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Conserved domains on  [gi|2528041503|ref|WP_288988640|]
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peptidylprolyl isomerase SurA [uncultured Pseudoalteromonas sp.]

Protein Classification

peptidylprolyl isomerase family protein( domain architecture ID 1005302)

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

CATH:  3.10.50.40
EC:  5.2.1.8
Gene Ontology:  GO:0003755|GO:0042277|GO:0051082|GO:0006457
SCOP:  4002409

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10770 super family cl35947
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 21-426 5.50e-154

peptidyl-prolyl cis-trans isomerase SurA; Provisional


The actual alignment was detected with superfamily member PRK10770:

Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 442.26  E-value: 5.50e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503  21 FAAPVEIDKVIGIVNQGVILKSEVDTIVDRVKKQAEEQNQQLPKDETLRVQAIERLVNQTLMMQMAERMGLEISDSQLDQ 100
Cdd:PRK10770    1 FAAPQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAQQAGQQLPDDATLRHQILERLIMDNIILQMAQKMGVKISDEQLDQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 101 TLANMAKEQGGTIADLRRTIEASGESFQAYREEIRKEITTQQVTRANVDRRIYVSDQEIDNLLKIMDSQGQNAEEYDIGH 180
Cdd:PRK10770   81 AIANIAAQNNMTLDQMRSRLAYDGLNYNTYRNQIRKEMIISEVRNNEVRRRITILPQEVDSLAKQIGNQNDASTELNLSH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 181 ILIDIPSAASADDVSSAKTRADKVIELLQDGQEFKRIAISSSSGSKALEGGQLGWMGINEMPSLFAEAVKGKKKDAIIGP 260
Cdd:PRK10770  161 ILIPLPENPTQDQVDEAESQARSIVDQARNGADFGKLAIAYSADQQALKGGQMGWGRIQELPGLFAQALSTAKKGDIVGP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 261 LRSGAGFHIIKVQDVRG-RQVVETTEVKSRHILIKPSIILSEEKARTMLAGFVKDLRAGDADFAELAKEHSQDPGSALKG 339
Cdd:PRK10770  241 IRSGVGFHILKVNDLRGeSQNISVTEVHARHILLKPSPIMTDEQARAKLEQIAADIKSGKTTFAAAAKEFSQDPGSANQG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 340 GQYDWTDPTTYVPAFRDTLLSLDKNEISEPFRSQFGWHIVQLLDKRVADKTEQAKRNRAHGMLFNRKFKEESFNWQQEMR 419
Cdd:PRK10770  321 GDLGWATPDIFDPAFRDALMRLNKGQISAPVHSSFGWHLIELLDTRQVDKTDAAQKDRAYRMLFNRKFSEEAQTWMQEQR 400


                  ....*..
gi 2528041503 420 EQAHVEI 426
Cdd:PRK10770  401 ASAYVKI 407
 
Name Accession Description Interval E-value
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 21-426 5.50e-154

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 442.26  E-value: 5.50e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503  21 FAAPVEIDKVIGIVNQGVILKSEVDTIVDRVKKQAEEQNQQLPKDETLRVQAIERLVNQTLMMQMAERMGLEISDSQLDQ 100
Cdd:PRK10770    1 FAAPQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAQQAGQQLPDDATLRHQILERLIMDNIILQMAQKMGVKISDEQLDQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 101 TLANMAKEQGGTIADLRRTIEASGESFQAYREEIRKEITTQQVTRANVDRRIYVSDQEIDNLLKIMDSQGQNAEEYDIGH 180
Cdd:PRK10770   81 AIANIAAQNNMTLDQMRSRLAYDGLNYNTYRNQIRKEMIISEVRNNEVRRRITILPQEVDSLAKQIGNQNDASTELNLSH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 181 ILIDIPSAASADDVSSAKTRADKVIELLQDGQEFKRIAISSSSGSKALEGGQLGWMGINEMPSLFAEAVKGKKKDAIIGP 260
Cdd:PRK10770  161 ILIPLPENPTQDQVDEAESQARSIVDQARNGADFGKLAIAYSADQQALKGGQMGWGRIQELPGLFAQALSTAKKGDIVGP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 261 LRSGAGFHIIKVQDVRG-RQVVETTEVKSRHILIKPSIILSEEKARTMLAGFVKDLRAGDADFAELAKEHSQDPGSALKG 339
Cdd:PRK10770  241 IRSGVGFHILKVNDLRGeSQNISVTEVHARHILLKPSPIMTDEQARAKLEQIAADIKSGKTTFAAAAKEFSQDPGSANQG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 340 GQYDWTDPTTYVPAFRDTLLSLDKNEISEPFRSQFGWHIVQLLDKRVADKTEQAKRNRAHGMLFNRKFKEESFNWQQEMR 419
Cdd:PRK10770  321 GDLGWATPDIFDPAFRDALMRLNKGQISAPVHSSFGWHLIELLDTRQVDKTDAAQKDRAYRMLFNRKFSEEAQTWMQEQR 400


                  ....*..
gi 2528041503 420 EQAHVEI 426
Cdd:PRK10770  401 ASAYVKI 407
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 279-424 2.83e-38

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 135.47  E-value: 2.83e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 279 QVVETTEVKSRHILIKPSIILSEEKARTMLAGFVKDLRAGdADFAELAKEHSQDPGSALKGGQYDWTDPTTYVPAFRDTL 358
Cdd:COG0760     2 QFDSPEEVRASHILVKVPPSEDRAKAEAKAEELLAQLKAG-ADFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEAA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2528041503 359 LSLDKNEISEPFRSQFGWHIVQLLDKRVADKTE-QAKRNRAHGMLFNRKFKEesfnWQQEMREQAHV 424
Cdd:COG0760    81 FALKPGEISGPVKTQFGYHIIKVEDRRPAETPPfEEVKQQIRQELFQQALEA----WLEELRKKAKI 143
SurA_N pfam09312
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 27-143 1.50e-35

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: 127.40  E-value: 1.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503  27 IDKVIGIVNQGVILKSEVDTIVDRVKKQAEEQNQQLPKDETLRVQAIERLVNQTLMMQMAERMGLEISDSQLDQTLANMA 106
Cdd:pfam09312   1 LDRIVAVVNDGVILQSELDRRVDTVKRNLQQQGTQLPPDAVLERQVLERLILERIQLQMAEKTGIRVDDAELNQAIARIA 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2528041503 107 KEQGGTIADLRRTIEASGESFQAYREEIRKEITTQQV 143
Cdd:pfam09312  81 QQNNLTLDQLRQALAADGLSYDKFREQIRKEIIISRL 117
 
Name Accession Description Interval E-value
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 21-426 5.50e-154

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 442.26  E-value: 5.50e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503  21 FAAPVEIDKVIGIVNQGVILKSEVDTIVDRVKKQAEEQNQQLPKDETLRVQAIERLVNQTLMMQMAERMGLEISDSQLDQ 100
Cdd:PRK10770    1 FAAPQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAQQAGQQLPDDATLRHQILERLIMDNIILQMAQKMGVKISDEQLDQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 101 TLANMAKEQGGTIADLRRTIEASGESFQAYREEIRKEITTQQVTRANVDRRIYVSDQEIDNLLKIMDSQGQNAEEYDIGH 180
Cdd:PRK10770   81 AIANIAAQNNMTLDQMRSRLAYDGLNYNTYRNQIRKEMIISEVRNNEVRRRITILPQEVDSLAKQIGNQNDASTELNLSH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 181 ILIDIPSAASADDVSSAKTRADKVIELLQDGQEFKRIAISSSSGSKALEGGQLGWMGINEMPSLFAEAVKGKKKDAIIGP 260
Cdd:PRK10770  161 ILIPLPENPTQDQVDEAESQARSIVDQARNGADFGKLAIAYSADQQALKGGQMGWGRIQELPGLFAQALSTAKKGDIVGP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 261 LRSGAGFHIIKVQDVRG-RQVVETTEVKSRHILIKPSIILSEEKARTMLAGFVKDLRAGDADFAELAKEHSQDPGSALKG 339
Cdd:PRK10770  241 IRSGVGFHILKVNDLRGeSQNISVTEVHARHILLKPSPIMTDEQARAKLEQIAADIKSGKTTFAAAAKEFSQDPGSANQG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 340 GQYDWTDPTTYVPAFRDTLLSLDKNEISEPFRSQFGWHIVQLLDKRVADKTEQAKRNRAHGMLFNRKFKEESFNWQQEMR 419
Cdd:PRK10770  321 GDLGWATPDIFDPAFRDALMRLNKGQISAPVHSSFGWHLIELLDTRQVDKTDAAQKDRAYRMLFNRKFSEEAQTWMQEQR 400


                  ....*..
gi 2528041503 420 EQAHVEI 426
Cdd:PRK10770  401 ASAYVKI 407
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 279-424 2.83e-38

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 135.47  E-value: 2.83e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 279 QVVETTEVKSRHILIKPSIILSEEKARTMLAGFVKDLRAGdADFAELAKEHSQDPGSALKGGQYDWTDPTTYVPAFRDTL 358
Cdd:COG0760     2 QFDSPEEVRASHILVKVPPSEDRAKAEAKAEELLAQLKAG-ADFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEAA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2528041503 359 LSLDKNEISEPFRSQFGWHIVQLLDKRVADKTE-QAKRNRAHGMLFNRKFKEesfnWQQEMREQAHV 424
Cdd:COG0760    81 FALKPGEISGPVKTQFGYHIIKVEDRRPAETPPfEEVKQQIRQELFQQALEA----WLEELRKKAKI 143
SurA_N pfam09312
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 27-143 1.50e-35

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: 127.40  E-value: 1.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503  27 IDKVIGIVNQGVILKSEVDTIVDRVKKQAEEQNQQLPKDETLRVQAIERLVNQTLMMQMAERMGLEISDSQLDQTLANMA 106
Cdd:pfam09312   1 LDRIVAVVNDGVILQSELDRRVDTVKRNLQQQGTQLPPDAVLERQVLERLILERIQLQMAEKTGIRVDDAELNQAIARIA 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2528041503 107 KEQGGTIADLRRTIEASGESFQAYREEIRKEITTQQV 143
Cdd:pfam09312  81 QQNNLTLDQLRQALAADGLSYDKFREQIRKEIIISRL 117
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 285-385 1.31e-25

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: 100.52  E-value: 1.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 285 EVKSRHILIK--PSIILSEEKARTMLAGFVKDLRAGdADFAELAKEHSQDPGSALKGGQYDWTDPTTYVPAFRDTLLSLD 362
Cdd:pfam13616  15 SVKASHILISysQAVSRTEEEAKAKADSLLAALKNG-ADFAALAKTYSDDPASKNNGGDLGWFTKGQMVKEFEDAVFSLK 93

                          90       100
                  ....*....|....*....|...
gi 2528041503 363 KNEISEPFRSQFGWHIVQLLDKR 385
Cdd:pfam13616  94 VGEISGVVKTQFGFHIIKVTDKK 116
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 290-383 4.68e-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: 98.14  E-value: 4.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 290 HILIK--PSIILSEEKARTMLAGFVKDLRAGDADFAELAKEHSQDPGSALKGGQYDWTDPTTYVPAFRDTLLSLDKNEIS 367
Cdd:pfam00639   1 HILIKtpEASERDRAEAKAKAEEILEQLKSGEDSFAELARKYSDDCPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEIS 80

                          90
                  ....*....|....*.
gi 2528041503 368 EPFRSQFGWHIVQLLD 383
Cdd:pfam00639  81 GPVETRFGFHIIKLTD 96
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 168-289 6.82e-21

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 88.48  E-value: 6.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 168 SQGQNAEEYDIGHILIDIPSAASADDvssAKTRADKVIELLQDGQEFKRIAI--SSSSGSKAlEGGQLGWMGINEMPSLF 245
Cdd:COG0760     1 DQFDSPEEVRASHILVKVPPSEDRAK---AEAKAEELLAQLKAGADFAELAKeySQDPGSAA-NGGDLGWFSRGQLVPEF 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2528041503 246 AEAVKGKKKDAIIGPLRSGAGFHIIKVQDVRGRQVVETTEVKSR 289
Cdd:COG0760    77 EEAAFALKPGEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKQQ 120
prsA PRK00059
peptidylprolyl isomerase; Provisional
 2-303 1.61e-16

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 80.14  E-value: 1.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503   2 NLKKLLTSA---VLTFSL--CQSAFAAPVEIDK-VIGIVNQGVILKSEVDT--IVDRVKKQAEEQ-NQQLPKDE------ 66
Cdd:PRK00059    3 SIKKLVASLlvgVFIFSAvgCNMIEKTPEAIAKsTVATVNGEKITRGDLDKdpKMQQVLEQLKQQyGDNYEKNEqvkeqi 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503  67 -TLRVQAIERLVNQTLMMQMAERMGLEISDSQL----DQTLANMAKEQGGTIADLRRTIEASGESFQAYREEIRKEITTQ 141
Cdd:PRK00059   83 kQQKEQILDSLITEKVLLQKAKELKLIPSEEELnkevDKKINEIKKQFNNDEEQFEEALKATGFTEETFKEYLKNQIIIE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 142 QVTRaNVDRRIYVSDQEID---NLLKimDSQGQNAEEYDIGHILIDipsaasaddvssAKTRADKVIELLQDGQEFKRIA 218
Cdd:PRK00059  163 KVIN-EVVKDVKVTDKDAQkyyNENK--SKFTEKPNTMHLAHILVK------------TEDEAKKVKKRLDKGEDFAKVA 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 219 --ISSSSGSKAlEGGQLGWMGINE--MPSLFAEAVKGKKKDAIIGPLRSGAGFHIIKVQDVRGRQVVETTEVKSRhilIK 294
Cdd:PRK00059  228 keVSQDPGSKD-KGGDLGDVPYSDsgYDKEFMDGAKALKEGEISAPVKTQFGYHIIKAIKKKEYPVKPFDSVKED---IK 303


                  ....*....
gi 2528041503 295 pSIILSEEK 303
Cdd:PRK00059  304 -KQLLQEKQ 311
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 180-274 8.16e-16

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: 72.72  E-value: 8.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 180 HILIdIPSAASADDVSSAKTRADKVIELLQDGQE-FKRIAIS-SSSGSKALEGGQLGWMGINEMPSLFAEAVKGKKKDAI 257
Cdd:pfam00639   1 HILI-KTPEASERDRAEAKAKAEEILEQLKSGEDsFAELARKySDDCPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEI 79

                          90
                  ....*....|....*..
gi 2528041503 258 IGPLRSGAGFHIIKVQD 274
Cdd:pfam00639  80 SGPVETRFGFHIIKLTD 96
prsA PRK03095
peptidylprolyl isomerase PrsA;
285-394 9.09e-16

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 77.34  E-value: 9.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 285 EVKSRHILIKpsiilSEEKARTmlagfVKDLRAGDADFAELAKEHSQDPGSALKGGQYDWTDPTTYVPAFRDTLLSLDKN 364
Cdd:PRK03095  132 EIKASHILVK-----DEATAKK-----VKEELGQGKSFEELAKQYSEDTGSKEKGGDLGFFGAGKMVKEFEDAAYKLKKD 201

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2528041503 365 EISEPFRSQFGWHIVQLLDKRVADKT-EQAK 394
Cdd:PRK03095  202 EVSEPVKSQFGYHIIKVTDIKEPEKSfEQSK 232
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 161-276 1.97e-15

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: 72.01  E-value: 1.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 161 NLLKIMDsQGQNAEEYDIGHILIDIPSAASADDvSSAKTRADKVIELLQDGQEFKRIA--ISSSSGSKAlEGGQLGWMGI 238
Cdd:pfam13616   2 SLSKLVD-KKSAPDSVKASHILISYSQAVSRTE-EEAKAKADSLLAALKNGADFAALAktYSDDPASKN-NGGDLGWFTK 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2528041503 239 NEMPSLFAEAVKGKKKDAIIGPLRSGAGFHIIKVQDVR 276
Cdd:pfam13616  79 GQMVKEFEDAVFSLKVGEISGVVKTQFGFHIIKVTDKK 116
prsA PRK00059
peptidylprolyl isomerase; Provisional
 279-384 7.54e-15

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 75.13  E-value: 7.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 279 QVVETTEVKSRHILIKpsiilSEEKARTmlagfVKDLRAGDADFAELAKEHSQDPGSALKGGQYDW--TDPTTYVPAFRD 356
Cdd:PRK00059  190 FTEKPNTMHLAHILVK-----TEDEAKK-----VKKRLDKGEDFAKVAKEVSQDPGSKDKGGDLGDvpYSDSGYDKEFMD 259

                          90       100
                  ....*....|....*....|....*...
gi 2528041503 357 TLLSLDKNEISEPFRSQFGWHIVQLLDK 384
Cdd:PRK00059  260 GAKALKEGEISAPVKTQFGYHIIKAIKK 287
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 49-288 1.82e-13

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 72.35  E-value: 1.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503  49 DRVKKQAEEQNQQLPKDE----TLRVQAIERLVNQTLMMQMAERMGLEISDSQLDQTLANMAKEQGGTIADLRR---TIE 121
Cdd:PRK10788   64 NRLQQQLGDQFSELAANEgymkQLRQQVLNRLIDEALLDQYARELGLGISDEQVKQAIFATPAFQTDGKFDNNKylaILN 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 122 ASGESFQAYREEIRKEITTQQVTRA----------NVDR-----------------------RIYVSDQEIDNLLKIMDS 168
Cdd:PRK10788  144 QMGMTADQYAQALRQQLTTQQLINGvagtdfmlpgETDElaalvaqqrvvreatidvnalaaKQTVTDEEIKSYYDQNKN 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 169 QGQNAEEYDIGHILIDIPSAASADDVSSA--------------------------KTRAD--KVIELLQDGQEFKRIAIS 220
Cdd:PRK10788  224 NFMAPEQFKVSYIKLDAATMQQKITVSDAdiqayydqhqdqftqperkrysiiqtKTEAEakAVLDELKKGADFATLAKE 303

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2528041503 221 SSSGS-KALEGGQLGWMGINEMPSLFAEAvKGKKKDAIIGPLRSGAGFHIIKVQDVRGRQVVETTEVKS 288
Cdd:PRK10788  304 KSTDIiSARNGGDLGWLEPATTPDELKNA-GLKEKGQLSGVIKSSVGFLIVRLDDIQPAKVKPLSEVRD 371
SurA_N_3 pfam13624
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 34-143 3.68e-13

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: 66.83  E-value: 3.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503  34 VNQGVILKSEVDTIVDRVKKQAEEQNQQ-----LPKDETLRVQAIERLVNQTLMMQMAERMGLEISDSQLDQTLANMA-- 106
Cdd:pfam13624  44 VNGEKISRAEFQRAYRRQLDQLRQQFGPnldaeLLDELGLRQQVLDQLIDRALLLQEAKKLGLAVSDEEVRQAIASIPaf 123

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2528041503 107 KEQGGTIADL-RRTIEASGESFQAYREEIRKEITTQQV 143
Cdd:pfam13624 124 QEDGKFDKERyRQLLRANGLTPAEFEASLRQDLLLQQL 161
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 285-418 1.25e-12

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 68.07  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 285 EVKSRHILIKpsiilsEEKArtmlAGFVKDLRAGDADFAELAKEHSQDPGSALKGGQYDWTDPTTYVPAFRDTLLSLDKN 364
Cdd:PRK02998  134 EMKVSHILVK------DEKT----AKEVKEKVNNGEDFAALAKQYSEDTGSKEQGGEISGFAPGQTVKEFEEAAYKLDAG 203

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2528041503 365 EISEPFRSQFGWHIVQLLDKRVADKTEQAKRNrAHGMLFNRKFKEESFNWQQEM 418
Cdd:PRK02998  204 QVSEPVKTTYGYHIIKVTDKKELKPFDEVKDS-IRKDLEQQRLQDTTGKWKQQV 256
prsA PRK03002
peptidylprolyl isomerase PrsA;
285-385 2.23e-11

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 64.19  E-value: 2.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 285 EVKSRHILIKpsiilSEEKARTMlagfVKDLRAGdADFAELAKEHSQDPGSALKGGQYDWTDPTTYVPAFRDTLLSLDKN 364
Cdd:PRK03002  136 EIKASHILVS-----DENEAKEI----KKKLDAG-ASFEELAKQESQDLLSKEKGGDLGYFNSGRMAPEFETAAYKLKVG 205

                          90       100
                  ....*....|....*....|.
gi 2528041503 365 EISEPFRSQFGWHIVQLLDKR 385
Cdd:PRK03002  206 QISNPVKSPNGYHIIKLTDKK 226
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 281-383 6.47e-11

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 59.27  E-value: 6.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 281 VETTEVKSRHILIKPS-------------IILSEEKARTMLAGFVKDLRAGDADFAELAKEHSqDPGSALKGGQYDWTDP 347
Cdd:PTZ00356    1 MEGDTVRAAHLLIKHTgsrnpvsrrtgkpVTRSKEEAIKELAKWREQIVSGEKTFEEIARQRS-DCGSAAKGGDLGFFGR 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2528041503 348 TTYVPAFRDTLLSLDKNEISEPFRSQFGWHIVQLLD 383
Cdd:PTZ00356   80 GQMQKPFEDAAFALKVGEISDIVHTDSGVHIILRLA 115
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 290-382 1.72e-08

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 51.56  E-value: 1.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 290 HILIKpsiilsEEKartMLAGFVKDLRAGdADFAELAKEHSQDPgSALKGGQYDWTDPTTYVPAFRDTLLSLDKNEISEP 369
Cdd:PRK15441    9 HILVK------EEK---LALDLLEQIKNG-ADFGKLAKKHSICP-SGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGP 77

                          90
                  ....*....|...
gi 2528041503 370 FRSQFGWHIVQLL 382
Cdd:PRK15441   78 LHTQFGYHIIKVL 90
prsA PRK03095
peptidylprolyl isomerase PrsA;
201-276 2.06e-07

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 52.30  E-value: 2.06e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2528041503 201 ADKVIELLQDGQEFKRIA--ISSSSGSKAlEGGQLGWMGINEMPSLFAEAVKGKKKDAIIGPLRSGAGFHIIKVQDVR 276
Cdd:PRK03095  146 AKKVKEELGQGKSFEELAkqYSEDTGSKE-KGGDLGFFGAGKMVKEFEDAAYKLKKDEVSEPVKSQFGYHIIKVTDIK 222
SurA_N_2 pfam13623
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 30-105 3.58e-07

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: 49.50  E-value: 3.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503  30 VIGIVNQGVILKSEVDTIVDRVKKQAEEQ-----NQQLPKDETLRVQAIERLVNQTLMMQMAERMGLEISDSQLDQTLAN 104
Cdd:pfam13623  42 VVAEVNGEEISYQEFQQAVENQRNRLRQQlgqnfDPAELDEAQLREQVWDQLVREKLLLQEAEKLGLTVSDEELVDAIQG 121


                  .
gi 2528041503 105 M 105
Cdd:pfam13623 122 N 122
prsA PRK04405
peptidylprolyl isomerase; Provisional
 284-382 1.58e-06

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 49.40  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 284 TEVKSRHILIKpsiilSEEKARTMlagfVKDLRAGdADFAELAKEHSQDPGSALKGGQ---YDWTDpTTYVPAFRDTLLS 360
Cdd:PRK04405  143 PKVTVQHILVS-----KKSTAETV----IKKLKDG-KDFAKLAKKYSTDTATKNKGGKlsaFDSTD-TTLDSTFKTAAFK 211

                          90       100
                  ....*....|....*....|...
gi 2528041503 361 LDKNEI-SEPFRSQFGWHIVQLL 382
Cdd:PRK04405  212 LKNGEYtTTPVKTTYGYEVIKMI 234
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
299-394 1.31e-05

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 44.35  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 299 LSEEKARTMLAGFVKDLRAG-DADFAELAKehsqdpGSALKGGQYDWTDPTTYVP-AFRDTLLSLDKNEISEPFRSQFGW 376
Cdd:pfam13145  27 ILVFKDQVAADAALALLKAGaLEDFAALAK------GEGIKAATLDIVESAELLPeELAKAAFALKPGEVSGPIKTGNGY 100

                          90       100
                  ....*....|....*....|
gi 2528041503 377 HIVQLLDKRVADKT--EQAK 394
Cdd:pfam13145 101 YVVRVTEIKPAQPLpfEEAK 120
prsA PRK01326
foldase protein PrsA; Reviewed
 300-412 2.59e-05

foldase protein PrsA; Reviewed


Pssm-ID: 179281 [Multi-domain]  Cd Length: 310  Bit Score: 45.96  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 300 SEEKARTMLagfvKDLRAGDADFAELAKEHSQDPGsalKGGQYDWTDPTTYVP-AFRDTLLSLDKNEISE------PFRS 372
Cdd:PRK01326  155 NEDKAKSVL----EEAKAEGADFAQIAKENTTTKE---KKGEYKFDSGSTNVPeQVKKAAFALDEDGVSDvisvldPTAY 227

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2528041503 373 QFGWHIVQLLDKRVADKTEQAKRNRAHGMLFNRKFKEESF 412
Cdd:PRK01326  228 QSKYYIVKVTKKTEKKSDWKDYKKRLKAIILAQKQNDSNF 267
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 212-271 1.01e-04

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 41.55  E-value: 1.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 212 QEFKRIAISSSSGSKALEGGQLGWMGINEMPSLFAEAVKGKKKDAIIGPLRSGAGFHIIK 271
Cdd:PTZ00356   53 KTFEEIARQRSDCGSAAKGGDLGFFGRGQMQKPFEDAAFALKVGEISDIVHTDSGVHIIL 112
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 201-272 1.38e-03

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 37.70  E-value: 1.38e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2528041503 201 ADKVIELLQDGQEFKRIAISSSSGSKALEGGQLGWMGINEMPSLFAEAVKGKKKDAIIGPLRSGAGFHIIKV 272
Cdd:PRK15441   18 ALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGYHIIKV 89
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 79-274 4.65e-03

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 38.80  E-value: 4.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503  79 QTLMMQMAERMGLE---ISDSQLDQTLANmAKEQGGTiaDLRRTIEASG-ESFQAYREEIRKEITTQQVTRANVdrriyv 154
Cdd:PRK02998   52 STLYQMVLSKALLDkykVSDEEAKKQVEE-AKDKMGD--NFKSTLEQVGlKNEDELKEKMKPEIAFEKAIKATV------ 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 155 SDQEIDNLLKimdsqgqnaEEYDIGHILidipsaasaddVSSAKTrADKVIELLQDGQEFKRIA--ISSSSGSKAlEGGQ 232
Cdd:PRK02998  123 TEKDVKDNYK---------PEMKVSHIL-----------VKDEKT-AKEVKEKVNNGEDFAALAkqYSEDTGSKE-QGGE 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2528041503 233 LGWMGINEMPSLFAEAVKGKKKDAIIGPLRSGAGFHIIKVQD 274
Cdd:PRK02998  181 ISGFAPGQTVKEFEEAAYKLDAGQVSEPVKTTYGYHIIKVTD 222
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
194-287 5.42e-03

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 36.65  E-value: 5.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 194 VSSAKTRADKVIELLQDGQEFKRIAISSSSGSKAlegGQLGWMGINEMPSL-FAEAVKGKKKDAIIGPLRSGAGFHIIKV 272
Cdd:pfam13145  29 VFKDQVAADAALALLKAGALEDFAALAKGEGIKA---ATLDIVESAELLPEeLAKAAFALKPGEVSGPIKTGNGYYVVRV 105

                          90
                  ....*....|....*
gi 2528041503 273 QDVRGRQVVETTEVK 287
Cdd:pfam13145 106 TEIKPAQPLPFEEAK 120
prsA PRK03002
peptidylprolyl isomerase PrsA;
196-274 7.42e-03

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 37.99  E-value: 7.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528041503 196 SAKTRADKVIELLQDGQEFKRIAISSSS--GSKAlEGGQLGWMGINEMPSLFAEAVKGKKKDAIIGPLRSGAGFHIIKVQ 273
Cdd:PRK03002  145 SDENEAKEIKKKLDAGASFEELAKQESQdlLSKE-KGGDLGYFNSGRMAPEFETAAYKLKVGQISNPVKSPNGYHIIKLT 223


                  .
gi 2528041503 274 D 274
Cdd:PRK03002  224 D 224
 
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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