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Conserved domains on  [gi|1822620892|ref|NP_001366014|]
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pyrroline-5-carboxylate reductase 1, mitochondrial isoform b [Mus musculus]

Protein Classification

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

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

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 5.54e-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: 299.67  E-value: 5.54e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892   1 MSVGFIGAGQLAFALAKGFTAAGVlAAHKIMASSPDMDQATvsAL-RKIGVNLTPHNKETVRHSDVLFLAVKPHIIPFIL 79
Cdd:COG0345     3 MKIGFIGAGNMGSAIIKGLLKSGV-PPEDIIVSDRSPERLE--ALaERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892  80 DEIGANIEDRHIVVSCAAGVTINSIEKkltAFQPAPKVIRCMTNTPVVVREGVTVYATGTHAQVEDGRLVEQLMGSVGFC 159
Cdd:COG0345    80 EELAPLLDPDKLVISIAAGVTLATLEE---ALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892 160 TEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLDSEQHPSQLKDNVCSPGGATI 239
Cdd:COG0345   157 VWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTI 236

                         250       260
                  ....*....|....*....|....*....
gi 1822620892 240 HALHVLESGGFRSLLINAVEASCIRTREL 268
Cdd:COG0345   237 AGLKVLEEGGLRAAVIEAVEAAAERSKEL 265
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-268 5.54e-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: 299.67  E-value: 5.54e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892   1 MSVGFIGAGQLAFALAKGFTAAGVlAAHKIMASSPDMDQATvsAL-RKIGVNLTPHNKETVRHSDVLFLAVKPHIIPFIL 79
Cdd:COG0345     3 MKIGFIGAGNMGSAIIKGLLKSGV-PPEDIIVSDRSPERLE--ALaERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892  80 DEIGANIEDRHIVVSCAAGVTINSIEKkltAFQPAPKVIRCMTNTPVVVREGVTVYATGTHAQVEDGRLVEQLMGSVGFC 159
Cdd:COG0345    80 EELAPLLDPDKLVISIAAGVTLATLEE---ALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892 160 TEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLDSEQHPSQLKDNVCSPGGATI 239
Cdd:COG0345   157 VWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTI 236

                         250       260
                  ....*....|....*....|....*....
gi 1822620892 240 HALHVLESGGFRSLLINAVEASCIRTREL 268
Cdd:COG0345   237 AGLKVLEEGGLRAAVIEAVEAAAERSKEL 265
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 1-268 9.30e-96

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 283.77  E-value: 9.30e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892   1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASsPDMDQATVSALRKIGVNLTPHNKETVRHSDVLFLAVKPHIIPFILD 80
Cdd:PLN02688    1 FRVGFIGAGKMAEAIARGLVASGVVPPSRISTA-DDSNPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892  81 EIGANIEDRHIVVSCAAGVTINSIEKKLtafqPAPKVIRCMTNTPVVVREGVTVYATGTHAQVEDGRLVEQLMGSVGFCT 160
Cdd:PLN02688   80 ELRPLLSKDKLLVSVAAGITLADLQEWA----GGRRVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIW 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892 161 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLDSEQHPSQLKDNVCSPGGATIH 240
Cdd:PLN02688  156 VVDEKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIA 235

                         250       260
                  ....*....|....*....|....*...
gi 1822620892 241 ALHVLESGGFRSLLINAVEASCIRTREL 268
Cdd:PLN02688  236 GVHELEKGGFRAALMNAVVAAAKRSREL 263
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 47-267 9.89e-83

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: 249.87  E-value: 9.89e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892  47 KIGVNLTPHNKETVRHSDVLFLAVKPHIIPFILDEIGANIEDRHIVVSCAAGVTINSIEKKLTAFQPapkVIRCMTNTPV 126
Cdd:TIGR00112  28 ELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLLGGTRR---VVRVMPNTPA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892 127 VVREGVTVYATGTHAQVEDGRLVEQLMGSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLG 206
Cdd:TIGR00112 105 KVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEALADAGVKQGLPRELALELA 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822620892 207 AQALLGAAKMLLDSEQHPSQLKDNVCSPGGATIHALHVLESGGFRSLLINAVEASCIRTRE 267
Cdd:TIGR00112 185 AQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAVRRSRE 245
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 164-267 3.69e-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: 159.10  E-value: 3.69e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892 164 EDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLDSEQHPSQLKDNVCSPGGATIHALH 243
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80

                          90       100
                  ....*....|....*....|....
gi 1822620892 244 VLESGGFRSLLINAVEASCIRTRE 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 5.54e-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: 299.67  E-value: 5.54e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892   1 MSVGFIGAGQLAFALAKGFTAAGVlAAHKIMASSPDMDQATvsAL-RKIGVNLTPHNKETVRHSDVLFLAVKPHIIPFIL 79
Cdd:COG0345     3 MKIGFIGAGNMGSAIIKGLLKSGV-PPEDIIVSDRSPERLE--ALaERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892  80 DEIGANIEDRHIVVSCAAGVTINSIEKkltAFQPAPKVIRCMTNTPVVVREGVTVYATGTHAQVEDGRLVEQLMGSVGFC 159
Cdd:COG0345    80 EELAPLLDPDKLVISIAAGVTLATLEE---ALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892 160 TEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLDSEQHPSQLKDNVCSPGGATI 239
Cdd:COG0345   157 VWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTI 236

                         250       260
                  ....*....|....*....|....*....
gi 1822620892 240 HALHVLESGGFRSLLINAVEASCIRTREL 268
Cdd:COG0345   237 AGLKVLEEGGLRAAVIEAVEAAAERSKEL 265
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 1-268 9.30e-96

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 283.77  E-value: 9.30e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892   1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASsPDMDQATVSALRKIGVNLTPHNKETVRHSDVLFLAVKPHIIPFILD 80
Cdd:PLN02688    1 FRVGFIGAGKMAEAIARGLVASGVVPPSRISTA-DDSNPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892  81 EIGANIEDRHIVVSCAAGVTINSIEKKLtafqPAPKVIRCMTNTPVVVREGVTVYATGTHAQVEDGRLVEQLMGSVGFCT 160
Cdd:PLN02688   80 ELRPLLSKDKLLVSVAAGITLADLQEWA----GGRRVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIW 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892 161 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLDSEQHPSQLKDNVCSPGGATIH 240
Cdd:PLN02688  156 VVDEKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIA 235

                         250       260
                  ....*....|....*....|....*...
gi 1822620892 241 ALHVLESGGFRSLLINAVEASCIRTREL 268
Cdd:PLN02688  236 GVHELEKGGFRAALMNAVVAAAKRSREL 263
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 1-268 7.87e-88

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 263.54  E-value: 7.87e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892   1 MSVGFIGAGQLAFALAKGFTAAGVlAAHKIMASSPDMDQATvSALRKIGVNLTPHNKETVRHSDVLFLAVKPHIIPFILD 80
Cdd:PRK11880    3 KKIGFIGGGNMASAIIGGLLASGV-PAKDIIVSDPSPEKRA-ALAEEYGVRAATDNQEAAQEADVVVLAVKPQVMEEVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892  81 EIGANIEDrhIVVSCAAGVTINSIEKKLTAFQPapkVIRCMTNTPVVVREGVTVYATGTHAQVEDGRLVEQLMGSVGFCT 160
Cdd:PRK11880   81 ELKGQLDK--LVVSIAAGVTLARLERLLGADLP---VVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGKVV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892 161 EVE-EDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLDSEQHPSQLKDNVCSPGGATI 239
Cdd:PRK11880  156 WVDdEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESGEHPAELRDNVTSPGGTTI 235

                         250       260
                  ....*....|....*....|....*....
gi 1822620892 240 HALHVLESGGFRSLLINAVEASCIRTREL 268
Cdd:PRK11880  236 AALRVLEEKGLRAAVIEAVQAAAKRSKEL 264
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 47-267 9.89e-83

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: 249.87  E-value: 9.89e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892  47 KIGVNLTPHNKETVRHSDVLFLAVKPHIIPFILDEIGANIEDRHIVVSCAAGVTINSIEKKLTAFQPapkVIRCMTNTPV 126
Cdd:TIGR00112  28 ELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLLGGTRR---VVRVMPNTPA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892 127 VVREGVTVYATGTHAQVEDGRLVEQLMGSVGFCTEVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLG 206
Cdd:TIGR00112 105 KVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEALADAGVKQGLPRELALELA 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822620892 207 AQALLGAAKMLLDSEQHPSQLKDNVCSPGGATIHALHVLESGGFRSLLINAVEASCIRTRE 267
Cdd:TIGR00112 185 AQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAVRRSRE 245
PTZ00431 PTZ00431
pyrroline carboxylate reductase; Provisional
 1-268 5.25e-51

pyrroline carboxylate reductase; Provisional


Pssm-ID: 173621 [Multi-domain]  Cd Length: 260  Bit Score: 169.36  E-value: 5.25e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892   1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDQATVSALRKigvnltphNKETVRHSDVLFLAVKPHIIPFILD 80
Cdd:PTZ00431    4 IRVGFIGLGKMGSALAYGIENSNIIGKENIYYHTPSKKNTPFVYLQS--------NEELAKTCDIIVLAVKPDLAGKVLL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892  81 EIGANIEDRhIVVSCAAGVTINSIEKKLTAfqpAPKVIRCMTNTPVVVREGVTVYATGTHAQVEDGRLVEQLMGSVGFCT 160
Cdd:PTZ00431   76 EIKPYLGSK-LLISICGGLNLKTLEEMVGV---EAKIVRVMPNTPSLVGQGSLVFCANNNVDSTDKKKVIDIFSACGIIQ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892 161 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLDSEQHPSQLKDNVCSPGGATIH 240
Cdd:PTZ00431  152 EIKEKDMDIATAISGCGPAYVFLFIESLIDAGVKNGLNRDVSKNLVLQTILGSVHMVKASDQPVQQLKDDVCSPGGITIV 231

                         250       260
                  ....*....|....*....|....*...
gi 1822620892 241 ALHVLESGGFRSLLINAVEASCIRTREL 268
Cdd:PTZ00431  232 GLYTLEKHAFKYTVMDAVESACQKSKSM 259
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 164-267 3.69e-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: 159.10  E-value: 3.69e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892 164 EDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLDSEQHPSQLKDNVCSPGGATIHALH 243
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80

                          90       100
                  ....*....|....*....|....
gi 1822620892 244 VLESGGFRSLLINAVEASCIRTRE 267
Cdd:pfam14748  81 VLEEGGFRGAVIEAVEAATKRAKE 104
PRK07679 PRK07679
pyrroline-5-carboxylate reductase; Reviewed
 1-268 1.01e-48

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 181079 [Multi-domain]  Cd Length: 279  Bit Score: 163.79  E-value: 1.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892   1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDQATVSALRKIGVNLTPHNKETVRHSDVLFLAVKPHIIPFILD 80
Cdd:PRK07679    4 QNISFLGAGSIAEAIIGGLLHANVVKGEQITVSNRSNETRLQELHQKYGVKGTHNKKELLTDANILFLAMKPKDVAEALI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892  81 EIGANIEDRHIVVSCAAGVTINSIEKKLTAFQPapkVIRCMTNTPVVVREGVTVYATGTHAQVEDGRLVEQLMGSVGFCT 160
Cdd:PRK07679   84 PFKEYIHNNQLIISLLAGVSTHSIRNLLQKDVP---IIRAMPNTSAAILKSATAISPSKHATAEHIQTAKALFETIGLVS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892 161 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLDSEQHPSQLKDNVCSPGGATIH 240
Cdd:PRK07679  161 VVEEEDMHAVTALSGSGPAYIYYVVEAMEKAAKKIGLKEDVAKSLILQTMIGAAEMLKASEKHPSILRKEITSPGGTTEA 240

                         250       260
                  ....*....|....*....|....*...
gi 1822620892 241 ALHVLESGGFRSLLINAVEASCIRTREL 268
Cdd:PRK07679  241 GIEVLQEHRFQQALISCITQATQRSHNL 268
PRK07680 PRK07680
late competence protein ComER; Validated
 1-248 8.21e-23

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 95.42  E-value: 8.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892   1 MSVGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDQATVSALRKIGVNLTPHNKETVRHSDVLFLAVKPHIIPFILD 80
Cdd:PRK07680    1 MNIGFIGTGNMGTILIEAFLESGAVKPSQLTITNRTPAKAYHIKERYPGIHVAKTIEEVISQSDLIFICVKPLDIYPLLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892  81 EIGANIEDRHIVVSCAAGVTINSIEKKLTAfQPApKVIRCMTNTpvvVREGVTVYATGTHAQVEDGRLVEQLMGSVGFCT 160
Cdd:PRK07680   81 KLAPHLTDEHCLVSITSPISVEQLETLVPC-QVA-RIIPSITNR---ALSGASLFTFGSRCSEEDQQKLERLFSNISTPL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892 161 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKM-GLPRRLAVRLGAQALLGAAKmLLDSEQH-PSQLKDNVCSPGGAT 238
Cdd:PRK07680  156 VIEEDITRVSSDIVSCGPAFFSYLLQRFIDAAVEEtNISKEEATTLASEMLIGMGK-LLEKGLYtLPTLQEKVCVKGGIT 234

                         250
                  ....*....|
gi 1822620892 239 IHALHVLESG 248
Cdd:PRK07680  235 GEGIKVLEEE 244
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
4-98 1.51e-19

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 81.51  E-value: 1.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892   4 GFIGAGQLAFALAKGFTAAGvlaAHKIM-ASSPDMDQATVSAlRKIGVNLTP-HNKETVRHSDVLFLAVKPHIIPFILDE 81
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAG---PHEVVvANSRNPEKAEELA-EEYGVGATAvDNEEAAEEADVVFLAVKPEDAPDVLSE 76

                          90
                  ....*....|....*..
gi 1822620892  82 IgANIEDRHIVVSCAAG 98
Cdd:pfam03807  77 L-SDLLKGKIVISIAAG 92
PRK06928 PRK06928
pyrroline-5-carboxylate reductase; Reviewed
 3-238 1.76e-12

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235888 [Multi-domain]  Cd Length: 277  Bit Score: 66.33  E-value: 1.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892   3 VGFIGAGQLAFALAKGFTAAGVLAAHKIMASSPDMDQATVSALRKI-GVNLTPHNKETVRHSDVLFLAVKP-HIIPFILD 80
Cdd:PRK06928    4 IGFIGYGSMADMIATKLLETEVATPEEIILYSSSKNEHFNQLYDKYpTVELADNEAEIFTKCDHSFICVPPlAVLPLLKD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892  81 EIGANIEDRHiVVSCAAGVTINSIEKKLTAFQpAPKVIRCMTNtpvVVREGVTVYATGTHAQVEDGRLVEQLMGSVGFCT 160
Cdd:PRK06928   84 CAPVLTPDRH-VVSIAAGVSLDDLLEITPGLQ-VSRLIPSLTS---AVGVGTSLVAHAETVNEANKSRLEETLSHFSHVM 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1822620892 161 EVEEDLIDAVTGLSGSGPAYAFTALDALADGGVKMG-LPRRLAVRLGAQALLGAAKMLLDSEQHPSQLKDNVCSPGGAT 238
Cdd:PRK06928  159 TIREENMDIASNLTSSSPGFIAAIFEEFAEAAVRNSsLSDEEAFQFLNFALAGTGKLLVEEDYTFSGTIERVATKGGIT 237
PRK06476 PRK06476
pyrroline-5-carboxylate reductase; Reviewed
 1-266 2.65e-11

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235812 [Multi-domain]  Cd Length: 258  Bit Score: 62.73  E-value: 2.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892   1 MSVGFIGAGQLAFALAKGFTAAGVLAAHkIMASSPDMDQATVSALRKIGVNLTPHNKETVRHSDVLFLAVKPHIIPFILD 80
Cdd:PRK06476    1 MKIGFIGTGAITEAMVTGLLTSPADVSE-IIVSPRNAQIAARLAERFPKVRIAKDNQAVVDRSDVVFLAVRPQIAEEVLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892  81 EIgaNIEDRHIVVSCAAGVTINSIEKkltAFQPAPKVIRCMTNTPVVVREGVT-VYAtgTHAQVEDgrLVEQLMGSVGFC 159
Cdd:PRK06476   80 AL--RFRPGQTVISVIAATDRAALLE---WIGHDVKLVRAIPLPFVAERKGVTaIYP--PDPFVAA--LFDALGTAVECD 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892 160 TEVEEDLIDAVTGLSGSgpaYaFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLDSEQHP-SQLKDNVCSPGGAT 238
Cdd:PRK06476  151 SEEEYDLLAAASALMAT---Y-FGILETATGWLEEQGLKRQKARAYLAPLFASLAQDAVRSTKTDfSALSREFSTKGGLN 226

                         250       260
                  ....*....|....*....|....*...
gi 1822620892 239 IHALHVLESGGFRSLLINAVEASCIRTR 266
Cdd:PRK06476  227 EQVLNDFSRQGGYAALTDALDRVLRRIN 254
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
3-96 6.26e-08

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


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 52.09  E-value: 6.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620892   3 VGFIGAGQLAFALAKGFTAAGvlaaHKIMASSPDMDQATvSALRKIGVNLTP-HNKETVRHSDVLFLAVKPHIIPFILDE 81
Cdd:COG2085     1 IGIIGTGNIGSALARRLAAAG----HEVVIGSRDPEKAA-ALAAELGPGARAgTNAEAAAAADVVVLAVPYEAVPDVLES 75

                          90
                  ....*....|....*
gi 1822620892  82 IGANIEDRhIVVSCA 96
Cdd:COG2085    76 LGDALAGK-IVIDAT 89
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 1-71 2.09e-05

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


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 45.19  E-value: 2.09e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1822620892   1 MSVGFIGAGQLAFALAKGFTAAGvlaaHKIMA-SSPDmDQATVSALRKIGVNLTPHNKETVRHSDVLFLAVK 71
Cdd:COG5495     4 MKIGIIGAGRVGTALAAALRAAG----HEVVGvYSRS-PASAERAAALLGAVPALDLEELAAEADLVLLAVP 70
 
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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