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Conserved domains on  [gi|490240515|ref|WP_004138776|]
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MULTISPECIES: nitrogen fixation protein NifM [Klebsiella]

Protein Classification

nifM_nitrog family protein( domain architecture ID 11495649)

nifM_nitrog family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
nifM_nitrog TIGR02933
nitrogen fixation protein NifM; Members of this protein family, found in a subset of ...
6-258 5.41e-128

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: 363.40  E-value: 5.41e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490240515    6 RFARQRLARSRWNRDPAALDPADTPAFEQAWQRQCHMEQTIVARVPEG--DIPAALLENIAASLAIWLDEGDFAPPERAA 83
Cdd:TIGR02933   1 RYSRWKLAHEMWNCAPGELSPDQLQQFDQAWQRQRHIEQAVVRAADEIgvVIPPSLLEEAPQALAQALDEQALDAAERRA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490240515   84 IVRHHARLELAFADIARQAPQPDLSTVQAWYLRHQTQFMRPEQRLTRHLLLTV-DNDREAVHQRILGLYRQINASRDAFA 162
Cdd:TIGR02933  81 MLAHHLRLEAQLACVCAQAPQPDDADVEAWYRRHAEQFKRPEQRLTRHLLLTVnEDDREAVRTRILAILRRLRGKPAAFA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490240515  163 PLAQRHSHCPSALEEGRLGWISRGLLYPQLETALFSLAENALSLPIASELGWHLLWCEAIRPAAPMEPQQALESARDYLW 242
Cdd:TIGR02933 161 EQAMRHSHCPTAMEGGLLGWVSRGLLYPQLDAALFQLAEGELSPPIESEIGWHLLLCEAIRPARPLTLEEALPRARDRLQ 240
                         250
                  ....*....|....*.
gi 490240515  243 QQSQQRHQRQWLEQMI 258
Cdd:TIGR02933 241 LRQQKAYQRQWLVQLI 256
 
Name Accession Description Interval E-value
nifM_nitrog TIGR02933
nitrogen fixation protein NifM; Members of this protein family, found in a subset of ...
6-258 5.41e-128

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: 363.40  E-value: 5.41e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490240515    6 RFARQRLARSRWNRDPAALDPADTPAFEQAWQRQCHMEQTIVARVPEG--DIPAALLENIAASLAIWLDEGDFAPPERAA 83
Cdd:TIGR02933   1 RYSRWKLAHEMWNCAPGELSPDQLQQFDQAWQRQRHIEQAVVRAADEIgvVIPPSLLEEAPQALAQALDEQALDAAERRA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490240515   84 IVRHHARLELAFADIARQAPQPDLSTVQAWYLRHQTQFMRPEQRLTRHLLLTV-DNDREAVHQRILGLYRQINASRDAFA 162
Cdd:TIGR02933  81 MLAHHLRLEAQLACVCAQAPQPDDADVEAWYRRHAEQFKRPEQRLTRHLLLTVnEDDREAVRTRILAILRRLRGKPAAFA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490240515  163 PLAQRHSHCPSALEEGRLGWISRGLLYPQLETALFSLAENALSLPIASELGWHLLWCEAIRPAAPMEPQQALESARDYLW 242
Cdd:TIGR02933 161 EQAMRHSHCPTAMEGGLLGWVSRGLLYPQLDAALFQLAEGELSPPIESEIGWHLLLCEAIRPARPLTLEEALPRARDRLQ 240
                         250
                  ....*....|....*.
gi 490240515  243 QQSQQRHQRQWLEQMI 258
Cdd:TIGR02933 241 LRQQKAYQRQWLVQLI 256
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
120-257 5.63e-27

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 101.96  E-value: 5.63e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490240515 120 QFMRPEQRLTRHLLLTVD--NDREAVHQRILGLYRQINASRDaFAPLAQRHSHCP-SALEEGRLGWISRGLLYPQLETAL 196
Cdd:COG0760    2 QFDSPEEVRASHILVKVPpsEDRAKAEAKAEELLAQLKAGAD-FAELAKEYSQDPgSAANGGDLGWFSRGQLVPEFEEAA 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490240515 197 FSLAENALSLPIASELGWHLLWCEAIRPAAPMEPQQALESARDYLWqqsqQRHQRQWLEQM 257
Cdd:COG0760   81 FALKPGEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQELF----QQALEAWLEEL 137
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
131-217 1.46e-19

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: 80.81  E-value: 1.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490240515  131 HLLLTVD----NDREAVHQRILGLYRQINASRDAFAPLAQRHSH-CPSALEEGRLGWISRGLLYPQLETALFSLAENALS 205
Cdd:pfam00639   1 HILIKTPeaseRDRAEAKAKAEEILEQLKSGEDSFAELARKYSDdCPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEIS 80
                          90
                  ....*....|..
gi 490240515  206 LPIASELGWHLL 217
Cdd:pfam00639  81 GPVETRFGFHII 92
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
122-217 7.73e-09

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 52.34  E-value: 7.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490240515 122 MRPEQRLTRHLLLTVDNDREAVHQRI--------------LGLYR-QINASRDAFAPLAQRHSHCPSALEEGRLGWISRG 186
Cdd:PTZ00356   1 MEGDTVRAAHLLIKHTGSRNPVSRRTgkpvtrskeeaikeLAKWReQIVSGEKTFEEIARQRSDCGSAAKGGDLGFFGRG 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 490240515 187 LLYPQLETALFSLAENALSLPIASELGWHLL 217
Cdd:PTZ00356  81 QMQKPFEDAAFALKVGEISDIVHTDSGVHII 111
 
Name Accession Description Interval E-value
nifM_nitrog TIGR02933
nitrogen fixation protein NifM; Members of this protein family, found in a subset of ...
6-258 5.41e-128

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: 363.40  E-value: 5.41e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490240515    6 RFARQRLARSRWNRDPAALDPADTPAFEQAWQRQCHMEQTIVARVPEG--DIPAALLENIAASLAIWLDEGDFAPPERAA 83
Cdd:TIGR02933   1 RYSRWKLAHEMWNCAPGELSPDQLQQFDQAWQRQRHIEQAVVRAADEIgvVIPPSLLEEAPQALAQALDEQALDAAERRA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490240515   84 IVRHHARLELAFADIARQAPQPDLSTVQAWYLRHQTQFMRPEQRLTRHLLLTV-DNDREAVHQRILGLYRQINASRDAFA 162
Cdd:TIGR02933  81 MLAHHLRLEAQLACVCAQAPQPDDADVEAWYRRHAEQFKRPEQRLTRHLLLTVnEDDREAVRTRILAILRRLRGKPAAFA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490240515  163 PLAQRHSHCPSALEEGRLGWISRGLLYPQLETALFSLAENALSLPIASELGWHLLWCEAIRPAAPMEPQQALESARDYLW 242
Cdd:TIGR02933 161 EQAMRHSHCPTAMEGGLLGWVSRGLLYPQLDAALFQLAEGELSPPIESEIGWHLLLCEAIRPARPLTLEEALPRARDRLQ 240
                         250
                  ....*....|....*.
gi 490240515  243 QQSQQRHQRQWLEQMI 258
Cdd:TIGR02933 241 LRQQKAYQRQWLVQLI 256
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
120-257 5.63e-27

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 101.96  E-value: 5.63e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490240515 120 QFMRPEQRLTRHLLLTVD--NDREAVHQRILGLYRQINASRDaFAPLAQRHSHCP-SALEEGRLGWISRGLLYPQLETAL 196
Cdd:COG0760    2 QFDSPEEVRASHILVKVPpsEDRAKAEAKAEELLAQLKAGAD-FAELAKEYSQDPgSAANGGDLGWFSRGQLVPEFEEAA 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490240515 197 FSLAENALSLPIASELGWHLLWCEAIRPAAPMEPQQALESARDYLWqqsqQRHQRQWLEQM 257
Cdd:COG0760   81 FALKPGEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQELF----QQALEAWLEEL 137
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
131-217 1.46e-19

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: 80.81  E-value: 1.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490240515  131 HLLLTVD----NDREAVHQRILGLYRQINASRDAFAPLAQRHSH-CPSALEEGRLGWISRGLLYPQLETALFSLAENALS 205
Cdd:pfam00639   1 HILIKTPeaseRDRAEAKAKAEEILEQLKSGEDSFAELARKYSDdCPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEIS 80
                          90
                  ....*....|..
gi 490240515  206 LPIASELGWHLL 217
Cdd:pfam00639  81 GPVETRFGFHII 92
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
105-239 1.02e-11

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 60.53  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490240515  105 PDLSTVQAWYLRHQTQFMRPEQRLTRHLLLTVDNDREAVHQRILGlyrqinASRDAFAPLAQRhshcpSALEEGRLGW-I 183
Cdd:pfam13145   1 VTEEELKAYYEENKDEFSTPEGRLLEILVFKDQVAADAALALLKA------GALEDFAALAKG-----EGIKAATLDIvE 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 490240515  184 SRGLLYPQLETALFSLAENALSLPIASELGWHLLWCEAIRPAAPMEpqqaLESARD 239
Cdd:pfam13145  70 SAELLPEELAKAAFALKPGEVSGPIKTGNGYYVVRVTEIKPAQPLP----FEEAKD 121
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
122-217 7.73e-09

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 52.34  E-value: 7.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490240515 122 MRPEQRLTRHLLLTVDNDREAVHQRI--------------LGLYR-QINASRDAFAPLAQRHSHCPSALEEGRLGWISRG 186
Cdd:PTZ00356   1 MEGDTVRAAHLLIKHTGSRNPVSRRTgkpvtrskeeaikeLAKWReQIVSGEKTFEEIARQRSDCGSAAKGGDLGFFGRG 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 490240515 187 LLYPQLETALFSLAENALSLPIASELGWHLL 217
Cdd:PTZ00356  81 QMQKPFEDAAFALKVGEISDIVHTDSGVHII 111
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
124-216 8.52e-09

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: 52.37  E-value: 8.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490240515  124 PEQRLTRHLLLTVDND----REAVHQRILGLYRQINASRDaFAPLAQRHSHCPSALEE-GRLGWISRGLLYPQLETALFS 198
Cdd:pfam13616  13 PDSVKASHILISYSQAvsrtEEEAKAKADSLLAALKNGAD-FAALAKTYSDDPASKNNgGDLGWFTKGQMVKEFEDAVFS 91
                          90
                  ....*....|....*...
gi 490240515  199 LAENALSLPIASELGWHL 216
Cdd:pfam13616  92 LKVGEISGVVKTQFGFHI 109
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
130-217 1.25e-07

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 52.05  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490240515 130 RHLLLT---VDNDREAvHQRILGLYRQINASRDAFAPLAQRHSHCP-SALEEGRLGWISRGLLYPQLETALFSLAENALS 205
Cdd:PRK10770 270 RHILLKpspIMTDEQA-RAKLEQIAADIKSGKTTFAAAAKEFSQDPgSANQGGDLGWATPDIFDPAFRDALMRLNKGQIS 348
                         90
                 ....*....|..
gi 490240515 206 LPIASELGWHLL 217
Cdd:PRK10770 349 APVHSSFGWHLI 360
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
148-217 1.80e-06

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 45.40  E-value: 1.80e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490240515 148 LGLYRQINASRDaFAPLAQRHSHCPSALEEGRLGWISRGLLYPQLETALFSLAENALSLPIASELGWHLL 217
Cdd:PRK15441  19 LDLLEQIKNGAD-FGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGYHII 87
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
110-225 9.05e-05

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 43.46  E-value: 9.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490240515 110 VQAWYLRHQTQFMRPEQRltRHLLLTVDNDREAvhQRILGlyrQINASRDaFAPLAQRHSHCP-SALEEGRLGWISRGLL 188
Cdd:PRK10788 254 IQAYYDQHQDQFTQPERK--RYSIIQTKTEAEA--KAVLD---ELKKGAD-FATLAKEKSTDIiSARNGGDLGWLEPATT 325
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 490240515 189 YPQLETAlfSLAENA-LSLPIASELGWHLLWCEAIRPA 225
Cdd:PRK10788 326 PDELKNA--GLKEKGqLSGVIKSSVGFLIVRLDDIQPA 361
prsA PRK03002
peptidylprolyl isomerase PrsA;
123-217 6.44e-04

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 40.30  E-value: 6.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490240515 123 RPEQRLTrHLLltVDNDREAvhqrilglyRQINASRDA---FAPLAQRHSHCPSALEEG-RLGWISRGLLYPQLETALFS 198
Cdd:PRK03002 134 KPEIKAS-HIL--VSDENEA---------KEIKKKLDAgasFEELAKQESQDLLSKEKGgDLGYFNSGRMAPEFETAAYK 201
                         90
                 ....*....|....*....
gi 490240515 199 LAENALSLPIASELGWHLL 217
Cdd:PRK03002 202 LKVGQISNPVKSPNGYHII 220
 
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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