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Conserved domains on  [gi|374683105|gb|AEZ63338|]
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macrophage infectivity potentiator, partial [Legionella sp. F3602]

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
28-193 1.32e-45

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: 149.56  E-value: 1.32e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374683105  28 SYSIGADLGKNFKNQGID-INPDALAKGMQDGMSGAQLILTEQQMKDVLNKFQKDLMAKRSAEFNKKAEEnkskGDAFLS 106
Cdd:PRK11570  14 SYGIGLQVGQQLSESGLEgLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAMAAE----GVKFLE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374683105 107 SNKSKNGVVVLPSGLQYKVIEAGSGSKPGKSDTVTVEYTGTLIDGTVFDSTEKTGKPATFEVSQVIPGWTEALQLMPAGS 186
Cdd:PRK11570  90 ENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIEALTLMPVGS 169

                 ....*..
gi 374683105 187 TWEIYVP 193
Cdd:PRK11570 170 KWELTIP 176
 
Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
28-193 1.32e-45

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 149.56  E-value: 1.32e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374683105  28 SYSIGADLGKNFKNQGID-INPDALAKGMQDGMSGAQLILTEQQMKDVLNKFQKDLMAKRSAEFNKKAEEnkskGDAFLS 106
Cdd:PRK11570  14 SYGIGLQVGQQLSESGLEgLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAMAAE----GVKFLE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374683105 107 SNKSKNGVVVLPSGLQYKVIEAGSGSKPGKSDTVTVEYTGTLIDGTVFDSTEKTGKPATFEVSQVIPGWTEALQLMPAGS 186
Cdd:PRK11570  90 ENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIEALTLMPVGS 169

                 ....*..
gi 374683105 187 TWEIYVP 193
Cdd:PRK11570 170 KWELTIP 176
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
24-125 1.36e-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: 117.60  E-value: 1.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374683105   24 KDKLSYSIGADLGKNFKNQGIDINPDALAKGMQDGMSGAQLiLTEQQMKDVLNKFQKDLMAKRSaefnKKAEENKSKGDA 103
Cdd:pfam01346   1 KDKVSYAIGLQIGQQLKQQGIELDLDAFLAGLKDALAGKPL-LTDEEAQEALQAFQEKLQAKQE----EQAEKNKAEGEA 75
                          90       100
                  ....*....|....*....|..
gi 374683105  104 FLSSNKSKNGVVVLPSGLQYKV 125
Cdd:pfam01346  76 FLAENKKKEGVKTTESGLQYKV 97
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
121-193 4.38e-34

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 116.43  E-value: 4.38e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 374683105 121 LQYKVIEAGSGSKPGKSDTVTVEYTGTLIDGTVFDSTEKTGKPATFEVS--QVIPGWTEALQLMPAGSTWEIYVP 193
Cdd:COG0545    1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIP 75
 
Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
28-193 1.32e-45

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 149.56  E-value: 1.32e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374683105  28 SYSIGADLGKNFKNQGID-INPDALAKGMQDGMSGAQLILTEQQMKDVLNKFQKDLMAKRSAEFNKKAEEnkskGDAFLS 106
Cdd:PRK11570  14 SYGIGLQVGQQLSESGLEgLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAMAAE----GVKFLE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374683105 107 SNKSKNGVVVLPSGLQYKVIEAGSGSKPGKSDTVTVEYTGTLIDGTVFDSTEKTGKPATFEVSQVIPGWTEALQLMPAGS 186
Cdd:PRK11570  90 ENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIEALTLMPVGS 169

                 ....*..
gi 374683105 187 TWEIYVP 193
Cdd:PRK11570 170 KWELTIP 176
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
1-193 6.36e-36

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 126.42  E-value: 6.36e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374683105   1 AAIMGLAMST--AMAATDATSLV---------TDKDKLSYSIGADLGKNFKNQ-------GIDINPDALAKGMQDGMSGA 62
Cdd:PRK10902  11 ATTMAVALNApiTFAADAAKPAAtadskaafkNDDQQSAYALGASLGRYMENSlkeqeklGIKLDKDQLIAGVQDAFADK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374683105  63 QLiLTEQQMKDVLNKFQKDLMAKRSAEFNKKAEENKSKGDAFLSSNKSKNGVVVLPSGLQYKVIEAGSGSKPGKSDTVTV 142
Cdd:PRK10902  91 SK-LSDQEIEQTLQAFEARVKSAAQAKMEKDAADNEAKGKKYREKFAKEKGVKTTSTGLLYKVEKEGTGEAPKDSDTVVV 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 374683105 143 EYTGTLIDGTVFDSTEKTGKPATFEVSQVIPGWTEALQLMPAGSTWEIYVP 193
Cdd:PRK10902 170 NYKGTLIDGKEFDNSYTRGEPLSFRLDGVIPGWTEGLKNIKKGGKIKLVIP 220
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
24-125 1.36e-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: 117.60  E-value: 1.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374683105   24 KDKLSYSIGADLGKNFKNQGIDINPDALAKGMQDGMSGAQLiLTEQQMKDVLNKFQKDLMAKRSaefnKKAEENKSKGDA 103
Cdd:pfam01346   1 KDKVSYAIGLQIGQQLKQQGIELDLDAFLAGLKDALAGKPL-LTDEEAQEALQAFQEKLQAKQE----EQAEKNKAEGEA 75
                          90       100
                  ....*....|....*....|..
gi 374683105  104 FLSSNKSKNGVVVLPSGLQYKV 125
Cdd:pfam01346  76 FLAENKKKEGVKTTESGLQYKV 97
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
121-193 4.38e-34

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 116.43  E-value: 4.38e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 374683105 121 LQYKVIEAGSGSKPGKSDTVTVEYTGTLIDGTVFDSTEKTGKPATFEVS--QVIPGWTEALQLMPAGSTWEIYVP 193
Cdd:COG0545    1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIP 75
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
132-193 1.40e-21

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 84.17  E-value: 1.40e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 374683105  132 SKPGKSDTVTVEYTGTLIDGTVFDSTEKTGKPATFEV--SQVIPGWTEALQLMPAGSTWEIYVP 193
Cdd:pfam00254   3 EKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLgsGQVIPGWDEGLVGMKVGEKRKLTIP 66
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
138-193 3.93e-09

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 52.80  E-value: 3.93e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 374683105 138 DTVTVEYTGTLIDGTVFDSTEKtGKPATFEV--SQVIPGWTEALQLMPAGSTWEIYVP 193
Cdd:COG1047    5 DVVTLHYTLKLEDGEVFDSTFE-GEPLEFLHgaGQLIPGLEEALEGMEVGDKKTVTLP 61
 
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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