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Conserved domains on  [gi|1994014896|gb|QSB57600|]
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peptidylprolyl isomerase SurA [Klebsiella aerogenes]

Protein Classification

peptidylprolyl isomerase SurA( domain architecture ID 11484933)

peptidylprolyl isomerase SurA protein is a periplasmic molecular chaperone that facilitates correct folding of outer membrane porins, catalyzing the interconversion of cis- and trans-peptidylproline

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 19-428 0e+00

peptidyl-prolyl cis-trans isomerase SurA; Provisional


:

Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 808.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896  19 FAAPQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAGQAGQQLPDDATLRHQILERLIMDQIVLQMGQKMGVKVSDDQLDQ 98
Cdd:PRK10770    1 FAAPQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAQQAGQQLPDDATLRHQILERLIMDNIILQMAQKMGVKISDEQLDQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896  99 AIANIAKQNNMSMDQMRSRLAYEGINYNTYRNQIRKEMLISEVRNNEVRRRITVLPQEVEALAKQIGDQNDASTELNLSH 178
Cdd:PRK10770   81 AIANIAAQNNMTLDQMRSRLAYDGLNYNTYRNQIRKEMIISEVRNNEVRRRITILPQEVDSLAKQIGNQNDASTELNLSH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 179 ILIALPENPTSDQVAAAEEQAKSVVEQARSGANFGKLAITYSADQQALKGGQMGWGRIQELPGIFAQALSTAKKGDVVGP 258
Cdd:PRK10770  161 ILIPLPENPTQDQVDEAESQARSIVDQARNGADFGKLAIAYSADQQALKGGQMGWGRIQELPGLFAQALSTAKKGDIVGP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 259 IRSGVGFHILKVNDMRGGSQNISVTEVHARHILLKPSPIMNDAQAQAKLEQIAADIKSGKTTFDKAAKEFSQDPGSANQG 338
Cdd:PRK10770  241 IRSGVGFHILKVNDLRGESQNISVTEVHARHILLKPSPIMTDEQARAKLEQIAADIKSGKTTFAAAAKEFSQDPGSANQG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 339 GDLGWATPDIFDPAFRDALMRLNKGQTSGPVHSSFGWHLIQLMDTRNVDRTDAAQKDRAYRMLMNRKFSEEAATWMQEQR 418
Cdd:PRK10770  321 GDLGWATPDIFDPAFRDALMRLNKGQISAPVHSSFGWHLIELLDTRQVDKTDAAQKDRAYRMLFNRKFSEEAQTWMQEQR 400

                         410
                  ....*....|
gi 1994014896 419 ASAYVKILSN 428
Cdd:PRK10770  401 ASAYVKILSN 410
 
Name Accession Description Interval E-value
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 19-428 0e+00

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 808.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896  19 FAAPQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAGQAGQQLPDDATLRHQILERLIMDQIVLQMGQKMGVKVSDDQLDQ 98
Cdd:PRK10770    1 FAAPQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAQQAGQQLPDDATLRHQILERLIMDNIILQMAQKMGVKISDEQLDQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896  99 AIANIAKQNNMSMDQMRSRLAYEGINYNTYRNQIRKEMLISEVRNNEVRRRITVLPQEVEALAKQIGDQNDASTELNLSH 178
Cdd:PRK10770   81 AIANIAAQNNMTLDQMRSRLAYDGLNYNTYRNQIRKEMIISEVRNNEVRRRITILPQEVDSLAKQIGNQNDASTELNLSH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 179 ILIALPENPTSDQVAAAEEQAKSVVEQARSGANFGKLAITYSADQQALKGGQMGWGRIQELPGIFAQALSTAKKGDVVGP 258
Cdd:PRK10770  161 ILIPLPENPTQDQVDEAESQARSIVDQARNGADFGKLAIAYSADQQALKGGQMGWGRIQELPGLFAQALSTAKKGDIVGP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 259 IRSGVGFHILKVNDMRGGSQNISVTEVHARHILLKPSPIMNDAQAQAKLEQIAADIKSGKTTFDKAAKEFSQDPGSANQG 338
Cdd:PRK10770  241 IRSGVGFHILKVNDLRGESQNISVTEVHARHILLKPSPIMTDEQARAKLEQIAADIKSGKTTFAAAAKEFSQDPGSANQG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 339 GDLGWATPDIFDPAFRDALMRLNKGQTSGPVHSSFGWHLIQLMDTRNVDRTDAAQKDRAYRMLMNRKFSEEAATWMQEQR 418
Cdd:PRK10770  321 GDLGWATPDIFDPAFRDALMRLNKGQISAPVHSSFGWHLIELLDTRQVDKTDAAQKDRAYRMLFNRKFSEEAQTWMQEQR 400

                         410
                  ....*....|
gi 1994014896 419 ASAYVKILSN 428
Cdd:PRK10770  401 ASAYVKILSN 410
SurA_N pfam09312
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 38-142 1.38e-47

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: 158.98  E-value: 1.38e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896  38 LESDVDGLMQSVKLNAGQAGQQLPDDATLRHQILERLIMDQIVLQMGQKMGVKVSDDQLDQAIANIAKQNNMSMDQMRSR 117
Cdd:pfam09312  14 LQSELDRRVDTVKRNLQQQGTQLPPDAVLERQVLERLILERIQLQMAEKTGIRVDDAELNQAIARIAQQNNLTLDQLRQA 93

                          90       100
                  ....*....|....*....|....*
gi 1994014896 118 LAYEGINYNTYRNQIRKEMLISEVR 142
Cdd:pfam09312  94 LAADGLSYDKFREQIRKEIIISRLR 118
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 277-423 2.44e-46

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 156.27  E-value: 2.44e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 277 SQNISVTEVHARHILLKPSPIMNDAQAQAKLEQIAADIKSGKTtFDKAAKEFSQDPGSANQGGDLGWATPDIFDPAFRDA 356
Cdd:COG0760     1 DQFDSPEEVRASHILVKVPPSEDRAKAEAKAEELLAQLKAGAD-FAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEA 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1994014896 357 LMRLNKGQTSGPVHSSFGWHLIQLMDTRNV-DRTDAAQKDRAYRMLmnrkFSEEAATWMQEQRASAYV 423
Cdd:COG0760    80 AFALKPGEISGPVKTQFGYHIIKVEDRRPAeTPPFEEVKQQIRQEL----FQQALEAWLEELRKKAKI 143
nifM_nitrog TIGR02933
nitrogen fixation protein NifM; Members of this protein family, found in a subset of ...
 288-416 4.23e-10

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


Pssm-ID: 131979 [Multi-domain]  Cd Length: 256  Bit Score: 59.86  E-value: 4.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 288 RHILLKPSPimNDAQA-QAKLEQIAADIKSGKTTFDKAAKEFSQDPgSANQGGDLGWATPDIFDPAFRDALMRLNKGQTS 366
Cdd:TIGR02933 127 RHLLLTVNE--DDREAvRTRILAILRRLRGKPAAFAEQAMRHSHCP-TAMEGGLLGWVSRGLLYPQLDAALFQLAEGELS 203

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1994014896 367 GPVHSSFGWHLI---QLMDTRNVDRTDAAQKDRAYRMLMNRKfsEEAATWMQE 416
Cdd:TIGR02933 204 PPIESEIGWHLLlceAIRPARPLTLEEALPRARDRLQLRQQK--AYQRQWLVQ 254
 
Name Accession Description Interval E-value
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 19-428 0e+00

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 808.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896  19 FAAPQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAGQAGQQLPDDATLRHQILERLIMDQIVLQMGQKMGVKVSDDQLDQ 98
Cdd:PRK10770    1 FAAPQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAQQAGQQLPDDATLRHQILERLIMDNIILQMAQKMGVKISDEQLDQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896  99 AIANIAKQNNMSMDQMRSRLAYEGINYNTYRNQIRKEMLISEVRNNEVRRRITVLPQEVEALAKQIGDQNDASTELNLSH 178
Cdd:PRK10770   81 AIANIAAQNNMTLDQMRSRLAYDGLNYNTYRNQIRKEMIISEVRNNEVRRRITILPQEVDSLAKQIGNQNDASTELNLSH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 179 ILIALPENPTSDQVAAAEEQAKSVVEQARSGANFGKLAITYSADQQALKGGQMGWGRIQELPGIFAQALSTAKKGDVVGP 258
Cdd:PRK10770  161 ILIPLPENPTQDQVDEAESQARSIVDQARNGADFGKLAIAYSADQQALKGGQMGWGRIQELPGLFAQALSTAKKGDIVGP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 259 IRSGVGFHILKVNDMRGGSQNISVTEVHARHILLKPSPIMNDAQAQAKLEQIAADIKSGKTTFDKAAKEFSQDPGSANQG 338
Cdd:PRK10770  241 IRSGVGFHILKVNDLRGESQNISVTEVHARHILLKPSPIMTDEQARAKLEQIAADIKSGKTTFAAAAKEFSQDPGSANQG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 339 GDLGWATPDIFDPAFRDALMRLNKGQTSGPVHSSFGWHLIQLMDTRNVDRTDAAQKDRAYRMLMNRKFSEEAATWMQEQR 418
Cdd:PRK10770  321 GDLGWATPDIFDPAFRDALMRLNKGQISAPVHSSFGWHLIELLDTRQVDKTDAAQKDRAYRMLFNRKFSEEAQTWMQEQR 400

                         410
                  ....*....|
gi 1994014896 419 ASAYVKILSN 428
Cdd:PRK10770  401 ASAYVKILSN 410
SurA_N pfam09312
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 38-142 1.38e-47

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: 158.98  E-value: 1.38e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896  38 LESDVDGLMQSVKLNAGQAGQQLPDDATLRHQILERLIMDQIVLQMGQKMGVKVSDDQLDQAIANIAKQNNMSMDQMRSR 117
Cdd:pfam09312  14 LQSELDRRVDTVKRNLQQQGTQLPPDAVLERQVLERLILERIQLQMAEKTGIRVDDAELNQAIARIAQQNNLTLDQLRQA 93

                          90       100
                  ....*....|....*....|....*
gi 1994014896 118 LAYEGINYNTYRNQIRKEMLISEVR 142
Cdd:pfam09312  94 LAADGLSYDKFREQIRKEIIISRLR 118
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 277-423 2.44e-46

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 156.27  E-value: 2.44e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 277 SQNISVTEVHARHILLKPSPIMNDAQAQAKLEQIAADIKSGKTtFDKAAKEFSQDPGSANQGGDLGWATPDIFDPAFRDA 356
Cdd:COG0760     1 DQFDSPEEVRASHILVKVPPSEDRAKAEAKAEELLAQLKAGAD-FAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEA 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1994014896 357 LMRLNKGQTSGPVHSSFGWHLIQLMDTRNV-DRTDAAQKDRAYRMLmnrkFSEEAATWMQEQRASAYV 423
Cdd:COG0760    80 AFALKPGEISGPVKTQFGYHIIKVEDRRPAeTPPFEEVKQQIRQEL----FQQALEAWLEELRKKAKI 143
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 289-382 8.31e-33

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: 118.94  E-value: 8.31e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 289 HILLKPSPIMND--AQAQAKLEQIAADIKSGKTTFDKAAKEFSQDPGSANQGGDLGWATPDIFDPAFRDALMRLNKGQTS 366
Cdd:pfam00639   1 HILIKTPEASERdrAEAKAKAEEILEQLKSGEDSFAELARKYSDDCPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEIS 80

                          90
                  ....*....|....*.
gi 1994014896 367 GPVHSSFGWHLIQLMD 382
Cdd:pfam00639  81 GPVETRFGFHIIKLTD 96
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 166-315 1.14e-28

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 109.66  E-value: 1.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 166 DQNDASTELNLSHILIALPENptsDQVAAAEEQAKSVVEQARSGANFGKLAITYSADQQ-ALKGGQMGWGRIQELPGIFA 244
Cdd:COG0760     1 DQFDSPEEVRASHILVKVPPS---EDRAKAEAKAEELLAQLKAGADFAELAKEYSQDPGsAANGGDLGWFSRGQLVPEFE 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1994014896 245 QALSTAKKGDVVGPIRSGVGFHILKVNDMRGGSQnISVTEV--HARHILLKPspimndaQAQAKLEQIAADIK 315
Cdd:COG0760    78 EAAFALKPGEISGPVKTQFGYHIIKVEDRRPAET-PPFEEVkqQIRQELFQQ-------ALEAWLEELRKKAK 142
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 265-384 2.66e-26

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: 102.45  E-value: 2.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 265 FHILKVNDMRGGSQNisvteVHARHILLK--PSPIMNDAQAQAKLEQIAADIKSGkTTFDKAAKEFSQDPGSANQGGDLG 342
Cdd:pfam13616   1 YSLSKLVDKKSAPDS-----VKASHILISysQAVSRTEEEAKAKADSLLAALKNG-ADFAALAKTYSDDPASKNNGGDLG 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1994014896 343 WATPDIFDPAFRDALMRLNKGQTSGPVHSSFGWHLIQLMDTR 384
Cdd:pfam13616  75 WFTKGQMVKEFEDAVFSLKVGEISGVVKTQFGFHIIKVTDKK 116
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 178-272 9.74e-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: 97.37  E-value: 9.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 178 HILIALPEnPTSDQVAAAEEQAKSVVEQARSGAN-FGKLAITYSAD-QQALKGGQMGWGRIQELPGIFAQALSTAKKGDV 255
Cdd:pfam00639   1 HILIKTPE-ASERDRAEAKAKAEEILEQLKSGEDsFAELARKYSDDcPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEI 79

                          90
                  ....*....|....*..
gi 1994014896 256 VGPIRSGVGFHILKVND 272
Cdd:pfam00639  80 SGPVETRFGFHIIKLTD 96
prsA PRK00059
peptidylprolyl isomerase; Provisional
 55-425 4.50e-19

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 87.84  E-value: 4.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896  55 QAGQQLpddATLRHQILERLIMDQIVLQMGQKMGVKVSDDQL----DQAIANIAKQNNMSMDQMRSRLAYEGINYNTYRN 130
Cdd:PRK00059   77 QVKEQI---KQQKEQILDSLITEKVLLQKAKELKLIPSEEELnkevDKKINEIKKQFNNDEEQFEEALKATGFTEETFKE 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 131 QIRKEMLISEVRnNEVRRRITVlpqevealakqigDQNDASTELNlshilialpenptsdqvaaaeEQAKSVVEQArsga 210
Cdd:PRK00059  154 YLKNQIIIEKVI-NEVVKDVKV-------------TDKDAQKYYN---------------------ENKSKFTEKP---- 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 211 nfgklaitysadqqalkggqmgwgriqelpgifaqalstakkgdvvgpirsgvgfhilkvndmrggsqnisvTEVHARHI 290
Cdd:PRK00059  195 ------------------------------------------------------------------------NTMHLAHI 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 291 LLKpspimNDAQAQAkleqIAADIKSGKtTFDKAAKEFSQDPGSANQGGDLGWATPDI--FDPAFRDALMRLNKGQTSGP 368
Cdd:PRK00059  203 LVK-----TEDEAKK----VKKRLDKGE-DFAKVAKEVSQDPGSKDKGGDLGDVPYSDsgYDKEFMDGAKALKEGEISAP 272

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1994014896 369 VHSSFGWHLIQLMDTRNVDRTDAAQ-KDRAYRMLMNRKFSEEAATWMQEQRASAYVKI 425
Cdd:PRK00059  273 VKTQFGYHIIKAIKKKEYPVKPFDSvKEDIKKQLLQEKQSEVFKKKIEEWKKALKVKK 330
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 161-274 1.45e-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: 80.87  E-value: 1.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 161 AKQIGDQNDASTELNLSHILIALpENPTSDQVAAAEEQAKSVVEQARSGANFGKLAITYSADQ-QALKGGQMGW---GRI 236
Cdd:pfam13616   3 LSKLVDKKSAPDSVKASHILISY-SQAVSRTEEEAKAKADSLLAALKNGADFAALAKTYSDDPaSKNNGGDLGWftkGQM 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1994014896 237 QELpgiFAQALSTAKKGDVVGPIRSGVGFHILKVNDMR 274
Cdd:pfam13616  82 VKE---FEDAVFSLKVGEISGVVKTQFGFHIIKVTDKK 116
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 285-379 3.50e-16

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 74.29  E-value: 3.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 285 VHARHILLKPSPIMN-------------DAQAQAKLEQIAADIKSGKTTFDKAAKEFSqDPGSANQGGDLGWATPDIFDP 351
Cdd:PTZ00356    6 VRAAHLLIKHTGSRNpvsrrtgkpvtrsKEEAIKELAKWREQIVSGEKTFEEIARQRS-DCGSAAKGGDLGFFGRGQMQK 84

                          90       100
                  ....*....|....*....|....*...
gi 1994014896 352 AFRDALMRLNKGQTSGPVHSSFGWHLIQ 379
Cdd:PTZ00356   85 PFEDAAFALKVGEISDIVHTDSGVHIIL 112
prsA PRK03095
peptidylprolyl isomerase PrsA;
284-389 9.28e-16

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 77.34  E-value: 9.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 284 EVHARHILLKPspimndaQAQAKleQIAADIKSGKTtFDKAAKEFSQDPGSANQGGDLGWATPDIFDPAFRDALMRLNKG 363
Cdd:PRK03095  132 EIKASHILVKD-------EATAK--KVKEELGQGKS-FEELAKQYSEDTGSKEKGGDLGFFGAGKMVKEFEDAAYKLKKD 201

                          90       100
                  ....*....|....*....|....*.
gi 1994014896 364 QTSGPVHSSFGWHLIQLMDTRNVDRT 389
Cdd:PRK03095  202 EVSEPVKSQFGYHIIKVTDIKEPEKS 227
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 65-287 3.51e-14

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 74.28  E-value: 3.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896  65 TLRHQILERLIMDQIVLQMGQKMGVKVSDDQLDQAIANI-AKQNNMSMDQMR--SRLAYEGINYNTYRNQIRKEM----L 137
Cdd:PRK10788   86 QLRQQVLNRLIDEALLDQYARELGLGISDEQVKQAIFATpAFQTDGKFDNNKylAILNQMGMTADQYAQALRQQLttqqL 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 138 ISEVRNNEVrrritVLPQEVEALA------------------------------KQIGDQND----ASTELNLSHILI-- 181
Cdd:PRK10788  166 INGVAGTDF-----MLPGETDELAalvaqqrvvreatidvnalaakqtvtdeeiKSYYDQNKnnfmAPEQFKVSYIKLda 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 182 -ALPENPTSDQVA-------------------------AAEEQAKSVVEQARSGANFGKLAITYSADQ-QALKGGQMGWG 234
Cdd:PRK10788  241 aTMQQKITVSDADiqayydqhqdqftqperkrysiiqtKTEAEAKAVLDELKKGADFATLAKEKSTDIiSARNGGDLGWL 320

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1994014896 235 RIQELPGIFAQAlSTAKKGDVVGPIRSGVGFHILKVNDMRgGSQNISVTEVHA 287
Cdd:PRK10788  321 EPATTPDELKNA-GLKEKGQLSGVIKSSVGFLIVRLDDIQ-PAKVKPLSEVRD 371
prsA PRK03002
peptidylprolyl isomerase PrsA;
284-425 6.24e-13

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 68.81  E-value: 6.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 284 EVHARHILlkpspIMNDAQAQakleQIAADIKSGkTTFDKAAKEFSQDPGSANQGGDLGWATPDIFDPAFRDALMRLNKG 363
Cdd:PRK03002  136 EIKASHIL-----VSDENEAK----EIKKKLDAG-ASFEELAKQESQDLLSKEKGGDLGYFNSGRMAPEFETAAYKLKVG 205

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1994014896 364 QTSGPVHSSFGWHLIQLMDTRNVDRTDAAqKDRAYRMLMNRKFSEEA--ATWMQEQRASAYVKI 425
Cdd:PRK03002  206 QISNPVKSPNGYHIIKLTDKKDLKPYDEV-KDSIRKNLEEERTADPIfgKKLLQSELKKANIKI 268
prsA PRK03095
peptidylprolyl isomerase PrsA;
69-274 6.72e-13

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 68.87  E-value: 6.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896  69 QILERLIMDQIVLQmgqkmGVKVSDDQLDQAIANIAKQNNmsmDQMRSRLAYEGINYNTYRNQIRKEmlisevrnnevrr 148
Cdd:PRK03095   51 QVLNNMVMEKVLIK-----NYKVEDKEVDKKYDEMKKQYG---DQFDTLLKQQGIKEETLKTGVRAQ------------- 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 149 ritvLPQEvEALAKQIGDQN---DASTELNLSHILIAlpenptsdqvaaAEEQAKSVVEQARSGANFGKLAITYSADQQA 225
Cdd:PRK03095  110 ----LAQE-KAIEKTITDKElkdNYKPEIKASHILVK------------DEATAKKVKEELGQGKSFEELAKQYSEDTGS 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1994014896 226 L-KGGQMGWGRIQELPGIFAQALSTAKKGDVVGPIRSGVGFHILKVNDMR 274
Cdd:PRK03095  173 KeKGGDLGFFGAGKMVKEFEDAAYKLKKDEVSEPVKSQFGYHIIKVTDIK 222
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 284-416 8.25e-13

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 68.46  E-value: 8.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 284 EVHARHILLKPspimndaQAQAKleQIAADIKSGKTtFDKAAKEFSQDPGSANQGGDLGWATPDIFDPAFRDALMRLNKG 363
Cdd:PRK02998  134 EMKVSHILVKD-------EKTAK--EVKEKVNNGED-FAALAKQYSEDTGSKEQGGEISGFAPGQTVKEFEEAAYKLDAG 203

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1994014896 364 QTSGPVHSSFGWHLIQLMDTRNVDRTDaAQKDRAYRMLMNRKFSEEAATWMQE 416
Cdd:PRK02998  204 QVSEPVKTTYGYHIIKVTDKKELKPFD-EVKDSIRKDLEQQRLQDTTGKWKQQ 255
SurA_N_3 pfam13624
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 51-142 6.03e-12

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: 63.36  E-value: 6.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896  51 LNAGQAGQQLPDDATLRHQILERLIMDQIVLQMGQKMGVKVSDDQLDQAIANIA---KQNNMSMDQMRSRLAYEGINYNT 127
Cdd:pfam13624  68 QFGPNLDAELLDELGLRQQVLDQLIDRALLLQEAKKLGLAVSDEEVRQAIASIPafqEDGKFDKERYRQLLRANGLTPAE 147

                          90
                  ....*....|....*
gi 1994014896 128 YRNQIRKEMLISEVR 142
Cdd:pfam13624 148 FEASLRQDLLLQQLL 162
nifM_nitrog TIGR02933
nitrogen fixation protein NifM; Members of this protein family, found in a subset of ...
 288-416 4.23e-10

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


Pssm-ID: 131979 [Multi-domain]  Cd Length: 256  Bit Score: 59.86  E-value: 4.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 288 RHILLKPSPimNDAQA-QAKLEQIAADIKSGKTTFDKAAKEFSQDPgSANQGGDLGWATPDIFDPAFRDALMRLNKGQTS 366
Cdd:TIGR02933 127 RHLLLTVNE--DDREAvRTRILAILRRLRGKPAAFAEQAMRHSHCP-TAMEGGLLGWVSRGLLYPQLDAALFQLAEGELS 203

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1994014896 367 GPVHSSFGWHLI---QLMDTRNVDRTDAAQKDRAYRMLMNRKfsEEAATWMQE 416
Cdd:TIGR02933 204 PPIESEIGWHLLlceAIRPARPLTLEEALPRARDRLQLRQQK--AYQRQWLVQ 254
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
301-382 8.56e-08

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 50.52  E-value: 8.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 301 AQAQAKLEQIAADIKsgKTTFDKAAKEFSqdpGSANQGGDLGWATPD-IFDPAFRDALMRLNKGQTSGPVHSSFGWHLIQ 379
Cdd:pfam13145  30 FKDQVAADAALALLK--AGALEDFAALAK---GEGIKAATLDIVESAeLLPEELAKAAFALKPGEVSGPIKTGNGYYVVR 104


                  ...
gi 1994014896 380 LMD 382
Cdd:pfam13145 105 VTE 107
prsA PRK03002
peptidylprolyl isomerase PrsA;
90-274 2.19e-07

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 52.25  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896  90 KVSDDQLDQAIANIAKQNNmsmDQMRSRLAYEGI-NYNTYRNQIRKEMLISEVrnneVRRRITvlPQEVEALAKqigdqn 168
Cdd:PRK03002   70 KVSDDDVDKEVQKAKSQYG---DQFKNVLKNNGLkDEADFKNQIKFKLAMNEA----IKKSVT--EKDVKDHYK------ 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 169 dasTELNLSHILIalpenptSDqvaaaEEQAKSVVEQARSGANFGKLAITYSADQQAL-KGGQMGWGRIQELPGIFAQAL 247
Cdd:PRK03002  135 ---PEIKASHILV-------SD-----ENEAKEIKKKLDAGASFEELAKQESQDLLSKeKGGDLGYFNSGRMAPEFETAA 199

                         170       180
                  ....*....|....*....|....*..
gi 1994014896 248 STAKKGDVVGPIRSGVGFHILKVNDMR 274
Cdd:PRK03002  200 YKLKVGQISNPVKSPNGYHIIKLTDKK 226
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 63-274 3.57e-07

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 51.51  E-value: 3.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896  63 DATLRHQILERLIMDQivlqmgqkmgVKVSDDQldqaianIAKQNNMSMDQMrsrlayeGINYNTYRNQIRkemLISEVR 142
Cdd:PRK02998   51 ESTLYQMVLSKALLDK----------YKVSDEE-------AKKQVEEAKDKM-------GDNFKSTLEQVG---LKNEDE 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 143 NNEVRRRITVLPQEVEALAKQIGDQNDASTELNLSHILIAlpenptsdqvaaAEEQAKSVVEQARSGANFGKLAITYSAD 222
Cdd:PRK02998  104 LKEKMKPEIAFEKAIKATVTEKDVKDNYKPEMKVSHILVK------------DEKTAKEVKEKVNNGEDFAALAKQYSED 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1994014896 223 QQALKGGqmgwGRIQEL-PGI----FAQALSTAKKGDVVGPIRSGVGFHILKVNDMR 274
Cdd:PRK02998  172 TGSKEQG----GEISGFaPGQtvkeFEEAAYKLDAGQVSEPVKTTYGYHIIKVTDKK 224
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
192-278 4.23e-07

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 48.59  E-value: 4.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 192 VAAAEEQAKSVVEQARSGANFGKLAItysADQQALKGGQMGWGRIQE-LPGIFAQALSTAKKGDVVGPIRSGVGFHILKV 270
Cdd:pfam13145  29 VFKDQVAADAALALLKAGALEDFAAL---AKGEGIKAATLDIVESAElLPEELAKAAFALKPGEVSGPIKTGNGYYVVRV 105


                  ....*...
gi 1994014896 271 NDMRGGSQ 278
Cdd:pfam13145 106 TEIKPAQP 113
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
 12-146 6.71e-07

FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440310 [Multi-domain]  Cd Length: 424  Bit Score: 51.28  E-value: 6.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896  12 AMIANTSFAAPQVVdkvaavvnngvvLESDVDGLMQSVKLNAGQAGQQLP--DDATLRHQILER--------LIMDQIVl 81
Cdd:COG0544   292 ALVENNEFDLPEAL------------VEREIDRLLEQAEQQLQQQGLQDTgkTEEELREEFREQaerrvklgLILDEIA- 358

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1994014896  82 qmgQKMGVKVSDDQLDQAIANIAKQNNMSMDQMRsrlayeginyNTYRNQIRKEMLISEVRNNEV 146
Cdd:COG0544   359 ---KKENIEVTDEEVEAEIEEMAQQYGMPPEEVK----------EYLQNPGQLEQLRADVLEEKV 410
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 287-381 9.53e-07

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 46.94  E-value: 9.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 287 ARHILLKPSPImndaqAQAKLEQIaadiKSGkTTFDKAAKEFSQDPgSANQGGDLGWATPDIFDPAFRDALMRLNKGQTS 366
Cdd:PRK15441    7 ALHILVKEEKL-----ALDLLEQI----KNG-ADFGKLAKKHSICP-SGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPT 75

                          90
                  ....*....|....*
gi 1994014896 367 GPVHSSFGWHLIQLM 381
Cdd:PRK15441   76 GPLHTQFGYHIIKVL 90
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 196-270 3.81e-06

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 45.01  E-value: 3.81e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1994014896 196 EEQAKSVVEQARSGANFGKLAITYSADQQALKGGQMGWGRIQELPGIFAQALSTAKKGDVVGPIRSGVGFHILKV 270
Cdd:PRK15441   15 EKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGYHIIKV 89
prsA PRK04405
peptidylprolyl isomerase; Provisional
 50-270 6.18e-06

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 47.86  E-value: 6.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896  50 KLNAGQAGQQlpddaTLRHQILERlimdqiVLQmgQKMGVKVSDDQLDQAIANIAKQNNMSMDqmrSRLAYEGINYNTYR 129
Cdd:PRK04405   47 EMKQSSAGKT-----VLANMIIYR------ALE--KQYGKKVSTKKVDKQYNSYKKQYGSSFD---SVLSQNGMTTSSFK 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 130 NQIRKEMLISEVrnneVRRRITVLPQEVEALAKqigdqnDASTELNLSHILIAlpenptsdqvaaAEEQAKSVVEQARSG 209
Cdd:PRK04405  111 QNLRTNLLSEAA----LKKLKKVTNSQLKKAWK------SYQPKVTVQHILVS------------KKSTAETVIKKLKDG 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1994014896 210 ANFGKLAITYSADQQAL-KGGQMGWGRIQE--LPGIFAQALSTAKKGDVVG-PIRSGVGFHILKV 270
Cdd:PRK04405  169 KDFAKLAKKYSTDTATKnKGGKLSAFDSTDttLDSTFKTAAFKLKNGEYTTtPVKTTYGYEVIKM 233
SurA_N_2 pfam13623
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 54-103 8.41e-06

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: 45.26  E-value: 8.41e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1994014896  54 GQAGQQLPDDATLRHQILERLIMDQIVLQMGQKMGVKVSDDQLDQAIANI 103
Cdd:pfam13623  73 QNFDPAELDEAQLREQVWDQLVREKLLLQEAEKLGLTVSDEELVDAIQGN 122
nifM_nitrog TIGR02933
nitrogen fixation protein NifM; Members of this protein family, found in a subset of ...
 56-268 4.88e-05

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


Pssm-ID: 131979 [Multi-domain]  Cd Length: 256  Bit Score: 44.84  E-value: 4.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896  56 AGQQLPDDATLRHQILER-LIMDQIVLQMGQKMGVKVSDDQLDQAIANIAKQnnmsmdqmrsrLAYEGINYNTYRNQIRK 134
Cdd:TIGR02933  16 PGELSPDQLQQFDQAWQRqRHIEQAVVRAADEIGVVIPPSLLEEAPQALAQA-----------LDEQALDAAERRAMLAH 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896 135 EMLISEVRNNEVRRRITVLPQEVEALAKQIGDQNDASTELNLSHILIALPENPTSdqvaAAEEQAKSVVEQARSG-ANFG 213
Cdd:TIGR02933  85 HLRLEAQLACVCAQAPQPDDADVEAWYRRHAEQFKRPEQRLTRHLLLTVNEDDRE----AVRTRILAILRRLRGKpAAFA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1994014896 214 KLAITYSADQQALKGGQMGWGRIQELPGIFAQALSTAKKGDVVGPIRSGVGFHIL 268
Cdd:TIGR02933 161 EQAMRHSHCPTAMEGGLLGWVSRGLLYPQLDAALFQLAEGELSPPIESEIGWHLL 215
prsA PRK01326
foldase protein PrsA; Reviewed
 78-216 7.27e-05

foldase protein PrsA; Reviewed


Pssm-ID: 179281 [Multi-domain]  Cd Length: 310  Bit Score: 44.42  E-value: 7.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014896  78 QIVLQM------GQKMGVKVSDDQLDQAIANIAKQNNMSMDQMrsrLAYEGINYNTYRNQIRKEMLIS-EVRnnevrrri 150
Cdd:PRK01326   55 QAMLNLtisrvfEKQYGDKVSDKEVEKAYAKTAKQYGASFSRA---LAQAGLTPETYKAQIRTSKLVEyAVK-------- 123

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1994014896 151 tvlpqevEALAKQIGDQNDASTELNLShilialPEnpTSDQVAA--AEEQAKSVVEQAR-SGANFGKLA 216
Cdd:PRK01326  124 -------EAAKKELTDEAYKKAYEEYT------PE--VTAQIIRldNEDKAKSVLEEAKaEGADFAQIA 177
 
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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