEEN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458042 114 AKKDGVVTTASGLQYKITKKADGPQPKPTDVVTVHYTGKLTNGTTFDSSVDRGSPIDLPVSGVIPGWVEGLQLMHVGEKV 193
Cdd:PRK11570  92 AKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIEALTLMPVGSKW 171
                        170       180       190
                 ....*....|....*....|....*....|....
gi 516458042 194 ELYIPSDLAYGAQSPSPAIPANSVLVFDLELLGI 227
Cdd:PRK11570 172 ELTIPHELAYGERGAGASIPPFSTLVFEVELLEI 205
 
Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
34-227 4.05e-66

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 203.49  E-value: 4.05e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458042  34 KASYGIGLNMGKSLAQEGMDDLDSKAVAQGIEDAVGKKEQKLKDDELVEAFAALQKRAEERMAKMSEESAAAGKKFLEDN 113
Cdd:PRK11570  12 QASYGIGLQVGQQLSESGLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAMAAEGVKFLEEN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458042 114 AKKDGVVTTASGLQYKITKKADGPQPKPTDVVTVHYTGKLTNGTTFDSSVDRGSPIDLPVSGVIPGWVEGLQLMHVGEKV 193
Cdd:PRK11570  92 AKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIEALTLMPVGSKW 171
                        170       180       190
                 ....*....|....*....|....*....|....
gi 516458042 194 ELYIPSDLAYGAQSPSPAIPANSVLVFDLELLGI 227
Cdd:PRK11570 172 ELTIPHELAYGERGAGASIPPFSTLVFEVELLEI 205
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
126-227 2.55e-55

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 172.29  E-value: 2.55e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458042 126 LQYKITKKADGPQPKPTDVVTVHYTGKLTNGTTFDSSVDRGSPIDLPVS--GVIPGWVEGLQLMHVGEKVELYIPSDLAY 203
Cdd:COG0545    1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80
                         90       100
                 ....*....|....*....|....
gi 516458042 204 GAQSPSPAIPANSVLVFDLELLGI 227
Cdd:COG0545   81 GERGAGGVIPPNSTLVFEVELLDV 104
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
138-225 2.40e-36

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 123.85  E-value: 2.40e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458042  138 QPKPTDVVTVHYTGKLTNGTTFDSSVDRGSPIDLPV--SGVIPGWVEGLQLMHVGEKVELYIPSDLAYGAQ-SPSPAIPA 214
Cdd:pfam00254   4 KAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLgsGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEgLAGPVIPP 83
                          90
                  ....*....|.
gi 516458042  215 NSVLVFDLELL 225
Cdd:pfam00254  84 NATLVFEVELL 94
 
Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
34-227 4.05e-66

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 203.49  E-value: 4.05e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458042  34 KASYGIGLNMGKSLAQEGMDDLDSKAVAQGIEDAVGKKEQKLKDDELVEAFAALQKRAEERMAKMSEESAAAGKKFLEDN 113
Cdd:PRK11570  12 QASYGIGLQVGQQLSESGLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAMAAEGVKFLEEN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458042 114 AKKDGVVTTASGLQYKITKKADGPQPKPTDVVTVHYTGKLTNGTTFDSSVDRGSPIDLPVSGVIPGWVEGLQLMHVGEKV 193
Cdd:PRK11570  92 AKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIEALTLMPVGSKW 171
                        170       180       190
                 ....*....|....*....|....*....|....
gi 516458042 194 ELYIPSDLAYGAQSPSPAIPANSVLVFDLELLGI 227
Cdd:PRK11570 172 ELTIPHELAYGERGAGASIPPFSTLVFEVELLEI 205
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
126-227 2.55e-55

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 172.29  E-value: 2.55e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458042 126 LQYKITKKADGPQPKPTDVVTVHYTGKLTNGTTFDSSVDRGSPIDLPVS--GVIPGWVEGLQLMHVGEKVELYIPSDLAY 203
Cdd:COG0545    1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80
                         90       100
                 ....*....|....*....|....
gi 516458042 204 GAQSPSPAIPANSVLVFDLELLGI 227
Cdd:COG0545   81 GERGAGGVIPPNSTLVFEVELLDV 104
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
6-243 8.61e-54

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 174.18  E-value: 8.61e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458042   6 LAAAVAL---VSLVLAGCDSQTSVE------LKTPAQKASYGIGLNMGK----SLA-QEGMD-DLDSKAVAQGIEDAVGK 70
Cdd:PRK10902  10 LATTMAValnAPITFAADAAKPAATadskaaFKNDDQQSAYALGASLGRymenSLKeQEKLGiKLDKDQLIAGVQDAFAD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458042  71 KeQKLKDDELVEAFAALQKR----AEERMAKMSEESAAAGKKFLEDNAKKDGVVTTASGLQYKITKKADGPQPKPTDVVT 146
Cdd:PRK10902  90 K-SKLSDQEIEQTLQAFEARvksaAQAKMEKDAADNEAKGKKYREKFAKEKGVKTTSTGLLYKVEKEGTGEAPKDSDTVV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458042 147 VHYTGKLTNGTTFDSSVDRGSPIDLPVSGVIPGWVEGLQLMHVGEKVELYIPSDLAYGaQSPSPAIPANSVLVFDLELLG 226
Cdd:PRK10902 169 VNYKGTLIDGKEFDNSYTRGEPLSFRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYG-KAGVPGIPANSTLVFDVELLD 247
                        250
                 ....*....|....*...
gi 516458042 227 IKDPAKAEA-PDAPAAKK 243
Cdd:PRK10902 248 VKPAPKADAkPEADAKAA 265
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
138-225 2.40e-36

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 123.85  E-value: 2.40e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458042  138 QPKPTDVVTVHYTGKLTNGTTFDSSVDRGSPIDLPV--SGVIPGWVEGLQLMHVGEKVELYIPSDLAYGAQ-SPSPAIPA 214
Cdd:pfam00254   4 KAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLgsGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEgLAGPVIPP 83
                          90
                  ....*....|.
gi 516458042  215 NSVLVFDLELL 225
Cdd:pfam00254  84 NATLVFEVELL 94
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
32-130 8.60e-34

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: 117.21  E-value: 8.60e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516458042   32 AQKASYGIGLNMGKSLAQEGmDDLDSKAVAQGIEDAVgKKEQKLKDDELVEAFAALQKRAEERMAKMSEESAAAGKKFLE 111
Cdd:pfam01346   1 KDKVSYAIGLQIGQQLKQQG-IELDLDAFLAGLKDAL-AGKPLLTDEEAQEALQAFQEKLQAKQEEQAEKNKAEGEAFLA 78
                          90
                  ....*....|....*....
gi 516458042  112 DNAKKDGVVTTASGLQYKI 130
Cdd:pfam01346  79 ENKKKEGVKTTESGLQYKV 97
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
140-209 4.14e-11

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 58.96  E-value: 4.14e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516458042 140 KPTDVVTVHYTGKLTNGTTFDSSVDRGsPIDLPV--SGVIPGWVEGLQLMHVGEKVELYIPSDLAYGAQSPS 209
Cdd:COG1047    2 EKGDVVTLHYTLKLEDGEVFDSTFEGE-PLEFLHgaGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGERDPE 72
 
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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