|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10770 |
PRK10770 |
peptidyl-prolyl cis-trans isomerase SurA; Provisional |
19-431 |
0e+00 |
|
peptidyl-prolyl cis-trans isomerase SurA; Provisional
Pssm-ID: 236758 [Multi-domain] Cd Length: 413 Bit Score: 819.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 19 FAAPQEVDKVAAVVDNGVVLQSDIDGLLQSVKMNAQQSGQQVPDDSTLRHQILERLIMDNIQLQMAKKMGITITDQALDK 98
Cdd:PRK10770 1 FAAPQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAQQAGQQLPDDATLRHQILERLIMDNIILQMAQKMGVKISDEQLDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 99 AIADIAAQNRMTLAQMRSRLAADGLSYDTYREQIRKEMLTSEVRNNEVRRRITILPQEVESLAKQMGNQVSGDTELNLSH 178
Cdd:PRK10770 81 AIANIAAQNNMTLDQMRSRLAYDGLNYNTYRNQIRKEMIISEVRNNEVRRRITILPQEVDSLAKQIGNQNDASTELNLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 179 ILIPLPENPTQQQVDQAEDLANKLVADIKGGADFGKLAIANSADSQALKGGQMGWGKLQELPSLFAERLQSAHKGEIVGP 258
Cdd:PRK10770 161 ILIPLPENPTQDQVDEAESQARSIVDQARNGADFGKLAIAYSADQQALKGGQMGWGRIQELPGLFAQALSTAKKGDIVGP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 259 IRSGVGFHILKVNDMRGADQTISVTEVNARHILLKPSPMMTDEQARAKLEAAAAEIKSGKTSFATIAKEISQDPGSAMQG 338
Cdd:PRK10770 241 IRSGVGFHILKVNDLRGESQNISVTEVHARHILLKPSPIMTDEQARAKLEQIAADIKSGKTTFAAAAKEFSQDPGSANQG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 339 GELGWASPDIYDPAFRDALMKLKKGEISAPVHSSFGWHLIQLVDTRQVDKTDAAQKERAYRMLFNRKFAEEAQTWMQEQR 418
Cdd:PRK10770 321 GDLGWATPDIFDPAFRDALMRLNKGQISAPVHSSFGWHLIELLDTRQVDKTDAAQKDRAYRMLFNRKFSEEAQTWMQEQR 400
|
410
....*....|...
gi 488139280 419 AAAYVKILDGSNA 431
Cdd:PRK10770 401 ASAYVKILSNSNA 413
|
|
| SurA_N |
pfam09312 |
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ... |
25-142 |
2.38e-57 |
|
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: 184.40 E-value: 2.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 25 VDKVAAVVDNGVVLQSDIDGLLQSVKMNAQQSGQQVPDDSTLRHQILERLIMDNIQLQMAKKMGITITDQALDKAIADIA 104
Cdd:pfam09312 1 LDRIVAVVNDGVILQSELDRRVDTVKRNLQQQGTQLPPDAVLERQVLERLILERIQLQMAEKTGIRVDDAELNQAIARIA 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 488139280 105 AQNRMTLAQMRSRLAADGLSYDTYREQIRKEMLTSEVR 142
Cdd:pfam09312 81 QQNNLTLDQLRQALAADGLSYDKFREQIRKEIIISRLR 118
|
|
| SurA |
COG0760 |
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ... |
277-423 |
1.72e-41 |
|
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440523 [Multi-domain] Cd Length: 143 Bit Score: 143.95 E-value: 1.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 277 DQTISVTEVNARHILLKPSPMMTDEQARAKLEAAAAEIKSGKtSFATIAKEISQDPGSAMQGGELGWASPDIYDPAFRDA 356
Cdd:COG0760 1 DQFDSPEEVRASHILVKVPPSEDRAKAEAKAEELLAQLKAGA-DFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488139280 357 LMKLKKGEISAPVHSSFGWHLIQLVDTRQVDKTD-AAQKERAYRMLFNRKFaeeaQTWMQEQRAAAYV 423
Cdd:COG0760 80 AFALKPGEISGPVKTQFGYHIIKVEDRRPAETPPfEEVKQQIRQELFQQAL----EAWLEELRKKAKI 143
|
|
| nifM_nitrog |
TIGR02933 |
nitrogen fixation protein NifM; Members of this protein family, found in a subset of ... |
313-416 |
1.57e-12 |
|
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: 67.18 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 313 EIKSGKTSFATIAKEISQDPgSAMQGGELGWASPDIYDPAFRDALMKLKKGEISAPVHSSFGWHLI---QLVDTRQVDKT 389
Cdd:TIGR02933 151 RLRGKPAAFAEQAMRHSHCP-TAMEGGLLGWVSRGLLYPQLDAALFQLAEGELSPPIESEIGWHLLlceAIRPARPLTLE 229
|
90 100
....*....|....*....|....*..
gi 488139280 390 DAAqkERAYRMLFNRKFAEEAQTWMQE 416
Cdd:TIGR02933 230 EAL--PRARDRLQLRQQKAYQRQWLVQ 254
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10770 |
PRK10770 |
peptidyl-prolyl cis-trans isomerase SurA; Provisional |
19-431 |
0e+00 |
|
peptidyl-prolyl cis-trans isomerase SurA; Provisional
Pssm-ID: 236758 [Multi-domain] Cd Length: 413 Bit Score: 819.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 19 FAAPQEVDKVAAVVDNGVVLQSDIDGLLQSVKMNAQQSGQQVPDDSTLRHQILERLIMDNIQLQMAKKMGITITDQALDK 98
Cdd:PRK10770 1 FAAPQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAQQAGQQLPDDATLRHQILERLIMDNIILQMAQKMGVKISDEQLDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 99 AIADIAAQNRMTLAQMRSRLAADGLSYDTYREQIRKEMLTSEVRNNEVRRRITILPQEVESLAKQMGNQVSGDTELNLSH 178
Cdd:PRK10770 81 AIANIAAQNNMTLDQMRSRLAYDGLNYNTYRNQIRKEMIISEVRNNEVRRRITILPQEVDSLAKQIGNQNDASTELNLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 179 ILIPLPENPTQQQVDQAEDLANKLVADIKGGADFGKLAIANSADSQALKGGQMGWGKLQELPSLFAERLQSAHKGEIVGP 258
Cdd:PRK10770 161 ILIPLPENPTQDQVDEAESQARSIVDQARNGADFGKLAIAYSADQQALKGGQMGWGRIQELPGLFAQALSTAKKGDIVGP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 259 IRSGVGFHILKVNDMRGADQTISVTEVNARHILLKPSPMMTDEQARAKLEAAAAEIKSGKTSFATIAKEISQDPGSAMQG 338
Cdd:PRK10770 241 IRSGVGFHILKVNDLRGESQNISVTEVHARHILLKPSPIMTDEQARAKLEQIAADIKSGKTTFAAAAKEFSQDPGSANQG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 339 GELGWASPDIYDPAFRDALMKLKKGEISAPVHSSFGWHLIQLVDTRQVDKTDAAQKERAYRMLFNRKFAEEAQTWMQEQR 418
Cdd:PRK10770 321 GDLGWATPDIFDPAFRDALMRLNKGQISAPVHSSFGWHLIELLDTRQVDKTDAAQKDRAYRMLFNRKFSEEAQTWMQEQR 400
|
410
....*....|...
gi 488139280 419 AAAYVKILDGSNA 431
Cdd:PRK10770 401 ASAYVKILSNSNA 413
|
|
| SurA_N |
pfam09312 |
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ... |
25-142 |
2.38e-57 |
|
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: 184.40 E-value: 2.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 25 VDKVAAVVDNGVVLQSDIDGLLQSVKMNAQQSGQQVPDDSTLRHQILERLIMDNIQLQMAKKMGITITDQALDKAIADIA 104
Cdd:pfam09312 1 LDRIVAVVNDGVILQSELDRRVDTVKRNLQQQGTQLPPDAVLERQVLERLILERIQLQMAEKTGIRVDDAELNQAIARIA 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 488139280 105 AQNRMTLAQMRSRLAADGLSYDTYREQIRKEMLTSEVR 142
Cdd:pfam09312 81 QQNNLTLDQLRQALAADGLSYDKFREQIRKEIIISRLR 118
|
|
| SurA |
COG0760 |
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ... |
277-423 |
1.72e-41 |
|
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440523 [Multi-domain] Cd Length: 143 Bit Score: 143.95 E-value: 1.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 277 DQTISVTEVNARHILLKPSPMMTDEQARAKLEAAAAEIKSGKtSFATIAKEISQDPGSAMQGGELGWASPDIYDPAFRDA 356
Cdd:COG0760 1 DQFDSPEEVRASHILVKVPPSEDRAKAEAKAEELLAQLKAGA-DFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488139280 357 LMKLKKGEISAPVHSSFGWHLIQLVDTRQVDKTD-AAQKERAYRMLFNRKFaeeaQTWMQEQRAAAYV 423
Cdd:COG0760 80 AFALKPGEISGPVKTQFGYHIIKVEDRRPAETPPfEEVKQQIRQELFQQAL----EAWLEELRKKAKI 143
|
|
| SurA |
COG0760 |
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ... |
166-294 |
3.58e-26 |
|
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440523 [Multi-domain] Cd Length: 143 Bit Score: 102.73 E-value: 3.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 166 NQVSGDTELNLSHILIPLPENptqQQVDQAEDLANKLVADIKGGADFGKLAIANSADSQ-ALKGGQMGWGKLQELPSLFA 244
Cdd:COG0760 1 DQFDSPEEVRASHILVKVPPS---EDRAKAEAKAEELLAQLKAGADFAELAKEYSQDPGsAANGGDLGWFSRGQLVPEFE 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 488139280 245 ERLQSAHKGEIVGPIRSGVGFHILKVNDMRGAdQTISVTEV--NARHILLKP 294
Cdd:COG0760 78 EAAFALKPGEISGPVKTQFGYHIIKVEDRRPA-ETPPFEEVkqQIRQELFQQ 128
|
|
| Rotamase |
pfam00639 |
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ... |
289-382 |
5.49e-26 |
|
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: 100.84 E-value: 5.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 289 HILLKPSPMMTDEQARAKLEAAA--AEIKSGKTSFATIAKEISQDPGSAMQGGELGWASPDIYDPAFRDALMKLKKGEIS 366
Cdd:pfam00639 1 HILIKTPEASERDRAEAKAKAEEilEQLKSGEDSFAELARKYSDDCPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEIS 80
|
90
....*....|....*.
gi 488139280 367 APVHSSFGWHLIQLVD 382
Cdd:pfam00639 81 GPVETRFGFHIIKLTD 96
|
|
| Rotamase_3 |
pfam13616 |
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ... |
265-384 |
3.16e-23 |
|
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: 93.97 E-value: 3.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 265 FHILKVNDMRGAdqtisVTEVNARHILLK--PSPMMTDEQARAKLEAAAAEIKSGkTSFATIAKEISQDPGSAMQGGELG 342
Cdd:pfam13616 1 YSLSKLVDKKSA-----PDSVKASHILISysQAVSRTEEEAKAKADSLLAALKNG-ADFAALAKTYSDDPASKNNGGDLG 74
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 488139280 343 WASPDIYDPAFRDALMKLKKGEISAPVHSSFGWHLIQLVDTR 384
Cdd:pfam13616 75 WFTKGQMVKEFEDAVFSLKVGEISGVVKTQFGFHIIKVTDKK 116
|
|
| Rotamase |
pfam00639 |
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ... |
178-272 |
2.68e-21 |
|
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: 87.74 E-value: 2.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 178 HILIPLPEnPTQQQVDQAEDLANKLVADIKGGAD-FGKLAIANSAD-SQALKGGQMGWGKLQELPSLFAERLQSAHKGEI 255
Cdd:pfam00639 1 HILIKTPE-ASERDRAEAKAKAEEILEQLKSGEDsFAELARKYSDDcPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEI 79
|
90
....*....|....*..
gi 488139280 256 VGPIRSGVGFHILKVND 272
Cdd:pfam00639 80 SGPVETRFGFHIIKLTD 96
|
|
| prsA |
PRK00059 |
peptidylprolyl isomerase; Provisional |
278-427 |
5.11e-21 |
|
peptidylprolyl isomerase; Provisional
Pssm-ID: 234605 [Multi-domain] Cd Length: 336 Bit Score: 93.24 E-value: 5.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 278 QTISVTEVNARHILLKpspmmTDEQARAKLEaaaaEIKSGKTsFATIAKEISQDPGSAMQGGELGWASPDI--YDPAFRD 355
Cdd:PRK00059 190 FTEKPNTMHLAHILVK-----TEDEAKKVKK----RLDKGED-FAKVAKEVSQDPGSKDKGGDLGDVPYSDsgYDKEFMD 259
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488139280 356 ALMKLKKGEISAPVHSSFGWHLIQLVDTRQVDKTDAAQ-KERAYRMLFNRKFAEEAQTWMQEQRAAAYVKILD 427
Cdd:PRK00059 260 GAKALKEGEISAPVKTQFGYHIIKAIKKKEYPVKPFDSvKEDIKKQLLQEKQSEVFKKKIEEWKKALKVKKYE 332
|
|
| prsA |
PRK00059 |
peptidylprolyl isomerase; Provisional |
1-272 |
8.54e-18 |
|
peptidylprolyl isomerase; Provisional
Pssm-ID: 234605 [Multi-domain] Cd Length: 336 Bit Score: 83.99 E-value: 8.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 1 MKNWRTLILGLVICAnTAFAA---------PQEVDK-VAAVVDNGVVLQSDIDGLLQSVKMNAQ---QSGQQVPDDS--- 64
Cdd:PRK00059 1 MKSIKKLVASLLVGV-FIFSAvgcnmiektPEAIAKsTVATVNGEKITRGDLDKDPKMQQVLEQlkqQYGDNYEKNEqvk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 65 ----TLRHQILERLIMDNIQLQMAKKMGITITDQAL----DKAIADIAAQNRMTLAQMRSRLAADGLSYDTYREQIRKEM 136
Cdd:PRK00059 80 eqikQQKEQILDSLITEKVLLQKAKELKLIPSEEELnkevDKKINEIKKQFNNDEEQFEEALKATGFTEETFKEYLKNQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 137 LTSEVRNnEVRRRITILPQEVESL---AKQMgnQVSGDTELNLSHILIplpenptqqqvdQAEDLANKLVADIKGGADFG 213
Cdd:PRK00059 160 IIEKVIN-EVVKDVKVTDKDAQKYyneNKSK--FTEKPNTMHLAHILV------------KTEDEAKKVKKRLDKGEDFA 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488139280 214 KLAIANSADSQAL-KGGQMGwgKLQELPS----LFAERLQSAHKGEIVGPIRSGVGFHILKVND 272
Cdd:PRK00059 225 KVAKEVSQDPGSKdKGGDLG--DVPYSDSgydkEFMDGAKALKEGEISAPVKTQFGYHIIKAIK 286
|
|
| prsA |
PRK03095 |
peptidylprolyl isomerase PrsA; |
284-427 |
5.80e-17 |
|
peptidylprolyl isomerase PrsA;
Pssm-ID: 179537 [Multi-domain] Cd Length: 287 Bit Score: 80.81 E-value: 5.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 284 EVNARHILLKpspmmtDEQARAKLEAaaaEIKSGKtSFATIAKEISQDPGSAMQGGELGWASPDIYDPAFRDALMKLKKG 363
Cdd:PRK03095 132 EIKASHILVK------DEATAKKVKE---ELGQGK-SFEELAKQYSEDTGSKEKGGDLGFFGAGKMVKEFEDAAYKLKKD 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488139280 364 EISAPVHSSFGWHLIQLVDTRQVDKTDAAQKERAYRMLFNRKfAEEAQ---TWMQEQRAAAYVKILD 427
Cdd:PRK03095 202 EVSEPVKSQFGYHIIKVTDIKEPEKSFEQSKADIKKELVQKK-AQDGEfmnDLMMKEIKKADVKVDD 267
|
|
| Rotamase_3 |
pfam13616 |
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ... |
161-274 |
5.58e-16 |
|
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: 73.56 E-value: 5.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 161 AKQMGNQVSGDTELNLSHILIPLPENPTQQQvDQAEDLANKLVADIKGGADFGKLAIANSAD-SQALKGGQMGW-GKLQE 238
Cdd:pfam13616 3 LSKLVDKKSAPDSVKASHILISYSQAVSRTE-EEAKAKADSLLAALKNGADFAALAKTYSDDpASKNNGGDLGWfTKGQM 81
|
90 100 110
....*....|....*....|....*....|....*.
gi 488139280 239 LPsLFAERLQSAHKGEIVGPIRSGVGFHILKVNDMR 274
Cdd:pfam13616 82 VK-EFEDAVFSLKVGEISGVVKTQFGFHIIKVTDKK 116
|
|
| SurA_N_3 |
pfam13624 |
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ... |
28-142 |
1.89e-14 |
|
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: 70.68 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 28 VAAVVDNGVVLQSDIDGLLQSVKMN-AQQSGQQVP----DDSTLRHQILERLIMDNIQLQMAKKMGITITDQALDKAIAD 102
Cdd:pfam13624 40 AVAKVNGEKISRAEFQRAYRRQLDQlRQQFGPNLDaellDELGLRQQVLDQLIDRALLLQEAKKLGLAVSDEEVRQAIAS 119
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 488139280 103 IAA---QNRMTLAQMRSRLAADGLSYDTYREQIRKEMLTSEVR 142
Cdd:pfam13624 120 IPAfqeDGKFDKERYRQLLRANGLTPAEFEASLRQDLLLQQLL 162
|
|
| prsA |
PRK03002 |
peptidylprolyl isomerase PrsA; |
284-427 |
6.25e-14 |
|
peptidylprolyl isomerase PrsA;
Pssm-ID: 101162 [Multi-domain] Cd Length: 285 Bit Score: 71.89 E-value: 6.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 284 EVNARHILLkpspmmTDEQARAkleaaaaEIKS---GKTSFATIAKEISQDPGSAMQGGELGWASPDIYDPAFRDALMKL 360
Cdd:PRK03002 136 EIKASHILV------SDENEAK-------EIKKkldAGASFEELAKQESQDLLSKEKGGDLGYFNSGRMAPEFETAAYKL 202
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488139280 361 KKGEISAPVHSSFGWHLIQLVDTRQVDKTDAAqKERAYRMLFNRKFAEEA--QTWMQEQRAAAYVKILD 427
Cdd:PRK03002 203 KVGQISNPVKSPNGYHIIKLTDKKDLKPYDEV-KDSIRKNLEEERTADPIfgKKLLQSELKKANIKIND 270
|
|
| PRK10788 |
PRK10788 |
periplasmic folding chaperone; Provisional |
65-273 |
1.64e-13 |
|
periplasmic folding chaperone; Provisional
Pssm-ID: 182731 [Multi-domain] Cd Length: 623 Bit Score: 72.35 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 65 TLRHQILERLIMDNIQLQMAKKMGITITDQALDKAIADIAA---QNRMTLAQMRSRLAADGLSYDTYREQIRKEMLTSEV 141
Cdd:PRK10788 86 QLRQQVLNRLIDEALLDQYARELGLGISDEQVKQAIFATPAfqtDGKFDNNKYLAILNQMGMTADQYAQALRQQLTTQQL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 142 RN----------NEVRRRITILPQ---------EVESLAKQmgNQVSgDTELN-----------------LSHI------ 179
Cdd:PRK10788 166 INgvagtdfmlpGETDELAALVAQqrvvreatiDVNALAAK--QTVT-DEEIKsyydqnknnfmapeqfkVSYIkldaat 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 180 ---LIPLPENPTQQQVDQ-------------------AEDLANKLVADIKGGADFGKLAIANSADS-QALKGGQMGWGKL 236
Cdd:PRK10788 243 mqqKITVSDADIQAYYDQhqdqftqperkrysiiqtkTEAEAKAVLDELKKGADFATLAKEKSTDIiSARNGGDLGWLEP 322
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 488139280 237 QELPslfaERLQSA---HKGEIVGPIRSGVGFHILKVNDM 273
Cdd:PRK10788 323 ATTP----DELKNAglkEKGQLSGVIKSSVGFLIVRLDDI 358
|
|
| prsA |
PRK02998 |
peptidylprolyl isomerase; Reviewed |
284-416 |
3.10e-13 |
|
peptidylprolyl isomerase; Reviewed
Pssm-ID: 179522 [Multi-domain] Cd Length: 283 Bit Score: 69.61 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 284 EVNARHILLKpspmmtDEQARAKLEAaaaEIKSGKtSFATIAKEISQDPGSAMQGGELGWASPDIYDPAFRDALMKLKKG 363
Cdd:PRK02998 134 EMKVSHILVK------DEKTAKEVKE---KVNNGE-DFAALAKQYSEDTGSKEQGGEISGFAPGQTVKEFEEAAYKLDAG 203
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 488139280 364 EISAPVHSSFGWHLIQLVDTRQVDKTDaAQKERAYRMLFNRKFAEEAQTWMQE 416
Cdd:PRK02998 204 QVSEPVKTTYGYHIIKVTDKKELKPFD-EVKDSIRKDLEQQRLQDTTGKWKQQ 255
|
|
| nifM_nitrog |
TIGR02933 |
nitrogen fixation protein NifM; Members of this protein family, found in a subset of ... |
313-416 |
1.57e-12 |
|
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: 67.18 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 313 EIKSGKTSFATIAKEISQDPgSAMQGGELGWASPDIYDPAFRDALMKLKKGEISAPVHSSFGWHLI---QLVDTRQVDKT 389
Cdd:TIGR02933 151 RLRGKPAAFAEQAMRHSHCP-TAMEGGLLGWVSRGLLYPQLDAALFQLAEGELSPPIESEIGWHLLlceAIRPARPLTLE 229
|
90 100
....*....|....*....|....*..
gi 488139280 390 DAAqkERAYRMLFNRKFAEEAQTWMQE 416
Cdd:TIGR02933 230 EAL--PRARDRLQLRQQKAYQRQWLVQ 254
|
|
| PTZ00356 |
PTZ00356 |
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional |
285-379 |
4.21e-12 |
|
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
Pssm-ID: 185573 [Multi-domain] Cd Length: 115 Bit Score: 62.74 E-value: 4.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 285 VNARHILLK------PSPMMTD-------EQARAKLEAAAAEIKSGKTSFATIAKEISqDPGSAMQGGELGWASPDIYDP 351
Cdd:PTZ00356 6 VRAAHLLIKhtgsrnPVSRRTGkpvtrskEEAIKELAKWREQIVSGEKTFEEIARQRS-DCGSAAKGGDLGFFGRGQMQK 84
|
90 100
....*....|....*....|....*...
gi 488139280 352 AFRDALMKLKKGEISAPVHSSFGWHLIQ 379
Cdd:PTZ00356 85 PFEDAAFALKVGEISDIVHTDSGVHIIL 112
|
|
| PRK15441 |
PRK15441 |
peptidyl-prolyl cis-trans isomerase C; Provisional |
194-270 |
1.02e-07 |
|
peptidyl-prolyl cis-trans isomerase C; Provisional
Pssm-ID: 185338 [Multi-domain] Cd Length: 93 Bit Score: 49.64 E-value: 1.02e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488139280 194 QAEDLANKLVADIKGGADFGKLAIANSADSQALKGGQMGWGKLQELPSLFAERLQSAHKGEIVGPIRSGVGFHILKV 270
Cdd:PRK15441 13 KEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGYHIIKV 89
|
|
| prsA |
PRK03095 |
peptidylprolyl isomerase PrsA; |
54-279 |
7.05e-07 |
|
peptidylprolyl isomerase PrsA;
Pssm-ID: 179537 [Multi-domain] Cd Length: 287 Bit Score: 50.76 E-value: 7.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 54 QQSGQQVpddstLRHQILERLIMDNIQLQmakkmgititDQALDKAIADIAAQNrmtlaqmrsrlaadGLSYDTYREQ-- 131
Cdd:PRK03095 46 TQAGKQV-----LNNMVMEKVLIKNYKVE----------DKEVDKKYDEMKKQY--------------GDQFDTLLKQqg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 132 IRKEMLTSEVRNNEVRRRI---TILPQEVESLAKQmgnqvsgdtELNLSHILIplpenptqqqvdQAEDLANKLVADIKG 208
Cdd:PRK03095 97 IKEETLKTGVRAQLAQEKAiekTITDKELKDNYKP---------EIKASHILV------------KDEATAKKVKEELGQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488139280 209 GADFGKLAIANSADSQAL-KGGQMGWGKLQELPSLFAERLQSAHKGEIVGPIRSGVGFHILKVNDMRGADQT 279
Cdd:PRK03095 156 GKSFEELAKQYSEDTGSKeKGGDLGFFGAGKMVKEFEDAAYKLKKDEVSEPVKSQFGYHIIKVTDIKEPEKS 227
|
|
| prsA |
PRK04405 |
peptidylprolyl isomerase; Provisional |
313-383 |
9.30e-07 |
|
peptidylprolyl isomerase; Provisional
Pssm-ID: 235295 [Multi-domain] Cd Length: 298 Bit Score: 50.17 E-value: 9.30e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488139280 313 EIKSGKtSFATIAKEISQDPGSAMQGGEL-GWASPD-IYDPAFRDALMKLKKGEISA-PVHSSFGWHLIQLVDT 383
Cdd:PRK04405 164 KLKDGK-DFAKLAKKYSTDTATKNKGGKLsAFDSTDtTLDSTFKTAAFKLKNGEYTTtPVKTTYGYEVIKMIKH 236
|
|
| Rotamase_2 |
pfam13145 |
PPIC-type PPIASE domain; |
184-279 |
2.60e-05 |
|
PPIC-type PPIASE domain;
Pssm-ID: 432992 [Multi-domain] Cd Length: 121 Bit Score: 43.58 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 184 PENPTQQQVDQAEDLANKLV-ADIKGGADFGKLAIANSADSQAlkgGQMGWGKLQELPSL-FAERLQSAHKGEIVGPIRS 261
Cdd:pfam13145 20 PEGRLLEILVFKDQVAADAAlALLKAGALEDFAALAKGEGIKA---ATLDIVESAELLPEeLAKAAFALKPGEVSGPIKT 96
|
90
....*....|....*...
gi 488139280 262 GVGFHILKVNDMRGADQT 279
Cdd:pfam13145 97 GNGYYVVRVTEIKPAQPL 114
|
|
| SurA_N_2 |
pfam13623 |
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ... |
28-109 |
3.11e-05 |
|
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: 43.72 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 28 VAAVVDNGVVLQSDIDGLLQSVKMNA-QQSGQQVP----DDSTLRHQILERLIMDNIQLQMAKKMGITITDQALDKAIAD 102
Cdd:pfam13623 42 VVAEVNGEEISYQEFQQAVENQRNRLrQQLGQNFDpaelDEAQLREQVWDQLVREKLLLQEAEKLGLTVSDEELVDAIQG 121
|
....*..
gi 488139280 103 IAAQNRM 109
Cdd:pfam13623 122 NPAILQQ 128
|
|
| nifM_nitrog |
TIGR02933 |
nitrogen fixation protein NifM; Members of this protein family, found in a subset of ... |
50-278 |
5.81e-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: 44.45 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 50 KMNAQQSGQQVPDDSTLRHQILER-LIMDNIQLQMAKKMGITITDQALDKAIADIAAQnrmtlaqmrsrLAADGLSYDTY 128
Cdd:TIGR02933 10 EMWNCAPGELSPDQLQQFDQAWQRqRHIEQAVVRAADEIGVVIPPSLLEEAPQALAQA-----------LDEQALDAAER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 129 REQIRKEMLTSEVRNNEVRRRITILPQEVESLAKQMGNQVSGDTELNLSHILIPLPENPTQQQVDQAEDLANKLVADikg 208
Cdd:TIGR02933 79 RAMLAHHLRLEAQLACVCAQAPQPDDADVEAWYRRHAEQFKRPEQRLTRHLLLTVNEDDREAVRTRILAILRRLRGK--- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488139280 209 GADFGKLAIANSADSQALKGGQMGW---GKLqeLPSLFAErLQSAHKGEIVGPIRSGVGFHILKVNDMRGADQ 278
Cdd:TIGR02933 156 PAAFAEQAMRHSHCPTAMEGGLLGWvsrGLL--YPQLDAA-LFQLAEGELSPPIESEIGWHLLLCEAIRPARP 225
|
|
| Rotamase_2 |
pfam13145 |
PPIC-type PPIASE domain; |
320-382 |
8.96e-05 |
|
PPIC-type PPIASE domain;
Pssm-ID: 432992 [Multi-domain] Cd Length: 121 Bit Score: 42.04 E-value: 8.96e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488139280 320 SFATIAKEISQDpgsamqGGELGWASPD-IYDPAFRDALMKLKKGEISAPVHSSFGWHLIQLVD 382
Cdd:pfam13145 50 DFAALAKGEGIK------AATLDIVESAeLLPEELAKAAFALKPGEVSGPIKTGNGYYVVRVTE 107
|
|
| PRK15441 |
PRK15441 |
peptidyl-prolyl cis-trans isomerase C; Provisional |
287-381 |
1.66e-04 |
|
peptidyl-prolyl cis-trans isomerase C; Provisional
Pssm-ID: 185338 [Multi-domain] Cd Length: 93 Bit Score: 40.39 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 287 ARHILLKPSPMMTDeqarakleaAAAEIKSGkTSFATIAKEISQDPgSAMQGGELGWASPDIYDPAFRDALMKLKKGEIS 366
Cdd:PRK15441 7 ALHILVKEEKLALD---------LLEQIKNG-ADFGKLAKKHSICP-SGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPT 75
|
90
....*....|....*
gi 488139280 367 APVHSSFGWHLIQLV 381
Cdd:PRK15441 76 GPLHTQFGYHIIKVL 90
|
|
| prsA |
PRK02998 |
peptidylprolyl isomerase; Reviewed |
1-274 |
3.07e-03 |
|
peptidylprolyl isomerase; Reviewed
Pssm-ID: 179522 [Multi-domain] Cd Length: 283 Bit Score: 39.18 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 1 MKNWRTLILGLVICANTAFAAPQEVDKVAAVvDNGVVLQSDIDGLLQsvkmnaQQSGQQvpddsTLRHQILERLIMDNIQ 80
Cdd:PRK02998 1 MKKKKLFLGTIISCVVLALSACGSSDNVVTS-KVGNITEKELSKELR------QKYGES-----TLYQMVLSKALLDKYK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 81 lqmakkmgitITDQALDKAIAdiAAQNRMTlAQMRSRLAADGL-SYDTYREQIRKEMLTsevrnnEVRRRITILPQEVES 159
Cdd:PRK02998 69 ----------VSDEEAKKQVE--EAKDKMG-DNFKSTLEQVGLkNEDELKEKMKPEIAF------EKAIKATVTEKDVKD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 160 LAKqmgnqvsgdTELNLSHILIplpenptqqqvdQAEDLANKLVADIKGGADFGKLAIANSADSQAL-KGGQM-GWGKLQ 237
Cdd:PRK02998 130 NYK---------PEMKVSHILV------------KDEKTAKEVKEKVNNGEDFAALAKQYSEDTGSKeQGGEIsGFAPGQ 188
|
250 260 270
....*....|....*....|....*....|....*..
gi 488139280 238 ELPSlFAERLQSAHKGEIVGPIRSGVGFHILKVNDMR 274
Cdd:PRK02998 189 TVKE-FEEAAYKLDAGQVSEPVKTTYGYHIIKVTDKK 224
|
|
| prsA |
PRK03002 |
peptidylprolyl isomerase PrsA; |
173-274 |
3.25e-03 |
|
peptidylprolyl isomerase PrsA;
Pssm-ID: 101162 [Multi-domain] Cd Length: 285 Bit Score: 39.15 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139280 173 ELNLSHILIplpenptqqqvdQAEDLANKLVADIKGGADFGKLAIANSAD-SQALKGGQMGWGKLQELPSLFAERLQSAH 251
Cdd:PRK03002 136 EIKASHILV------------SDENEAKEIKKKLDAGASFEELAKQESQDlLSKEKGGDLGYFNSGRMAPEFETAAYKLK 203
|
90 100
....*....|....*....|...
gi 488139280 252 KGEIVGPIRSGVGFHILKVNDMR 274
Cdd:PRK03002 204 VGQISNPVKSPNGYHIIKLTDKK 226
|
|
| |
