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Conserved domains on  [gi|350285398|gb|AEQ28025|]
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Mip, partial [Legionella sp. 91-004]

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
29-202 7.69e-49

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: 158.04  E-value: 7.69e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285398  29 SYSIGIDLGKNFQRQGID-VNPEVLAKGMQDGLTGSKQLLTdqqmKEVLTKFQKDLMEKRTAEFNKNAEENKQKGETFLK 107
Cdd:PRK11570  14 SYGIGLQVGQQLSESGLEgLLPEALVAGLADALEGKHPAVP----VDVVHRALREIHERADAVRRERQQAMAAEGVKFLE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285398 108 ENKAKDGIVTLPSGLQYKILEAGKGKKPTKDDTVTVEYTGRLINGEVFDSTEKTGKPATFKLSQVIPGWTEALQLMPEGS 187
Cdd:PRK11570  90 ENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIEALTLMPVGS 169
                        170
                 ....*....|....*
gi 350285398 188 TWEIYVPADLAYGPR 202
Cdd:PRK11570 170 KWELTIPHELAYGER 184
 
Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
29-202 7.69e-49

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 158.04  E-value: 7.69e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285398  29 SYSIGIDLGKNFQRQGID-VNPEVLAKGMQDGLTGSKQLLTdqqmKEVLTKFQKDLMEKRTAEFNKNAEENKQKGETFLK 107
Cdd:PRK11570  14 SYGIGLQVGQQLSESGLEgLLPEALVAGLADALEGKHPAVP----VDVVHRALREIHERADAVRRERQQAMAAEGVKFLE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285398 108 ENKAKDGIVTLPSGLQYKILEAGKGKKPTKDDTVTVEYTGRLINGEVFDSTEKTGKPATFKLSQVIPGWTEALQLMPEGS 187
Cdd:PRK11570  90 ENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIEALTLMPVGS 169
                        170
                 ....*....|....*
gi 350285398 188 TWEIYVPADLAYGPR 202
Cdd:PRK11570 170 KWELTIPHELAYGER 184
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
122-202 1.38e-41

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 136.08  E-value: 1.38e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285398 122 LQYKILEAGKGKKPTKDDTVTVEYTGRLINGEVFDSTEKTGKPATFKLS--QVIPGWTEALQLMPEGSTWEIYVPADLAY 199
Cdd:COG0545    1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80

                 ...
gi 350285398 200 GPR 202
Cdd:COG0545   81 GER 83
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
25-126 2.50e-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: 2.50e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285398   25 KDKLSYSIGIDLGKNFQRQGIDVNPEVLAKGMQDGLTGsKQLLTDQQMKEVLTKFQKDLMEKRTAEfnknAEENKQKGET 104
Cdd:pfam01346   1 KDKVSYAIGLQIGQQLKQQGIELDLDAFLAGLKDALAG-KPLLTDEEAQEALQAFQEKLQAKQEEQ----AEKNKAEGEA 75
                          90       100
                  ....*....|....*....|..
gi 350285398  105 FLKENKAKDGIVTLPSGLQYKI 126
Cdd:pfam01346  76 FLAENKKKEGVKTTESGLQYKV 97
 
Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
29-202 7.69e-49

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 158.04  E-value: 7.69e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285398  29 SYSIGIDLGKNFQRQGID-VNPEVLAKGMQDGLTGSKQLLTdqqmKEVLTKFQKDLMEKRTAEFNKNAEENKQKGETFLK 107
Cdd:PRK11570  14 SYGIGLQVGQQLSESGLEgLLPEALVAGLADALEGKHPAVP----VDVVHRALREIHERADAVRRERQQAMAAEGVKFLE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285398 108 ENKAKDGIVTLPSGLQYKILEAGKGKKPTKDDTVTVEYTGRLINGEVFDSTEKTGKPATFKLSQVIPGWTEALQLMPEGS 187
Cdd:PRK11570  90 ENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIEALTLMPVGS 169
                        170
                 ....*....|....*
gi 350285398 188 TWEIYVPADLAYGPR 202
Cdd:PRK11570 170 KWELTIPHELAYGER 184
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
122-202 1.38e-41

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 136.08  E-value: 1.38e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285398 122 LQYKILEAGKGKKPTKDDTVTVEYTGRLINGEVFDSTEKTGKPATFKLS--QVIPGWTEALQLMPEGSTWEIYVPADLAY 199
Cdd:COG0545    1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80

                 ...
gi 350285398 200 GPR 202
Cdd:COG0545   81 GER 83
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
2-204 6.34e-39

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 134.51  E-value: 6.34e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285398   2 AALMSFAMTT--TMAANDVQT---------LQTEKDKLSYSIGIDLG-------KNFQRQGIDVNPEVLAKGMQDGLTGs 63
Cdd:PRK10902  11 ATTMAVALNApiTFAADAAKPaatadskaaFKNDDQQSAYALGASLGrymenslKEQEKLGIKLDKDQLIAGVQDAFAD- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285398  64 KQLLTDQQMKEVLTKFQKDLMEKRTAEFNKNAEENKQKGETFLKENKAKDGIVTLPSGLQYKILEAGKGKKPTKDDTVTV 143
Cdd:PRK10902  90 KSKLSDQEIEQTLQAFEARVKSAAQAKMEKDAADNEAKGKKYREKFAKEKGVKTTSTGLLYKVEKEGTGEAPKDSDTVVV 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 350285398 144 EYTGRLINGEVFDSTEKTGKPATFKLSQVIPGWTEALQLMPEGSTWEIYVPADLAYGPRSV 204
Cdd:PRK10902 170 NYKGTLIDGKEFDNSYTRGEPLSFRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGV 230
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
25-126 2.50e-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: 2.50e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350285398   25 KDKLSYSIGIDLGKNFQRQGIDVNPEVLAKGMQDGLTGsKQLLTDQQMKEVLTKFQKDLMEKRTAEfnknAEENKQKGET 104
Cdd:pfam01346   1 KDKVSYAIGLQIGQQLKQQGIELDLDAFLAGLKDALAG-KPLLTDEEAQEALQAFQEKLQAKQEEQ----AEKNKAEGEA 75
                          90       100
                  ....*....|....*....|..
gi 350285398  105 FLKENKAKDGIVTLPSGLQYKI 126
Cdd:pfam01346  76 FLAENKKKEGVKTTESGLQYKV 97
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
131-204 4.80e-26

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 96.11  E-value: 4.80e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 350285398  131 KGKKPTKDDTVTVEYTGRLINGEVFDSTEKTGKPATFKL--SQVIPGWTEALQLMPEGSTWEIYVPADLAYGPRSV 204
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLgsGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGL 76
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
136-202 2.84e-14

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 66.66  E-value: 2.84e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 350285398 136 TKDDTVTVEYTGRLINGEVFDSTEKtGKPATFKL--SQVIPGWTEALQLMPEGSTWEIYVPADLAYGPR 202
Cdd:COG1047    2 EKGDVVTLHYTLKLEDGEVFDSTFE-GEPLEFLHgaGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGER 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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