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Conserved domains on  [gi|499723807|ref|WP_011404541|]
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peptidylprolyl isomerase [Salinibacter ruber]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 13434083)

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
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 196-292 2.68e-24

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: 96.60  E-value: 2.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807  196 HI-VRYPKPTEASRQQAKSLITSVRDSIVNGGASLEAMARQFSAPDAAGTASGALTDVNLNDLVPEFAAVASRTPVGQIS 274
Cdd:pfam00639   1 HIlIKTPEASERDRAEAKAKAEEILEQLKSGEDSFAELARKYSDDCPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEIS 80

                          90
                  ....*....|....*...
gi 499723807  275 QPFynESQNGFHILRIDA 292
Cdd:pfam00639  81 GPV--ETRFGFHIIKLTD 96
prsA super family cl35053
peptidylprolyl isomerase; Provisional
 47-298 3.93e-17

peptidylprolyl isomerase; Provisional


The actual alignment was detected with superfamily member PRK00059:

Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 82.45  E-value: 3.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807  47 AVVGDEIVLKSEVDQL--VRRQTRQQNVSY-----SNSLWMEALRQ--------LVDQKLLAEQARrDTTITVSDQQLSD 111
Cdd:PRK00059  39 ATVNGEKITRGDLDKDpkMQQVLEQLKQQYgdnyeKNEQVKEQIKQqkeqildsLITEKVLLQKAK-ELKLIPSEEELNK 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807 112 QLDRRISQY-VERAGSEERLEQAYgKSILEIKEQFREDLRGQILSQQLRRRRMQSIDITPSEVRQWFEQiPQDSLPQLPK 190
Cdd:PRK00059 118 EVDKKINEIkKQFNNDEEQFEEAL-KATGFTEETFKEYLKNQIIIEKVINEVVKDVKVTDKDAQKYYNE-NKSKFTEKPN 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807 191 TVRLSHIVrypKPTEASRQQAKSLItsvrdsivNGGASLEAMARQFSAPDAAGTASGALTDVNLND--LVPEFAAVASRT 268
Cdd:PRK00059 196 TMHLAHIL---VKTEDEAKKVKKRL--------DKGEDFAKVAKEVSQDPGSKDKGGDLGDVPYSDsgYDKEFMDGAKAL 264

                        250       260       270
                 ....*....|....*....|....*....|
gi 499723807 269 PVGQISQPFynESQNGFHILRIDAKDGSTV 298
Cdd:PRK00059 265 KEGEISAPV--KTQFGYHIIKAIKKKEYPV 292
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 295-449 2.73e-15

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


:

Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 72.69  E-value: 2.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807 295 GSTVDLHHVLIKPNAPTGK-RAKEYLSAVRDTLVNNEDvsFERMARRHSEEDRTAQNGGrvtdpesgarDL---VLDALG 370
Cdd:COG0760    6 PEEVRASHILVKVPPSEDRaKAEAKAEELLAQLKAGAD--FAELAKEYSQDPGSAANGG----------DLgwfSRGQLV 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499723807 371 PSWTRTIRPLEAGDISEPSRVQllnddEAYHIVRLDRRVPAHRASLETDYEQIRQRALQdkrsRKMREWTDQLREKIYV 449
Cdd:COG0760   74 PEFEEAAFALKPGEISGPVKTQ-----FGYHIIKVEDRRPAETPPFEEVKQQIRQELFQ----QALEAWLEELRKKAKI 143
 
Name Accession Description Interval E-value
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 196-292 2.68e-24

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: 96.60  E-value: 2.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807  196 HI-VRYPKPTEASRQQAKSLITSVRDSIVNGGASLEAMARQFSAPDAAGTASGALTDVNLNDLVPEFAAVASRTPVGQIS 274
Cdd:pfam00639   1 HIlIKTPEASERDRAEAKAKAEEILEQLKSGEDSFAELARKYSDDCPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEIS 80

                          90
                  ....*....|....*...
gi 499723807  275 QPFynESQNGFHILRIDA 292
Cdd:pfam00639  81 GPV--ETRFGFHIIKLTD 96
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 189-303 7.71e-19

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 82.70  E-value: 7.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807 189 PKTVRLSHIVRYPKPTEaSRQQAKSLITSVRDSIvNGGASLEAMARQFSAPDAAGTASGALTDVNLNDLVPEFAAVASRT 268
Cdd:COG0760    6 PEEVRASHILVKVPPSE-DRAKAEAKAEELLAQL-KAGADFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEAAFAL 83

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 499723807 269 PVGQISQPFynESQNGFHILRIDAK-DGSTVDLHHV 303
Cdd:COG0760   84 KPGEISGPV--KTQFGYHIIKVEDRrPAETPPFEEV 117
prsA PRK00059
peptidylprolyl isomerase; Provisional
 47-298 3.93e-17

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 82.45  E-value: 3.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807  47 AVVGDEIVLKSEVDQL--VRRQTRQQNVSY-----SNSLWMEALRQ--------LVDQKLLAEQARrDTTITVSDQQLSD 111
Cdd:PRK00059  39 ATVNGEKITRGDLDKDpkMQQVLEQLKQQYgdnyeKNEQVKEQIKQqkeqildsLITEKVLLQKAK-ELKLIPSEEELNK 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807 112 QLDRRISQY-VERAGSEERLEQAYgKSILEIKEQFREDLRGQILSQQLRRRRMQSIDITPSEVRQWFEQiPQDSLPQLPK 190
Cdd:PRK00059 118 EVDKKINEIkKQFNNDEEQFEEAL-KATGFTEETFKEYLKNQIIIEKVINEVVKDVKVTDKDAQKYYNE-NKSKFTEKPN 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807 191 TVRLSHIVrypKPTEASRQQAKSLItsvrdsivNGGASLEAMARQFSAPDAAGTASGALTDVNLND--LVPEFAAVASRT 268
Cdd:PRK00059 196 TMHLAHIL---VKTEDEAKKVKKRL--------DKGEDFAKVAKEVSQDPGSKDKGGDLGDVPYSDsgYDKEFMDGAKAL 264

                        250       260       270
                 ....*....|....*....|....*....|
gi 499723807 269 PVGQISQPFynESQNGFHILRIDAKDGSTV 298
Cdd:PRK00059 265 KEGEISAPV--KTQFGYHIIKAIKKKEYPV 292
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 295-449 2.73e-15

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 72.69  E-value: 2.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807 295 GSTVDLHHVLIKPNAPTGK-RAKEYLSAVRDTLVNNEDvsFERMARRHSEEDRTAQNGGrvtdpesgarDL---VLDALG 370
Cdd:COG0760    6 PEEVRASHILVKVPPSEDRaKAEAKAEELLAQLKAGAD--FAELAKEYSQDPGSAANGG----------DLgwfSRGQLV 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499723807 371 PSWTRTIRPLEAGDISEPSRVQllnddEAYHIVRLDRRVPAHRASLETDYEQIRQRALQdkrsRKMREWTDQLREKIYV 449
Cdd:COG0760   74 PEFEEAAFALKPGEISGPVKTQ-----FGYHIIKVEDRRPAETPPFEEVKQQIRQELFQ----QALEAWLEELRKKAKI 143
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 302-407 1.98e-11

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: 60.39  E-value: 1.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807  302 HVLIKPNAPTGK---RAKEYLSAVRDTLVNNEDvSFERMARRHSEEDRTAQNGGRVTDPESGardlvldALGPSWTRTIR 378
Cdd:pfam00639   1 HILIKTPEASERdraEAKAKAEEILEQLKSGED-SFAELARKYSDDCPSAANGGDLGWFTRG-------QLPPEFEKAAF 72

                          90       100
                  ....*....|....*....|....*....
gi 499723807  379 PLEAGDISEPSRVqllndDEAYHIVRLDR 407
Cdd:pfam00639  73 ALKPGEISGPVET-----RFGFHIIKLTD 96
SurA_N_3 pfam13624
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 46-159 2.92e-09

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: 56.04  E-value: 2.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807   46 AAVVGDEIVLKSEVDQLVRRQTRQQNVSYSNSLWME----------ALRQLVDQKLLAEQArRDTTITVSDQQLSDQLdR 115
Cdd:pfam13624  41 VAKVNGEKISRAEFQRAYRRQLDQLRQQFGPNLDAElldelglrqqVLDQLIDRALLLQEA-KKLGLAVSDEEVRQAI-A 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 499723807  116 RISQYVER-AGSEERLEQ---AYGKSileiKEQFREDLRGQILSQQLR 159
Cdd:pfam13624 119 SIPAFQEDgKFDKERYRQllrANGLT----PAEFEASLRQDLLLQQLL 162
prsA PRK03002
peptidylprolyl isomerase PrsA;
226-294 1.28e-05

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 46.85  E-value: 1.28e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807 226 GASLEAMARQFSAPDAAGTASGALTDVNLNDLVPEFAAVASRTPVGQISQPFynESQNGFHILRI-DAKD 294
Cdd:PRK03002 160 GASFEELAKQESQDLLSKEKGGDLGYFNSGRMAPEFETAAYKLKVGQISNPV--KSPNGYHIIKLtDKKD 227
 
Name Accession Description Interval E-value
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 196-292 2.68e-24

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: 96.60  E-value: 2.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807  196 HI-VRYPKPTEASRQQAKSLITSVRDSIVNGGASLEAMARQFSAPDAAGTASGALTDVNLNDLVPEFAAVASRTPVGQIS 274
Cdd:pfam00639   1 HIlIKTPEASERDRAEAKAKAEEILEQLKSGEDSFAELARKYSDDCPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEIS 80

                          90
                  ....*....|....*...
gi 499723807  275 QPFynESQNGFHILRIDA 292
Cdd:pfam00639  81 GPV--ETRFGFHIIKLTD 96
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 189-303 7.71e-19

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 82.70  E-value: 7.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807 189 PKTVRLSHIVRYPKPTEaSRQQAKSLITSVRDSIvNGGASLEAMARQFSAPDAAGTASGALTDVNLNDLVPEFAAVASRT 268
Cdd:COG0760    6 PEEVRASHILVKVPPSE-DRAKAEAKAEELLAQL-KAGADFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEAAFAL 83

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 499723807 269 PVGQISQPFynESQNGFHILRIDAK-DGSTVDLHHV 303
Cdd:COG0760   84 KPGEISGPV--KTQFGYHIIKVEDRrPAETPPFEEV 117
prsA PRK00059
peptidylprolyl isomerase; Provisional
 47-298 3.93e-17

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 82.45  E-value: 3.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807  47 AVVGDEIVLKSEVDQL--VRRQTRQQNVSY-----SNSLWMEALRQ--------LVDQKLLAEQARrDTTITVSDQQLSD 111
Cdd:PRK00059  39 ATVNGEKITRGDLDKDpkMQQVLEQLKQQYgdnyeKNEQVKEQIKQqkeqildsLITEKVLLQKAK-ELKLIPSEEELNK 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807 112 QLDRRISQY-VERAGSEERLEQAYgKSILEIKEQFREDLRGQILSQQLRRRRMQSIDITPSEVRQWFEQiPQDSLPQLPK 190
Cdd:PRK00059 118 EVDKKINEIkKQFNNDEEQFEEAL-KATGFTEETFKEYLKNQIIIEKVINEVVKDVKVTDKDAQKYYNE-NKSKFTEKPN 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807 191 TVRLSHIVrypKPTEASRQQAKSLItsvrdsivNGGASLEAMARQFSAPDAAGTASGALTDVNLND--LVPEFAAVASRT 268
Cdd:PRK00059 196 TMHLAHIL---VKTEDEAKKVKKRL--------DKGEDFAKVAKEVSQDPGSKDKGGDLGDVPYSDsgYDKEFMDGAKAL 264

                        250       260       270
                 ....*....|....*....|....*....|
gi 499723807 269 PVGQISQPFynESQNGFHILRIDAKDGSTV 298
Cdd:PRK00059 265 KEGEISAPV--KTQFGYHIIKAIKKKEYPV 292
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 40-451 7.06e-16

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 79.40  E-value: 7.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807  40 QVVDRIAAVVGDEIVLKSEVD---QLVRRQTRQ--QNVSYSNSLWMEALRQLVDQKLLAEQARRdTTITVSDQQLsDQLD 114
Cdd:PRK10770   5 QVVDKVAAVVNNGVVLESDVDglmQSVKLNAQQagQQLPDDATLRHQILERLIMDNIILQMAQK-MGVKISDEQL-DQAI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807 115 RRISQYVERAGSEERLEQAY-GKSILEIKEQFRED-LRGQILSQQLRRRrmqsIDITPSEVRQWFEQIpqDSLPQLPKTV 192
Cdd:PRK10770  83 ANIAAQNNMTLDQMRSRLAYdGLNYNTYRNQIRKEmIISEVRNNEVRRR----ITILPQEVDSLAKQI--GNQNDASTEL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807 193 RLSHI-VRYPK-PTEASRQQAKSLITSVRDSIvNGGASLEAMARQFSApDAAGTASGALTDVNLNDLVPEFAAVASRTPV 270
Cdd:PRK10770 157 NLSHIlIPLPEnPTQDQVDEAESQARSIVDQA-RNGADFGKLAIAYSA-DQQALKGGQMGWGRIQELPGLFAQALSTAKK 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807 271 GQISQPFynESQNGFHILRIDAKDGST-------VDLHHVLIKPNA-PTGKRAKEYLSAVRDTlVNNEDVSFERMARRHS 342
Cdd:PRK10770 235 GDIVGPI--RSGVGFHILKVNDLRGESqnisvteVHARHILLKPSPiMTDEQARAKLEQIAAD-IKSGKTTFAAAAKEFS 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807 343 EEDRTAQNGGrvtdpesgarDL---VLDALGPSWTRTIRPLEAGDISEPSRVQLlnddeAYHIVRL--DRRVPahraslE 417
Cdd:PRK10770 312 QDPGSANQGG----------DLgwaTPDIFDPAFRDALMRLNKGQISAPVHSSF-----GWHLIELldTRQVD------K 370

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 499723807 418 TDYEQiRQRALQDKRSRKMRE----WTDQLREKIYVDI 451
Cdd:PRK10770 371 TDAAQ-KDRAYRMLFNRKFSEeaqtWMQEQRASAYVKI 407
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 295-449 2.73e-15

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 72.69  E-value: 2.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807 295 GSTVDLHHVLIKPNAPTGK-RAKEYLSAVRDTLVNNEDvsFERMARRHSEEDRTAQNGGrvtdpesgarDL---VLDALG 370
Cdd:COG0760    6 PEEVRASHILVKVPPSEDRaKAEAKAEELLAQLKAGAD--FAELAKEYSQDPGSAANGG----------DLgwfSRGQLV 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499723807 371 PSWTRTIRPLEAGDISEPSRVQllnddEAYHIVRLDRRVPAHRASLETDYEQIRQRALQdkrsRKMREWTDQLREKIYV 449
Cdd:COG0760   74 PEFEEAAFALKPGEISGPVKTQ-----FGYHIIKVEDRRPAETPPFEEVKQQIRQELFQ----QALEAWLEELRKKAKI 143
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 187-293 8.82e-14

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: 67.39  E-value: 8.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807  187 QLPKTVRLSHI-VRYPKPTEASRQQAKSLItsvrDSI---VNGGASLEAMARQFSAPDAAGTASGALTDVNLNDLVPEFA 262
Cdd:pfam13616  11 SAPDSVKASHIlISYSQAVSRTEEEAKAKA----DSLlaaLKNGADFAALAKTYSDDPASKNNGGDLGWFTKGQMVKEFE 86

                          90       100       110
                  ....*....|....*....|....*....|.
gi 499723807  263 AVASRTPVGQISQPFynESQNGFHILRIDAK 293
Cdd:pfam13616  87 DAVFSLKVGEISGVV--KTQFGFHIIKVTDK 115
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 302-407 1.98e-11

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: 60.39  E-value: 1.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807  302 HVLIKPNAPTGK---RAKEYLSAVRDTLVNNEDvSFERMARRHSEEDRTAQNGGRVTDPESGardlvldALGPSWTRTIR 378
Cdd:pfam00639   1 HILIKTPEASERdraEAKAKAEEILEQLKSGED-SFAELARKYSDDCPSAANGGDLGWFTRG-------QLPPEFEKAAF 72

                          90       100
                  ....*....|....*....|....*....
gi 499723807  379 PLEAGDISEPSRVqllndDEAYHIVRLDR 407
Cdd:pfam00639  73 ALKPGEISGPVET-----RFGFHIIKLTD 96
SurA_N_3 pfam13624
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 46-159 2.92e-09

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: 56.04  E-value: 2.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807   46 AAVVGDEIVLKSEVDQLVRRQTRQQNVSYSNSLWME----------ALRQLVDQKLLAEQArRDTTITVSDQQLSDQLdR 115
Cdd:pfam13624  41 VAKVNGEKISRAEFQRAYRRQLDQLRQQFGPNLDAElldelglrqqVLDQLIDRALLLQEA-KKLGLAVSDEEVRQAI-A 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 499723807  116 RISQYVER-AGSEERLEQ---AYGKSileiKEQFREDLRGQILSQQLR 159
Cdd:pfam13624 119 SIPAFQEDgKFDKERYRQllrANGLT----PAEFEASLRQDLLLQQLL 162
SurA_N pfam09312
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 42-159 1.20e-08

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: 430518 [Multi-domain]  Cd Length: 118  Bit Score: 53.05  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807   42 VDRIAAVVGDEIVLKSEVDQLVR---RQTRQQNVSY--SNSLWMEALRQLVDQKLLAEQARRdTTITVSDqqlsDQLDRR 116
Cdd:pfam09312   1 LDRIVAVVNDGVILQSELDRRVDtvkRNLQQQGTQLppDAVLERQVLERLILERIQLQMAEK-TGIRVDD----AELNQA 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 499723807  117 ISQYVERAG-SEERLEQAYGKSILEIKEqFREDLRGQILSQQLR 159
Cdd:pfam09312  76 IARIAQQNNlTLDQLRQALAADGLSYDK-FREQIRKEIIISRLR 118
prsA PRK03002
peptidylprolyl isomerase PrsA;
226-294 1.28e-05

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 46.85  E-value: 1.28e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807 226 GASLEAMARQFSAPDAAGTASGALTDVNLNDLVPEFAAVASRTPVGQISQPFynESQNGFHILRI-DAKD 294
Cdd:PRK03002 160 GASFEELAKQESQDLLSKEKGGDLGYFNSGRMAPEFETAAYKLKVGQISNPV--KSPNGYHIIKLtDKKD 227
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
168-298 4.14e-05

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 42.81  E-value: 4.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807  168 ITPSEVRQWFEQIPQDSlpQLPKTVRLSHIVrypKPTEASRQQAKSLitsvrdsiVNGGASLEAMARQFSAPDAAGTASG 247
Cdd:pfam13145   1 VTEEELKAYYEENKDEF--STPEGRLLEILV---FKDQVAADAALAL--------LKAGALEDFAALAKGEGIKAATLDI 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 499723807  248 ALTDvnlNDLVPEFAAVASRTPVGQISQPFynESQNGFHILRIDAKDGSTV 298
Cdd:pfam13145  68 VESA---ELLPEELAKAAFALKPGEVSGPI--KTGNGYYVVRVTEIKPAQP 113
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 223-293 3.72e-04

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 42.27  E-value: 3.72e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499723807 223 VNGGASLEAMARQFSAPDAAGTASGALTDVNLNDLVPEFAAVASRTPVGQISQPFynESQNGFHILRIDAK 293
Cdd:PRK02998 155 VNNGEDFAALAKQYSEDTGSKEQGGEISGFAPGQTVKEFEEAAYKLDAGQVSEPV--KTTYGYHIIKVTDK 223
SurA_N_2 pfam13623
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 45-113 4.45e-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: 463938  Cd Length: 145  Bit Score: 40.64  E-value: 4.45e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499723807   45 IAAVVGDEIVLKSEVDQLVRRQTRQQNVSYSNSLWME----------ALRQLVDQKLLAEQARRdTTITVSDQQLSDQL 113
Cdd:pfam13623  42 VVAEVNGEEISYQEFQQAVENQRNRLRQQLGQNFDPAeldeaqlreqVWDQLVREKLLLQEAEK-LGLTVSDEELVDAI 119
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 189-291 5.67e-04

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 39.62  E-value: 5.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499723807 189 PKTVRLSHIV------RYP------KPTEASRQQAKSLITSVRDSIVNGGASLEAMARQFSapDAAGTASGA-LTDVNLN 255
Cdd:PTZ00356   3 GDTVRAAHLLikhtgsRNPvsrrtgKPVTRSKEEAIKELAKWREQIVSGEKTFEEIARQRS--DCGSAAKGGdLGFFGRG 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 499723807 256 DLVPEFAAVASRTPVGQISQPFYNESqnGFH-ILRID 291
Cdd:PTZ00356  81 QMQKPFEDAAFALKVGEISDIVHTDS--GVHiILRLA 115
 
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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