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Conserved domains on  [gi|2627444|gb|AAB86697|]
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macrophage infectivity potentiator protein, partial [Legionella sp. G]

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
14-203 1.14e-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: 160.35  E-value: 1.14e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627444    14 MAAPdatSLPTDKDKLSYSIGADLGKNFKTQGID-ISPEALAKGMQDGMSGTQLILTEQQMKDVLNKFQKDLMAKRTSEF 92
Cdd:PRK11570   1 MTTP---TFDSIEAQASYGIGLQVGQQLSESGLEgLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627444    93 NKKADEnkskGEAFLVENKSKTGVVVLPSGLQYKIIDAGTGAKPGKADTVTVEYTGRLIDGTVFDSTDKTGKPATFQVSQ 172
Cdd:PRK11570  78 QAMAAE----GVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG 153
                        170       180       190
                 ....*....|....*....|....*....|.
gi 2627444   173 VIPGWTEALQLMPAGSTWEIYVPSALAYGSR 203
Cdd:PRK11570 154 VIPGWIEALTLMPVGSKWELTIPHELAYGER 184
 
Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
14-203 1.14e-49

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 160.35  E-value: 1.14e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627444    14 MAAPdatSLPTDKDKLSYSIGADLGKNFKTQGID-ISPEALAKGMQDGMSGTQLILTEQQMKDVLNKFQKDLMAKRTSEF 92
Cdd:PRK11570   1 MTTP---TFDSIEAQASYGIGLQVGQQLSESGLEgLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627444    93 NKKADEnkskGEAFLVENKSKTGVVVLPSGLQYKIIDAGTGAKPGKADTVTVEYTGRLIDGTVFDSTDKTGKPATFQVSQ 172
Cdd:PRK11570  78 QAMAAE----GVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG 153
                        170       180       190
                 ....*....|....*....|....*....|.
gi 2627444   173 VIPGWTEALQLMPAGSTWEIYVPSALAYGSR 203
Cdd:PRK11570 154 VIPGWIEALTLMPVGSKWELTIPHELAYGER 184
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
123-203 3.74e-40

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 132.61  E-value: 3.74e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627444  123 LQYKIIDAGTGAKPGKADTVTVEYTGRLIDGTVFDSTDKTGKPATFQVS--QVIPGWTEALQLMPAGSTWEIYVPSALAY 200
Cdd:COG0545   1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80

                ...
gi 2627444  201 GSR 203
Cdd:COG0545  81 GER 83
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
26-127 3.94e-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: 119.52  E-value: 3.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627444     26 KDKLSYSIGADLGKNFKTQGIDISPEALAKGMQDGMSGTQLiLTEQQMKDVLNKFQKDLMAKRtsefNKKADENKSKGEA 105
Cdd:pfam01346   1 KDKVSYAIGLQIGQQLKQQGIELDLDAFLAGLKDALAGKPL-LTDEEAQEALQAFQEKLQAKQ----EEQAEKNKAEGEA 75
                          90       100
                  ....*....|....*....|..
gi 2627444    106 FLVENKSKTGVVVLPSGLQYKI 127
Cdd:pfam01346  76 FLAENKKKEGVKTTESGLQYKV 97
 
Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
14-203 1.14e-49

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 160.35  E-value: 1.14e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627444    14 MAAPdatSLPTDKDKLSYSIGADLGKNFKTQGID-ISPEALAKGMQDGMSGTQLILTEQQMKDVLNKFQKDLMAKRTSEF 92
Cdd:PRK11570   1 MTTP---TFDSIEAQASYGIGLQVGQQLSESGLEgLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627444    93 NKKADEnkskGEAFLVENKSKTGVVVLPSGLQYKIIDAGTGAKPGKADTVTVEYTGRLIDGTVFDSTDKTGKPATFQVSQ 172
Cdd:PRK11570  78 QAMAAE----GVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG 153
                        170       180       190
                 ....*....|....*....|....*....|.
gi 2627444   173 VIPGWTEALQLMPAGSTWEIYVPSALAYGSR 203
Cdd:PRK11570 154 VIPGWIEALTLMPVGSKWELTIPHELAYGER 184
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
123-203 3.74e-40

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 132.61  E-value: 3.74e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627444  123 LQYKIIDAGTGAKPGKADTVTVEYTGRLIDGTVFDSTDKTGKPATFQVS--QVIPGWTEALQLMPAGSTWEIYVPSALAY 200
Cdd:COG0545   1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80

                ...
gi 2627444  201 GSR 203
Cdd:COG0545  81 GER 83
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
3-205 1.02e-38

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 134.12  E-value: 1.02e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627444     3 AAVMGLALST--AMAAPDATSLP---------TDKDKLSYSIGADLGK----NFKTQ---GIDISPEALAKGMQDGMSGT 64
Cdd:PRK10902  11 ATTMAVALNApiTFAADAAKPAAtadskaafkNDDQQSAYALGASLGRymenSLKEQeklGIKLDKDQLIAGVQDAFADK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627444    65 QLiLTEQQMKDVLNKFQKDLMAKRTSEFNKKADENKSKGEAFLVENKSKTGVVVLPSGLQYKIIDAGTGAKPGKADTVTV 144
Cdd:PRK10902  91 SK-LSDQEIEQTLQAFEARVKSAAQAKMEKDAADNEAKGKKYREKFAKEKGVKTTSTGLLYKVEKEGTGEAPKDSDTVVV 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2627444   145 EYTGRLIDGTVFDSTDKTGKPATFQVSQVIPGWTEALQLMPAGSTWEIYVPSALAYGSRSV 205
Cdd:PRK10902 170 NYKGTLIDGKEFDNSYTRGEPLSFRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGV 230
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
26-127 3.94e-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: 119.52  E-value: 3.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2627444     26 KDKLSYSIGADLGKNFKTQGIDISPEALAKGMQDGMSGTQLiLTEQQMKDVLNKFQKDLMAKRtsefNKKADENKSKGEA 105
Cdd:pfam01346   1 KDKVSYAIGLQIGQQLKQQGIELDLDAFLAGLKDALAGKPL-LTDEEAQEALQAFQEKLQAKQ----EEQAEKNKAEGEA 75
                          90       100
                  ....*....|....*....|..
gi 2627444    106 FLVENKSKTGVVVLPSGLQYKI 127
Cdd:pfam01346  76 FLAENKKKEGVKTTESGLQYKV 97
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
135-205 2.28e-25

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 94.19  E-value: 2.28e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2627444    135 KPGKADTVTVEYTGRLIDGTVFDSTDKTGKPATFQV--SQVIPGWTEALQLMPAGSTWEIYVPSALAYGSRSV 205
Cdd:pfam00254   4 KAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLgsGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGL 76
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
140-203 2.18e-12

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 61.66  E-value: 2.18e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2627444  140 DTVTVEYTGRLIDGTVFDSTDKtGKPATFQV--SQVIPGWTEALQLMPAGSTWEIYVPSALAYGSR 203
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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