NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|119508439|ref|NP_079688|]
View 

pyrroline-5-carboxylate reductase 3 [Mus musculus]

Protein Classification

pyrroline-5-carboxylate reductase family protein( domain architecture ID 11417420)

pyrroline-5-carboxylate reductase family protein similar to pyrroline-5-carboxylate reductase that catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline

CATH:  1.10.3730.10|3.40.50.720
EC:  1.-.-.-
Gene Ontology:  GO:0004735|GO:0055129

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 8-273 6.90e-103

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


:

Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 300.44  E-value: 6.90e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439   8 PRRVGFVGAGRMAEAIARGLIQAGkVEAKQVLASAPTDNNLCHFRA-LGCQTTHSNHEVLQNCPLVIFATKPQVLPTVLA 86
Cdd:COG0345    2 SMKIGFIGAGNMGSAIIKGLLKSG-VPPEDIIVSDRSPERLEALAErYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  87 EVAPIVTTEHIIVSVAAGISLSTMEGLLPPNTRVLRVSPNLPCVVQEGAMVMARGHHAGNDDAELLQNLLEACGQCIEVP 166
Cdd:COG0345   81 ELAPLLDPDKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439 167 ESYVDIHTGLSGSGVAFVCTFSEALAEGAIKMGMPSGLAHRIAAQTLLGTAKMLQQEGKHPAQLRTDVLTPAGTTIHGLH 246
Cdd:COG0345  161 EELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTIAGLK 240

                        250       260
                 ....*....|....*....|....*..
gi 119508439 247 ALERGGFRAATMSAVEAATCRAKELSK 273
Cdd:COG0345  241 VLEEGGLRAAVIEAVEAAAERSKELGK 267
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 8-273 6.90e-103

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 300.44  E-value: 6.90e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439   8 PRRVGFVGAGRMAEAIARGLIQAGkVEAKQVLASAPTDNNLCHFRA-LGCQTTHSNHEVLQNCPLVIFATKPQVLPTVLA 86
Cdd:COG0345    2 SMKIGFIGAGNMGSAIIKGLLKSG-VPPEDIIVSDRSPERLEALAErYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  87 EVAPIVTTEHIIVSVAAGISLSTMEGLLPPNTRVLRVSPNLPCVVQEGAMVMARGHHAGNDDAELLQNLLEACGQCIEVP 166
Cdd:COG0345   81 ELAPLLDPDKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439 167 ESYVDIHTGLSGSGVAFVCTFSEALAEGAIKMGMPSGLAHRIAAQTLLGTAKMLQQEGKHPAQLRTDVLTPAGTTIHGLH 246
Cdd:COG0345  161 EELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTIAGLK 240

                        250       260
                 ....*....|....*....|....*..
gi 119508439 247 ALERGGFRAATMSAVEAATCRAKELSK 273
Cdd:COG0345  241 VLEEGGLRAAVIEAVEAAAERSKELGK 267
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 10-273 4.00e-95

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 280.69  E-value: 4.00e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  10 RVGFVGAGRMAEAIARGLIQAGKVEAKQVLASAPTDNNLC-HFRALGCQTTHSNHEVLQNCPLVIFATKPQVLPTVLAEV 88
Cdd:PLN02688   2 RVGFIGAGKMAEAIARGLVASGVVPPSRISTADDSNPARRdVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLTEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  89 APIVTTEHIIVSVAAGISLSTMEGLLPPNtRVLRVSPNLPCVVQEGAMVMARGHHAGNDDAELLQNLLEACGQCIEVPES 168
Cdd:PLN02688  82 RPLLSKDKLLVSVAAGITLADLQEWAGGR-RVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIWVVDEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439 169 YVDIHTGLSGSGVAFVCTFSEALAEGAIKMGMPSGLAHRIAAQTLLGTAKMLQQEGKHPAQLRTDVLTPAGTTIHGLHAL 248
Cdd:PLN02688 161 LLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIAGVHEL 240

                        250       260
                 ....*....|....*....|....*
gi 119508439 249 ERGGFRAATMSAVEAATCRAKELSK 273
Cdd:PLN02688 241 EKGGFRAALMNAVVAAAKRSRELSK 265
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 27-270 2.25e-75

pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline biosynthesis. Among the four paralogs in Bacillus subtilis (proG, proH, proI, and comER), ComER is the most divergent and does not prevent proline auxotrophy from mutation of the other three. It is excluded from the seed and scores between the trusted and noise cutoffs. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 272911 [Multi-domain]  Cd Length: 245  Bit Score: 229.84  E-value: 2.25e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439   27 LIQAGKVEAKQVLASAPTDNNL-CHFRALGCQTTHSNHEVLQNCPLVIFATKPQVLPTVLAEVAPIVTTEHIIVSVAAGI 105
Cdd:TIGR00112   1 LLKAGALAPYDIYVINRSPEKLaALAKELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  106 SLSTMEGLLPPNTRVLRVSPNLPCVVQEGAMVMARGHHAGNDDAELLQNLLEACGQCIEVPESYVDIHTGLSGSGVAFVC 185
Cdd:TIGR00112  81 TLEKLSQLLGGTRRVVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  186 TFSEALAEGAIKMGMPSGLAHRIAAQTLLGTAKMLQQEGKHPAQLRTDVLTPAGTTIHGLHALERGGFRAATMSAVEAAT 265
Cdd:TIGR00112 161 LFIEALADAGVKQGLPRELALELAAQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAV 240


                  ....*
gi 119508439  266 CRAKE 270
Cdd:TIGR00112 241 RRSRE 245
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 167-270 2.30e-42

Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of two domains, an N-terminal catalytic domain (pfam03807) and a C-terminal dimerization domain. This is the dimerization domain.


Pssm-ID: 464294 [Multi-domain]  Cd Length: 104  Bit Score: 140.61  E-value: 2.30e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  167 ESYVDIHTGLSGSGVAFVCTFSEALAEGAIKMGMPSGLAHRIAAQTLLGTAKMLQQEGKHPAQLRTDVLTPAGTTIHGLH 246
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80

                          90       100
                  ....*....|....*....|....
gi 119508439  247 ALERGGFRAATMSAVEAATCRAKE 270
Cdd:pfam14748  81 VLEEGGFRGAVIEAVEAATKRAKE 104
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 8-273 6.90e-103

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 300.44  E-value: 6.90e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439   8 PRRVGFVGAGRMAEAIARGLIQAGkVEAKQVLASAPTDNNLCHFRA-LGCQTTHSNHEVLQNCPLVIFATKPQVLPTVLA 86
Cdd:COG0345    2 SMKIGFIGAGNMGSAIIKGLLKSG-VPPEDIIVSDRSPERLEALAErYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  87 EVAPIVTTEHIIVSVAAGISLSTMEGLLPPNTRVLRVSPNLPCVVQEGAMVMARGHHAGNDDAELLQNLLEACGQCIEVP 166
Cdd:COG0345   81 ELAPLLDPDKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439 167 ESYVDIHTGLSGSGVAFVCTFSEALAEGAIKMGMPSGLAHRIAAQTLLGTAKMLQQEGKHPAQLRTDVLTPAGTTIHGLH 246
Cdd:COG0345  161 EELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTIAGLK 240

                        250       260
                 ....*....|....*....|....*..
gi 119508439 247 ALERGGFRAATMSAVEAATCRAKELSK 273
Cdd:COG0345  241 VLEEGGLRAAVIEAVEAAAERSKELGK 267
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 10-273 4.00e-95

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 280.69  E-value: 4.00e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  10 RVGFVGAGRMAEAIARGLIQAGKVEAKQVLASAPTDNNLC-HFRALGCQTTHSNHEVLQNCPLVIFATKPQVLPTVLAEV 88
Cdd:PLN02688   2 RVGFIGAGKMAEAIARGLVASGVVPPSRISTADDSNPARRdVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLTEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  89 APIVTTEHIIVSVAAGISLSTMEGLLPPNtRVLRVSPNLPCVVQEGAMVMARGHHAGNDDAELLQNLLEACGQCIEVPES 168
Cdd:PLN02688  82 RPLLSKDKLLVSVAAGITLADLQEWAGGR-RVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIWVVDEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439 169 YVDIHTGLSGSGVAFVCTFSEALAEGAIKMGMPSGLAHRIAAQTLLGTAKMLQQEGKHPAQLRTDVLTPAGTTIHGLHAL 248
Cdd:PLN02688 161 LLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIAGVHEL 240

                        250       260
                 ....*....|....*....|....*
gi 119508439 249 ERGGFRAATMSAVEAATCRAKELSK 273
Cdd:PLN02688 241 EKGGFRAALMNAVVAAAKRSRELSK 265
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 9-274 6.71e-84

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 251.99  E-value: 6.71e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439   9 RRVGFVGAGRMAEAIARGLIQAGkVEAKQVLASAPTDNNLCHFRA-LGCQTTHSNHEVLQNCPLVIFATKPQVLPTVLAE 87
Cdd:PRK11880   3 KKIGFIGGGNMASAIIGGLLASG-VPAKDIIVSDPSPEKRAALAEeYGVRAATDNQEAAQEADVVVLAVKPQVMEEVLSE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  88 VAPIVTTehIIVSVAAGISLSTMEGLLPPNTRVLRVSPNLPCVVQEGAMVMARGHHAGNDDAELLQNLLEACGQCIEVP- 166
Cdd:PRK11880  82 LKGQLDK--LVVSIAAGVTLARLERLLGADLPVVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGKVVWVDd 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439 167 ESYVDIHTGLSGSGVAFVCTFSEALAEGAIKMGMPSGLAHRIAAQTLLGTAKMLQQEGKHPAQLRTDVLTPAGTTIHGLH 246
Cdd:PRK11880 160 EKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESGEHPAELRDNVTSPGGTTIAALR 239

                        250       260
                 ....*....|....*....|....*...
gi 119508439 247 ALERGGFRAATMSAVEAATCRAKELSKK 274
Cdd:PRK11880 240 VLEEKGLRAAVIEAVQAAAKRSKELGKE 267
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 27-270 2.25e-75

pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline biosynthesis. Among the four paralogs in Bacillus subtilis (proG, proH, proI, and comER), ComER is the most divergent and does not prevent proline auxotrophy from mutation of the other three. It is excluded from the seed and scores between the trusted and noise cutoffs. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 272911 [Multi-domain]  Cd Length: 245  Bit Score: 229.84  E-value: 2.25e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439   27 LIQAGKVEAKQVLASAPTDNNL-CHFRALGCQTTHSNHEVLQNCPLVIFATKPQVLPTVLAEVAPIVTTEHIIVSVAAGI 105
Cdd:TIGR00112   1 LLKAGALAPYDIYVINRSPEKLaALAKELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  106 SLSTMEGLLPPNTRVLRVSPNLPCVVQEGAMVMARGHHAGNDDAELLQNLLEACGQCIEVPESYVDIHTGLSGSGVAFVC 185
Cdd:TIGR00112  81 TLEKLSQLLGGTRRVVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  186 TFSEALAEGAIKMGMPSGLAHRIAAQTLLGTAKMLQQEGKHPAQLRTDVLTPAGTTIHGLHALERGGFRAATMSAVEAAT 265
Cdd:TIGR00112 161 LFIEALADAGVKQGLPRELALELAAQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAV 240


                  ....*
gi 119508439  266 CRAKE 270
Cdd:TIGR00112 241 RRSRE 245
PTZ00431 PTZ00431
pyrroline carboxylate reductase; Provisional
 10-271 1.00e-49

pyrroline carboxylate reductase; Provisional


Pssm-ID: 173621 [Multi-domain]  Cd Length: 260  Bit Score: 164.74  E-value: 1.00e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  10 RVGFVGAGRMAEAIARGLIQAGKVEAKQVLASAPTDNNLChFRALgcqttHSNHEVLQNCPLVIFATKPQVLPTVLAEVA 89
Cdd:PTZ00431   5 RVGFIGLGKMGSALAYGIENSNIIGKENIYYHTPSKKNTP-FVYL-----QSNEELAKTCDIIVLAVKPDLAGKVLLEIK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  90 PIVTTEhIIVSVAAGISLSTMEGLLPPNTRVLRVSPNLPCVVQEGAMVMARGHHAGNDDAELLQNLLEACGQCIEVPESY 169
Cdd:PTZ00431  79 PYLGSK-LLISICGGLNLKTLEEMVGVEAKIVRVMPNTPSLVGQGSLVFCANNNVDSTDKKKVIDIFSACGIIQEIKEKD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439 170 VDIHTGLSGSGVAFVCTFSEALAEGAIKMGMPSGLAHRIAAQTLLGTAKMLQQEGKHPAQLRTDVLTPAGTTIHGLHALE 249
Cdd:PTZ00431 158 MDIATAISGCGPAYVFLFIESLIDAGVKNGLNRDVSKNLVLQTILGSVHMVKASDQPVQQLKDDVCSPGGITIVGLYTLE 237

                        250       260
                 ....*....|....*....|..
gi 119508439 250 RGGFRAATMSAVEAATCRAKEL 271
Cdd:PTZ00431 238 KHAFKYTVMDAVESACQKSKSM 259
PRK07679 PRK07679
pyrroline-5-carboxylate reductase; Reviewed
 9-273 2.14e-47

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 181079 [Multi-domain]  Cd Length: 279  Bit Score: 159.16  E-value: 2.14e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439   9 RRVGFVGAGRMAEAIARGLIQAGKVEAKQVLASAPTDNNLCHF--RALGCQTTHSNHEVLQNCPLVIFATKPQVLPTVLA 86
Cdd:PRK07679   4 QNISFLGAGSIAEAIIGGLLHANVVKGEQITVSNRSNETRLQElhQKYGVKGTHNKKELLTDANILFLAMKPKDVAEALI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  87 EVAPIVTTEHIIVSVAAGISLSTMEGLLPPNTRVLRVSPNLPCVVQEGAMVMARGHHAGNDDAELLQNLLEACGQCIEVP 166
Cdd:PRK07679  84 PFKEYIHNNQLIISLLAGVSTHSIRNLLQKDVPIIRAMPNTSAAILKSATAISPSKHATAEHIQTAKALFETIGLVSVVE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439 167 ESYVDIHTGLSGSGVAFVCTFSEALAEGAIKMGMPSGLAHRIAAQTLLGTAKMLQQEGKHPAQLRTDVLTPAGTTIHGLH 246
Cdd:PRK07679 164 EEDMHAVTALSGSGPAYIYYVVEAMEKAAKKIGLKEDVAKSLILQTMIGAAEMLKASEKHPSILRKEITSPGGTTEAGIE 243

                        250       260
                 ....*....|....*....|....*..
gi 119508439 247 ALERGGFRAATMSAVEAATCRAKELSK 273
Cdd:PRK07679 244 VLQEHRFQQALISCITQATQRSHNLGK 270
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 167-270 2.30e-42

Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of two domains, an N-terminal catalytic domain (pfam03807) and a C-terminal dimerization domain. This is the dimerization domain.


Pssm-ID: 464294 [Multi-domain]  Cd Length: 104  Bit Score: 140.61  E-value: 2.30e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  167 ESYVDIHTGLSGSGVAFVCTFSEALAEGAIKMGMPSGLAHRIAAQTLLGTAKMLQQEGKHPAQLRTDVLTPAGTTIHGLH 246
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80

                          90       100
                  ....*....|....*....|....
gi 119508439  247 ALERGGFRAATMSAVEAATCRAKE 270
Cdd:pfam14748  81 VLEEGGFRGAVIEAVEAATKRAKE 104
PRK06928 PRK06928
pyrroline-5-carboxylate reductase; Reviewed
 10-244 7.19e-22

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235888 [Multi-domain]  Cd Length: 277  Bit Score: 92.14  E-value: 7.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  10 RVGFVGAGRMAEAIARGLIQAGKVEAKQVLASAPTDNNlcHFRAL-----GCQTTHSNHEVLQNCPLvIFATKP--QVLP 82
Cdd:PRK06928   3 KIGFIGYGSMADMIATKLLETEVATPEEIILYSSSKNE--HFNQLydkypTVELADNEAEIFTKCDH-SFICVPplAVLP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  83 TvLAEVAPIVTTEHIIVSVAAGISLSTMEGLlPPNTRVLRVSPNLPCVVQEGAMVMARGHHAGNDDAELLQNLLEACGQC 162
Cdd:PRK06928  80 L-LKDCAPVLTPDRHVVSIAAGVSLDDLLEI-TPGLQVSRLIPSLTSAVGVGTSLVAHAETVNEANKSRLEETLSHFSHV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439 163 IEVPESYVDIHTGLSGSGVAFVCTFSEALAEGAIKMgmpSGLAHRIAAQ----TLLGTAKMLQQEGKHPAQLRTDVLTPA 238
Cdd:PRK06928 158 MTIREENMDIASNLTSSSPGFIAAIFEEFAEAAVRN---SSLSDEEAFQflnfALAGTGKLLVEEDYTFSGTIERVATKG 234


                 ....*.
gi 119508439 239 GTTIHG 244
Cdd:PRK06928 235 GITAEG 240
PRK07680 PRK07680
late competence protein ComER; Validated
 10-251 8.48e-19

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 83.48  E-value: 8.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  10 RVGFVGAGRMAEAIARGLIQAGKVEAKQVLASAPTDNNLCHF--RALGCQTTHSNHEVLQNCPLVIFATKPQVLPTVLAE 87
Cdd:PRK07680   2 NIGFIGTGNMGTILIEAFLESGAVKPSQLTITNRTPAKAYHIkeRYPGIHVAKTIEEVISQSDLIFICVKPLDIYPLLQK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  88 VAPIVTTEHIIVSVAAGISLSTMEGLLPpnTRVLRVSPNLPCVVQEGAMVMARGHHAGNDDAELLQNLLEACGQCIEVPE 167
Cdd:PRK07680  82 LAPHLTDEHCLVSITSPISVEQLETLVP--CQVARIIPSITNRALSGASLFTFGSRCSEEDQQKLERLFSNISTPLVIEE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439 168 SYVDIHTGLSGSGVAFVCTFSEALAEGAIKM-GMPSGLAHRIAAQTLLGTAKMLQQEGKHPAQLRTDVLTPAGTTIHGLH 246
Cdd:PRK07680 160 DITRVSSDIVSCGPAFFSYLLQRFIDAAVEEtNISKEEATTLASEMLIGMGKLLEKGLYTLPTLQEKVCVKGGITGEGIK 239


                 ....*
gi 119508439 247 ALERG 251
Cdd:PRK07680 240 VLEEE 244
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
12-104 2.54e-11

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 58.78  E-value: 2.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439   12 GFVGAGRMAEAIARGLIQAGKVEAkqVLASAPTDNNLCHF-RALGCQTTH-SNHEVLQNCPLVIFATKPQVLPTVLAEVA 89
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAGPHEV--VVANSRNPEKAEELaEEYGVGATAvDNEEAAEEADVVFLAVKPEDAPDVLSELS 78

                          90
                  ....*....|....*
gi 119508439   90 PIVtTEHIIVSVAAG 104
Cdd:pfam03807  79 DLL-KGKIVISIAAG 92
PRK06476 PRK06476
pyrroline-5-carboxylate reductase; Reviewed
 10-263 5.51e-09

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235812 [Multi-domain]  Cd Length: 258  Bit Score: 55.41  E-value: 5.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  10 RVGFVGAGRMAEAIARGLIQAGKVEAKQVLA--SAPTDNNLCH-FRALgcQTTHSNHEVLQNCPLVIFATKPQVLPTVLA 86
Cdd:PRK06476   2 KIGFIGTGAITEAMVTGLLTSPADVSEIIVSprNAQIAARLAErFPKV--RIAKDNQAVVDRSDVVFLAVRPQIAEEVLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  87 EVApiVTTEHIIVSVAAGISLSTMEGLLPPNTRVLRVSPnLPCVVQEgamvmaRGHHAGNDDAELLQNLLEACGQCIEV- 165
Cdd:PRK06476  80 ALR--FRPGQTVISVIAATDRAALLEWIGHDVKLVRAIP-LPFVAER------KGVTAIYPPDPFVAALFDALGTAVECd 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439 166 -PESYVDIHTGLSGSGVAFvcTFSEALAEGAIKMGMPSGLAHRIAAQTLLGTAKMLQQEGKHP-AQLRTDVLTPAGTTIH 243
Cdd:PRK06476 151 sEEEYDLLAAASALMATYF--GILETATGWLEEQGLKRQKARAYLAPLFASLAQDAVRSTKTDfSALSREFSTKGGLNEQ 228

                        250       260
                 ....*....|....*....|
gi 119508439 244 GLHALERGGFRAATMSAVEA 263
Cdd:PRK06476 229 VLNDFSRQGGYAALTDALDR 248
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 10-113 1.41e-04

Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 42.49  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  10 RVGFVGAGRMAEAIARGLIQAGkVEAKQVLASapTDNNLCHFRA-LGCQTTHSNHEVLQNCPLVIFATKPQVLPTVLAEV 88
Cdd:COG5495    5 KIGIIGAGRVGTALAAALRAAG-HEVVGVYSR--SPASAERAAAlLGAVPALDLEELAAEADLVLLAVPDDAIAEVAAGL 81

                         90       100
                 ....*....|....*....|....*..
gi 119508439  89 A--PIVTTEHIIVSVAAGISLSTMEGL 113
Cdd:COG5495   82 AaaGALRPGQLVVHTSGALGSDVLAPA 108
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 9-119 3.71e-04

Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440056 [Multi-domain]  Cd Length: 278  Bit Score: 41.27  E-value: 3.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439   9 RRVGFVGAGRMAEAIARGLIQAGKveAKQVLASAPTDNNLCHFRALGC--QTTHSNHEVLQNCPLVIFATKPQVLPTVLA 86
Cdd:COG0287    2 MRIAIIGLGLIGGSLALALKRAGL--AHEVVGVDRSPETLERALELGVidRAATDLEEAVADADLVVLAVPVGATIEVLA 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 119508439  87 EVAPIVTTEHIIV---SVAAGIsLSTMEGLLPPNTR 119
Cdd:COG0287   80 ELAPHLKPGAIVTdvgSVKGAV-VEAAEALLPDGVR 114
GpsA COG0240
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
 10-156 1.13e-03

Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440010 [Multi-domain]  Cd Length: 327  Bit Score: 39.63  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  10 RVGFVGAGRMAEAIArgliqagkveakQVLASAPTDNNL-CHFRAL--GCQTTHSNH-------------------EVLQ 67
Cdd:COG0240    2 KIAVLGAGSWGTALA------------KVLARNGHEVTLwGRDPEVaeEINETRENPrylpgvklpenlratsdleEALA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508439  68 NCPLVIFATKPQVLPTVLAEVAPIVTTEHIIVSVAAGISLSTMEGL-------LPPNTRVLRVS-PNLpcvvqegAMVMA 139
Cdd:COG0240   70 GADLVLLAVPSQALREVLEQLAPLLPPGAPVVSATKGIEPGTGLLMseviaeeLPGALRIAVLSgPSF-------AEEVA 142

                        170       180
                 ....*....|....*....|....
gi 119508439 140 RGHH-----AGNDD--AELLQNLL 156
Cdd:COG0240  143 RGLPtavvvASEDEevAERLQELL 166
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH