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Conserved domains on  [gi|1958788675|ref|XP_038934748|]
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pyrroline-5-carboxylate reductase 3 isoform X1 [Rattus norvegicus]

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

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List of domain hits

 Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 8-288 2.67e-95

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: 281.57  E-value: 2.67e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675   8 PRRVGFVGAGRMAEAIAQGLIRAGkVEAKQVLASAPTDKNLCHFRA-LGCQTTHSNHEVLQNCPLVIFATKPQVLPAVLA 86
Cdd:COG0345     2 SMKIGFIGAGNMGSAIIKGLLKSG-VPPEDIIVSDRSPERLEALAErYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675  87 EVAPVVTTEHIIVSVAAGISLSSMEEApslrlpdtelssvqlLPPKTRVLRVSPNLPCVVQEGAMVMTRGHHAGNEDAKL 166
Cdd:COG0345    81 ELAPLLDPDKLVISIAAGVTLATLEEA---------------LGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDREL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675 167 LQNLLEACGQCIEVPESYVDIHTGLSGSGVAFVCTFSEALAEGAIKMGMPSDLAHRIAAQTLLGTAKMLQQEGKHPAQLR 246
Cdd:COG0345   146 VEALFSAVGKVVWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELR 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1958788675 247 TDVLTPAGTTIHGLHALEQGGFRAAAMSAVEAATCRAKELSK 288
Cdd:COG0345   226 DRVTSPGGTTIAGLKVLEEGGLRAAVIEAVEAAAERSKELGK 267
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 8-288 2.67e-95

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: 281.57  E-value: 2.67e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675   8 PRRVGFVGAGRMAEAIAQGLIRAGkVEAKQVLASAPTDKNLCHFRA-LGCQTTHSNHEVLQNCPLVIFATKPQVLPAVLA 86
Cdd:COG0345     2 SMKIGFIGAGNMGSAIIKGLLKSG-VPPEDIIVSDRSPERLEALAErYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675  87 EVAPVVTTEHIIVSVAAGISLSSMEEApslrlpdtelssvqlLPPKTRVLRVSPNLPCVVQEGAMVMTRGHHAGNEDAKL 166
Cdd:COG0345    81 ELAPLLDPDKLVISIAAGVTLATLEEA---------------LGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDREL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675 167 LQNLLEACGQCIEVPESYVDIHTGLSGSGVAFVCTFSEALAEGAIKMGMPSDLAHRIAAQTLLGTAKMLQQEGKHPAQLR 246
Cdd:COG0345   146 VEALFSAVGKVVWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELR 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1958788675 247 TDVLTPAGTTIHGLHALEQGGFRAAAMSAVEAATCRAKELSK 288
Cdd:COG0345   226 DRVTSPGGTTIAGLKVLEEGGLRAAVIEAVEAAAERSKELGK 267
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 10-288 2.05e-88

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 264.13  E-value: 2.05e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675  10 RVGFVGAGRMAEAIAQGLIRAGKVEAKQVLASAPTDKNLC-HFRALGCQTTHSNHEVLQNCPLVIFATKPQVLPAVLAEV 88
Cdd:PLN02688    2 RVGFIGAGKMAEAIARGLVASGVVPPSRISTADDSNPARRdVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLTEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675  89 APVVTTEHIIVSVAAGISLSSMEEAPslrlpdtelssvqllpPKTRVLRVSPNLPCVVQEGAMVMTRGHHAGNEDAKLLQ 168
Cdd:PLN02688   82 RPLLSKDKLLVSVAAGITLADLQEWA----------------GGRRVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675 169 NLLEACGQCIEVPESYVDIHTGLSGSGVAFVCTFSEALAEGAIKMGMPSDLAHRIAAQTLLGTAKMLQQEGKHPAQLRTD 248
Cdd:PLN02688  146 TLFGAVGKIWVVDEKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDM 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958788675 249 VLTPAGTTIHGLHALEQGGFRAAAMSAVEAATCRAKELSK 288
Cdd:PLN02688  226 VTSPGGTTIAGVHELEKGGFRAALMNAVVAAAKRSRELSK 265
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 27-285 5.68e-69

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: 214.05  E-value: 5.68e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675  27 LIRAGKVEAKQVLASAP-TDKNLCHFRALGCQTTHSNHEVLQNCPLVIFATKPQVLPAVLAEVAPVVTTEHIIVSVAAGI 105
Cdd:TIGR00112   1 LLKAGALAPYDIYVINRsPEKLAALAKELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675 106 SLSSMEeapslrlpdtelssvQLLPPKTRVLRVSPNLPCVVQEGAMVMTRGHHAGNEDAKLLQNLLEACGQCIEVPESYV 185
Cdd:TIGR00112  81 TLEKLS---------------QLLGGTRRVVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALM 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675 186 DIHTGLSGSGVAFVCTFSEALAEGAIKMGMPSDLAHRIAAQTLLGTAKMLQQEGKHPAQLRTDVLTPAGTTIHGLHALEQ 265
Cdd:TIGR00112 146 DAVTALSGSGPAYVFLFIEALADAGVKQGLPRELALELAAQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEE 225

                         250       260
                  ....*....|....*....|
gi 1958788675 266 GGFRAAAMSAVEAATCRAKE 285
Cdd:TIGR00112 226 KGVRGAVIEAIEAAVRRSRE 245
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 182-269 4.07e-37

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: 127.51  E-value: 4.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675 182 ESYVDIHTGLSGSGVAFVCTFSEALAEGAIKMGMPSDLAHRIAAQTLLGTAKMLQQEGKHPAQLRTDVLTPAGTTIHGLH 261
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80


                  ....*...
gi 1958788675 262 ALEQGGFR 269
Cdd:pfam14748  81 VLEEGGFR 88
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 8-288 2.67e-95

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: 281.57  E-value: 2.67e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675   8 PRRVGFVGAGRMAEAIAQGLIRAGkVEAKQVLASAPTDKNLCHFRA-LGCQTTHSNHEVLQNCPLVIFATKPQVLPAVLA 86
Cdd:COG0345     2 SMKIGFIGAGNMGSAIIKGLLKSG-VPPEDIIVSDRSPERLEALAErYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675  87 EVAPVVTTEHIIVSVAAGISLSSMEEApslrlpdtelssvqlLPPKTRVLRVSPNLPCVVQEGAMVMTRGHHAGNEDAKL 166
Cdd:COG0345    81 ELAPLLDPDKLVISIAAGVTLATLEEA---------------LGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDREL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675 167 LQNLLEACGQCIEVPESYVDIHTGLSGSGVAFVCTFSEALAEGAIKMGMPSDLAHRIAAQTLLGTAKMLQQEGKHPAQLR 246
Cdd:COG0345   146 VEALFSAVGKVVWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELR 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1958788675 247 TDVLTPAGTTIHGLHALEQGGFRAAAMSAVEAATCRAKELSK 288
Cdd:COG0345   226 DRVTSPGGTTIAGLKVLEEGGLRAAVIEAVEAAAERSKELGK 267
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 10-288 2.05e-88

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 264.13  E-value: 2.05e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675  10 RVGFVGAGRMAEAIAQGLIRAGKVEAKQVLASAPTDKNLC-HFRALGCQTTHSNHEVLQNCPLVIFATKPQVLPAVLAEV 88
Cdd:PLN02688    2 RVGFIGAGKMAEAIARGLVASGVVPPSRISTADDSNPARRdVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLTEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675  89 APVVTTEHIIVSVAAGISLSSMEEAPslrlpdtelssvqllpPKTRVLRVSPNLPCVVQEGAMVMTRGHHAGNEDAKLLQ 168
Cdd:PLN02688   82 RPLLSKDKLLVSVAAGITLADLQEWA----------------GGRRVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675 169 NLLEACGQCIEVPESYVDIHTGLSGSGVAFVCTFSEALAEGAIKMGMPSDLAHRIAAQTLLGTAKMLQQEGKHPAQLRTD 248
Cdd:PLN02688  146 TLFGAVGKIWVVDEKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDM 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958788675 249 VLTPAGTTIHGLHALEQGGFRAAAMSAVEAATCRAKELSK 288
Cdd:PLN02688  226 VTSPGGTTIAGVHELEKGGFRAALMNAVVAAAKRSRELSK 265
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 9-289 3.84e-76

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 233.11  E-value: 3.84e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675   9 RRVGFVGAGRMAEAIAQGLIRAGkVEAKQVLASAPTDKNLCHFRA-LGCQTTHSNHEVLQNCPLVIFATKPQVLPAVLAE 87
Cdd:PRK11880    3 KKIGFIGGGNMASAIIGGLLASG-VPAKDIIVSDPSPEKRAALAEeYGVRAATDNQEAAQEADVVVLAVKPQVMEEVLSE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675  88 VAPVVTTehIIVSVAAGISLSSMEEapslrlpdtelssvqLLPPKTRVLRVSPNLPCVVQEGAMVMTRGHHAGNEDAKLL 167
Cdd:PRK11880   82 LKGQLDK--LVVSIAAGVTLARLER---------------LLGADLPVVRAMPNTPALVGAGMTALTANALVSAEDRELV 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675 168 QNLLEACGQCIEVP-ESYVDIHTGLSGSGVAFVCTFSEALAEGAIKMGMPSDLAHRIAAQTLLGTAKMLQQEGKHPAQLR 246
Cdd:PRK11880  145 ENLLSAFGKVVWVDdEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESGEHPAELR 224

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1958788675 247 TDVLTPAGTTIHGLHALEQGGFRAAAMSAVEAATCRAKELSKK 289
Cdd:PRK11880  225 DNVTSPGGTTIAALRVLEEKGLRAAVIEAVQAAAKRSKELGKE 267
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 27-285 5.68e-69

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: 214.05  E-value: 5.68e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675  27 LIRAGKVEAKQVLASAP-TDKNLCHFRALGCQTTHSNHEVLQNCPLVIFATKPQVLPAVLAEVAPVVTTEHIIVSVAAGI 105
Cdd:TIGR00112   1 LLKAGALAPYDIYVINRsPEKLAALAKELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675 106 SLSSMEeapslrlpdtelssvQLLPPKTRVLRVSPNLPCVVQEGAMVMTRGHHAGNEDAKLLQNLLEACGQCIEVPESYV 185
Cdd:TIGR00112  81 TLEKLS---------------QLLGGTRRVVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALM 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675 186 DIHTGLSGSGVAFVCTFSEALAEGAIKMGMPSDLAHRIAAQTLLGTAKMLQQEGKHPAQLRTDVLTPAGTTIHGLHALEQ 265
Cdd:TIGR00112 146 DAVTALSGSGPAYVFLFIEALADAGVKQGLPRELALELAAQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEE 225

                         250       260
                  ....*....|....*....|
gi 1958788675 266 GGFRAAAMSAVEAATCRAKE 285
Cdd:TIGR00112 226 KGVRGAVIEAIEAAVRRSRE 245
PTZ00431 PTZ00431
pyrroline carboxylate reductase; Provisional
 10-269 2.87e-44

pyrroline carboxylate reductase; Provisional


Pssm-ID: 173621 [Multi-domain]  Cd Length: 260  Bit Score: 151.26  E-value: 2.87e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675  10 RVGFVGAGRMAEAIAQGLIRAGKVEAKQVLASAPTDKNLChFRALgcqttHSNHEVLQNCPLVIFATKPQVLPAVLAEVA 89
Cdd:PTZ00431    5 RVGFIGLGKMGSALAYGIENSNIIGKENIYYHTPSKKNTP-FVYL-----QSNEELAKTCDIIVLAVKPDLAGKVLLEIK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675  90 PVVTTEhIIVSVAAGISLSSMEEapslrlpdtelssvqLLPPKTRVLRVSPNLPCVVQEGAMVMTRGHHAGNEDAKLLQN 169
Cdd:PTZ00431   79 PYLGSK-LLISICGGLNLKTLEE---------------MVGVEAKIVRVMPNTPSLVGQGSLVFCANNNVDSTDKKKVID 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675 170 LLEACGQCIEVPESYVDIHTGLSGSGVAFVCTFSEALAEGAIKMGMPSDLAHRIAAQTLLGTAKMLQQEGKHPAQLRTDV 249
Cdd:PTZ00431  143 IFSACGIIQEIKEKDMDIATAISGCGPAYVFLFIESLIDAGVKNGLNRDVSKNLVLQTILGSVHMVKASDQPVQQLKDDV 222

                         250       260
                  ....*....|....*....|
gi 1958788675 250 LTPAGTTIHGLHALEQGGFR 269
Cdd:PTZ00431  223 CSPGGITIVGLYTLEKHAFK 242
PRK07679 PRK07679
pyrroline-5-carboxylate reductase; Reviewed
 9-288 1.10e-40

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 181079 [Multi-domain]  Cd Length: 279  Bit Score: 142.22  E-value: 1.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675   9 RRVGFVGAGRMAEAIAQGLIRAGKVEAKQVLASAPTDKNLCHF--RALGCQTTHSNHEVLQNCPLVIFATKPQVLPAVLA 86
Cdd:PRK07679    4 QNISFLGAGSIAEAIIGGLLHANVVKGEQITVSNRSNETRLQElhQKYGVKGTHNKKELLTDANILFLAMKPKDVAEALI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675  87 EVAPVVTTEHIIVSVAAGISLSSMEeapslrlpdtelssvQLLPPKTRVLRVSPNLPCVVQEGAMVMTRGHHAGNEDAKL 166
Cdd:PRK07679   84 PFKEYIHNNQLIISLLAGVSTHSIR---------------NLLQKDVPIIRAMPNTSAAILKSATAISPSKHATAEHIQT 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675 167 LQNLLEACGQCIEVPESyvDIH--TGLSGSGVAFVCTFSEALAEGAIKMGMPSDLAHRIAAQTLLGTAKMLQQEGKHPAQ 244
Cdd:PRK07679  149 AKALFETIGLVSVVEEE--DMHavTALSGSGPAYIYYVVEAMEKAAKKIGLKEDVAKSLILQTMIGAAEMLKASEKHPSI 226

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958788675 245 LRTDVLTPAGTTIHGLHALEQGGFRAAAMSAVEAATCRAKELSK 288
Cdd:PRK07679  227 LRKEITSPGGTTEAGIEVLQEHRFQQALISCITQATQRSHNLGK 270
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 182-269 4.07e-37

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: 127.51  E-value: 4.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675 182 ESYVDIHTGLSGSGVAFVCTFSEALAEGAIKMGMPSDLAHRIAAQTLLGTAKMLQQEGKHPAQLRTDVLTPAGTTIHGLH 261
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80


                  ....*...
gi 1958788675 262 ALEQGGFR 269
Cdd:pfam14748  81 VLEEGGFR 88
PRK06928 PRK06928
pyrroline-5-carboxylate reductase; Reviewed
 10-259 7.29e-20

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235888 [Multi-domain]  Cd Length: 277  Bit Score: 86.75  E-value: 7.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675  10 RVGFVGAGRMAEAIAQGLIRAGKVEAKQVLASAPTDKNlcHFRAL-----GCQTTHSNHEVLQNCPLvIFATKP--QVLP 82
Cdd:PRK06928    3 KIGFIGYGSMADMIATKLLETEVATPEEIILYSSSKNE--HFNQLydkypTVELADNEAEIFTKCDH-SFICVPplAVLP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675  83 aVLAEVAPVVTTEHIIVSVAAGISLSSMEEAPslrlpdtelssvqllpPKTRVLRVSPNLPCVVQEGAMVMTRGHHAGNE 162
Cdd:PRK06928   80 -LLKDCAPVLTPDRHVVSIAAGVSLDDLLEIT----------------PGLQVSRLIPSLTSAVGVGTSLVAHAETVNEA 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675 163 DAKLLQNLLEACGQCIEVPESYVDIHTGLSGSGVAFVCTFSEALAEGAIKMGMPSDL-AHRIAAQTLLGTAKMLQQEGKH 241
Cdd:PRK06928  143 NKSRLEETLSHFSHVMTIREENMDIASNLTSSSPGFIAAIFEEFAEAAVRNSSLSDEeAFQFLNFALAGTGKLLVEEDYT 222

                         250
                  ....*....|....*...
gi 1958788675 242 PAQLRTDVLTPAGTTIHG 259
Cdd:PRK06928  223 FSGTIERVATKGGITAEG 240
PRK07680 PRK07680
late competence protein ComER; Validated
 10-266 1.12e-19

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 86.18  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675  10 RVGFVGAGRMAEAIAQGLIRAGKVEAKQVLASAPTDKNLCHF--RALGCQTTHSNHEVLQNCPLVIFATKPQVLPAVLAE 87
Cdd:PRK07680    2 NIGFIGTGNMGTILIEAFLESGAVKPSQLTITNRTPAKAYHIkeRYPGIHVAKTIEEVISQSDLIFICVKPLDIYPLLQK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675  88 VAPVVTTEHIIVSVAAGISLSSMEEApslrlpdtelssvqlLPPKtrVLRVSPNLPCVVQEGAMVMTRGHHAGNEDAKLL 167
Cdd:PRK07680   82 LAPHLTDEHCLVSITSPISVEQLETL---------------VPCQ--VARIIPSITNRALSGASLFTFGSRCSEEDQQKL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675 168 QNLLEACGQCIEVPESYVDIHTGLSGSGVAFVCTFSEALAEGAIKM-GMPSDLAHRIAAQTLLGTAKMLQQEGKHPAQLR 246
Cdd:PRK07680  145 ERLFSNISTPLVIEEDITRVSSDIVSCGPAFFSYLLQRFIDAAVEEtNISKEEATTLASEMLIGMGKLLEKGLYTLPTLQ 224

                         250       260
                  ....*....|....*....|
gi 1958788675 247 TDVLTPAGTTIHGLHALEQG 266
Cdd:PRK07680  225 EKVCVKGGITGEGIKVLEEE 244
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
12-104 1.31e-11

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 59.55  E-value: 1.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675  12 GFVGAGRMAEAIAQGLIRAGKVEAkqVLASAPTDKNLCHF-RALGCQTTH-SNHEVLQNCPLVIFATKPQVLPAVLAEVA 89
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAGPHEV--VVANSRNPEKAEELaEEYGVGATAvDNEEAAEEADVVFLAVKPEDAPDVLSELS 78

                          90
                  ....*....|....*
gi 1958788675  90 PVVtTEHIIVSVAAG 104
Cdd:pfam03807  79 DLL-KGKIVISIAAG 92
GpsA COG0240
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
 10-135 1.01e-04

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: 43.10  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675  10 RVGFVGAGRMAEAIAQGLIRAG-KV-----EAKQV------------LASAPTDKNLchfralgcQTTHSNHEVLQNCPL 71
Cdd:COG0240     2 KIAVLGAGSWGTALAKVLARNGhEVtlwgrDPEVAeeinetrenpryLPGVKLPENL--------RATSDLEEALAGADL 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958788675  72 VIFATKPQVLPAVLAEVAPVVTTEHIIVSVAAGIslssmeEAPSLRLPdtelSSV--QLLPPKTRV 135
Cdd:COG0240    74 VLLAVPSQALREVLEQLAPLLPPGAPVVSATKGI------EPGTGLLM----SEViaEELPGALRI 129
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 10-99 1.02e-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: 42.88  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675  10 RVGFVGAGRMAEAIAQGLIRAGkVEAKQVLASapTDKNLCHFRA-LGCQTTHSNHEVLQNCPLVIFATKPQVLPAVLAEV 88
Cdd:COG5495     5 KIGIIGAGRVGTALAAALRAAG-HEVVGVYSR--SPASAERAAAlLGAVPALDLEELAAEADLVLLAVPDDAIAEVAAGL 81

                          90
                  ....*....|...
gi 1958788675  89 A--PVVTTEHIIV 99
Cdd:COG5495    82 AaaGALRPGQLVV 94
PRK06476 PRK06476
pyrroline-5-carboxylate reductase; Reviewed
 10-269 4.96e-04

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235812 [Multi-domain]  Cd Length: 258  Bit Score: 40.77  E-value: 4.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675  10 RVGFVGAGRMAEAIAQGLIRAGKVEAKQVLA--SAPTDKNLCH-FRALgcQTTHSNHEVLQNCPLVIFATKPQVLPAVLA 86
Cdd:PRK06476    2 KIGFIGTGAITEAMVTGLLTSPADVSEIIVSprNAQIAARLAErFPKV--RIAKDNQAVVDRSDVVFLAVRPQIAEEVLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675  87 EVApvVTTEHIIVSVAAGISLSSMEEapslrlpdtelssvqLLPPKTRVLRVSPnLPCVVQEgamvmtRGHHAGNEDAKL 166
Cdd:PRK06476   80 ALR--FRPGQTVISVIAATDRAALLE---------------WIGHDVKLVRAIP-LPFVAER------KGVTAIYPPDPF 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675 167 LQNLLEACGQCIEV--PESYVDIHTGLSGSGVAFvcTFSEALAEGAIKMGMPSDLAHRIAAQTLLGTAKMLQQEGKHP-A 243
Cdd:PRK06476  136 VAALFDALGTAVECdsEEEYDLLAAASALMATYF--GILETATGWLEEQGLKRQKARAYLAPLFASLAQDAVRSTKTDfS 213

                         250       260
                  ....*....|....*....|....*.
gi 1958788675 244 QLRTDVLTPAGTTIHGLHALEQGGFR 269
Cdd:PRK06476  214 ALSREFSTKGGLNEQVLNDFSRQGGY 239
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
11-92 8.90e-03

Predicted dinucleotide-binding enzyme [General function prediction only];


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 36.69  E-value: 8.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958788675  11 VGFVGAGRMAEAIAQGLIRAG-KVeakqVLASAPTDKnLCHFRA-LGCQTTH-SNHEVLQNCPLVIFATKPQVLPAVLAE 87
Cdd:COG2085     1 IGIIGTGNIGSALARRLAAAGhEV----VIGSRDPEK-AAALAAeLGPGARAgTNAEAAAAADVVVLAVPYEAVPDVLES 75


                  ....*
gi 1958788675  88 VAPVV 92
Cdd:COG2085    76 LGDAL 80
 
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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