NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1091152376|gb|OHQ82510|]
View 

peptidylprolyl isomerase [Staphylococcus sp. HMSC074C12]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 1001668)

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:0003755
PubMed:  12871165|7925971

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, ...
 143-267 7.93e-27

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


:

Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 102.73  E-value: 7.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376 143 KASHILIKVKSSSSDKEglsdkkAKEKAEKIQKEVEKNpDKFGEIAKKESMDSSSAKKDGSLGYVVKGQMVSKFEKALFK 222
Cdd:COG0760    10 RASHILVKVPPSEDRAK------AEAKAEELLAQLKAG-ADFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEAAFA 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1091152376 223 LKEGQVSDVVKTDYGYHVIK-----ADKESDFDKQKSKLKAKLIEQKVQK 267
Cdd:COG0760    83 LKPGEISGPVKTQFGYHIIKvedrrPAETPPFEEVKQQIRQELFQQALEA 132
Rotamase_2 super family cl29122
PPIC-type PPIASE domain;
14-305 2.53e-25

PPIC-type PPIASE domain;


The actual alignment was detected with superfamily member PRK03095:

Pssm-ID: 452928 [Multi-domain]  Cd Length: 287  Bit Score: 102.76  E-value: 2.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376  14 SALLLGACGSnatdSESNTLISSKAGDVKVKDVMNKIGDEQIASTSFSIALNKILADKYKdkVDTKDIDDEIKKEQKQYG 93
Cdd:PRK03095   12 SVIALSACGT----SSSDKIVTSKAGDITKDEFYEQMKTQAGKQVLNNMVMEKVLIKNYK--VEDKEVDKKYDEMKKQYG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376  94 gkDQFESMLKQQGMSLDDYKEQKKLAAYQKQllADKVKVSDKELKENTK---KASHILIKVKSSSSDkeglsdkkakeka 170
Cdd:PRK03095   86 --DQFDTLLKQQGIKEETLKTGVRAQLAQEK--AIEKTITDKELKDNYKpeiKASHILVKDEATAKK------------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376 171 ekiQKEVEKNPDKFGEIAKKESMDSSSAKKDGSLGYVVKGQMVSKFEKALFKLKEGQVSDVVKTDYGYHVIKA----DKE 246
Cdd:PRK03095  149 ---VKEELGQGKSFEELAKQYSEDTGSKEKGGDLGFFGAGKMVKEFEDAAYKLKKDEVSEPVKSQFGYHIIKVtdikEPE 225

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1091152376 247 SDFDKQKSKLKAKLIEQKVQkDPKILTNAYKDLLKEYDVDYKDSDIKKAVENTILNPEK 305
Cdd:PRK03095  226 KSFEQSKADIKKELVQKKAQ-DGEFMNDLMMKEIKKADVKVDDKDLKDLFEEKKADAKK 283
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 143-267 7.93e-27

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 102.73  E-value: 7.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376 143 KASHILIKVKSSSSDKEglsdkkAKEKAEKIQKEVEKNpDKFGEIAKKESMDSSSAKKDGSLGYVVKGQMVSKFEKALFK 222
Cdd:COG0760    10 RASHILVKVPPSEDRAK------AEAKAEELLAQLKAG-ADFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEAAFA 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1091152376 223 LKEGQVSDVVKTDYGYHVIK-----ADKESDFDKQKSKLKAKLIEQKVQK 267
Cdd:COG0760    83 LKPGEISGPVKTQFGYHIIKvedrrPAETPPFEEVKQQIRQELFQQALEA 132
prsA PRK03095
peptidylprolyl isomerase PrsA;
14-305 2.53e-25

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 102.76  E-value: 2.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376  14 SALLLGACGSnatdSESNTLISSKAGDVKVKDVMNKIGDEQIASTSFSIALNKILADKYKdkVDTKDIDDEIKKEQKQYG 93
Cdd:PRK03095   12 SVIALSACGT----SSSDKIVTSKAGDITKDEFYEQMKTQAGKQVLNNMVMEKVLIKNYK--VEDKEVDKKYDEMKKQYG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376  94 gkDQFESMLKQQGMSLDDYKEQKKLAAYQKQllADKVKVSDKELKENTK---KASHILIKVKSSSSDkeglsdkkakeka 170
Cdd:PRK03095   86 --DQFDTLLKQQGIKEETLKTGVRAQLAQEK--AIEKTITDKELKDNYKpeiKASHILVKDEATAKK------------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376 171 ekiQKEVEKNPDKFGEIAKKESMDSSSAKKDGSLGYVVKGQMVSKFEKALFKLKEGQVSDVVKTDYGYHVIKA----DKE 246
Cdd:PRK03095  149 ---VKEELGQGKSFEELAKQYSEDTGSKEKGGDLGFFGAGKMVKEFEDAAYKLKKDEVSEPVKSQFGYHIIKVtdikEPE 225

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1091152376 247 SDFDKQKSKLKAKLIEQKVQkDPKILTNAYKDLLKEYDVDYKDSDIKKAVENTILNPEK 305
Cdd:PRK03095  226 KSFEQSKADIKKELVQKKAQ-DGEFMNDLMMKEIKKADVKVDDKDLKDLFEEKKADAKK 283
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 146-245 6.08e-25

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: 96.21  E-value: 6.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376 146 HILIKVKSSSSDKEglsdKKAKEKAEKIQKEVEKNPDKFGEIAKKESMDSSSAKKDGSLGYVVKGQMVSKFEKALFKLKE 225
Cdd:pfam00639   1 HILIKTPEASERDR----AEAKAKAEEILEQLKSGEDSFAELARKYSDDCPSAANGGDLGWFTRGQLPPEFEKAAFALKP 76

                          90       100
                  ....*....|....*....|
gi 1091152376 226 GQVSDVVKTDYGYHVIKADK 245
Cdd:pfam00639  77 GEISGPVETRFGFHIIKLTD 96
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 143-242 1.12e-18

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 80.07  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376 143 KASHILIKVKSS---SSDKEG----LSDKKAKEKAEKIQKEVEKNPDKFGEIAKKESmDSSSAKKDGSLGYVVKGQMVSK 215
Cdd:PTZ00356    7 RAAHLLIKHTGSrnpVSRRTGkpvtRSKEEAIKELAKWREQIVSGEKTFEEIARQRS-DCGSAAKGGDLGFFGRGQMQKP 85

                          90       100
                  ....*....|....*....|....*..
gi 1091152376 216 FEKALFKLKEGQVSDVVKTDYGYHVIK 242
Cdd:PTZ00356   86 FEDAAFALKVGEISDIVHTDSGVHIIL 112
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 143-267 7.93e-27

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 102.73  E-value: 7.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376 143 KASHILIKVKSSSSDKEglsdkkAKEKAEKIQKEVEKNpDKFGEIAKKESMDSSSAKKDGSLGYVVKGQMVSKFEKALFK 222
Cdd:COG0760    10 RASHILVKVPPSEDRAK------AEAKAEELLAQLKAG-ADFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEAAFA 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1091152376 223 LKEGQVSDVVKTDYGYHVIK-----ADKESDFDKQKSKLKAKLIEQKVQK 267
Cdd:COG0760    83 LKPGEISGPVKTQFGYHIIKvedrrPAETPPFEEVKQQIRQELFQQALEA 132
prsA PRK03095
peptidylprolyl isomerase PrsA;
14-305 2.53e-25

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 102.76  E-value: 2.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376  14 SALLLGACGSnatdSESNTLISSKAGDVKVKDVMNKIGDEQIASTSFSIALNKILADKYKdkVDTKDIDDEIKKEQKQYG 93
Cdd:PRK03095   12 SVIALSACGT----SSSDKIVTSKAGDITKDEFYEQMKTQAGKQVLNNMVMEKVLIKNYK--VEDKEVDKKYDEMKKQYG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376  94 gkDQFESMLKQQGMSLDDYKEQKKLAAYQKQllADKVKVSDKELKENTK---KASHILIKVKSSSSDkeglsdkkakeka 170
Cdd:PRK03095   86 --DQFDTLLKQQGIKEETLKTGVRAQLAQEK--AIEKTITDKELKDNYKpeiKASHILVKDEATAKK------------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376 171 ekiQKEVEKNPDKFGEIAKKESMDSSSAKKDGSLGYVVKGQMVSKFEKALFKLKEGQVSDVVKTDYGYHVIKA----DKE 246
Cdd:PRK03095  149 ---VKEELGQGKSFEELAKQYSEDTGSKEKGGDLGFFGAGKMVKEFEDAAYKLKKDEVSEPVKSQFGYHIIKVtdikEPE 225

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1091152376 247 SDFDKQKSKLKAKLIEQKVQkDPKILTNAYKDLLKEYDVDYKDSDIKKAVENTILNPEK 305
Cdd:PRK03095  226 KSFEQSKADIKKELVQKKAQ-DGEFMNDLMMKEIKKADVKVDDKDLKDLFEEKKADAKK 283
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 146-245 6.08e-25

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: 96.21  E-value: 6.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376 146 HILIKVKSSSSDKEglsdKKAKEKAEKIQKEVEKNPDKFGEIAKKESMDSSSAKKDGSLGYVVKGQMVSKFEKALFKLKE 225
Cdd:pfam00639   1 HILIKTPEASERDR----AEAKAKAEEILEQLKSGEDSFAELARKYSDDCPSAANGGDLGWFTRGQLPPEFEKAAFALKP 76

                          90       100
                  ....*....|....*....|
gi 1091152376 226 GQVSDVVKTDYGYHVIKADK 245
Cdd:pfam00639  77 GEISGPVETRFGFHIIKLTD 96
prsA PRK03002
peptidylprolyl isomerase PrsA;
1-293 8.81e-23

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 95.77  E-value: 8.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376   1 MKIMNKLIVPVTASALLLGACGSNatdSESNTLISSKAGDVKVKDVMNKIGDEQIASTSFSIALNKILADKYKdkVDTKD 80
Cdd:PRK03002    1 MRGKHIFIITALISILMLSACGQK---NSSATVATATDSTITKSDFEKQLKDRYGKDMLYEMMAQDVITKKYK--VSDDD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376  81 IDDEIKKEQKQYGgkDQFESMLKQQGMS-LDDYKEQKKLAAYQKQllADKVKVSDKELKENTK---KASHILIKVKSSSs 156
Cdd:PRK03002   76 VDKEVQKAKSQYG--DQFKNVLKNNGLKdEADFKNQIKFKLAMNE--AIKKSVTEKDVKDHYKpeiKASHILVSDENEA- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376 157 dkeglsdkkakekaekiqKEVEKNPD---KFGEIAKKESMDSSSAKKDGSLGYVVKGQMVSKFEKALFKLKEGQVSDVVK 233
Cdd:PRK03002  151 ------------------KEIKKKLDagaSFEELAKQESQDLLSKEKGGDLGYFNSGRMAPEFETAAYKLKVGQISNPVK 212

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1091152376 234 TDYGYHVIKADKESD---FDKQKSKLKAKLIEQKVqKDPKILTNAYKDLLKEYDVDYKDSDIK 293
Cdd:PRK03002  213 SPNGYHIIKLTDKKDlkpYDEVKDSIRKNLEEERT-ADPIFGKKLLQSELKKANIKINDSELE 274
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 15-293 1.05e-22

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 95.42  E-value: 1.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376  15 ALLLGACGSnatdseSNTLISSKAGDVKVKDVMNKIGDEQIASTSFSIALNKILADKYKDKvdtkdiDDEIKKEQKQYGG 94
Cdd:PRK02998   16 VLALSACGS------SDNVVTSKVGNITEKELSKELRQKYGESTLYQMVLSKALLDKYKVS------DEEAKKQVEEAKD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376  95 K--DQFESMLKQQGM-SLDDYKEQKKLA-AYQKqllADKVKVSDKELKENTK---KASHILIKVKSSSSDKeglsdkkak 167
Cdd:PRK02998   84 KmgDNFKSTLEQVGLkNEDELKEKMKPEiAFEK---AIKATVTEKDVKDNYKpemKVSHILVKDEKTAKEV--------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376 168 ekaekiqKEVEKNPDKFGEIAKKESMDSSSAKKDGSLGYVVKGQMVSKFEKALFKLKEGQVSDVVKTDYGYHVIKADKES 247
Cdd:PRK02998  152 -------KEKVNNGEDFAALAKQYSEDTGSKEQGGEISGFAPGQTVKEFEEAAYKLDAGQVSEPVKTTYGYHIIKVTDKK 224

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1091152376 248 D---FDKQKSKLKAKLIEQKVQK-DPKILTNAYKDLLKEYDVDYKDSDIK 293
Cdd:PRK02998  225 ElkpFDEVKDSIRKDLEQQRLQDtTGKWKQQVVNDLLKDADIKVNDKEFK 274
prsA PRK04405
peptidylprolyl isomerase; Provisional
 1-298 1.76e-22

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 95.23  E-value: 1.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376   1 MKIMNKLIVPVTASALL---LGACGSNATdsesnTLISSKAGDVKVKDVMNKIGDEQIASTSF-SIALNKILADKYKDKV 76
Cdd:PRK04405    1 MKKKMKKWALAAASAGLalsLAGCSSNQA-----TVATYSGGKITQSQYYKEMKQSSAGKTVLaNMIIYRALEKQYGKKV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376  77 DTKDIDDEIKKEQKQYGgkDQFESMLKQQGMSLDDYKEQKKLAAYQKQLLADKVKVSDKELKENTKK------ASHILIK 150
Cdd:PRK04405   76 STKKVDKQYNSYKKQYG--SSFDSVLSQNGMTTSSFKQNLRTNLLSEAALKKLKKVTNSQLKKAWKSyqpkvtVQHILVS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376 151 VKSSSSDkeglsdkkakekaekIQKEVEKNPDkFGEIAKKESMDSSSAKKDGSLGYV--VKGQMVSKFEKALFKLKEGQV 228
Cdd:PRK04405  154 KKSTAET---------------VIKKLKDGKD-FAKLAKKYSTDTATKNKGGKLSAFdsTDTTLDSTFKTAAFKLKNGEY 217

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1091152376 229 SDV-VKTDYGYHVIKADK---ESDFDKQKSKLKAKLIeQKVQKDPKILTNAYKDLLKEYDVDYKDSDIKKAVEN 298
Cdd:PRK04405  218 TTTpVKTTYGYEVIKMIKhpaKGTFSDHKKALTKQIY-AKWASDSSVMQRVISKVLKKANVSIKDKDLKDALSS 290
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 143-242 1.12e-18

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 80.07  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376 143 KASHILIKVKSS---SSDKEG----LSDKKAKEKAEKIQKEVEKNPDKFGEIAKKESmDSSSAKKDGSLGYVVKGQMVSK 215
Cdd:PTZ00356    7 RAAHLLIKHTGSrnpVSRRTGkpvtRSKEEAIKELAKWREQIVSGEKTFEEIARQRS-DCGSAAKGGDLGFFGRGQMQKP 85

                          90       100
                  ....*....|....*....|....*..
gi 1091152376 216 FEKALFKLKEGQVSDVVKTDYGYHVIK 242
Cdd:PTZ00356   86 FEDAAFALKVGEISDIVHTDSGVHIIL 112
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 130-243 4.32e-18

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: 78.56  E-value: 4.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376 130 VKVSDKELKENTKKASHILIkvksSSSDKEGLSDKKAKEKAEKIqKEVEKNPDKFGEIAKKESMDSSSAKKDGSLGYVVK 209
Cdd:pfam13616   4 SKLVDKKSAPDSVKASHILI----SYSQAVSRTEEEAKAKADSL-LAALKNGADFAALAKTYSDDPASKNNGGDLGWFTK 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1091152376 210 GQMVSKFEKALFKLKEGQVSDVVKTDYGYHVIKA 243
Cdd:pfam13616  79 GQMVKEFEDAVFSLKVGEISGVVKTQFGFHIIKV 112
prsA PRK00059
peptidylprolyl isomerase; Provisional
 79-267 6.64e-15

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 74.36  E-value: 6.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376  79 KDIDDEIKKEQKQ-YGGKDQFESMLKQQGMSLDDYKEQKK----LAAYQKQLLADkVKVSDKELKE-------------N 140
Cdd:PRK00059  117 KEVDKKINEIKKQfNNDEEQFEEALKATGFTEETFKEYLKnqiiIEKVINEVVKD-VKVTDKDAQKyynenkskftekpN 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376 141 TKKASHILIKVKSSSSDkeglsdkkakekaekIQKEVEKNPDkFGEIAKKESMDSSSAKKDGSLGYV--VKGQMVSKFEK 218
Cdd:PRK00059  196 TMHLAHILVKTEDEAKK---------------VKKRLDKGED-FAKVAKEVSQDPGSKDKGGDLGDVpySDSGYDKEFMD 259

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1091152376 219 ALFKLKEGQVSDVVKTDYGYHVIKADKE-----SDFDKQKSKLKAKLIEQKVQK 267
Cdd:PRK00059  260 GAKALKEGEISAPVKTQFGYHIIKAIKKkeypvKPFDSVKEDIKKQLLQEKQSE 313
prsA PRK01326
foldase protein PrsA; Reviewed
 13-290 1.05e-11

foldase protein PrsA; Reviewed


Pssm-ID: 179281 [Multi-domain]  Cd Length: 310  Bit Score: 64.45  E-value: 1.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376  13 ASALLLGACGSNatdSESNTLISSKAGDVKVKDVMNKIGDEQIASTS-FSIALNKILADKYKDKVDTKDIDDEIKKEQKQ 91
Cdd:PRK01326   13 LSVATLAACSKT---NENTKVISMKGDTITVSDFYNQVKNNPSAQQAmLNLTISRVFEKQYGDKVSDKEVEKAYAKTAKQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376  92 YGgkDQFESMLKQQGMSLDDYKEQ---KKLAAYQKQLLADKVKVSD---KELKENTKKASHILIKVKSSSSDKEGLSDKK 165
Cdd:PRK01326   90 YG--ASFSRALAQAGLTPETYKAQirtSKLVEYAVKEAAKKELTDEaykKAYEEYTPEVTAQIIRLDNEDKAKSVLEEAK 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376 166 AKEKA-EKIQKEVEKNPDKFGEIakkeSMDSSSAkkdgslgyvvkgQMVSKFEKALFKLKEGQVSDVVKT------DYGY 238
Cdd:PRK01326  168 AEGADfAQIAKENTTTKEKKGEY----KFDSGST------------NVPEQVKKAAFALDEDGVSDVISVldptayQSKY 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1091152376 239 HVI----KADKESDFDKQKSKLKAKLIEQKvQKDPKILTNAYKDLLKEYDVDYKDS 290
Cdd:PRK01326  232 YIVkvtkKTEKKSDWKDYKKRLKAIILAQK-QNDSNFQNKVIAKALDKANVKIKDK 286
PRK12450 PRK12450
foldase protein PrsA; Reviewed
 1-289 9.18e-11

foldase protein PrsA; Reviewed


Pssm-ID: 138982 [Multi-domain]  Cd Length: 309  Bit Score: 61.64  E-value: 9.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376   1 MKIMNKLIVPVT--ASALLLGACGSNatdSESNTLISSKAGDVKVKDVMNKIGDEQIASTS-FSIALNKILADKYKDKVD 77
Cdd:PRK12450    1 MKQMNKLITGVVtlATVVTLSACQSS---HNNTKLVSMKGDTITVSDFYNETKNTELAQKAmLSLVISRVFETQYANKVS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376  78 TKDIDDEIKKEQKQYGGkdQFESMLKQQGMSLDDYKEQ---KKLAAYQKQLLADKVKVSDKELKENTKKASHILIKVKSS 154
Cdd:PRK12450   78 DKEVEKAYKQTADQYGT--SFKTVLAQSGLTPETYKKQirlTKLVEYAVKEQAKNETISKKDYRQAYDAYTPTMTAEIMQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376 155 SSDKEglsdkkakeKAEKIQKEVEKNPDKFGEIAKKESmdSSSAKKDGSLGYVVKGQMVSKFEKALFKLKEGQVSDVVK- 233
Cdd:PRK12450  156 FEKEE---------DAKAALEAVKAEGADFAAIAKEKT--IAADKKTTYTFDSGETTLPAEVVRAASGLKEGNRSEIITa 224

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091152376 234 -----TDYGYHVI----KADKESDFDKQKSKLKAKLIEQKVQkDPKILTNAYKDLLKEYDVDYKD 289
Cdd:PRK12450  225 ldpatSKRTYHIIkvtkKATKKADWKAYQKRLKDIIVTGKLK-DPDFQNKVIAKALDKANVKIKD 288
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 141-242 1.76e-07

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 48.48  E-value: 1.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376 141 TKKASHILIKVKSSSSDkeglsdkkakekaekIQKEVEKNPDkFGEIAKKESMdSSSAKKDGSLGYVVKGQMVSKFEKAL 220
Cdd:PRK15441    4 TAAALHILVKEEKLALD---------------LLEQIKNGAD-FGKLAKKHSI-CPSGKRGGDLGEFRQGQMVPAFDKVV 66

                          90       100
                  ....*....|....*....|..
gi 1091152376 221 FKLKEGQVSDVVKTDYGYHVIK 242
Cdd:PRK15441   67 FSCPVLEPTGPLHTQFGYHIIK 88
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 143-242 4.48e-06

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 47.81  E-value: 4.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376 143 KASHILIKVKSSssdkegLSDKKAKEKAEKIQKEVEKNPDKFGEIAKKESMDSSSAKKDGSLGYVVKGQMVSKFEKALFK 222
Cdd:PRK10770  268 HARHILLKPSPI------MTDEQARAKLEQIAADIKSGKTTFAAAAKEFSQDPGSANQGGDLGWATPDIFDPAFRDALMR 341

                          90       100
                  ....*....|....*....|
gi 1091152376 223 LKEGQVSDVVKTDYGYHVIK 242
Cdd:PRK10770  342 LNKGQISAPVHSSFGWHLIE 361
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 179-258 1.15e-05

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 46.93  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091152376 179 KNPDKFGEIAKKESMDSSSAKKDGSLGYVVKGQMVSKFEKAlfKLKE-GQVSDVVKTDYGYHVIKADkesdfDKQKSKLK 257
Cdd:PRK10788  292 KKGADFATLAKEKSTDIISARNGGDLGWLEPATTPDELKNA--GLKEkGQLSGVIKSSVGFLIVRLD-----DIQPAKVK 364


                  .
gi 1091152376 258 A 258
Cdd:PRK10788  365 P 365
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
182-245 5.30e-03

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 36.27  E-value: 5.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091152376 182 DKFGEIAKKESMDSSSAKKDGSLGYVVKGQMVSK-FEKALFKLKEGQVSDVVKTDYGYHVIKADK 245
Cdd:pfam13145  43 LKAGALEDFAALAKGEGIKAATLDIVESAELLPEeLAKAAFALKPGEVSGPIKTGNGYYVVRVTE 107
 
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