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Conserved domains on  [gi|41152299|ref|NP_957120|]
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pyrroline-5-carboxylate reductase 1a [Danio rerio]

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]; ...
 1-268 1.66e-102

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: 301.21  E-value: 1.66e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299   1 MSVGFIGAGQLAHALVKGFTAAGViATHRITASSPDTDLPTVIGlRKMGAFFTTSNKETVSKSDVLFLAVKPHIIPFVLD 80
Cdd:COG0345   3 MKIGFIGAGNMGSAIIKGLLKSGV-PPEDIIVSDRSPERLEALA-ERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299  81 EIGPDIEDRHLIVSCAAGVTISSIEKKLlqyRSAPKVIRCMTNTPVVVREGATVYATGTHAEVEDGKLLEQLMASVGYCT 160
Cdd:COG0345  81 ELAPLLDPDKLVISIAAGVTLATLEEAL---GGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVV 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299 161 EVEEDLIDAVTGLSGSGPAYAFTAVDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLESEQHPGQLKDNVASPGGATIH 240
Cdd:COG0345 158 WVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTIA 237

                       250       260
                ....*....|....*....|....*...
gi 41152299 241 ALHVMESGGFRSLLINAVEASCIRTREL 268
Cdd:COG0345 238 GLKVLEEGGLRAAVIEAVEAAAERSKEL 265
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-268 1.66e-102

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: 301.21  E-value: 1.66e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299   1 MSVGFIGAGQLAHALVKGFTAAGViATHRITASSPDTDLPTVIGlRKMGAFFTTSNKETVSKSDVLFLAVKPHIIPFVLD 80
Cdd:COG0345   3 MKIGFIGAGNMGSAIIKGLLKSGV-PPEDIIVSDRSPERLEALA-ERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299  81 EIGPDIEDRHLIVSCAAGVTISSIEKKLlqyRSAPKVIRCMTNTPVVVREGATVYATGTHAEVEDGKLLEQLMASVGYCT 160
Cdd:COG0345  81 ELAPLLDPDKLVISIAAGVTLATLEEAL---GGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVV 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299 161 EVEEDLIDAVTGLSGSGPAYAFTAVDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLESEQHPGQLKDNVASPGGATIH 240
Cdd:COG0345 158 WVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTIA 237

                       250       260
                ....*....|....*....|....*...
gi 41152299 241 ALHVMESGGFRSLLINAVEASCIRTREL 268
Cdd:COG0345 238 GLKVLEEGGLRAAVIEAVEAAAERSKEL 265
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 1-268 4.79e-97

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 287.24  E-value: 4.79e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299    1 MSVGFIGAGQLAHALVKGFTAAGVIATHRITASsPDTDLPTVIGLRKMGAFFTTSNKETVSKSDVLFLAVKPHIIPFVLD 80
Cdd:PLN02688   1 FRVGFIGAGKMAEAIARGLVASGVVPPSRISTA-DDSNPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299   81 EIGPDIEDRHLIVSCAAGVTISSIEKKLLQYRsapkVIRCMTNTPVVVREGATVYATGTHAEVEDGKLLEQLMASVGYCT 160
Cdd:PLN02688  80 ELRPLLSKDKLLVSVAAGITLADLQEWAGGRR----VVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIW 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299  161 EVEEDLIDAVTGLSGSGPAYAFTAVDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLESEQHPGQLKDNVASPGGATIH 240
Cdd:PLN02688 156 VVDEKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIA 235

                        250       260
                 ....*....|....*....|....*...
gi 41152299  241 ALHVMESGGFRSLLINAVEASCIRTREL 268
Cdd:PLN02688 236 GVHELEKGGFRAALMNAVVAAAKRSREL 263
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 47-267 1.16e-81

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: 247.56  E-value: 1.16e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299    47 KMGAFFTTSNKETVSKSDVLFLAVKPHIIPFVLDEIGPDIEDRHLIVSCAAGVTISSIEKKLLQYRsapKVIRCMTNTPV 126
Cdd:TIGR00112  28 ELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLLGGTR---RVVRVMPNTPA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299   127 VVREGATVYATGTHAEVEDGKLLEQLMASVGYCTEVEEDLIDAVTGLSGSGPAYAFTAVDALADGGVKMGLPRRLAVRLG 206
Cdd:TIGR00112 105 KVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEALADAGVKQGLPRELALELA 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41152299   207 AQALLGAAKMLLESEQHPGQLKDNVASPGGATIHALHVMESGGFRSLLINAVEASCIRTRE 267
Cdd:TIGR00112 185 AQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAVRRSRE 245
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 164-267 2.81e-49

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: 159.48  E-value: 2.81e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299   164 EDLIDAVTGLSGSGPAYAFTAVDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLESEQHPGQLKDNVASPGGATIHALH 243
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80

                          90       100
                  ....*....|....*....|....
gi 41152299   244 VMESGGFRSLLINAVEASCIRTRE 267
Cdd:pfam14748  81 VLEEGGFRGAVIEAVEAATKRAKE 104
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-268 1.66e-102

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: 301.21  E-value: 1.66e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299   1 MSVGFIGAGQLAHALVKGFTAAGViATHRITASSPDTDLPTVIGlRKMGAFFTTSNKETVSKSDVLFLAVKPHIIPFVLD 80
Cdd:COG0345   3 MKIGFIGAGNMGSAIIKGLLKSGV-PPEDIIVSDRSPERLEALA-ERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299  81 EIGPDIEDRHLIVSCAAGVTISSIEKKLlqyRSAPKVIRCMTNTPVVVREGATVYATGTHAEVEDGKLLEQLMASVGYCT 160
Cdd:COG0345  81 ELAPLLDPDKLVISIAAGVTLATLEEAL---GGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVV 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299 161 EVEEDLIDAVTGLSGSGPAYAFTAVDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLESEQHPGQLKDNVASPGGATIH 240
Cdd:COG0345 158 WVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTIA 237

                       250       260
                ....*....|....*....|....*...
gi 41152299 241 ALHVMESGGFRSLLINAVEASCIRTREL 268
Cdd:COG0345 238 GLKVLEEGGLRAAVIEAVEAAAERSKEL 265
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 1-268 4.79e-97

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 287.24  E-value: 4.79e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299    1 MSVGFIGAGQLAHALVKGFTAAGVIATHRITASsPDTDLPTVIGLRKMGAFFTTSNKETVSKSDVLFLAVKPHIIPFVLD 80
Cdd:PLN02688   1 FRVGFIGAGKMAEAIARGLVASGVVPPSRISTA-DDSNPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299   81 EIGPDIEDRHLIVSCAAGVTISSIEKKLLQYRsapkVIRCMTNTPVVVREGATVYATGTHAEVEDGKLLEQLMASVGYCT 160
Cdd:PLN02688  80 ELRPLLSKDKLLVSVAAGITLADLQEWAGGRR----VVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIW 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299  161 EVEEDLIDAVTGLSGSGPAYAFTAVDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLESEQHPGQLKDNVASPGGATIH 240
Cdd:PLN02688 156 VVDEKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIA 235

                        250       260
                 ....*....|....*....|....*...
gi 41152299  241 ALHVMESGGFRSLLINAVEASCIRTREL 268
Cdd:PLN02688 236 GVHELEKGGFRAALMNAVVAAAKRSREL 263
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 1-268 4.62e-86

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 259.31  E-value: 4.62e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299    1 MSVGFIGAGQLAHALVKGFTAAGVIAtHRITASSPDTDLPTVIgLRKMGAFFTTSNKETVSKSDVLFLAVKPHIIPFVLD 80
Cdd:PRK11880   3 KKIGFIGGGNMASAIIGGLLASGVPA-KDIIVSDPSPEKRAAL-AEEYGVRAATDNQEAAQEADVVVLAVKPQVMEEVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299   81 EIGPDIEDrhLIVSCAAGVTISSIEKKLLQYRsapKVIRCMTNTPVVVREGATVYATGTHAEVEDGKLLEQLMASVGYCT 160
Cdd:PRK11880  81 ELKGQLDK--LVVSIAAGVTLARLERLLGADL---PVVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGKVV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299  161 EVE-EDLIDAVTGLSGSGPAYAFTAVDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLESEQHPGQLKDNVASPGGATI 239
Cdd:PRK11880 156 WVDdEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESGEHPAELRDNVTSPGGTTI 235

                        250       260
                 ....*....|....*....|....*....
gi 41152299  240 HALHVMESGGFRSLLINAVEASCIRTREL 268
Cdd:PRK11880 236 AALRVLEEKGLRAAVIEAVQAAAKRSKEL 264
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 47-267 1.16e-81

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: 247.56  E-value: 1.16e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299    47 KMGAFFTTSNKETVSKSDVLFLAVKPHIIPFVLDEIGPDIEDRHLIVSCAAGVTISSIEKKLLQYRsapKVIRCMTNTPV 126
Cdd:TIGR00112  28 ELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLLGGTR---RVVRVMPNTPA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299   127 VVREGATVYATGTHAEVEDGKLLEQLMASVGYCTEVEEDLIDAVTGLSGSGPAYAFTAVDALADGGVKMGLPRRLAVRLG 206
Cdd:TIGR00112 105 KVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEALADAGVKQGLPRELALELA 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41152299   207 AQALLGAAKMLLESEQHPGQLKDNVASPGGATIHALHVMESGGFRSLLINAVEASCIRTRE 267
Cdd:TIGR00112 185 AQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAVRRSRE 245
PTZ00431 PTZ00431
pyrroline carboxylate reductase; Provisional
 1-268 3.21e-50

pyrroline carboxylate reductase; Provisional


Pssm-ID: 173621 [Multi-domain]  Cd Length: 260  Bit Score: 167.44  E-value: 3.21e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299    1 MSVGFIGAGQLAHALVKGFTAAGVIATHRITASSPdtdlptvigLRKMGAF-FTTSNKETVSKSDVLFLAVKPHIIPFVL 79
Cdd:PTZ00431   4 IRVGFIGLGKMGSALAYGIENSNIIGKENIYYHTP---------SKKNTPFvYLQSNEELAKTCDIIVLAVKPDLAGKVL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299   80 DEIGPDIEDRHLIVSCAaGVTISSIEKKLlqyRSAPKVIRCMTNTPVVVREGATVYATGTHAEVEDGKLLEQLMASVGYC 159
Cdd:PTZ00431  75 LEIKPYLGSKLLISICG-GLNLKTLEEMV---GVEAKIVRVMPNTPSLVGQGSLVFCANNNVDSTDKKKVIDIFSACGII 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299  160 TEVEEDLIDAVTGLSGSGPAYAFTAVDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLESEQHPGQLKDNVASPGGATI 239
Cdd:PTZ00431 151 QEIKEKDMDIATAISGCGPAYVFLFIESLIDAGVKNGLNRDVSKNLVLQTILGSVHMVKASDQPVQQLKDDVCSPGGITI 230

                        250       260
                 ....*....|....*....|....*....
gi 41152299  240 HALHVMESGGFRSLLINAVEASCIRTREL 268
Cdd:PTZ00431 231 VGLYTLEKHAFKYTVMDAVESACQKSKSM 259
PRK07679 PRK07679
pyrroline-5-carboxylate reductase; Reviewed
 1-268 5.86e-50

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 181079 [Multi-domain]  Cd Length: 279  Bit Score: 167.25  E-value: 5.86e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299    1 MSVGFIGAGQLAHALVKGFTAAGVIATHRITAS--SPDTDLPTVigLRKMGAFFTTSNKETVSKSDVLFLAVKPHIIPFV 78
Cdd:PRK07679   4 QNISFLGAGSIAEAIIGGLLHANVVKGEQITVSnrSNETRLQEL--HQKYGVKGTHNKKELLTDANILFLAMKPKDVAEA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299   79 LDEIGPDIEDRHLIVSCAAGVTISSIEKkLLQyRSAPkVIRCMTNTPVVVREGATVYATGTHAEVEDGKLLEQLMASVGY 158
Cdd:PRK07679  82 LIPFKEYIHNNQLIISLLAGVSTHSIRN-LLQ-KDVP-IIRAMPNTSAAILKSATAISPSKHATAEHIQTAKALFETIGL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299  159 CTEVEEDLIDAVTGLSGSGPAYAFTAVDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLESEQHPGQLKDNVASPGGAT 238
Cdd:PRK07679 159 VSVVEEEDMHAVTALSGSGPAYIYYVVEAMEKAAKKIGLKEDVAKSLILQTMIGAAEMLKASEKHPSILRKEITSPGGTT 238

                        250       260       270
                 ....*....|....*....|....*....|
gi 41152299  239 IHALHVMESGGFRSLLINAVEASCIRTREL 268
Cdd:PRK07679 239 EAGIEVLQEHRFQQALISCITQATQRSHNL 268
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 164-267 2.81e-49

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: 159.48  E-value: 2.81e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299   164 EDLIDAVTGLSGSGPAYAFTAVDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLESEQHPGQLKDNVASPGGATIHALH 243
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80

                          90       100
                  ....*....|....*....|....
gi 41152299   244 VMESGGFRSLLINAVEASCIRTRE 267
Cdd:pfam14748  81 VLEEGGFRGAVIEAVEAATKRAKE 104
PRK07680 PRK07680
late competence protein ComER; Validated
 1-277 1.04e-23

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 97.74  E-value: 1.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299    1 MSVGFIGAGQLAHALVKGFTAAGVIATHRITASSPDTDLPTVIGLRKMGAFFTTSNKETVSKSDVLFLAVKPHIIPFVLD 80
Cdd:PRK07680   1 MNIGFIGTGNMGTILIEAFLESGAVKPSQLTITNRTPAKAYHIKERYPGIHVAKTIEEVISQSDLIFICVKPLDIYPLLQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299   81 EIGPDIEDRHLIVSCAAGVTISSIEKKLLQyrSAPKVIRCMTNTpvvVREGATVYATGTHAEVEDGKLLEQLMASVGYCT 160
Cdd:PRK07680  81 KLAPHLTDEHCLVSITSPISVEQLETLVPC--QVARIIPSITNR---ALSGASLFTFGSRCSEEDQQKLERLFSNISTPL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299  161 EVEEDLIDAVTGLSGSGPAYAFTAVDALADGGVKM-GLPRRLAVRLGAQALLGAAKMLLESEQHPGQLKDNVASPGGATI 239
Cdd:PRK07680 156 VIEEDITRVSSDIVSCGPAFFSYLLQRFIDAAVEEtNISKEEATTLASEMLIGMGKLLEKGLYTLPTLQEKVCVKGGITG 235

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 41152299  240 HALHVMESGgfrsllINAVEASCIRTRELQYLADQEKI 277
Cdd:PRK07680 236 EGIKVLEEE------VGDMFHRLFQRTHEKFDEDLEKV 267
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
4-98 3.26e-16

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 72.65  E-value: 3.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299     4 GFIGAGQLAHALVKGFTAAGviATHRITASSPDTDLPTVIGLRKMGAFFTTSNKETVSKSDVLFLAVKPHIIPFVLDEIg 83
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAG--PHEVVVANSRNPEKAEELAEEYGVGATAVDNEEAAEEADVVFLAVKPEDAPDVLSEL- 77

                          90
                  ....*....|....*
gi 41152299    84 PDIEDRHLIVSCAAG 98
Cdd:pfam03807  78 SDLLKGKIVISIAAG 92
PRK06928 PRK06928
pyrroline-5-carboxylate reductase; Reviewed
 3-238 1.80e-14

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235888 [Multi-domain]  Cd Length: 277  Bit Score: 72.11  E-value: 1.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299    3 VGFIGAGQLAHALVKGFTAAGVIATHRI---TASSPD------TDLPTVIglrkmgafFTTSNKETVSKSDVLFLAVKP- 72
Cdd:PRK06928   4 IGFIGYGSMADMIATKLLETEVATPEEIilySSSKNEhfnqlyDKYPTVE--------LADNEAEIFTKCDHSFICVPPl 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299   73 HIIPfVLDEIGPDI-EDRHlIVSCAAGVTISsiekKLLQYRSAPKVIRCMTNTPVVVREGATVYATGTHAEVEDGKLLEQ 151
Cdd:PRK06928  76 AVLP-LLKDCAPVLtPDRH-VVSIAAGVSLD----DLLEITPGLQVSRLIPSLTSAVGVGTSLVAHAETVNEANKSRLEE 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299  152 LMASVGYCTEVEEDLIDAVTGLSGSGPAYAFTAVDALADGGVKMG-LPRRLAVRLGAQALLGAAKMLLESEQHPGQLKDN 230
Cdd:PRK06928 150 TLSHFSHVMTIREENMDIASNLTSSSPGFIAAIFEEFAEAAVRNSsLSDEEAFQFLNFALAGTGKLLVEEDYTFSGTIER 229


                 ....*...
gi 41152299  231 VASPGGAT 238
Cdd:PRK06928 230 VATKGGIT 237
PRK06476 PRK06476
pyrroline-5-carboxylate reductase; Reviewed
 1-266 5.58e-10

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235812 [Multi-domain]  Cd Length: 258  Bit Score: 58.87  E-value: 5.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299    1 MSVGFIGAGQLAHALVKGFTAAGVIATHRI-------TASSPDTDLPTVIglrkmgafFTTSNKETVSKSDVLFLAVKPH 73
Cdd:PRK06476   1 MKIGFIGTGAITEAMVTGLLTSPADVSEIIvsprnaqIAARLAERFPKVR--------IAKDNQAVVDRSDVVFLAVRPQ 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299   74 IIPFVLDEIgpDIEDRHLIVSCAAGVTISSIEKKLlqyRSAPKVIRCMTNTPVVVREGAT-VYAtgTHAEVEDgkLLEQL 152
Cdd:PRK06476  73 IAEEVLRAL--RFRPGQTVISVIAATDRAALLEWI---GHDVKLVRAIPLPFVAERKGVTaIYP--PDPFVAA--LFDAL 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299  153 MASVGYCTEVEEDLIDAVTGLSGSgpaYaFTAVDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLESEQHP-GQLKDNV 231
Cdd:PRK06476 144 GTAVECDSEEEYDLLAAASALMAT---Y-FGILETATGWLEEQGLKRQKARAYLAPLFASLAQDAVRSTKTDfSALSREF 219

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 41152299  232 ASPGGATIHALHVMESGGFRSLLINAVEASCIRTR 266
Cdd:PRK06476 220 STKGGLNEQVLNDFSRQGGYAALTDALDRVLRRIN 254
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 1-82 2.18e-03

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


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 39.02  E-value: 2.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152299   1 MSVGFIGAGQLAHALVKGFTAAGviatHRIT---ASSPDtdlptviGLRKMGAF----FTTSNKETVSKSDVLFLAVKPH 73
Cdd:COG5495   4 MKIGIIGAGRVGTALAAALRAAG----HEVVgvySRSPA-------SAERAAALlgavPALDLEELAAEADLVLLAVPDD 72


                ....*....
gi 41152299  74 IIPFVLDEI 82
Cdd:COG5495  73 AIAEVAAGL 81
 
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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