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Conserved domains on  [gi|1875944664|gb|QLJ29989|]
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FKBP-type peptidyl-prolyl cis-trans isomerase [Serratia marcescens]

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

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List of domain hits

Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
1-206 1.27e-157

peptidyl-prolyl cis-trans isomerase; Provisional


:

Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 433.84  E-value: 1.27e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875944664   1 MTTPSFDSVEAQASYGIGLQVGQQLQESGLEGLQPEALLAGLRDALEGNAPAVPVDVVHRALREIHERADAVRRERQQAM 80
Cdd:PRK11570    1 MTTPTFDSIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875944664  81 AVEGQKFLDDNAKRDDVTLTESGLQFSVLEQGNGPIPSRQDRVRVHYTGRLINGDVFDSSVERGQPAEFPVSGVIPGWIE 160
Cdd:PRK11570   81 AAEGVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1875944664 161 ALTLMPVGSKWQLYIPHNLAYGERGAGASIPPFSALVFDVELLEIL 206
Cdd:PRK11570  161 ALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVFEVELLEIL 206
 
Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
1-206 1.27e-157

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 433.84  E-value: 1.27e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875944664   1 MTTPSFDSVEAQASYGIGLQVGQQLQESGLEGLQPEALLAGLRDALEGNAPAVPVDVVHRALREIHERADAVRRERQQAM 80
Cdd:PRK11570    1 MTTPTFDSIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875944664  81 AVEGQKFLDDNAKRDDVTLTESGLQFSVLEQGNGPIPSRQDRVRVHYTGRLINGDVFDSSVERGQPAEFPVSGVIPGWIE 160
Cdd:PRK11570   81 AAEGVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1875944664 161 ALTLMPVGSKWQLYIPHNLAYGERGAGASIPPFSALVFDVELLEIL 206
Cdd:PRK11570  161 ALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVFEVELLEIL 206
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
104-205 1.40e-53

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 166.51  E-value: 1.40e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875944664 104 LQFSVLEQGNGPIPSRQDRVRVHYTGRLINGDVFDSSVERGQPAEFPVS--GVIPGWIEALTLMPVGSKWQLYIPHNLAY 181
Cdd:COG0545     1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80
                          90       100
                  ....*....|....*....|....
gi 1875944664 182 GERGAGASIPPFSALVFDVELLEI 205
Cdd:COG0545    81 GERGAGGVIPPNSTLVFEVELLDV 104
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
117-203 3.79e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 124.62  E-value: 3.79e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875944664 117 PSRQDRVRVHYTGRLINGDVFDSSVERGQPAEFPV-SG-VIPGWIEALTLMPVGSKWQLYIPHNLAYGERG-AGASIPPF 193
Cdd:pfam00254   5 AKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLgSGqVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPVIPPN 84
                          90
                  ....*....|
gi 1875944664 194 SALVFDVELL 203
Cdd:pfam00254  85 ATLVFEVELL 94
 
Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
1-206 1.27e-157

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 433.84  E-value: 1.27e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875944664   1 MTTPSFDSVEAQASYGIGLQVGQQLQESGLEGLQPEALLAGLRDALEGNAPAVPVDVVHRALREIHERADAVRRERQQAM 80
Cdd:PRK11570    1 MTTPTFDSIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875944664  81 AVEGQKFLDDNAKRDDVTLTESGLQFSVLEQGNGPIPSRQDRVRVHYTGRLINGDVFDSSVERGQPAEFPVSGVIPGWIE 160
Cdd:PRK11570   81 AAEGVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1875944664 161 ALTLMPVGSKWQLYIPHNLAYGERGAGASIPPFSALVFDVELLEIL 206
Cdd:PRK11570  161 ALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVFEVELLEIL 206
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
104-205 1.40e-53

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 166.51  E-value: 1.40e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875944664 104 LQFSVLEQGNGPIPSRQDRVRVHYTGRLINGDVFDSSVERGQPAEFPVS--GVIPGWIEALTLMPVGSKWQLYIPHNLAY 181
Cdd:COG0545     1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80
                          90       100
                  ....*....|....*....|....
gi 1875944664 182 GERGAGASIPPFSALVFDVELLEI 205
Cdd:COG0545    81 GERGAGGVIPPNSTLVFEVELLDV 104
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
6-205 4.10e-42

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 142.98  E-value: 4.10e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875944664   6 FDSVEAQASYGIGLQVGQQLQESGLE------GLQPEALLAGLRDALEGNAPAVPVDVvHRALREIHERADAVRRERQQA 79
Cdd:PRK10902   41 FKNDDQQSAYALGASLGRYMENSLKEqeklgiKLDKDQLIAGVQDAFADKSKLSDQEI-EQTLQAFEARVKSAAQAKMEK 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875944664  80 MAVE----GQKFLDDNAKRDDVTLTESGLQFSVLEQGNGPIPSRQDRVRVHYTGRLINGDVFDSSVERGQPAEFPVSGVI 155
Cdd:PRK10902  120 DAADneakGKKYREKFAKEKGVKTTSTGLLYKVEKEGTGEAPKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDGVI 199
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1875944664 156 PGWIEALTLMPVGSKWQLYIPHNLAYGERGAgASIPPFSALVFDVELLEI 205
Cdd:PRK10902  200 PGWTEGLKNIKKGGKIKLVIPPELAYGKAGV-PGIPANSTLVFDVELLDV 248
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
117-203 3.79e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 124.62  E-value: 3.79e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875944664 117 PSRQDRVRVHYTGRLINGDVFDSSVERGQPAEFPV-SG-VIPGWIEALTLMPVGSKWQLYIPHNLAYGERG-AGASIPPF 193
Cdd:pfam00254   5 AKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLgSGqVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPVIPPN 84
                          90
                  ....*....|
gi 1875944664 194 SALVFDVELL 203
Cdd:pfam00254  85 ATLVFEVELL 94
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
10-108 2.37e-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: 96.80  E-value: 2.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875944664  10 EAQASYGIGLQVGQQLQESGLEgLQPEALLAGLRDALEGNAPAVPvDVVHRALREIHERADAVRRERQQAMAVEGQKFLD 89
Cdd:pfam01346   1 KDKVSYAIGLQIGQQLKQQGIE-LDLDAFLAGLKDALAGKPLLTD-EEAQEALQAFQEKLQAKQEEQAEKNKAEGEAFLA 78
                          90
                  ....*....|....*....
gi 1875944664  90 DNAKRDDVTLTESGLQFSV 108
Cdd:pfam01346  79 ENKKKEGVKTTESGLQYKV 97
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
121-184 1.99e-09

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 53.57  E-value: 1.99e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1875944664 121 DRVRVHYTGRLINGDVFDSSVERgQPAEFPV--SGVIPGWIEALTLMPVGSKWQLYIPHNLAYGER 184
Cdd:COG1047     5 DVVTLHYTLKLEDGEVFDSTFEG-EPLEFLHgaGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGER 69
 
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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