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Conserved domains on  [gi|313870705|gb|ADR82237|]
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macrophage infectivity potentiator, partial [Legionella sp. ST18590]

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
48-224 1.32e-51

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: 166.13  E-value: 1.32e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870705  48 SYSIGADLGKNFKKQGIE-ISPSAMAKGLQDGMSGSQLLLTEDQMKDVLSKFQKDLMAKRNAEFTKKAEEnkskGEAFLS 126
Cdd:PRK11570  14 SYGIGLQVGQQLSESGLEgLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAMAAE----GVKFLE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870705 127 QNKTKEGVVTLPSGLQYKIIEKGNGAKPSKEDTVTVEYTGRLIDGQVFDSTDKTGKPATFKVSQVIPGWTEALQLMPAGS 206
Cdd:PRK11570  90 ENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIEALTLMPVGS 169
                        170
                 ....*....|....*...
gi 313870705 207 VWEVYVPASLAYGPRSVG 224
Cdd:PRK11570 170 KWELTIPHELAYGERGAG 187
 
Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
48-224 1.32e-51

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 166.13  E-value: 1.32e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870705  48 SYSIGADLGKNFKKQGIE-ISPSAMAKGLQDGMSGSQLLLTEDQMKDVLSKFQKDLMAKRNAEFTKKAEEnkskGEAFLS 126
Cdd:PRK11570  14 SYGIGLQVGQQLSESGLEgLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAMAAE----GVKFLE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870705 127 QNKTKEGVVTLPSGLQYKIIEKGNGAKPSKEDTVTVEYTGRLIDGQVFDSTDKTGKPATFKVSQVIPGWTEALQLMPAGS 206
Cdd:PRK11570  90 ENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIEALTLMPVGS 169
                        170
                 ....*....|....*...
gi 313870705 207 VWEVYVPASLAYGPRSVG 224
Cdd:PRK11570 170 KWELTIPHELAYGERGAG 187
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
141-225 4.98e-40

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 133.00  E-value: 4.98e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870705 141 LQYKIIEKGNGAKPSKEDTVTVEYTGRLIDGQVFDSTDKTGKPATFKVS--QVIPGWTEALQLMPAGSVWEVYVPASLAY 218
Cdd:COG0545    1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80

                 ....*..
gi 313870705 219 GPRSVGG 225
Cdd:COG0545   81 GERGAGG 87
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
45-145 5.10e-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: 5.10e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870705   45 DKLSYSIGADLGKNFKKQGIEISPSAMAKGLQDGMSGsQLLLTEDQMKDVLSKFQKDLMAKRNaeftKKAEENKSKGEAF 124
Cdd:pfam01346   2 DKVSYAIGLQIGQQLKQQGIELDLDAFLAGLKDALAG-KPLLTDEEAQEALQAFQEKLQAKQE----EQAEKNKAEGEAF 76
                          90       100
                  ....*....|....*....|.
gi 313870705  125 LSQNKTKEGVVTLPSGLQYKI 145
Cdd:pfam01346  77 LAENKKKEGVKTTESGLQYKV 97
 
Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
48-224 1.32e-51

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 166.13  E-value: 1.32e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870705  48 SYSIGADLGKNFKKQGIE-ISPSAMAKGLQDGMSGSQLLLTEDQMKDVLSKFQKDLMAKRNAEFTKKAEEnkskGEAFLS 126
Cdd:PRK11570  14 SYGIGLQVGQQLSESGLEgLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAMAAE----GVKFLE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870705 127 QNKTKEGVVTLPSGLQYKIIEKGNGAKPSKEDTVTVEYTGRLIDGQVFDSTDKTGKPATFKVSQVIPGWTEALQLMPAGS 206
Cdd:PRK11570  90 ENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIEALTLMPVGS 169
                        170
                 ....*....|....*...
gi 313870705 207 VWEVYVPASLAYGPRSVG 224
Cdd:PRK11570 170 KWELTIPHELAYGERGAG 187
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
141-225 4.98e-40

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 133.00  E-value: 4.98e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870705 141 LQYKIIEKGNGAKPSKEDTVTVEYTGRLIDGQVFDSTDKTGKPATFKVS--QVIPGWTEALQLMPAGSVWEVYVPASLAY 218
Cdd:COG0545    1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80

                 ....*..
gi 313870705 219 GPRSVGG 225
Cdd:COG0545   81 GERGAGG 87
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
43-225 4.17e-34

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 122.95  E-value: 4.17e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870705  43 DIDKLSYSIGADLG-------KNFKKQGIEISPSAMAKGLQDGMSGSQLLlTEDQMKDVLSKFQKDLMAKRNAEFTKKAE 115
Cdd:PRK10902  44 DDQQSAYALGASLGrymenslKEQEKLGIKLDKDQLIAGVQDAFADKSKL-SDQEIEQTLQAFEARVKSAAQAKMEKDAA 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870705 116 ENKSKGEAFLSQNKTKEGVVTLPSGLQYKIIEKGNGAKPSKEDTVTVEYTGRLIDGQVFDSTDKTGKPATFKVSQVIPGW 195
Cdd:PRK10902 123 DNEAKGKKYREKFAKEKGVKTTSTGLLYKVEKEGTGEAPKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDGVIPGW 202
                        170       180       190
                 ....*....|....*....|....*....|
gi 313870705 196 TEALQLMPAGSVWEVYVPASLAYGPRSVGG 225
Cdd:PRK10902 203 TEGLKNIKKGGKIKLVIPPELAYGKAGVPG 232
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
45-145 5.10e-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: 5.10e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870705   45 DKLSYSIGADLGKNFKKQGIEISPSAMAKGLQDGMSGsQLLLTEDQMKDVLSKFQKDLMAKRNaeftKKAEENKSKGEAF 124
Cdd:pfam01346   2 DKVSYAIGLQIGQQLKQQGIELDLDAFLAGLKDALAG-KPLLTDEEAQEALQAFQEKLQAKQE----EQAEKNKAEGEAF 76
                          90       100
                  ....*....|....*....|.
gi 313870705  125 LSQNKTKEGVVTLPSGLQYKI 145
Cdd:pfam01346  77 LAENKKKEGVKTTESGLQYKV 97
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
153-226 2.05e-25

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 94.96  E-value: 2.05e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313870705  153 KPSKEDTVTVEYTGRLIDGQVFDSTDKTGKPATFKV--SQVIPGWTEALQLMPAGSVWEVYVPASLAYGPRSVGGP 226
Cdd:pfam00254   4 KAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLgsGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGP 79
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
155-221 1.68e-12

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 62.43  E-value: 1.68e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 313870705 155 SKEDTVTVEYTGRLIDGQVFDSTDKtGKPATFKV--SQVIPGWTEALQLMPAGSVWEVYVPASLAYGPR 221
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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