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Conserved domains on  [gi|313870675|gb|ADR82222|]
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macrophage infectivity potentiator, partial [Legionella sp. ST7322]

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
34-210 4.68e-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: 158.81  E-value: 4.68e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870675  34 SYSIGADLGKNFKNQGID-INPDALAKGMQDGMSGAQLILTEQQMKDVLNKFQKDLMAKRSAEFNKKAEEnkakGEAFLS 112
Cdd:PRK11570  14 SYGIGLQVGQQLSESGLEgLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAMAAE----GVKFLE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870675 113 TNKSKSGVVVLPSGLQYKIIEAGTGAKPGKSDTVTVEYTGTLIDGTVFDSTEKAGKPATFQVSQVIPGWTEALQLMPAGS 192
Cdd:PRK11570  90 ENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIEALTLMPVGS 169
                        170
                 ....*....|....*...
gi 313870675 193 TWEIFVPSDLAYGPRSVG 210
Cdd:PRK11570 170 KWELTIPHELAYGERGAG 187
 
Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
34-210 4.68e-49

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 158.81  E-value: 4.68e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870675  34 SYSIGADLGKNFKNQGID-INPDALAKGMQDGMSGAQLILTEQQMKDVLNKFQKDLMAKRSAEFNKKAEEnkakGEAFLS 112
Cdd:PRK11570  14 SYGIGLQVGQQLSESGLEgLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAMAAE----GVKFLE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870675 113 TNKSKSGVVVLPSGLQYKIIEAGTGAKPGKSDTVTVEYTGTLIDGTVFDSTEKAGKPATFQVSQVIPGWTEALQLMPAGS 192
Cdd:PRK11570  90 ENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIEALTLMPVGS 169
                        170
                 ....*....|....*...
gi 313870675 193 TWEIFVPSDLAYGPRSVG 210
Cdd:PRK11570 170 KWELTIPHELAYGERGAG 187
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
127-211 2.04e-42

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 138.39  E-value: 2.04e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870675 127 LQYKIIEAGTGAKPGKSDTVTVEYTGTLIDGTVFDSTEKAGKPATFQVS--QVIPGWTEALQLMPAGSTWEIFVPSDLAY 204
Cdd:COG0545    1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80

                 ....*..
gi 313870675 205 GPRSVGG 211
Cdd:COG0545   81 GERGAGG 87
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
30-131 1.50e-35

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: 120.68  E-value: 1.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870675   30 KDKLSYSIGADLGKNFKNQGIDINPDALAKGMQDGMSGAQLiLTEQQMKDVLNKFQKDLMAKRSaefnKKAEENKAKGEA 109
Cdd:pfam01346   1 KDKVSYAIGLQIGQQLKQQGIELDLDAFLAGLKDALAGKPL-LTDEEAQEALQAFQEKLQAKQE----EQAEKNKAEGEA 75
                          90       100
                  ....*....|....*....|..
gi 313870675  110 FLSTNKSKSGVVVLPSGLQYKI 131
Cdd:pfam01346  76 FLAENKKKEGVKTTESGLQYKV 97
 
Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
34-210 4.68e-49

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 158.81  E-value: 4.68e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870675  34 SYSIGADLGKNFKNQGID-INPDALAKGMQDGMSGAQLILTEQQMKDVLNKFQKDLMAKRSAEFNKKAEEnkakGEAFLS 112
Cdd:PRK11570  14 SYGIGLQVGQQLSESGLEgLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAMAAE----GVKFLE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870675 113 TNKSKSGVVVLPSGLQYKIIEAGTGAKPGKSDTVTVEYTGTLIDGTVFDSTEKAGKPATFQVSQVIPGWTEALQLMPAGS 192
Cdd:PRK11570  90 ENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIEALTLMPVGS 169
                        170
                 ....*....|....*...
gi 313870675 193 TWEIFVPSDLAYGPRSVG 210
Cdd:PRK11570 170 KWELTIPHELAYGERGAG 187
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
127-211 2.04e-42

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 138.39  E-value: 2.04e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870675 127 LQYKIIEAGTGAKPGKSDTVTVEYTGTLIDGTVFDSTEKAGKPATFQVS--QVIPGWTEALQLMPAGSTWEIFVPSDLAY 204
Cdd:COG0545    1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80

                 ....*..
gi 313870675 205 GPRSVGG 211
Cdd:COG0545   81 GERGAGG 87
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
7-211 5.88e-42

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 142.59  E-value: 5.88e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870675   7 AAIMGLAMST--AMAATDATSLV---------TDKDKLSYSIGADLGKNFKNQ-------GIDINPDALAKGMQDGMSGA 68
Cdd:PRK10902  11 ATTMAVALNApiTFAADAAKPAAtadskaafkNDDQQSAYALGASLGRYMENSlkeqeklGIKLDKDQLIAGVQDAFADK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870675  69 QLiLTEQQMKDVLNKFQKDLMAKRSAEFNKKAEENKAKGEAFLSTNKSKSGVVVLPSGLQYKIIEAGTGAKPGKSDTVTV 148
Cdd:PRK10902  91 SK-LSDQEIEQTLQAFEARVKSAAQAKMEKDAADNEAKGKKYREKFAKEKGVKTTSTGLLYKVEKEGTGEAPKDSDTVVV 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313870675 149 EYTGTLIDGTVFDSTEKAGKPATFQVSQVIPGWTEALQLMPAGSTWEIFVPSDLAYGPRSVGG 211
Cdd:PRK10902 170 NYKGTLIDGKEFDNSYTRGEPLSFRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPG 232
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
30-131 1.50e-35

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: 120.68  E-value: 1.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870675   30 KDKLSYSIGADLGKNFKNQGIDINPDALAKGMQDGMSGAQLiLTEQQMKDVLNKFQKDLMAKRSaefnKKAEENKAKGEA 109
Cdd:pfam01346   1 KDKVSYAIGLQIGQQLKQQGIELDLDAFLAGLKDALAGKPL-LTDEEAQEALQAFQEKLQAKQE----EQAEKNKAEGEA 75
                          90       100
                  ....*....|....*....|..
gi 313870675  110 FLSTNKSKSGVVVLPSGLQYKI 131
Cdd:pfam01346  76 FLAENKKKEGVKTTESGLQYKV 97
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
139-211 7.78e-26

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 95.73  E-value: 7.78e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313870675  139 KPGKSDTVTVEYTGTLIDGTVFDSTEKAGKPATFQV--SQVIPGWTEALQLMPAGSTWEIFVPSDLAYGPRSVGG 211
Cdd:pfam00254   4 KAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLgsGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAG 78
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
144-207 1.12e-13

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 65.12  E-value: 1.12e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313870675 144 DTVTVEYTGTLIDGTVFDSTEKaGKPATFQV--SQVIPGWTEALQLMPAGSTWEIFVPSDLAYGPR 207
Cdd:COG1047    5 DVVTLHYTLKLEDGEVFDSTFE-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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