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Conserved domains on  [gi|2627450|gb|AAB86700|]
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macrophage infectivity potentiator protein, partial [Legionella sp. J]

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
23-205 5.71e-50

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: 161.12  E-value: 5.71e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627450    23 SLNSDMDKLSYSIGADLGKNFKKQGIE-ISPAAMAKGLQDGMSGGQLLLTEQQMKDVLNKFQKDLMAKRNAEFTKKAEEn 101
Cdd:PRK11570   5 TFDSIEAQASYGIGLQVGQQLSESGLEgLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAMAAE- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627450   102 kakGEAFMSQNKAKEGVVSLPSGLQYKIIQTGTGAKPAKDDTVTVEYTGKLIDGQVFDSTEKTGKPATFKVSQVIPGWTE 181
Cdd:PRK11570  84 ---GVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIE 160
                        170       180
                 ....*....|....*....|....
gi 2627450   182 ALQLMPAGSTWEVYVPAGLAYGPR 205
Cdd:PRK11570 161 ALTLMPVGSKWELTIPHELAYGER 184
 
Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
23-205 5.71e-50

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 161.12  E-value: 5.71e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627450    23 SLNSDMDKLSYSIGADLGKNFKKQGIE-ISPAAMAKGLQDGMSGGQLLLTEQQMKDVLNKFQKDLMAKRNAEFTKKAEEn 101
Cdd:PRK11570   5 TFDSIEAQASYGIGLQVGQQLSESGLEgLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAMAAE- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627450   102 kakGEAFMSQNKAKEGVVSLPSGLQYKIIQTGTGAKPAKDDTVTVEYTGKLIDGQVFDSTEKTGKPATFKVSQVIPGWTE 181
Cdd:PRK11570  84 ---GVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIE 160
                        170       180
                 ....*....|....*....|....
gi 2627450   182 ALQLMPAGSTWEVYVPAGLAYGPR 205
Cdd:PRK11570 161 ALTLMPVGSKWELTIPHELAYGER 184
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
125-205 5.90e-40

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 132.23  E-value: 5.90e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627450  125 LQYKIIQTGTGAKPAKDDTVTVEYTGKLIDGQVFDSTEKTGKPATFKVS--QVIPGWTEALQLMPAGSTWEVYVPAGLAY 202
Cdd:COG0545   1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80

                ...
gi 2627450  203 GPR 205
Cdd:COG0545  81 GER 83
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
28-129 4.26e-33

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: 114.13  E-value: 4.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627450     28 MDKLSYSIGADLGKNFKKQGIEISPAAMAKGLQDGMSGgQLLLTEQQMKDVLNKFQKDLMAKRNaeftKKAEENKAKGEA 107
Cdd:pfam01346   1 KDKVSYAIGLQIGQQLKQQGIELDLDAFLAGLKDALAG-KPLLTDEEAQEALQAFQEKLQAKQE----EQAEKNKAEGEA 75
                          90       100
                  ....*....|....*....|..
gi 2627450    108 FMSQNKAKEGVVSLPSGLQYKI 129
Cdd:pfam01346  76 FLAENKKKEGVKTTESGLQYKV 97
 
Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
23-205 5.71e-50

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 161.12  E-value: 5.71e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627450    23 SLNSDMDKLSYSIGADLGKNFKKQGIE-ISPAAMAKGLQDGMSGGQLLLTEQQMKDVLNKFQKDLMAKRNAEFTKKAEEn 101
Cdd:PRK11570   5 TFDSIEAQASYGIGLQVGQQLSESGLEgLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAMAAE- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627450   102 kakGEAFMSQNKAKEGVVSLPSGLQYKIIQTGTGAKPAKDDTVTVEYTGKLIDGQVFDSTEKTGKPATFKVSQVIPGWTE 181
Cdd:PRK11570  84 ---GVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIE 160
                        170       180
                 ....*....|....*....|....
gi 2627450   182 ALQLMPAGSTWEVYVPAGLAYGPR 205
Cdd:PRK11570 161 ALTLMPVGSKWELTIPHELAYGER 184
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
125-205 5.90e-40

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 132.23  E-value: 5.90e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627450  125 LQYKIIQTGTGAKPAKDDTVTVEYTGKLIDGQVFDSTEKTGKPATFKVS--QVIPGWTEALQLMPAGSTWEVYVPAGLAY 202
Cdd:COG0545   1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80

                ...
gi 2627450  203 GPR 205
Cdd:COG0545  81 GER 83
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
3-207 4.23e-35

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 124.88  E-value: 4.23e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627450     3 AVISMAMSTTIAAADATATTSLNSDMDKLSYSIGADLG-------KNFKKQGIEISPAAMAKGLQDGMSGgQLLLTEQQM 75
Cdd:PRK10902  20 APITFAADAAKPAATADSKAAFKNDDQQSAYALGASLGrymenslKEQEKLGIKLDKDQLIAGVQDAFAD-KSKLSDQEI 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627450    76 KDVLNKFQKDLMAKRNAEFTKKAEENKAKGEAFMSQNKAKEGVVSLPSGLQYKIIQTGTGAKPAKDDTVTVEYTGKLIDG 155
Cdd:PRK10902  99 EQTLQAFEARVKSAAQAKMEKDAADNEAKGKKYREKFAKEKGVKTTSTGLLYKVEKEGTGEAPKDSDTVVVNYKGTLIDG 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 2627450   156 QVFDSTEKTGKPATFKVSQVIPGWTEALQLMPAGSTWEVYVPAGLAYGPRSV 207
Cdd:PRK10902 179 KEFDNSYTRGEPLSFRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGV 230
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
28-129 4.26e-33

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: 114.13  E-value: 4.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627450     28 MDKLSYSIGADLGKNFKKQGIEISPAAMAKGLQDGMSGgQLLLTEQQMKDVLNKFQKDLMAKRNaeftKKAEENKAKGEA 107
Cdd:pfam01346   1 KDKVSYAIGLQIGQQLKQQGIELDLDAFLAGLKDALAG-KPLLTDEEAQEALQAFQEKLQAKQE----EQAEKNKAEGEA 75
                          90       100
                  ....*....|....*....|..
gi 2627450    108 FMSQNKAKEGVVSLPSGLQYKI 129
Cdd:pfam01346  76 FLAENKKKEGVKTTESGLQYKV 97
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
137-207 3.47e-25

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 93.80  E-value: 3.47e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2627450    137 KPAKDDTVTVEYTGKLIDGQVFDSTEKTGKPATFKV--SQVIPGWTEALQLMPAGSTWEVYVPAGLAYGPRSV 207
Cdd:pfam00254   4 KAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLgsGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGL 76
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
139-205 2.92e-15

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 69.36  E-value: 2.92e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2627450  139 AKDDTVTVEYTGKLIDGQVFDSTEKtGKPATFKV--SQVIPGWTEALQLMPAGSTWEVYVPAGLAYGPR 205
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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