NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1822620903|ref|NP_001366016|]
View 

pyrroline-5-carboxylate reductase 1, mitochondrial isoform c precursor [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]; ...
 11-255 8.31e-94

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: 278.10  E-value: 8.31e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903  11 VLAAHKIMASSPDMDQATvsALR-KIGVNLTPHNKETVRHSDVLFLAVKPHIIPFILDEIGANIEDRHIVVSCAAGVTIN 89
Cdd:COG0345    25 GVPPEDIIVSDRSPERLE--ALAeRYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVLEELAPLLDPDKLVISIAAGVTLA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903  90 SIEKkltAFQPAPKVIRCMTNTPVVVREGVTVYATGTHAQVEDGRLVEQLMGSVGFCTEVEEDLIDAVTGLSGSGPAYAF 169
Cdd:COG0345   103 TLEE---ALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWVDEELMDAVTALSGSGPAYVF 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903 170 TALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLDSEQHPSQLKDNVCSPGGATIHALHVLESGGFRSLLINAVEASC 249
Cdd:COG0345   180 LFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTIAGLKVLEEGGLRAAVIEAVEAAA 259


                  ....*.
gi 1822620903 250 IRTREL 255
Cdd:COG0345   260 ERSKEL 265
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 11-255 8.31e-94

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: 278.10  E-value: 8.31e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903  11 VLAAHKIMASSPDMDQATvsALR-KIGVNLTPHNKETVRHSDVLFLAVKPHIIPFILDEIGANIEDRHIVVSCAAGVTIN 89
Cdd:COG0345    25 GVPPEDIIVSDRSPERLE--ALAeRYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVLEELAPLLDPDKLVISIAAGVTLA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903  90 SIEKkltAFQPAPKVIRCMTNTPVVVREGVTVYATGTHAQVEDGRLVEQLMGSVGFCTEVEEDLIDAVTGLSGSGPAYAF 169
Cdd:COG0345   103 TLEE---ALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWVDEELMDAVTALSGSGPAYVF 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903 170 TALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLDSEQHPSQLKDNVCSPGGATIHALHVLESGGFRSLLINAVEASC 249
Cdd:COG0345   180 LFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTIAGLKVLEEGGLRAAVIEAVEAAA 259


                  ....*.
gi 1822620903 250 IRTREL 255
Cdd:COG0345   260 ERSKEL 265
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 18-255 1.22e-85

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 257.58  E-value: 1.22e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903  18 MASSPDMDQATVSALRKIGVNLTPHNKETVRHSDVLFLAVKPHIIPFILDEIGANIEDRHIVVSCAAGVTINSIEKKLta 97
Cdd:PLN02688   30 ISTADDSNPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLTELRPLLSKDKLLVSVAAGITLADLQEWA-- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903  98 fqPAPKVIRCMTNTPVVVREGVTVYATGTHAQVEDGRLVEQLMGSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALAD 177
Cdd:PLN02688  108 --GGRRVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIWVVDEKLLDAVTGLSGSGPAYIFLAIEALAD 185

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822620903 178 GGVKMGLPRRLAVRLGAQALLGAAKMLLDSEQHPSQLKDNVCSPGGATIHALHVLESGGFRSLLINAVEASCIRTREL 255
Cdd:PLN02688  186 GGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIAGVHELEKGGFRAALMNAVVAAAKRSREL 263
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 34-254 1.52e-84

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: 254.11  E-value: 1.52e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903  34 KIGVNLTPHNKETVRHSDVLFLAVKPHIIPFILDEIGANIEDRHIVVSCAAGVTINSIEKKLTAFQPapkVIRCMTNTPV 113
Cdd:TIGR00112  28 ELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLLGGTRR---VVRVMPNTPA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903 114 VVREGVTVYATGTHAQVEDGRLVEQLMGSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLG 193
Cdd:TIGR00112 105 KVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEALADAGVKQGLPRELALELA 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822620903 194 AQALLGAAKMLLDSEQHPSQLKDNVCSPGGATIHALHVLESGGFRSLLINAVEASCIRTRE 254
Cdd:TIGR00112 185 AQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAVRRSRE 245
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 151-254 1.60e-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: 162.18  E-value: 1.60e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903 151 EDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLDSEQHPSQLKDNVCSPGGATIHALH 230
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80

                          90       100
                  ....*....|....*....|....
gi 1822620903 231 VLESGGFRSLLINAVEASCIRTRE 254
Cdd:pfam14748  81 VLEEGGFRGAVIEAVEAATKRAKE 104
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 11-255 8.31e-94

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: 278.10  E-value: 8.31e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903  11 VLAAHKIMASSPDMDQATvsALR-KIGVNLTPHNKETVRHSDVLFLAVKPHIIPFILDEIGANIEDRHIVVSCAAGVTIN 89
Cdd:COG0345    25 GVPPEDIIVSDRSPERLE--ALAeRYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVLEELAPLLDPDKLVISIAAGVTLA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903  90 SIEKkltAFQPAPKVIRCMTNTPVVVREGVTVYATGTHAQVEDGRLVEQLMGSVGFCTEVEEDLIDAVTGLSGSGPAYAF 169
Cdd:COG0345   103 TLEE---ALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWVDEELMDAVTALSGSGPAYVF 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903 170 TALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLDSEQHPSQLKDNVCSPGGATIHALHVLESGGFRSLLINAVEASC 249
Cdd:COG0345   180 LFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTIAGLKVLEEGGLRAAVIEAVEAAA 259


                  ....*.
gi 1822620903 250 IRTREL 255
Cdd:COG0345   260 ERSKEL 265
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 18-255 1.22e-85

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 257.58  E-value: 1.22e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903  18 MASSPDMDQATVSALRKIGVNLTPHNKETVRHSDVLFLAVKPHIIPFILDEIGANIEDRHIVVSCAAGVTINSIEKKLta 97
Cdd:PLN02688   30 ISTADDSNPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLTELRPLLSKDKLLVSVAAGITLADLQEWA-- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903  98 fqPAPKVIRCMTNTPVVVREGVTVYATGTHAQVEDGRLVEQLMGSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALAD 177
Cdd:PLN02688  108 --GGRRVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIWVVDEKLLDAVTGLSGSGPAYIFLAIEALAD 185

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822620903 178 GGVKMGLPRRLAVRLGAQALLGAAKMLLDSEQHPSQLKDNVCSPGGATIHALHVLESGGFRSLLINAVEASCIRTREL 255
Cdd:PLN02688  186 GGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIAGVHELEKGGFRAALMNAVVAAAKRSREL 263
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 34-254 1.52e-84

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: 254.11  E-value: 1.52e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903  34 KIGVNLTPHNKETVRHSDVLFLAVKPHIIPFILDEIGANIEDRHIVVSCAAGVTINSIEKKLTAFQPapkVIRCMTNTPV 113
Cdd:TIGR00112  28 ELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLLGGTRR---VVRVMPNTPA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903 114 VVREGVTVYATGTHAQVEDGRLVEQLMGSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLG 193
Cdd:TIGR00112 105 KVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEALADAGVKQGLPRELALELA 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822620903 194 AQALLGAAKMLLDSEQHPSQLKDNVCSPGGATIHALHVLESGGFRSLLINAVEASCIRTRE 254
Cdd:TIGR00112 185 AQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAVRRSRE 245
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 12-255 7.94e-82

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 247.75  E-value: 7.94e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903  12 LAAHKIMASSPDMDQATvSALRKIGVNLTPHNKETVRHSDVLFLAVKPHIIPFILDEIGANIEDrhIVVSCAAGVTINSI 91
Cdd:PRK11880   26 VPAKDIIVSDPSPEKRA-ALAEEYGVRAATDNQEAAQEADVVVLAVKPQVMEEVLSELKGQLDK--LVVSIAAGVTLARL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903  92 EKKLTAFQPapkVIRCMTNTPVVVREGVTVYATGTHAQVEDGRLVEQLMGSVGFCTEVE-EDLIDAVTGLSGSGPAYAFT 170
Cdd:PRK11880  103 ERLLGADLP---VVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGKVVWVDdEKQMDAVTAVSGSGPAYVFL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903 171 ALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLDSEQHPSQLKDNVCSPGGATIHALHVLESGGFRSLLINAVEASCI 250
Cdd:PRK11880  180 FIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESGEHPAELRDNVTSPGGTTIAALRVLEEKGLRAAVIEAVQAAAK 259


                  ....*
gi 1822620903 251 RTREL 255
Cdd:PRK11880  260 RSKEL 264
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 151-254 1.60e-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: 162.18  E-value: 1.60e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903 151 EDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLDSEQHPSQLKDNVCSPGGATIHALH 230
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80

                          90       100
                  ....*....|....*....|....
gi 1822620903 231 VLESGGFRSLLINAVEASCIRTRE 254
Cdd:pfam14748  81 VLEEGGFRGAVIEAVEAATKRAKE 104
PTZ00431 PTZ00431
pyrroline carboxylate reductase; Provisional
 43-255 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 1822620903  43 NKETVRHSDVLFLAVKPHIIPFILDEIGANIEDRhIVVSCAAGVTINSIEKKLTAfqpAPKVIRCMTNTPVVVREGVTVY 122
Cdd:PTZ00431   51 NEELAKTCDIIVLAVKPDLAGKVLLEIKPYLGSK-LLISICGGLNLKTLEEMVGV---EAKIVRVMPNTPSLVGQGSLVF 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903 123 ATGTHAQVEDGRLVEQLMGSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAK 202
Cdd:PTZ00431  127 CANNNVDSTDKKKVIDIFSACGIIQEIKEKDMDIATAISGCGPAYVFLFIESLIDAGVKNGLNRDVSKNLVLQTILGSVH 206

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1822620903 203 MLLDSEQHPSQLKDNVCSPGGATIHALHVLESGGFRSLLINAVEASCIRTREL 255
Cdd:PTZ00431  207 MVKASDQPVQQLKDDVCSPGGITIVGLYTLEKHAFKYTVMDAVESACQKSKSM 259
PRK07679 PRK07679
pyrroline-5-carboxylate reductase; Reviewed
 33-255 3.02e-43

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 181079 [Multi-domain]  Cd Length: 279  Bit Score: 149.15  E-value: 3.02e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903  33 RKIGVNLTPHNKETVRHSDVLFLAVKPHIIPFILDEIGANIEDRHIVVSCAAGVTINSIEKKLTAFQPapkVIRCMTNTP 112
Cdd:PRK07679   49 QKYGVKGTHNKKELLTDANILFLAMKPKDVAEALIPFKEYIHNNQLIISLLAGVSTHSIRNLLQKDVP---IIRAMPNTS 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903 113 VVVREGVTVYATGTHAQVEDGRLVEQLMGSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRL 192
Cdd:PRK07679  126 AAILKSATAISPSKHATAEHIQTAKALFETIGLVSVVEEEDMHAVTALSGSGPAYIYYVVEAMEKAAKKIGLKEDVAKSL 205

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1822620903 193 GAQALLGAAKMLLDSEQHPSQLKDNVCSPGGATIHALHVLESGGFRSLLINAVEASCIRTREL 255
Cdd:PRK07679  206 ILQTMIGAAEMLKASEKHPSILRKEITSPGGTTEAGIEVLQEHRFQQALISCITQATQRSHNL 268
PRK07680 PRK07680
late competence protein ComER; Validated
 36-235 9.99e-18

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 80.79  E-value: 9.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903  36 GVNLTPHNKETVRHSDVLFLAVKPHIIPFILDEIGANIEDRHIVVSCAAGVTINSIEKKLTAfQPApKVIRCMTNTpvvV 115
Cdd:PRK07680   49 GIHVAKTIEEVISQSDLIFICVKPLDIYPLLQKLAPHLTDEHCLVSITSPISVEQLETLVPC-QVA-RIIPSITNR---A 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903 116 REGVTVYATGTHAQVEDGRLVEQLMGSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKM-GLPRRLAVRLGA 194
Cdd:PRK07680  124 LSGASLFTFGSRCSEEDQQKLERLFSNISTPLVIEEDITRVSSDIVSCGPAFFSYLLQRFIDAAVEEtNISKEEATTLAS 203

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1822620903 195 QALLGAAKmLLDSEQH-PSQLKDNVCSPGGATIHALHVLESG 235
Cdd:PRK07680  204 EMLIGMGK-LLEKGLYtLPTLQEKVCVKGGITGEGIKVLEEE 244
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
14-85 3.13e-11

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 58.78  E-value: 3.13e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1822620903  14 AHKIM-ASSPDMDQATVSAlRKIGVNLTP-HNKETVRHSDVLFLAVKPHIIPFILDEIgANIEDRHIVVSCAAG 85
Cdd:pfam03807  21 PHEVVvANSRNPEKAEELA-EEYGVGATAvDNEEAAEEADVVFLAVKPEDAPDVLSEL-SDLLKGKIVISIAAG 92
PRK06928 PRK06928
pyrroline-5-carboxylate reductase; Reviewed
 37-225 1.40e-09

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235888 [Multi-domain]  Cd Length: 277  Bit Score: 57.86  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903  37 VNLTPHNKETVRHSDVLFLAVKP-HIIPFILDEIGANIEDRHIVvSCAAGVTINSIEKKLTAFQpAPKVIRCMTNtpvVV 115
Cdd:PRK06928   52 VELADNEAEIFTKCDHSFICVPPlAVLPLLKDCAPVLTPDRHVV-SIAAGVSLDDLLEITPGLQ-VSRLIPSLTS---AV 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903 116 REGVTVYATGTHAQVEDGRLVEQLMGSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMG-LPRRLAVRLGA 194
Cdd:PRK06928  127 GVGTSLVAHAETVNEANKSRLEETLSHFSHVMTIREENMDIASNLTSSSPGFIAAIFEEFAEAAVRNSsLSDEEAFQFLN 206

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1822620903 195 QALLGAAKMLLDSEQHPSQLKDNVCSPGGAT 225
Cdd:PRK06928  207 FALAGTGKLLVEEDYTFSGTIERVATKGGIT 237
PRK06476 PRK06476
pyrroline-5-carboxylate reductase; Reviewed
 6-253 4.42e-08

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235812 [Multi-domain]  Cd Length: 258  Bit Score: 53.10  E-value: 4.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903   6 GCLLCVLAAHKIMASSPDMDQATVSALRKIGVNLTPHNKETVRHSDVLFLAVKPHIIPFILDEIgaNIEDRHIVVSCAAG 85
Cdd:PRK06476   18 GLLTSPADVSEIIVSPRNAQIAARLAERFPKVRIAKDNQAVVDRSDVVFLAVRPQIAEEVLRAL--RFRPGQTVISVIAA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903  86 VTINSIEKkltAFQPAPKVIRCMTNTPVVVREGVT-VYAtgTHAQVEDgrLVEQLMGSVGFCTEVEEDLIDAVTGLSGSg 164
Cdd:PRK06476   96 TDRAALLE---WIGHDVKLVRAIPLPFVAERKGVTaIYP--PDPFVAA--LFDALGTAVECDSEEEYDLLAAASALMAT- 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620903 165 paYaFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLDSEQHP-SQLKDNVCSPGGATIHALHVLESGGFRSLLIN 243
Cdd:PRK06476  168 --Y-FGILETATGWLEEQGLKRQKARAYLAPLFASLAQDAVRSTKTDfSALSREFSTKGGLNEQVLNDFSRQGGYAALTD 244

                         250
                  ....*....|
gi 1822620903 244 AVEASCIRTR 253
Cdd:PRK06476  245 ALDRVLRRIN 254
 
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