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Conserved domains on  [gi|1622875698|ref|XP_028691527|]
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pyrroline-5-carboxylate reductase 1, mitochondrial isoform X2 [Macaca mulatta]

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]; ...
 2-221 4.12e-91

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: 270.40  E-value: 4.12e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698   2 GVKLTPHNKEAVQHSDVLFLAVKPHIIPFILDEIGTHIEDRHIVVSCAAGVTIGSIEKKLSAfrpTPRVIRCMTNIPVVV 81
Cdd:COG0345    49 GVRVTTDNAEAAAQADVVVLAVKPQDLAEVLEELAPLLDPDKLVISIAAGVTLATLEEALGG---GAPVVRAMPNTPALV 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698  82 REGATVYATGTHAQVEDGRLLEQLLGSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQ 161
Cdd:COG0345   126 GEGVTALAAGEAVSEEDRELVEALFSAVGKVVWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQ 205

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698 162 ALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALHVLESGGFRSLLINAVEASCIRTREL 221
Cdd:COG0345   206 TVLGAAKLLLESGEHPAELRDRVTSPGGTTIAGLKVLEEGGLRAAVIEAVEAAAERSKEL 265
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 2-221 4.12e-91

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: 270.40  E-value: 4.12e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698   2 GVKLTPHNKEAVQHSDVLFLAVKPHIIPFILDEIGTHIEDRHIVVSCAAGVTIGSIEKKLSAfrpTPRVIRCMTNIPVVV 81
Cdd:COG0345    49 GVRVTTDNAEAAAQADVVVLAVKPQDLAEVLEELAPLLDPDKLVISIAAGVTLATLEEALGG---GAPVVRAMPNTPALV 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698  82 REGATVYATGTHAQVEDGRLLEQLLGSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQ 161
Cdd:COG0345   126 GEGVTALAAGEAVSEEDRELVEALFSAVGKVVWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQ 205

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698 162 ALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALHVLESGGFRSLLINAVEASCIRTREL 221
Cdd:COG0345   206 TVLGAAKLLLESGEHPAELRDRVTSPGGTTIAGLKVLEEGGLRAAVIEAVEAAAERSKEL 265
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 1-220 2.18e-86

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: 257.57  E-value: 2.18e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698   1 MGVKLTPHNKEAVQHSDVLFLAVKPHIIPFILDEIGTHIEDRHIVVSCAAGVTIGSIEKKLSAFRptpRVIRCMTNIPVV 80
Cdd:TIGR00112  29 LGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLLGGTR---RVVRVMPNTPAK 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698  81 VREGATVYATGTHAQVEDGRLLEQLLGSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGA 160
Cdd:TIGR00112 106 VGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEALADAGVKQGLPRELALELAA 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698 161 QALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALHVLESGGFRSLLINAVEASCIRTRE 220
Cdd:TIGR00112 186 QTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAVRRSRE 245
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 2-221 3.64e-81

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 245.25  E-value: 3.64e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698   2 GVKLTPHNKEAVQHSDVLFLAVKPHIIPFILDEIGTHIEDRHIVVSCAAGVTIgsieKKLSAFRPTPRVIRCMTNIPVVV 81
Cdd:PLN02688   48 GVKTAASNTEVVKSSDVIILAVKPQVVKDVLTELRPLLSKDKLLVSVAAGITL----ADLQEWAGGRRVVRVMPNTPCLV 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698  82 REGATVYATGTHAQVEDGRLLEQLLGSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQ 161
Cdd:PLN02688  124 GEAASVMSLGPAATADDRDLVATLFGAVGKIWVVDEKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQ 203

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698 162 ALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALHVLESGGFRSLLINAVEASCIRTREL 221
Cdd:PLN02688  204 TVLGAAKMVLETGKHPGQLKDMVTSPGGTTIAGVHELEKGGFRAALMNAVVAAAKRSREL 263
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 117-220 1.57e-50

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: 161.41  E-value: 1.57e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698 117 EDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALH 196
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80

                          90       100
                  ....*....|....*....|....
gi 1622875698 197 VLESGGFRSLLINAVEASCIRTRE 220
Cdd:pfam14748  81 VLEEGGFRGAVIEAVEAATKRAKE 104
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 2-221 4.12e-91

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: 270.40  E-value: 4.12e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698   2 GVKLTPHNKEAVQHSDVLFLAVKPHIIPFILDEIGTHIEDRHIVVSCAAGVTIGSIEKKLSAfrpTPRVIRCMTNIPVVV 81
Cdd:COG0345    49 GVRVTTDNAEAAAQADVVVLAVKPQDLAEVLEELAPLLDPDKLVISIAAGVTLATLEEALGG---GAPVVRAMPNTPALV 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698  82 REGATVYATGTHAQVEDGRLLEQLLGSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQ 161
Cdd:COG0345   126 GEGVTALAAGEAVSEEDRELVEALFSAVGKVVWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQ 205

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698 162 ALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALHVLESGGFRSLLINAVEASCIRTREL 221
Cdd:COG0345   206 TVLGAAKLLLESGEHPAELRDRVTSPGGTTIAGLKVLEEGGLRAAVIEAVEAAAERSKEL 265
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 1-220 2.18e-86

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: 257.57  E-value: 2.18e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698   1 MGVKLTPHNKEAVQHSDVLFLAVKPHIIPFILDEIGTHIEDRHIVVSCAAGVTIGSIEKKLSAFRptpRVIRCMTNIPVV 80
Cdd:TIGR00112  29 LGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLLGGTR---RVVRVMPNTPAK 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698  81 VREGATVYATGTHAQVEDGRLLEQLLGSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGA 160
Cdd:TIGR00112 106 VGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEALADAGVKQGLPRELALELAA 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698 161 QALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALHVLESGGFRSLLINAVEASCIRTRE 220
Cdd:TIGR00112 186 QTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAVRRSRE 245
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 2-221 3.64e-81

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 245.25  E-value: 3.64e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698   2 GVKLTPHNKEAVQHSDVLFLAVKPHIIPFILDEIGTHIEDRHIVVSCAAGVTIgsieKKLSAFRPTPRVIRCMTNIPVVV 81
Cdd:PLN02688   48 GVKTAASNTEVVKSSDVIILAVKPQVVKDVLTELRPLLSKDKLLVSVAAGITL----ADLQEWAGGRRVVRVMPNTPCLV 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698  82 REGATVYATGTHAQVEDGRLLEQLLGSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQ 161
Cdd:PLN02688  124 GEAASVMSLGPAATADDRDLVATLFGAVGKIWVVDEKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQ 203

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698 162 ALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALHVLESGGFRSLLINAVEASCIRTREL 221
Cdd:PLN02688  204 TVLGAAKMVLETGKHPGQLKDMVTSPGGTTIAGVHELEKGGFRAALMNAVVAAAKRSREL 263
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 2-221 1.43e-79

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 241.20  E-value: 1.43e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698   2 GVKLTPHNKEAVQHSDVLFLAVKPHIIPFILDEIGTHIEDrhIVVSCAAGVTIGSIEKKLSAFRPtprVIRCMTNIPVVV 81
Cdd:PRK11880   49 GVRAATDNQEAAQEADVVVLAVKPQVMEEVLSELKGQLDK--LVVSIAAGVTLARLERLLGADLP---VVRAMPNTPALV 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698  82 REGATVYATGTHAQVEDGRLLEQLLGSVGFCTEVE-EDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGA 160
Cdd:PRK11880  124 GAGMTALTANALVSAEDRELVENLLSAFGKVVWVDdEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAA 203

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622875698 161 QALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALHVLESGGFRSLLINAVEASCIRTREL 221
Cdd:PRK11880  204 QTVLGAAKLLLESGEHPAELRDNVTSPGGTTIAALRVLEEKGLRAAVIEAVQAAAKRSKEL 264
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 117-220 1.57e-50

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: 161.41  E-value: 1.57e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698 117 EDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALH 196
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80

                          90       100
                  ....*....|....*....|....
gi 1622875698 197 VLESGGFRSLLINAVEASCIRTRE 220
Cdd:pfam14748  81 VLEEGGFRGAVIEAVEAATKRAKE 104
PRK07679 PRK07679
pyrroline-5-carboxylate reductase; Reviewed
 2-227 2.12e-43

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 181079 [Multi-domain]  Cd Length: 279  Bit Score: 148.76  E-value: 2.12e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698   2 GVKLTPHNKEAVQHSDVLFLAVKPHIIPFILDEIGTHIEDRHIVVSCAAGVTIGSIEKKLSAFRPtprVIRCMTNIPVVV 81
Cdd:PRK07679   52 GVKGTHNKKELLTDANILFLAMKPKDVAEALIPFKEYIHNNQLIISLLAGVSTHSIRNLLQKDVP---IIRAMPNTSAAI 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698  82 REGATVYATGTHAQVEDGRLLEQLLGSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQ 161
Cdd:PRK07679  129 LKSATAISPSKHATAEHIQTAKALFETIGLVSVVEEEDMHAVTALSGSGPAYIYYVVEAMEKAAKKIGLKEDVAKSLILQ 208

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622875698 162 ALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALHVLESGGFRSLLINAVEASCIRTRELQSMADQ 227
Cdd:PRK07679  209 TMIGAAEMLKASEKHPSILRKEITSPGGTTEAGIEVLQEHRFQQALISCITQATQRSHNLGKTLEQ 274
PTZ00431 PTZ00431
pyrroline carboxylate reductase; Provisional
 9-221 3.93e-42

pyrroline carboxylate reductase; Provisional


Pssm-ID: 173621 [Multi-domain]  Cd Length: 260  Bit Score: 145.09  E-value: 3.93e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698   9 NKEAVQHSDVLFLAVKPHIIPFILDEIGTHIEDRhIVVSCAAGVTIGSIEKKLSAfrpTPRVIRCMTNIPVVVREGATVY 88
Cdd:PTZ00431   51 NEELAKTCDIIVLAVKPDLAGKVLLEIKPYLGSK-LLISICGGLNLKTLEEMVGV---EAKIVRVMPNTPSLVGQGSLVF 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698  89 ATGTHAQVEDGRLLEQLLGSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAK 168
Cdd:PTZ00431  127 CANNNVDSTDKKKVIDIFSACGIIQEIKEKDMDIATAISGCGPAYVFLFIESLIDAGVKNGLNRDVSKNLVLQTILGSVH 206

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622875698 169 MLLHSEQHPGQLKDNVSSPGGATIHALHVLESGGFRSLLINAVEASCIRTREL 221
Cdd:PTZ00431  207 MVKASDQPVQQLKDDVCSPGGITIVGLYTLEKHAFKYTVMDAVESACQKSKSM 259
PRK07680 PRK07680
late competence protein ComER; Validated
 2-201 6.68e-19

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 83.87  E-value: 6.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698   2 GVKLTPHNKEAVQHSDVLFLAVKPHIIPFILDEIGTHIEDRHIVVSCAAGVTIGSIEKKLSAfrPTPRVIRCMTNIpvvV 81
Cdd:PRK07680   49 GIHVAKTIEEVISQSDLIFICVKPLDIYPLLQKLAPHLTDEHCLVSITSPISVEQLETLVPC--QVARIIPSITNR---A 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698  82 REGATVYATGTHAQVEDGRLLEQLLGSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKM-GLPRRLAVRLGA 160
Cdd:PRK07680  124 LSGASLFTFGSRCSEEDQQKLERLFSNISTPLVIEEDITRVSSDIVSCGPAFFSYLLQRFIDAAVEEtNISKEEATTLAS 203

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1622875698 161 QALLGAAKMLLHSEQHPGQLKDNVSSPGGATIHALHVLESG 201
Cdd:PRK07680  204 EMLIGMGKLLEKGLYTLPTLQEKVCVKGGITGEGIKVLEEE 244
PRK06928 PRK06928
pyrroline-5-carboxylate reductase; Reviewed
 3-191 6.12e-10

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235888 [Multi-domain]  Cd Length: 277  Bit Score: 58.24  E-value: 6.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698   3 VKLTPHNKEAVQHSDVLFLAVKP-HIIPFILDEIGTHIEDRHIVvSCAAGVTIgsieKKLSAFRPTPRVIRCMTNIPVVV 81
Cdd:PRK06928   52 VELADNEAEIFTKCDHSFICVPPlAVLPLLKDCAPVLTPDRHVV-SIAAGVSL----DDLLEITPGLQVSRLIPSLTSAV 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698  82 REGATVYATGTHAQVEDGRLLEQLLGSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMG-LPRRLAVRLGA 160
Cdd:PRK06928  127 GVGTSLVAHAETVNEANKSRLEETLSHFSHVMTIREENMDIASNLTSSSPGFIAAIFEEFAEAAVRNSsLSDEEAFQFLN 206

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622875698 161 QALLGAAKMLLHSEQHPGQLKDNVSSPGGAT 191
Cdd:PRK06928  207 FALAGTGKLLVEEDYTFSGTIERVATKGGIT 237
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
1-51 1.59e-08

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 51.08  E-value: 1.59e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622875698   1 MGVKLTP-HNKEAVQHSDVLFLAVKPHIIPFILDEIgTHIEDRHIVVSCAAG 51
Cdd:pfam03807  42 YGVGATAvDNEEAAEEADVVFLAVKPEDAPDVLSEL-SDLLKGKIVISIAAG 92
PRK06476 PRK06476
pyrroline-5-carboxylate reductase; Reviewed
 9-219 1.71e-08

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235812 [Multi-domain]  Cd Length: 258  Bit Score: 53.87  E-value: 1.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698   9 NKEAVQHSDVLFLAVKPHIIPFILDEIgtHIEDRHIVVSCAAGVTIGSIEKklsAFRPTPRVIRCMTNIPVVVREGAT-V 87
Cdd:PRK06476   55 NQAVVDRSDVVFLAVRPQIAEEVLRAL--RFRPGQTVISVIAATDRAALLE---WIGHDVKLVRAIPLPFVAERKGVTaI 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698  88 YAtgTHAQVEDgrLLEQLLGSVGFCTEVEEDLIDAVTGLSGSgpaYaFTALDALADGGVKMGLPRRLAVRLGAQALLGAA 167
Cdd:PRK06476  130 YP--PDPFVAA--LFDALGTAVECDSEEEYDLLAAASALMAT---Y-FGILETATGWLEEQGLKRQKARAYLAPLFASLA 201

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622875698 168 KMLLHSEQHP-GQLKDNVSSPGGATIHALHVLESGGFRSLLINAVEASCIRTR 219
Cdd:PRK06476  202 QDAVRSTKTDfSALSREFSTKGGLNEQVLNDFSRQGGYAALTDALDRVLRRIN 254
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 5-123 7.73e-04

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 40.22  E-value: 7.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622875698   5 LTPHNKEAVQHSDVLFLAVKPHIIPFILDEIGTHIEDRHIVVSCAAGV-TIGSIEKKLsafrPTPRVIRCMTNIPVVVRE 83
Cdd:PRK06522   56 LAADDPAELGPQDLVILAVKAYQLPAALPSLAPLLGPDTPVLFLQNGVgHLEELAAYI----GPERVLGGVVTHAAELEG 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622875698  84 GATVYATGTHA--------QVEDGRLLEQLLGSVGFCTEVEEDLIDAV 123
Cdd:PRK06522  132 PGVVRHTGGGRlkigepdgESAAAEALADLLNAAGLDVEWSPDIRTEI 179
 
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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