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Conserved domains on  [gi|1382179207|ref|WP_108046358|]
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peptidylprolyl isomerase [Bosea sp. 124]

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, ...
 133-261 3.42e-50

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


:

Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 162.05  E-value: 3.42e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207 133 EEEVNARHILV---------EDEAQAKAVAERLKKGEDFAKVAAELSKDPGSGKEGGSLGWFTKDRMVPEFAEVAFKLTK 203
Cdd:COG0760     6 PEEVRASHILVkvppsedraKAEAKAEELLAQLKAGADFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEAAFALKP 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1382179207 204 GQVSDPVKSQFGWHVIKLEDKRAKPLPDFAAVKPQIDQYLERKAQQDIIVALREKAKI 261
Cdd:COG0760    86 GEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQELFQQALEAWLEELRKKAKI 143
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 133-261 3.42e-50

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 162.05  E-value: 3.42e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207 133 EEEVNARHILV---------EDEAQAKAVAERLKKGEDFAKVAAELSKDPGSGKEGGSLGWFTKDRMVPEFAEVAFKLTK 203
Cdd:COG0760     6 PEEVRASHILVkvppsedraKAEAKAEELLAQLKAGADFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEAAFALKP 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1382179207 204 GQVSDPVKSQFGWHVIKLEDKRAKPLPDFAAVKPQIDQYLERKAQQDIIVALREKAKI 261
Cdd:COG0760    86 GEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQELFQQALEAWLEELRKKAKI 143
prsA PRK00059
peptidylprolyl isomerase; Provisional
 115-262 4.12e-34

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 126.36  E-value: 4.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207 115 TPEAAKKLYDET-TKGMAPEEEVNARHILVEDEAQAKAVAERLKKGEDFAKVAAELSKDPGSGKEGGSLGW--FTKDRMV 191
Cdd:PRK00059  175 TDKDAQKYYNENkSKFTEKPNTMHLAHILVKTEDEAKKVKKRLDKGEDFAKVAKEVSQDPGSKDKGGDLGDvpYSDSGYD 254

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382179207 192 PEFAEVAFKLTKGQVSDPVKSQFGWHVIKLEDKRAKPLPDFAAVKPQIDQYLERKAQQDIIvalreKAKIE 262
Cdd:PRK00059  255 KEFMDGAKALKEGEISAPVKTQFGYHIIKAIKKKEYPVKPFDSVKEDIKKQLLQEKQSEVF-----KKKIE 320
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 118-225 5.28e-32

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


Pssm-ID: 404499 [Multi-domain]  Cd Length: 116  Bit Score: 114.39  E-value: 5.28e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207 118 AAKKLYDETTKGmapeEEVNARHILV---------EDEAQAKA--VAERLKKGEDFAKVAAELSKDPGSGKEGGSLGWFT 186
Cdd:pfam13616   2 SLSKLVDKKSAP----DSVKASHILIsysqavsrtEEEAKAKAdsLLAALKNGADFAALAKTYSDDPASKNNGGDLGWFT 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1382179207 187 KDRMVPEFAEVAFKLTKGQVSDPVKSQFGWHVIKLEDKR 225
Cdd:pfam13616  78 KGQMVKEFEDAVFSLKVGEISGVVKTQFGFHIIKVTDKK 116
nifM_nitrog TIGR02933
nitrogen fixation protein NifM; Members of this protein family, found in a subset of ...
 85-249 2.76e-11

nitrogen fixation protein NifM; Members of this protein family, found in a subset of nitrogen-fixing bacteria, are the nitrogen fixation protein NifM. NifM, homologous to peptidyl-prolyl cis-trans isomerases, appears to be an accessory protein for NifH, the Fe protein, also called component II or dinitrogenase reductase, of nitrogenase. [Central intermediary metabolism, Nitrogen fixation]


Pssm-ID: 131979 [Multi-domain]  Cd Length: 256  Bit Score: 62.17  E-value: 2.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207  85 DSPDFTA--RLAYFREKVLLDQFLTAEAKKAATPEAAK-KLY--DETTKGMAPEEEVNaRHILV---EDEAQA-----KA 151
Cdd:TIGR02933  69 DEQALDAaeRRAMLAHHLRLEAQLACVCAQAPQPDDADvEAWyrRHAEQFKRPEQRLT-RHLLLtvnEDDREAvrtriLA 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207 152 VAERLKKGED-FAKVAAELSKDPgSGKEGGSLGWFTKDRMVPEFAEVAFKLTKGQVSDPVKSQFGWHVIKLEDKR-AKPL 229
Cdd:TIGR02933 148 ILRRLRGKPAaFAEQAMRHSHCP-TAMEGGLLGWVSRGLLYPQLDAALFQLAEGELSPPIESEIGWHLLLCEAIRpARPL 226

                         170       180
                  ....*....|....*....|...
gi 1382179207 230 PDFAAVkPQIDQYL---ERKAQQ 249
Cdd:TIGR02933 227 TLEEAL-PRARDRLqlrQQKAYQ 248
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 133-261 3.42e-50

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 162.05  E-value: 3.42e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207 133 EEEVNARHILV---------EDEAQAKAVAERLKKGEDFAKVAAELSKDPGSGKEGGSLGWFTKDRMVPEFAEVAFKLTK 203
Cdd:COG0760     6 PEEVRASHILVkvppsedraKAEAKAEELLAQLKAGADFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEAAFALKP 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1382179207 204 GQVSDPVKSQFGWHVIKLEDKRAKPLPDFAAVKPQIDQYLERKAQQDIIVALREKAKI 261
Cdd:COG0760    86 GEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQELFQQALEAWLEELRKKAKI 143
prsA PRK00059
peptidylprolyl isomerase; Provisional
 115-262 4.12e-34

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 126.36  E-value: 4.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207 115 TPEAAKKLYDET-TKGMAPEEEVNARHILVEDEAQAKAVAERLKKGEDFAKVAAELSKDPGSGKEGGSLGW--FTKDRMV 191
Cdd:PRK00059  175 TDKDAQKYYNENkSKFTEKPNTMHLAHILVKTEDEAKKVKKRLDKGEDFAKVAKEVSQDPGSKDKGGDLGDvpYSDSGYD 254

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1382179207 192 PEFAEVAFKLTKGQVSDPVKSQFGWHVIKLEDKRAKPLPDFAAVKPQIDQYLERKAQQDIIvalreKAKIE 262
Cdd:PRK00059  255 KEFMDGAKALKEGEISAPVKTQFGYHIIKAIKKKEYPVKPFDSVKEDIKKQLLQEKQSEVF-----KKKIE 320
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 118-225 5.28e-32

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


Pssm-ID: 404499 [Multi-domain]  Cd Length: 116  Bit Score: 114.39  E-value: 5.28e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207 118 AAKKLYDETTKGmapeEEVNARHILV---------EDEAQAKA--VAERLKKGEDFAKVAAELSKDPGSGKEGGSLGWFT 186
Cdd:pfam13616   2 SLSKLVDKKSAP----DSVKASHILIsysqavsrtEEEAKAKAdsLLAALKNGADFAALAKTYSDDPASKNNGGDLGWFT 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1382179207 187 KDRMVPEFAEVAFKLTKGQVSDPVKSQFGWHVIKLEDKR 225
Cdd:pfam13616  78 KGQMVKEFEDAVFSLKVGEISGVVKTQFGFHIIKVTDKK 116
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 140-223 5.97e-28

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: 103.15  E-value: 5.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207 140 HILV-----------EDEAQAKAVAERLKKGED-FAKVAAELSKDPGSGKEGGSLGWFTKDRMVPEFAEVAFKLTKGQVS 207
Cdd:pfam00639   1 HILIktpeaserdraEAKAKAEEILEQLKSGEDsFAELARKYSDDCPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEIS 80

                          90
                  ....*....|....*.
gi 1382179207 208 DPVKSQFGWHVIKLED 223
Cdd:pfam00639  81 GPVETRFGFHIIKLTD 96
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 135-250 2.88e-27

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 106.98  E-value: 2.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207 135 EVNARHILVEDEAQAKAVAERLKKGEDFAKVAAELSKDPGSGKEGGSLGWFTKDRMVPEFAEVAFKLTKGQVSDPVKSQF 214
Cdd:PRK02998  134 EMKVSHILVKDEKTAKEVKEKVNNGEDFAALAKQYSEDTGSKEQGGEISGFAPGQTVKEFEEAAYKLDAGQVSEPVKTTY 213

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1382179207 215 GWHVIKLEDKraKPLPDFAAVKPQIDQYLERKAQQD 250
Cdd:PRK02998  214 GYHIIKVTDK--KELKPFDEVKDSIRKDLEQQRLQD 247
prsA PRK03095
peptidylprolyl isomerase PrsA;
111-250 3.86e-26

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 103.92  E-value: 3.86e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207 111 KKAATPEAAKKLYdettkgmapEEEVNARHILVEDEAQAKAVAERLKKGEDFAKVAAELSKDPGSGKEGGSLGWFTKDRM 190
Cdd:PRK03095  117 EKTITDKELKDNY---------KPEIKASHILVKDEATAKKVKEELGQGKSFEELAKQYSEDTGSKEKGGDLGFFGAGKM 187

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207 191 VPEFAEVAFKLTKGQVSDPVKSQFGWHVIKLEDKRAKPLPdFAAVKPQIDQYLERKAQQD 250
Cdd:PRK03095  188 VKEFEDAAYKLKKDEVSEPVKSQFGYHIIKVTDIKEPEKS-FEQSKADIKKELVQKKAQD 246
prsA PRK03002
peptidylprolyl isomerase PrsA;
112-250 2.02e-25

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 101.94  E-value: 2.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207 112 KAATPEAAKKLYDETTKGMAPEEEVNARHILVEDEAQAKAVAERLKKGEDFAKVAAELSKDPGSGKEGGSLGWFTKDRMV 191
Cdd:PRK03002  113 KLAMNEAIKKSVTEKDVKDHYKPEIKASHILVSDENEAKEIKKKLDAGASFEELAKQESQDLLSKEKGGDLGYFNSGRMA 192

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1382179207 192 PEFAEVAFKLTKGQVSDPVKSQFGWHVIKLEDKraKPLPDFAAVKPQIDQYLERKAQQD 250
Cdd:PRK03002  193 PEFETAAYKLKVGQISNPVKSPNGYHIIKLTDK--KDLKPYDEVKDSIRKNLEEERTAD 249
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 135-225 5.60e-24

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 100.20  E-value: 5.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207 135 EVNARHILV-------EDEAQAK--AVAERLKKGE-DFAKVAAELSKDPGSGKEGGSLGWFTKDRMVPEFAEVAFKLTKG 204
Cdd:PRK10770  266 EVHARHILLkpspimtDEQARAKleQIAADIKSGKtTFAAAAKEFSQDPGSANQGGDLGWATPDIFDPAFRDALMRLNKG 345

                          90       100
                  ....*....|....*....|.
gi 1382179207 205 QVSDPVKSQFGWHVIKLEDKR 225
Cdd:PRK10770  346 QISAPVHSSFGWHLIELLDTR 366
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 141-258 1.21e-18

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 85.45  E-value: 1.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207 141 ILVEDEAQAKAVAERLKKGEDFAKVAAELSKDPGSGKEGGSLGWFTKDRMVPEFAEVAFKlTKGQVSDPVKSQFGWHVIK 220
Cdd:PRK10788  276 IQTKTEAEAKAVLDELKKGADFATLAKEKSTDIISARNGGDLGWLEPATTPDELKNAGLK-EKGQLSGVIKSSVGFLIVR 354

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1382179207 221 LED---KRAKPLpdfAAVKPQIDQYLERKAQQDIIVALREK 258
Cdd:PRK10788  355 LDDiqpAKVKPL---SEVRDDIAAKVKQEKALDAYYALQQK 392
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 138-221 1.94e-16

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 72.75  E-value: 1.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207 138 ARHILVEDEAQAKAVAERLKKGEDFAKVAAELSKDPgSGKEGGSLGWFTKDRMVPEFAEVAFKLTKGQVSDPVKSQFGWH 217
Cdd:PRK15441    7 ALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICP-SGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGYH 85


                  ....
gi 1382179207 218 VIKL 221
Cdd:PRK15441   86 IIKV 89
prsA PRK04405
peptidylprolyl isomerase; Provisional
 133-250 5.35e-16

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 76.36  E-value: 5.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207 133 EEEVNARHILVEDEAQAKAVAERLKKGEDFAKVAAELSKDPGSGKEGGSLGWF--TKDRMVPEFAEVAFKLTKGQV-SDP 209
Cdd:PRK04405  142 QPKVTVQHILVSKKSTAETVIKKLKDGKDFAKLAKKYSTDTATKNKGGKLSAFdsTDTTLDSTFKTAAFKLKNGEYtTTP 221

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1382179207 210 VKSQFGWHVIKLEDKRAKplPDFAAVKPQIDQYLERKAQQD 250
Cdd:PRK04405  222 VKTTYGYEVIKMIKHPAK--GTFSDHKKALTKQIYAKWASD 260
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
115-237 4.29e-14

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 67.47  E-value: 4.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207 115 TPEAAKKLYDETtKGMAPEEEVNARHILVEDEAQAKAVAERLKKGEDFAKVAAELSkdpGSGKEGGSLGWFTKDRMVP-E 193
Cdd:pfam13145   2 TEEELKAYYEEN-KDEFSTPEGRLLEILVFKDQVAADAALALLKAGALEDFAALAK---GEGIKAATLDIVESAELLPeE 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1382179207 194 FAEVAFKLTKGQVSDPVKSQFGWHVIKLEDKRAKPLPDFAAVKP 237
Cdd:pfam13145  78 LAKAAFALKPGEVSGPIKTGNGYYVVRVTEIKPAQPLPFEEAKD 121
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 134-220 3.22e-12

peptidyl-prolyl cis-trans isomerase (PPIase); Provisional


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 61.97  E-value: 3.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207 134 EEVNARHILVE--------------------DEAQA--KAVAERLKKGE-DFAKVAAELSkDPGSGKEGGSLGWFTKDRM 190
Cdd:PTZ00356    4 DTVRAAHLLIKhtgsrnpvsrrtgkpvtrskEEAIKelAKWREQIVSGEkTFEEIARQRS-DCGSAAKGGDLGFFGRGQM 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1382179207 191 VPEFAEVAFKLTKGQVSDPVKSQFGWHVIK 220
Cdd:PTZ00356   83 QKPFEDAAFALKVGEISDIVHTDSGVHIIL 112
nifM_nitrog TIGR02933
nitrogen fixation protein NifM; Members of this protein family, found in a subset of ...
 85-249 2.76e-11

nitrogen fixation protein NifM; Members of this protein family, found in a subset of nitrogen-fixing bacteria, are the nitrogen fixation protein NifM. NifM, homologous to peptidyl-prolyl cis-trans isomerases, appears to be an accessory protein for NifH, the Fe protein, also called component II or dinitrogenase reductase, of nitrogenase. [Central intermediary metabolism, Nitrogen fixation]


Pssm-ID: 131979 [Multi-domain]  Cd Length: 256  Bit Score: 62.17  E-value: 2.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207  85 DSPDFTA--RLAYFREKVLLDQFLTAEAKKAATPEAAK-KLY--DETTKGMAPEEEVNaRHILV---EDEAQA-----KA 151
Cdd:TIGR02933  69 DEQALDAaeRRAMLAHHLRLEAQLACVCAQAPQPDDADvEAWyrRHAEQFKRPEQRLT-RHLLLtvnEDDREAvrtriLA 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207 152 VAERLKKGED-FAKVAAELSKDPgSGKEGGSLGWFTKDRMVPEFAEVAFKLTKGQVSDPVKSQFGWHVIKLEDKR-AKPL 229
Cdd:TIGR02933 148 ILRRLRGKPAaFAEQAMRHSHCP-TAMEGGLLGWVSRGLLYPQLDAALFQLAEGELSPPIESEIGWHLLLCEAIRpARPL 226

                         170       180
                  ....*....|....*....|...
gi 1382179207 230 PDFAAVkPQIDQYL---ERKAQQ 249
Cdd:TIGR02933 227 TLEEAL-PRARDRLqlrQQKAYQ 248
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 135-225 1.77e-10

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 60.91  E-value: 1.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207 135 EVNARHILV------------EDEAQAKAVAERLKKGEDFAKVAAELSKDPGSGKeGGSLGWFTKDRMVPEFAEVAFKLT 202
Cdd:PRK10770  155 ELNLSHILIplpenptqdqvdEAESQARSIVDQARNGADFGKLAIAYSADQQALK-GGQMGWGRIQELPGLFAQALSTAK 233

                          90       100
                  ....*....|....*....|...
gi 1382179207 203 KGQVSDPVKSQFGWHVIKLEDKR 225
Cdd:PRK10770  234 KGDIVGPIRSGVGFHILKVNDLR 256
prsA PRK01326
foldase protein PrsA; Reviewed
 97-258 1.38e-05

foldase protein PrsA; Reviewed


Pssm-ID: 179281 [Multi-domain]  Cd Length: 310  Bit Score: 45.57  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207  97 REKVLLDQFLTAEAKKAATPEAAKKLYDETTKgmapeeEVNARHILVEDEAQAKAVAERLK-KGEDFAKVAAELSKDPGs 175
Cdd:PRK01326  113 RTSKLVEYAVKEAAKKELTDEAYKKAYEEYTP------EVTAQIIRLDNEDKAKSVLEEAKaEGADFAQIAKENTTTKE- 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382179207 176 gkEGGSLGWFTKDRMVPE-FAEVAFKLTKGQVSDPVKS------QFGWHVIKLEDKRAKplpdfaavKPQIDQYLERKAQ 248
Cdd:PRK01326  186 --KKGEYKFDSGSTNVPEqVKKAAFALDEDGVSDVISVldptayQSKYYIVKVTKKTEK--------KSDWKDYKKRLKA 255

                         170
                  ....*....|
gi 1382179207 249 qdIIVALREK 258
Cdd:PRK01326  256 --IILAQKQN 263
 
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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