NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2030370408|ref|WP_211145164|]
View 

peptidylprolyl isomerase [Clostridium aciditolerans]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 110-244 3.01e-47

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


:

Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 153.58  E-value: 3.01e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408 110 FVEPEMVSAKHILV---------ETKEKAEEIISEINAGLSFEEAAQKYSSCP-SKDQGGNLGSFSRGQMVPEFEEAAFN 179
Cdd:COG0760     3 FDSPEEVRASHILVkvppsedraKAEAKAEELLAQLKAGADFAELAKEYSQDPgSAANGGDLGWFSRGQLVPEFEEAAFA 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2030370408 180 LEIGVVSEPVKTQFGYHLIKVEEKIESKAKQFNEVEGMIKNTLLQQrqtfKYSQLNGELREKYTV 244
Cdd:COG0760    83 LKPGEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQELFQQ----ALEAWLEELRKKAKI 143
cis_trans_EpsD super family cl26125
peptidyl-prolyl cis-trans isomerase, EpsD family; Members of this family belong to the ...
 5-146 1.47e-13

peptidyl-prolyl cis-trans isomerase, EpsD family; Members of this family belong to the peptidyl-prolyl cis-trans isomerase family and are found in loci associated with exopolysaccharide biosynthesis. All members are encoded near a homolog of EpsH, as detected by TIGR02602.


The actual alignment was detected with superfamily member TIGR02925:

Pssm-ID: 131971 [Multi-domain]  Cd Length: 232  Bit Score: 67.91  E-value: 1.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408   5 VLAVVNGAKITEGDLQGAIMRFPRERQGYlNTYNGKKQLLEEMISFELIYNYAKDSGMENEKEYVDLLERAKKEILTQTA 84
Cdd:TIGR02925  28 VAAKVNGVEISVHQLNYALQRTPNPGASS-DAARARRQVLDRLVDQELVVGKALEEKLDRSPDVVMALEAAKREILARAY 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2030370408  85 ISKVM-AQVTVTDSEVTDYYNANQQMFVEPEMVSAKHILVET-KEKAEEIISEINAGLSFEEAA 146
Cdd:TIGR02925 107 LRQLAgAQSKPSPEEAKSYFQEHPQLFAERKLYNLQEIALPPdMELLDELRAMVENGKPLEDIL 170
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 110-244 3.01e-47

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 153.58  E-value: 3.01e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408 110 FVEPEMVSAKHILV---------ETKEKAEEIISEINAGLSFEEAAQKYSSCP-SKDQGGNLGSFSRGQMVPEFEEAAFN 179
Cdd:COG0760     3 FDSPEEVRASHILVkvppsedraKAEAKAEELLAQLKAGADFAELAKEYSQDPgSAANGGDLGWFSRGQLVPEFEEAAFA 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2030370408 180 LEIGVVSEPVKTQFGYHLIKVEEKIESKAKQFNEVEGMIKNTLLQQrqtfKYSQLNGELREKYTV 244
Cdd:COG0760    83 LKPGEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQELFQQ----ALEAWLEELRKKAKI 143
prsA PRK00059
peptidylprolyl isomerase; Provisional
 2-233 1.88e-37

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 134.07  E-value: 1.88e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408   2 ENKVLAVVNGAKITEGDLQG---AIMRFPRERQGYLNTYNG-----------KKQLLEEMISFELI-------------- 53
Cdd:PRK00059   34 AKSTVATVNGEKITRGDLDKdpkMQQVLEQLKQQYGDNYEKneqvkeqikqqKEQILDSLITEKVLlqkakelklipsee 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408  54 ---------YNYAKDSGMENEKEYVDLLERA-----------KKEILTQTAISKVMAQVTVTDSEVTDYYNANQQMFVE- 112
Cdd:PRK00059  114 elnkevdkkINEIKKQFNNDEEQFEEALKATgfteetfkeylKNQIIIEKVINEVVKDVKVTDKDAQKYYNENKSKFTEk 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408 113 PEMVSAKHILVETKEKAEEIISEINAGLSFEEAAQKYSSCP-SKDQGGNLG--SFSRGQMVPEFEEAAFNLEIGVVSEPV 189
Cdd:PRK00059  194 PNTMHLAHILVKTEDEAKKVKKRLDKGEDFAKVAKEVSQDPgSKDKGGDLGdvPYSDSGYDKEFMDGAKALKEGEISAPV 273

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2030370408 190 KTQFGYHLIKVEEKIESKAKQFNEVEGMIKNTLLQQRQTFKYSQ 233
Cdd:PRK00059  274 KTQFGYHIIKAIKKKEYPVKPFDSVKEDIKKQLLQEKQSEVFKK 317
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 113-203 7.04e-29

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: 105.53  E-value: 7.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408 113 PEMVSAKHILV-----------ETKEKAEEIISEINAGLSFEEAAQKYSSCP-SKDQGGNLGSFSRGQMVPEFEEAAFNL 180
Cdd:pfam13616  13 PDSVKASHILIsysqavsrteeEAKAKADSLLAALKNGADFAALAKTYSDDPaSKNNGGDLGWFTKGQMVKEFEDAVFSL 92

                          90       100
                  ....*....|....*....|...
gi 2030370408 181 EIGVVSEPVKTQFGYHLIKVEEK 203
Cdd:pfam13616  93 KVGEISGVVKTQFGFHIIKVTDK 115
cis_trans_EpsD TIGR02925
peptidyl-prolyl cis-trans isomerase, EpsD family; Members of this family belong to the ...
 5-146 1.47e-13

peptidyl-prolyl cis-trans isomerase, EpsD family; Members of this family belong to the peptidyl-prolyl cis-trans isomerase family and are found in loci associated with exopolysaccharide biosynthesis. All members are encoded near a homolog of EpsH, as detected by TIGR02602.


Pssm-ID: 131971 [Multi-domain]  Cd Length: 232  Bit Score: 67.91  E-value: 1.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408   5 VLAVVNGAKITEGDLQGAIMRFPRERQGYlNTYNGKKQLLEEMISFELIYNYAKDSGMENEKEYVDLLERAKKEILTQTA 84
Cdd:TIGR02925  28 VAAKVNGVEISVHQLNYALQRTPNPGASS-DAARARRQVLDRLVDQELVVGKALEEKLDRSPDVVMALEAAKREILARAY 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2030370408  85 ISKVM-AQVTVTDSEVTDYYNANQQMFVEPEMVSAKHILVET-KEKAEEIISEINAGLSFEEAA 146
Cdd:TIGR02925 107 LRQLAgAQSKPSPEEAKSYFQEHPQLFAERKLYNLQEIALPPdMELLDELRAMVENGKPLEDIL 170
SurA_N_3 pfam13624
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 5-62 9.53e-04

SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a helical domain of unknown function. The C-terminus of the SurA protein folds back and forms part of this domain also but is not included in the current alignment.


Pssm-ID: 433358 [Multi-domain]  Cd Length: 162  Bit Score: 38.71  E-value: 9.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2030370408   5 VLAVVNGAKITEGDLQGAIMR-FPRERQGY--------LNTYNGKKQLLEEMISFELIYNYAKDSGM 62
Cdd:pfam13624  40 AVAKVNGEKISRAEFQRAYRRqLDQLRQQFgpnldaelLDELGLRQQVLDQLIDRALLLQEAKKLGL 106
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 110-244 3.01e-47

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 153.58  E-value: 3.01e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408 110 FVEPEMVSAKHILV---------ETKEKAEEIISEINAGLSFEEAAQKYSSCP-SKDQGGNLGSFSRGQMVPEFEEAAFN 179
Cdd:COG0760     3 FDSPEEVRASHILVkvppsedraKAEAKAEELLAQLKAGADFAELAKEYSQDPgSAANGGDLGWFSRGQLVPEFEEAAFA 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2030370408 180 LEIGVVSEPVKTQFGYHLIKVEEKIESKAKQFNEVEGMIKNTLLQQrqtfKYSQLNGELREKYTV 244
Cdd:COG0760    83 LKPGEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQELFQQ----ALEAWLEELRKKAKI 143
prsA PRK00059
peptidylprolyl isomerase; Provisional
 2-233 1.88e-37

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 134.07  E-value: 1.88e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408   2 ENKVLAVVNGAKITEGDLQG---AIMRFPRERQGYLNTYNG-----------KKQLLEEMISFELI-------------- 53
Cdd:PRK00059   34 AKSTVATVNGEKITRGDLDKdpkMQQVLEQLKQQYGDNYEKneqvkeqikqqKEQILDSLITEKVLlqkakelklipsee 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408  54 ---------YNYAKDSGMENEKEYVDLLERA-----------KKEILTQTAISKVMAQVTVTDSEVTDYYNANQQMFVE- 112
Cdd:PRK00059  114 elnkevdkkINEIKKQFNNDEEQFEEALKATgfteetfkeylKNQIIIEKVINEVVKDVKVTDKDAQKYYNENKSKFTEk 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408 113 PEMVSAKHILVETKEKAEEIISEINAGLSFEEAAQKYSSCP-SKDQGGNLG--SFSRGQMVPEFEEAAFNLEIGVVSEPV 189
Cdd:PRK00059  194 PNTMHLAHILVKTEDEAKKVKKRLDKGEDFAKVAKEVSQDPgSKDKGGDLGdvPYSDSGYDKEFMDGAKALKEGEISAPV 273

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2030370408 190 KTQFGYHLIKVEEKIESKAKQFNEVEGMIKNTLLQQRQTFKYSQ 233
Cdd:PRK00059  274 KTQFGYHIIKAIKKKEYPVKPFDSVKEDIKKQLLQEKQSEVFKK 317
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 56-226 5.27e-30

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 113.14  E-value: 5.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408  56 YAKDSGMENEKEyvdLLERAKKEILTQTAIskvmaQVTVTDSEVTDYYnanqqmfvEPEMvSAKHILVETKEKAEEIISE 135
Cdd:PRK02998   92 TLEQVGLKNEDE---LKEKMKPEIAFEKAI-----KATVTEKDVKDNY--------KPEM-KVSHILVKDEKTAKEVKEK 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408 136 INAGLSFEEAAQKYSSCP-SKDQGGNLGSFSRGQMVPEFEEAAFNLEIGVVSEPVKTQFGYHLIKVEEKIEskAKQFNEV 214
Cdd:PRK02998  155 VNNGEDFAALAKQYSEDTgSKEQGGEISGFAPGQTVKEFEEAAYKLDAGQVSEPVKTTYGYHIIKVTDKKE--LKPFDEV 232

                         170
                  ....*....|..
gi 2030370408 215 EGMIKNTLLQQR 226
Cdd:PRK02998  233 KDSIRKDLEQQR 244
prsA PRK03095
peptidylprolyl isomerase PrsA;
39-226 3.18e-29

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 111.24  E-value: 3.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408  39 GKKQLLEEMISFE-LIYNYAKDSGM------ENEKEYVD-----LLERAKKEILTQTAISKVMAQ-----VTVTDSEVTD 101
Cdd:PRK03095   48 AGKQVLNNMVMEKvLIKNYKVEDKEvdkkydEMKKQYGDqfdtlLKQQGIKEETLKTGVRAQLAQekaieKTITDKELKD 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408 102 YYnanqqmfvEPEmVSAKHILVETKEKAEEIISEINAGLSFEEAAQKYSSCP-SKDQGGNLGSFSRGQMVPEFEEAAFNL 180
Cdd:PRK03095  128 NY--------KPE-IKASHILVKDEATAKKVKEELGQGKSFEELAKQYSEDTgSKEKGGDLGFFGAGKMVKEFEDAAYKL 198

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2030370408 181 EIGVVSEPVKTQFGYHLIKVEEkIESKAKQFNEVEGMIKNTLLQQR 226
Cdd:PRK03095  199 KKDEVSEPVKSQFGYHIIKVTD-IKEPEKSFEQSKADIKKELVQKK 243
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 113-203 7.04e-29

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: 105.53  E-value: 7.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408 113 PEMVSAKHILV-----------ETKEKAEEIISEINAGLSFEEAAQKYSSCP-SKDQGGNLGSFSRGQMVPEFEEAAFNL 180
Cdd:pfam13616  13 PDSVKASHILIsysqavsrteeEAKAKADSLLAALKNGADFAALAKTYSDDPaSKNNGGDLGWFTKGQMVKEFEDAVFSL 92

                          90       100
                  ....*....|....*....|...
gi 2030370408 181 EIGVVSEPVKTQFGYHLIKVEEK 203
Cdd:pfam13616  93 KVGEISGVVKTQFGFHIIKVTDK 115
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 120-202 2.16e-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: 103.53  E-value: 2.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408 120 HILV-----------ETKEKAEEIISEINAG-LSFEEAAQKYSS-CPSKDQGGNLGSFSRGQMVPEFEEAAFNLEIGVVS 186
Cdd:pfam00639   1 HILIktpeaserdraEAKAKAEEILEQLKSGeDSFAELARKYSDdCPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEIS 80

                          90
                  ....*....|....*.
gi 2030370408 187 EPVKTQFGYHLIKVEE 202
Cdd:pfam00639  81 GPVETRFGFHIIKLTD 96
prsA PRK03002
peptidylprolyl isomerase PrsA;
55-240 4.19e-27

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 105.40  E-value: 4.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408  55 NYAKDSGMENEKEYvdlleraKKEILTQTAISKVMAQvTVTDSEVTDYYnanqqmfvEPEmVSAKHILVETKEKAEEIIS 134
Cdd:PRK03002   93 NVLKNNGLKDEADF-------KNQIKFKLAMNEAIKK-SVTEKDVKDHY--------KPE-IKASHILVSDENEAKEIKK 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408 135 EINAGLSFEEAAQKYSSCP-SKDQGGNLGSFSRGQMVPEFEEAAFNLEIGVVSEPVKTQFGYHLIKVEEKIEskAKQFNE 213
Cdd:PRK03002  156 KLDAGASFEELAKQESQDLlSKEKGGDLGYFNSGRMAPEFETAAYKLKVGQISNPVKSPNGYHIIKLTDKKD--LKPYDE 233

                         170       180       190
                  ....*....|....*....|....*....|
gi 2030370408 214 VEGMIKNTLLQQR---QTFKYSQLNGELRE 240
Cdd:PRK03002  234 VKDSIRKNLEEERtadPIFGKKLLQSELKK 263
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 114-200 9.83e-24

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 91.62  E-value: 9.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408 114 EMVSAKHILVETKEKAEEIISEINAGLSFEEAAQKYSSCPSKDQGGNLGSFSRGQMVPEFEEAAFNLEIGVVSEPVKTQF 193
Cdd:PRK15441    3 KTAAALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQF 82


                  ....*..
gi 2030370408 194 GYHLIKV 200
Cdd:PRK15441   83 GYHIIKV 89
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 111-199 1.50e-21

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 86.23  E-value: 1.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408 111 VEPEMVSAKHILVE------------------TKEKAEEIISEI-----NAGLSFEEAAQKYSSCPSKDQGGNLGSFSRG 167
Cdd:PTZ00356    1 MEGDTVRAAHLLIKhtgsrnpvsrrtgkpvtrSKEEAIKELAKWreqivSGEKTFEEIARQRSDCGSAAKGGDLGFFGRG 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2030370408 168 QMVPEFEEAAFNLEIGVVSEPVKTQFGYHLIK 199
Cdd:PTZ00356   81 QMQKPFEDAAFALKVGEISDIVHTDSGVHIIL 112
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
94-215 3.74e-18

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 77.48  E-value: 3.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408  94 VTDSEVTDYYNANQQMFVEPEMVSaKHILVETKEKAEEIISEINAGLSFEEAAQKYSSCPSKDQGGNLGSfSRGQMVPEF 173
Cdd:pfam13145   1 VTEEELKAYYEENKDEFSTPEGRL-LEILVFKDQVAADAALALLKAGALEDFAALAKGEGIKAATLDIVE-SAELLPEEL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2030370408 174 EEAAFNLEIGVVSEPVKTQFGYHLIKVEEKIESKAKQFNEVE 215
Cdd:pfam13145  79 AKAAFALKPGEVSGPIKTGNGYYVVRVTEIKPAQPLPFEEAK 120
prsA PRK04405
peptidylprolyl isomerase; Provisional
 112-200 4.10e-15

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 73.28  E-value: 4.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408 112 EPEmVSAKHILVETKEKAEEIISEINAGLSFEEAAQKYSS-CPSKDQGGNLGSF--SRGQMVPEFEEAAFNLEIG-VVSE 187
Cdd:PRK04405  142 QPK-VTVQHILVSKKSTAETVIKKLKDGKDFAKLAKKYSTdTATKNKGGKLSAFdsTDTTLDSTFKTAAFKLKNGeYTTT 220

                          90
                  ....*....|...
gi 2030370408 188 PVKTQFGYHLIKV 200
Cdd:PRK04405  221 PVKTTYGYEVIKM 233
cis_trans_EpsD TIGR02925
peptidyl-prolyl cis-trans isomerase, EpsD family; Members of this family belong to the ...
 5-146 1.47e-13

peptidyl-prolyl cis-trans isomerase, EpsD family; Members of this family belong to the peptidyl-prolyl cis-trans isomerase family and are found in loci associated with exopolysaccharide biosynthesis. All members are encoded near a homolog of EpsH, as detected by TIGR02602.


Pssm-ID: 131971 [Multi-domain]  Cd Length: 232  Bit Score: 67.91  E-value: 1.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408   5 VLAVVNGAKITEGDLQGAIMRFPRERQGYlNTYNGKKQLLEEMISFELIYNYAKDSGMENEKEYVDLLERAKKEILTQTA 84
Cdd:TIGR02925  28 VAAKVNGVEISVHQLNYALQRTPNPGASS-DAARARRQVLDRLVDQELVVGKALEEKLDRSPDVVMALEAAKREILARAY 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2030370408  85 ISKVM-AQVTVTDSEVTDYYNANQQMFVEPEMVSAKHILVET-KEKAEEIISEINAGLSFEEAA 146
Cdd:TIGR02925 107 LRQLAgAQSKPSPEEAKSYFQEHPQLFAERKLYNLQEIALPPdMELLDELRAMVENGKPLEDIL 170
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 99-202 3.33e-12

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 65.53  E-value: 3.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408  99 VTDYYNANQQMFVEPemVSAKHILVET---------KEKAEEIISEINAG-LSFEEAAQKYSSCP-SKDQGGNLGSFSRG 167
Cdd:PRK10770  252 VNDLRGESQNISVTE--VHARHILLKPspimtdeqaRAKLEQIAADIKSGkTTFAAAAKEFSQDPgSANQGGDLGWATPD 329

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2030370408 168 QMVPEFEEAAFNLEIGVVSEPVKTQFGYHLIKVEE 202
Cdd:PRK10770  330 IFDPAFRDALMRLNKGQISAPVHSSFGWHLIELLD 364
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 87-226 2.84e-10

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 60.02  E-value: 2.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408  87 KVMAQVTVTDSEVTDYYNANQQMFVEPEMVSAKHILVETKEKAEEIISEINAGLSFEEAAQKYSSCP-SKDQGGNLGSFS 165
Cdd:PRK10788  242 TMQQKITVSDADIQAYYDQHQDQFTQPERKRYSIIQTKTEAEAKAVLDELKKGADFATLAKEKSTDIiSARNGGDLGWLE 321

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2030370408 166 RGQMVPEFEEAafNL-EIGVVSEPVKTQFGYHLIKVEEKIESKAKQFNEVEGMIKNTLLQQR 226
Cdd:PRK10788  322 PATTPDELKNA--GLkEKGQLSGVIKSSVGFLIVRLDDIQPAKVKPLSEVRDDIAAKVKQEK 381
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 124-200 2.16e-04

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 42.04  E-value: 2.16e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2030370408 124 ETKEKAEEIISEINAGLSFEEAAQKYSSCPSKDQGGNLGsFSRGQMVPE-FEEAAFNLEIGVVSEPVKTQFGYHLIKV 200
Cdd:PRK10770  176 EAESQARSIVDQARNGADFGKLAIAYSADQQALKGGQMG-WGRIQELPGlFAQALSTAKKGDIVGPIRSGVGFHILKV 252
SurA_N_3 pfam13624
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 5-62 9.53e-04

SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a helical domain of unknown function. The C-terminus of the SurA protein folds back and forms part of this domain also but is not included in the current alignment.


Pssm-ID: 433358 [Multi-domain]  Cd Length: 162  Bit Score: 38.71  E-value: 9.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2030370408   5 VLAVVNGAKITEGDLQGAIMR-FPRERQGY--------LNTYNGKKQLLEEMISFELIYNYAKDSGM 62
Cdd:pfam13624  40 AVAKVNGEKISRAEFQRAYRRqLDQLRQQFgpnldaelLDELGLRQQVLDQLIDRALLLQEAKKLGL 106
prsA PRK01326
foldase protein PrsA; Reviewed
 116-227 2.26e-03

foldase protein PrsA; Reviewed


Pssm-ID: 179281 [Multi-domain]  Cd Length: 310  Bit Score: 38.64  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030370408 116 VSAKHILVETKEKAEEIISEINA-GLSFEEAAQKYSScpSKDQGGNLGSFSRGQMVPE-FEEAAFNLEIGVVSEPVKT-- 191
Cdd:PRK01326  146 VTAQIIRLDNEDKAKSVLEEAKAeGADFAQIAKENTT--TKEKKGEYKFDSGSTNVPEqVKKAAFALDEDGVSDVISVld 223

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2030370408 192 ----QFGYHLIKVEEKIESKAKqFNEVEGMIKNTLLQQRQ 227
Cdd:PRK01326  224 ptayQSKYYIVKVTKKTEKKSD-WKDYKKRLKAIILAQKQ 262
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH