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Conserved domains on  [gi|1084737144|gb|OGP80352|]
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hypothetical protein A2Z26_04780 [Deltaproteobacteria bacterium RBG_16_66_15]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 11433571)

peptidylprolyl isomerase (PPIase) accelerates the folding of proteins; it catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides

CATH:  3.10.50.40
EC:  5.2.1.8
Gene Ontology:  GO:0003755|GO:0006457
PubMed:  12871165
SCOP:  3000622

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
181-306 5.76e-14

Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 68.06  E-value: 5.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737144 181 TVPERIRVRQYLFDSAGPAAVA---------REKLLAGGP---------AGGDPASEGVDLGFFRREELPPELPAELFGL 242
Cdd:COG0760     4 DSPEEVRASHILVKVPPSEDRAkaeakaeelLAQLKAGADfaelakeysQDPGSAANGGDLGWFSRGQLVPEFEEAAFAL 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084737144 243 PEGGVSEPVPGDGVVSLFRITQREAARTRTLRSEETRIREAIlaprREEAFRRWLAQATAGAKV 306
Cdd:COG0760    84 KPGEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQEL----FQQALEAWLEELRKKAKI 143
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
181-306 5.76e-14

Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 68.06  E-value: 5.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737144 181 TVPERIRVRQYLFDSAGPAAVA---------REKLLAGGP---------AGGDPASEGVDLGFFRREELPPELPAELFGL 242
Cdd:COG0760     4 DSPEEVRASHILVKVPPSEDRAkaeakaeelLAQLKAGADfaelakeysQDPGSAANGGDLGWFSRGQLVPEFEEAAFAL 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084737144 243 PEGGVSEPVPGDGVVSLFRITQREAARTRTLRSEETRIREAIlaprREEAFRRWLAQATAGAKV 306
Cdd:COG0760    84 KPGEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQEL----FQQALEAWLEELRKKAKI 143
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
164-273 3.15e-11

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 59.76  E-value: 3.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737144 164 VTPQEVEAAFRKERDPGTVPERIRVRQYLFDSAGPAAVAREKLLAGgpAGGDPAS-------EGVDLGFFRREE-LPPEL 235
Cdd:pfam13145   1 VTEEELKAYYEENKDEFSTPEGRLLEILVFKDQVAADAALALLKAG--ALEDFAAlakgegiKAATLDIVESAElLPEEL 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1084737144 236 PAELFGLPEGGVSEPVPGDGVVSLFRITQREAARTRTL 273
Cdd:pfam13145  79 AKAAFALKPGEVSGPIKTGNGYYVVRVTEIKPAQPLPF 116
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
181-306 5.76e-14

Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 68.06  E-value: 5.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737144 181 TVPERIRVRQYLFDSAGPAAVA---------REKLLAGGP---------AGGDPASEGVDLGFFRREELPPELPAELFGL 242
Cdd:COG0760     4 DSPEEVRASHILVKVPPSEDRAkaeakaeelLAQLKAGADfaelakeysQDPGSAANGGDLGWFSRGQLVPEFEEAAFAL 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084737144 243 PEGGVSEPVPGDGVVSLFRITQREAARTRTLRSEETRIREAIlaprREEAFRRWLAQATAGAKV 306
Cdd:COG0760    84 KPGEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQEL----FQQALEAWLEELRKKAKI 143
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
164-273 3.15e-11

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 59.76  E-value: 3.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737144 164 VTPQEVEAAFRKERDPGTVPERIRVRQYLFDSAGPAAVAREKLLAGgpAGGDPAS-------EGVDLGFFRREE-LPPEL 235
Cdd:pfam13145   1 VTEEELKAYYEENKDEFSTPEGRLLEILVFKDQVAADAALALLKAG--ALEDFAAlakgegiKAATLDIVESAElLPEEL 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1084737144 236 PAELFGLPEGGVSEPVPGDGVVSLFRITQREAARTRTL 273
Cdd:pfam13145  79 AKAAFALKPGEVSGPIKTGNGYYVVRVTEIKPAQPLPF 116
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
217-251 5.42e-06

PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.


Pssm-ID: 425792 [Multi-domain]  Cd Length: 96  Bit Score: 44.21  E-value: 5.42e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1084737144 217 ASEGVDLGFFRREELPPELPAELFGLPEGGVSEPV 251
Cdd:pfam00639  49 AANGGDLGWFTRGQLPPEFEKAAFALKPGEISGPV 83
 
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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