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Conserved domains on  [gi|1105586757|emb|SHC25977|]
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Foldase protein PrsA precursor [Staphylococcus aureus]

Protein Classification

foldase protein PrsA( domain architecture ID 13439506)

foldase protein PrsA plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins

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

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, ...
 143-267 4.08e-31

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


:

Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 113.90  E-value: 4.08e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757 143 KASHILIKVKskksdkEGLDDKEAKQKAEEIQKEVSKDpSKFGEIAKKESMDTGSAKKDGELGYVLKGQTDKDFEKALFK 222
Cdd:COG0760    10 RASHILVKVP------PSEDRAKAEAKAEELLAQLKAG-ADFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEAAFA 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1105586757 223 LKDGEVSEVVKSSFGYHIIK-----ADKPTDFNSEKQSLKEKLVDQKVQK 267
Cdd:COG0760    83 LKPGEISGPVKTQFGYHIIKvedrrPAETPPFEEVKQQIRQELFQQALEA 132
Rotamase_2 super family cl29122
PPIC-type PPIASE domain;
3-305 1.09e-28

PPIC-type PPIASE domain;


The actual alignment was detected with superfamily member PRK03095:

Pssm-ID: 452928 [Multi-domain]  Cd Length: 287  Bit Score: 111.62  E-value: 1.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757   3 MINKLIVPVTASALLLGACGASATDSkentLISSKAGDVT---VADTMKKIGKDQIANASFTEmlnKILADKYKnkVNDK 79
Cdd:PRK03095    1 MKKAMLALAATSVIALSACGTSSSDK----IVTSKAGDITkdeFYEQMKTQAGKQVLNNMVME---KVLIKNYK--VEDK 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757  80 KIDEQIEKMQKQYGgkDKFEKALQQQGLTADKYKENLRTAAYHKELLSDKIkiSDSEIKEDSK---KASHILIKvkskks 156
Cdd:PRK03095   72 EVDKKYDEMKKQYG--DQFDTLLKQQGIKEETLKTGVRAQLAQEKAIEKTI--TDKELKDNYKpeiKASHILVK------ 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757 157 dkeglDDKEAKQKAEEIQKEVSkdpskFGEIAKKESMDTGSAKKDGELGYVLKGQTDKDFEKALFKLKDGEVSEVVKSSF 236
Cdd:PRK03095  142 -----DEATAKKVKEELGQGKS-----FEELAKQYSEDTGSKEKGGDLGFFGAGKMVKEFEDAAYKLKKDEVSEPVKSQF 211

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1105586757 237 GYHIIKA----DKPTDFNSEKQSLKEKLVDQKVQkNPKLLTDAYKDLLKEYDVDFKDRDIKSVVEDKILNPEK 305
Cdd:PRK03095  212 GYHIIKVtdikEPEKSFEQSKADIKKELVQKKAQ-DGEFMNDLMMKEIKKADVKVDDKDLKDLFEEKKADAKK 283
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 143-267 4.08e-31

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 113.90  E-value: 4.08e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757 143 KASHILIKVKskksdkEGLDDKEAKQKAEEIQKEVSKDpSKFGEIAKKESMDTGSAKKDGELGYVLKGQTDKDFEKALFK 222
Cdd:COG0760    10 RASHILVKVP------PSEDRAKAEAKAEELLAQLKAG-ADFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEAAFA 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1105586757 223 LKDGEVSEVVKSSFGYHIIK-----ADKPTDFNSEKQSLKEKLVDQKVQK 267
Cdd:COG0760    83 LKPGEISGPVKTQFGYHIIKvedrrPAETPPFEEVKQQIRQELFQQALEA 132
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 146-245 5.66e-31

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: 112.01  E-value: 5.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757 146 HILIKVKskksDKEGLDDKEAKQKAEEIQKEVSKDPSKFGEIAKKESMDTGSAKKDGELGYVLKGQTDKDFEKALFKLKD 225
Cdd:pfam00639   1 HILIKTP----EASERDRAEAKAKAEEILEQLKSGEDSFAELARKYSDDCPSAANGGDLGWFTRGQLPPEFEKAAFALKP 76

                          90       100
                  ....*....|....*....|
gi 1105586757 226 GEVSEVVKSSFGYHIIKADK 245
Cdd:pfam00639  77 GEISGPVETRFGFHIIKLTD 96
prsA PRK03095
peptidylprolyl isomerase PrsA;
3-305 1.09e-28

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 111.62  E-value: 1.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757   3 MINKLIVPVTASALLLGACGASATDSkentLISSKAGDVT---VADTMKKIGKDQIANASFTEmlnKILADKYKnkVNDK 79
Cdd:PRK03095    1 MKKAMLALAATSVIALSACGTSSSDK----IVTSKAGDITkdeFYEQMKTQAGKQVLNNMVME---KVLIKNYK--VEDK 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757  80 KIDEQIEKMQKQYGgkDKFEKALQQQGLTADKYKENLRTAAYHKELLSDKIkiSDSEIKEDSK---KASHILIKvkskks 156
Cdd:PRK03095   72 EVDKKYDEMKKQYG--DQFDTLLKQQGIKEETLKTGVRAQLAQEKAIEKTI--TDKELKDNYKpeiKASHILVK------ 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757 157 dkeglDDKEAKQKAEEIQKEVSkdpskFGEIAKKESMDTGSAKKDGELGYVLKGQTDKDFEKALFKLKDGEVSEVVKSSF 236
Cdd:PRK03095  142 -----DEATAKKVKEELGQGKS-----FEELAKQYSEDTGSKEKGGDLGFFGAGKMVKEFEDAAYKLKKDEVSEPVKSQF 211

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1105586757 237 GYHIIKA----DKPTDFNSEKQSLKEKLVDQKVQkNPKLLTDAYKDLLKEYDVDFKDRDIKSVVEDKILNPEK 305
Cdd:PRK03095  212 GYHIIKVtdikEPEKSFEQSKADIKKELVQKKAQ-DGEFMNDLMMKEIKKADVKVDDKDLKDLFEEKKADAKK 283
prsA PRK00059
peptidylprolyl isomerase; Provisional
 52-267 7.67e-18

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 82.84  E-value: 7.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757  52 KDQIANASFTEMLNKILADKYKNKVND----KKIDEQIEKMQKQ-YGGKDKFEKALQQQGLTADKYKENLRTAAYHKELL 126
Cdd:PRK00059   86 KEQILDSLITEKVLLQKAKELKLIPSEeelnKEVDKKINEIKKQfNNDEEQFEEALKATGFTEETFKEYLKNQIIIEKVI 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757 127 SD---KIKISDSEIK---EDSKK----------ASHILIKVkskksdkegldDKEAKQKAEEIQKEvskdpSKFGEIAKK 190
Cdd:PRK00059  166 NEvvkDVKVTDKDAQkyyNENKSkftekpntmhLAHILVKT-----------EDEAKKVKKRLDKG-----EDFAKVAKE 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757 191 ESMDTGSAKKDGELGYV--LKGQTDKDFEKALFKLKDGEVSEVVKSSFGYHIIKADKP-----TDFNSEKQSLKEKLVDQ 263
Cdd:PRK00059  230 VSQDPGSKDKGGDLGDVpySDSGYDKEFMDGAKALKEGEISAPVKTQFGYHIIKAIKKkeypvKPFDSVKEDIKKQLLQE 309


                  ....
gi 1105586757 264 KVQK 267
Cdd:PRK00059  310 KQSE 313
SurA_N_3 pfam13624
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 69-130 9.70e-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: 39.09  E-value: 9.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1105586757  69 ADKYKNKVNDKKIDEQIEKMQK-QYGGK---DKFEKALQQQGLTADKYKENLRtaayhKELLSDKI 130
Cdd:pfam13624 101 AKKLGLAVSDEEVRQAIASIPAfQEDGKfdkERYRQLLRANGLTPAEFEASLR-----QDLLLQQL 161
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 143-267 4.08e-31

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 113.90  E-value: 4.08e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757 143 KASHILIKVKskksdkEGLDDKEAKQKAEEIQKEVSKDpSKFGEIAKKESMDTGSAKKDGELGYVLKGQTDKDFEKALFK 222
Cdd:COG0760    10 RASHILVKVP------PSEDRAKAEAKAEELLAQLKAG-ADFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEAAFA 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1105586757 223 LKDGEVSEVVKSSFGYHIIK-----ADKPTDFNSEKQSLKEKLVDQKVQK 267
Cdd:COG0760    83 LKPGEISGPVKTQFGYHIIKvedrrPAETPPFEEVKQQIRQELFQQALEA 132
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 146-245 5.66e-31

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: 112.01  E-value: 5.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757 146 HILIKVKskksDKEGLDDKEAKQKAEEIQKEVSKDPSKFGEIAKKESMDTGSAKKDGELGYVLKGQTDKDFEKALFKLKD 225
Cdd:pfam00639   1 HILIKTP----EASERDRAEAKAKAEEILEQLKSGEDSFAELARKYSDDCPSAANGGDLGWFTRGQLPPEFEKAAFALKP 76

                          90       100
                  ....*....|....*....|
gi 1105586757 226 GEVSEVVKSSFGYHIIKADK 245
Cdd:pfam00639  77 GEISGPVETRFGFHIIKLTD 96
prsA PRK03095
peptidylprolyl isomerase PrsA;
3-305 1.09e-28

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 111.62  E-value: 1.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757   3 MINKLIVPVTASALLLGACGASATDSkentLISSKAGDVT---VADTMKKIGKDQIANASFTEmlnKILADKYKnkVNDK 79
Cdd:PRK03095    1 MKKAMLALAATSVIALSACGTSSSDK----IVTSKAGDITkdeFYEQMKTQAGKQVLNNMVME---KVLIKNYK--VEDK 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757  80 KIDEQIEKMQKQYGgkDKFEKALQQQGLTADKYKENLRTAAYHKELLSDKIkiSDSEIKEDSK---KASHILIKvkskks 156
Cdd:PRK03095   72 EVDKKYDEMKKQYG--DQFDTLLKQQGIKEETLKTGVRAQLAQEKAIEKTI--TDKELKDNYKpeiKASHILVK------ 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757 157 dkeglDDKEAKQKAEEIQKEVSkdpskFGEIAKKESMDTGSAKKDGELGYVLKGQTDKDFEKALFKLKDGEVSEVVKSSF 236
Cdd:PRK03095  142 -----DEATAKKVKEELGQGKS-----FEELAKQYSEDTGSKEKGGDLGFFGAGKMVKEFEDAAYKLKKDEVSEPVKSQF 211

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1105586757 237 GYHIIKA----DKPTDFNSEKQSLKEKLVDQKVQkNPKLLTDAYKDLLKEYDVDFKDRDIKSVVEDKILNPEK 305
Cdd:PRK03095  212 GYHIIKVtdikEPEKSFEQSKADIKKELVQKKAQ-DGEFMNDLMMKEIKKADVKVDDKDLKDLFEEKKADAKK 283
prsA PRK04405
peptidylprolyl isomerase; Provisional
 3-298 5.74e-27

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 107.18  E-value: 5.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757   3 MINKLIVPVTASALLLGACGASATDSKENTLISSKAGDVTVADTMKKIGKDQIANASFTEM-LNKILADKYKNKVNDKKI 81
Cdd:PRK04405    1 MKKKMKKWALAAASAGLALSLAGCSSNQATVATYSGGKITQSQYYKEMKQSSAGKTVLANMiIYRALEKQYGKKVSTKKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757  82 DEQIEKMQKQYGgkDKFEKALQQQGLTADKYKENLRTAAYHKELLSDKIKISDSEIKEDSKK------ASHILIkvkSKK 155
Cdd:PRK04405   81 DKQYNSYKKQYG--SSFDSVLSQNGMTTSSFKQNLRTNLLSEAALKKLKKVTNSQLKKAWKSyqpkvtVQHILV---SKK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757 156 SdkeglddkeakqKAEEIQKEVsKDPSKFGEIAKKESMDTGSAKKDGELGYVLKGQT--DKDFEKALFKLKDGEV-SEVV 232
Cdd:PRK04405  156 S------------TAETVIKKL-KDGKDFAKLAKKYSTDTATKNKGGKLSAFDSTDTtlDSTFKTAAFKLKNGEYtTTPV 222

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1105586757 233 KSSFGYHIIKADKPT---DFNSEKQSLKEKLVDQKVQkNPKLLTDAYKDLLKEYDVDFKDRDIKSVVED 298
Cdd:PRK04405  223 KTTYGYEVIKMIKHPakgTFSDHKKALTKQIYAKWAS-DSSVMQRVISKVLKKANVSIKDKDLKDALSS 290
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 15-297 3.11e-25

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 102.36  E-value: 3.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757  15 ALLLGACGASatdskeNTLISSKAGDVTVADTMKKIGKDQIANASFTEMLNKILADKYKnkVNDKKIDEQIEKMQKQYGg 94
Cdd:PRK02998   16 VLALSACGSS------DNVVTSKVGNITEKELSKELRQKYGESTLYQMVLSKALLDKYK--VSDEEAKKQVEEAKDKMG- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757  95 kDKFEKALQQQGL-TADKYKENLR-TAAYHKELlsdKIKISDSEIKEDSK---KASHILIKvkskksdkeglDDKEAKQK 169
Cdd:PRK02998   87 -DNFKSTLEQVGLkNEDELKEKMKpEIAFEKAI---KATVTEKDVKDNYKpemKVSHILVK-----------DEKTAKEV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757 170 AEEIQkevskDPSKFGEIAKKESMDTGSAKKDGELGYVLKGQTDKDFEKALFKLKDGEVSEVVKSSFGYHIIKADKPTD- 248
Cdd:PRK02998  152 KEKVN-----NGEDFAALAKQYSEDTGSKEQGGEISGFAPGQTVKEFEEAAYKLDAGQVSEPVKTTYGYHIIKVTDKKEl 226

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1105586757 249 --FNSEKQSLKEKLVDQKVQK-NPKLLTDAYKDLLKEYDVDFKDRDIKSVVE 297
Cdd:PRK02998  227 kpFDEVKDSIRKDLEQQRLQDtTGKWKQQVVNDLLKDADIKVNDKEFKDTFK 278
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 131-247 2.20e-24

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: 95.51  E-value: 2.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757 131 KISDSEIKEDSKKASHILIKVkskkSDKEGLDDKEAKQKAEEIqKEVSKDPSKFGEIAKKESMDTGSAKKDGELGYVLKG 210
Cdd:pfam13616   5 KLVDKKSAPDSVKASHILISY----SQAVSRTEEEAKAKADSL-LAALKNGADFAALAKTYSDDPASKNNGGDLGWFTKG 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1105586757 211 QTDKDFEKALFKLKDGEVSEVVKSSFGYHIIKADKPT 247
Cdd:pfam13616  80 QMVKEFEDAVFSLKVGEISGVVKTQFGFHIIKVTDKK 116
prsA PRK03002
peptidylprolyl isomerase PrsA;
1-293 2.38e-20

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 88.84  E-value: 2.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757   1 MKMINKLIVPVTASALLLGACGASATDSkenTLISSKAGDVTVADTMKKIgKDQIANASFTEMLNKILADKyKNKVNDKK 80
Cdd:PRK03002    1 MRGKHIFIITALISILMLSACGQKNSSA---TVATATDSTITKSDFEKQL-KDRYGKDMLYEMMAQDVITK-KYKVSDDD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757  81 IDEQIEKMQKQYGgkDKFEKALQQQGLtadKYKENLRTAAYHKELLSDKIK--ISDSEIKEDSK---KASHILIKvkskk 155
Cdd:PRK03002   76 VDKEVQKAKSQYG--DQFKNVLKNNGL---KDEADFKNQIKFKLAMNEAIKksVTEKDVKDHYKpeiKASHILVS----- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757 156 sdkeglDDKEAKqkaeEIQKEVSKDPSkFGEIAKKESMDTGSAKKDGELGYVLKGQTDKDFEKALFKLKDGEVSEVVKSS 235
Cdd:PRK03002  146 ------DENEAK----EIKKKLDAGAS-FEELAKQESQDLLSKEKGGDLGYFNSGRMAPEFETAAYKLKVGQISNPVKSP 214

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1105586757 236 FGYHIIKADKPTD---FNSEKQSLKEKLVDQKVqKNPKLLTDAYKDLLKEYDVDFKDRDIK 293
Cdd:PRK03002  215 NGYHIIKLTDKKDlkpYDEVKDSIRKNLEEERT-ADPIFGKKLLQSELKKANIKINDSELE 274
prsA PRK00059
peptidylprolyl isomerase; Provisional
 52-267 7.67e-18

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 82.84  E-value: 7.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757  52 KDQIANASFTEMLNKILADKYKNKVND----KKIDEQIEKMQKQ-YGGKDKFEKALQQQGLTADKYKENLRTAAYHKELL 126
Cdd:PRK00059   86 KEQILDSLITEKVLLQKAKELKLIPSEeelnKEVDKKINEIKKQfNNDEEQFEEALKATGFTEETFKEYLKNQIIIEKVI 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757 127 SD---KIKISDSEIK---EDSKK----------ASHILIKVkskksdkegldDKEAKQKAEEIQKEvskdpSKFGEIAKK 190
Cdd:PRK00059  166 NEvvkDVKVTDKDAQkyyNENKSkftekpntmhLAHILVKT-----------EDEAKKVKKRLDKG-----EDFAKVAKE 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757 191 ESMDTGSAKKDGELGYV--LKGQTDKDFEKALFKLKDGEVSEVVKSSFGYHIIKADKP-----TDFNSEKQSLKEKLVDQ 263
Cdd:PRK00059  230 VSQDPGSKDKGGDLGDVpySDSGYDKEFMDGAKALKEGEISAPVKTQFGYHIIKAIKKkeypvKPFDSVKEDIKKQLLQE 309


                  ....
gi 1105586757 264 KVQK 267
Cdd:PRK00059  310 KQSE 313
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 140-242 4.94e-17

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 75.45  E-value: 4.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757 140 DSKKASHILIKVK------SKKSDKE-GLDDKEAKQKAEEIQKEVSKDPSKFGEIAKKESmDTGSAKKDGELGYVLKGQT 212
Cdd:PTZ00356    4 DTVRAAHLLIKHTgsrnpvSRRTGKPvTRSKEEAIKELAKWREQIVSGEKTFEEIARQRS-DCGSAAKGGDLGFFGRGQM 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1105586757 213 DKDFEKALFKLKDGEVSEVVKSSFGYHIIK 242
Cdd:PTZ00356   83 QKPFEDAAFALKVGEISDIVHTDSGVHIIL 112
PRK12450 PRK12450
foldase protein PrsA; Reviewed
 1-290 7.87e-15

foldase protein PrsA; Reviewed


Pssm-ID: 138982 [Multi-domain]  Cd Length: 309  Bit Score: 73.59  E-value: 7.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757   1 MKMINKLIVPVT--ASALLLGACGASATDSKentLISSKAGDVTVADTMKKIGKDQIAN-ASFTEMLNKILADKYKNKVN 77
Cdd:PRK12450    1 MKQMNKLITGVVtlATVVTLSACQSSHNNTK---LVSMKGDTITVSDFYNETKNTELAQkAMLSLVISRVFETQYANKVS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757  78 DKKIDEQIEKMQKQYGGkdKFEKALQQQGLTADKYKENLRTAayhkellsdkiKISDSEIKEDSKKashiliKVKSKKSD 157
Cdd:PRK12450   78 DKEVEKAYKQTADQYGT--SFKTVLAQSGLTPETYKKQIRLT-----------KLVEYAVKEQAKN------ETISKKDY 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757 158 KEGLDDKEAKQKAEEIQKEVSKDPSKFGEIAKKESMDTGSAKK------DGELGYVLKGQTDK---DFEKALFKLKDGEV 228
Cdd:PRK12450  139 RQAYDAYTPTMTAEIMQFEKEEDAKAALEAVKAEGADFAAIAKektiaaDKKTTYTFDSGETTlpaEVVRAASGLKEGNR 218

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1105586757 229 SEVVK------SSFGYHII----KADKPTDFNSEKQSLKEKLVDQKVQkNPKLLTDAYKDLLKEYDVDFKDR 290
Cdd:PRK12450  219 SEIITaldpatSKRTYHIIkvtkKATKKADWKAYQKRLKDIIVTGKLK-DPDFQNKVIAKALDKANVKIKDK 289
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 143-242 1.17e-13

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 70.93  E-value: 1.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757 143 KASHILIKVKSKksdkegLDDKEAKQKAEEIQKEVSKDPSKFGEIAKKESMDTGSAKKDGELGYVLKGQTDKDFEKALFK 222
Cdd:PRK10770  268 HARHILLKPSPI------MTDEQARAKLEQIAADIKSGKTTFAAAAKEFSQDPGSANQGGDLGWATPDIFDPAFRDALMR 341

                          90       100
                  ....*....|....*....|
gi 1105586757 223 LKDGEVSEVVKSSFGYHIIK 242
Cdd:PRK10770  342 LNKGQISAPVHSSFGWHLIE 361
prsA PRK01326
foldase protein PrsA; Reviewed
 13-260 1.02e-10

foldase protein PrsA; Reviewed


Pssm-ID: 179281 [Multi-domain]  Cd Length: 310  Bit Score: 61.75  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757  13 ASALLLGACGASATDSKentLISSKAGDVTVADTMKKIGKDQIANASFTEM-LNKILADKYKNKVNDKKIDEQIEKMQKQ 91
Cdd:PRK01326   13 LSVATLAACSKTNENTK---VISMKGDTITVSDFYNQVKNNPSAQQAMLNLtISRVFEKQYGDKVSDKEVEKAYAKTAKQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757  92 YGgkDKFEKALQQQGLTADKYKENLRTAayhkellsdkiKISDSEIKEDSKKAshiLIKVKSKKSDKEGLDDKEAK---- 167
Cdd:PRK01326   90 YG--ASFSRALAQAGLTPETYKAQIRTS-----------KLVEYAVKEAAKKE---LTDEAYKKAYEEYTPEVTAQiirl 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757 168 ---QKAEEIQKEVSKDPSKFGEIAKKESMDTGsakKDGELGYVlKGQTD--KDFEKALFKLKDGEVSEVVKS------SF 236
Cdd:PRK01326  154 dneDKAKSVLEEAKAEGADFAQIAKENTTTKE---KKGEYKFD-SGSTNvpEQVKKAAFALDEDGVSDVISVldptayQS 229

                         250       260
                  ....*....|....*....|....
gi 1105586757 237 GYHIIKADKPTDFNSEKQSLKEKL 260
Cdd:PRK01326  230 KYYIVKVTKKTEKKSDWKDYKKRL 253
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 128-244 9.14e-08

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 53.47  E-value: 9.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757 128 DKIKISDSEIKE--DSKKASHI--------LIKVKSKKSDKEGLDdkEAKQKAEeiqkevskdpskFGEIAKKESMDTGS 197
Cdd:PRK10788  245 QKITVSDADIQAyyDQHQDQFTqperkrysIIQTKTEAEAKAVLD--ELKKGAD------------FATLAKEKSTDIIS 310

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1105586757 198 AKKDGELGYVLKGQTDKDFEKALFKLKdGEVSEVVKSSFGYHIIKAD 244
Cdd:PRK10788  311 ARNGGDLGWLEPATTPDELKNAGLKEK-GQLSGVIKSSVGFLIVRLD 356
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 144-242 3.58e-05

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 41.93  E-value: 3.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757 144 ASHILIKvkskksdkeglDDKEAKQKAEEIqkevsKDPSKFGEIAKKESMdTGSAKKDGELGYVLKGQTDKDFEKALFKL 223
Cdd:PRK15441    7 ALHILVK-----------EEKLALDLLEQI-----KNGADFGKLAKKHSI-CPSGKRGGDLGEFRQGQMVPAFDKVVFSC 69

                          90
                  ....*....|....*....
gi 1105586757 224 KDGEVSEVVKSSFGYHIIK 242
Cdd:PRK15441   70 PVLEPTGPLHTQFGYHIIK 88
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
162-245 4.96e-04

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 39.35  E-value: 4.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757 162 DDKEAKQKAEEIQKEVSKDPSKFGEIAKKESMDTGSAKKDGELgyvlkgqtDKDFEKALFKLKDGEVSEVVKSSFGYHII 241
Cdd:pfam13145  32 DQVAADAALALLKAGALEDFAALAKGEGIKAATLDIVESAELL--------PEELAKAAFALKPGEVSGPIKTGNGYYVV 103


                  ....
gi 1105586757 242 KADK 245
Cdd:pfam13145 104 RVTE 107
SurA_N_3 pfam13624
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 69-130 9.70e-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: 39.09  E-value: 9.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1105586757  69 ADKYKNKVNDKKIDEQIEKMQK-QYGGK---DKFEKALQQQGLTADKYKENLRtaayhKELLSDKI 130
Cdd:pfam13624 101 AKKLGLAVSDEEVRQAIASIPAfQEDGKfdkERYRQLLRANGLTPAEFEASLR-----QDLLLQQL 161
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 63-242 4.97e-03

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 38.18  E-value: 4.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757  63 MLNKIL--ADKYKNKVNDKKIDEQIEKMQKQ-YGGKDKFEKALQQQGLTADKYKENLRtaayhKELLSD---------KI 130
Cdd:PRK10770   58 MDNIILqmAQKMGVKISDEQLDQAIANIAAQnNMTLDQMRSRLAYDGLNYNTYRNQIR-----KEMIISevrnnevrrRI 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105586757 131 KISDSEIKEDSKKA------------SHILIKVKSKKSDKEGlddKEAKQKAEEIQKEvSKDPSKFGEIAKKESMDTgSA 198
Cdd:PRK10770  133 TILPQEVDSLAKQIgnqndastelnlSHILIPLPENPTQDQV---DEAESQARSIVDQ-ARNGADFGKLAIAYSADQ-QA 207

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1105586757 199 KKDGELGYVLKGQTDKDFEKALFKLKDGEVSEVVKSSFGYHIIK 242
Cdd:PRK10770  208 LKGGQMGWGRIQELPGLFAQALSTAKKGDIVGPIRSGVGFHILK 251
 
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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