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Conserved domains on  [gi|62896929|dbj|BAD96405|]
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Pyrroline-5-carboxylate reductase-like variant, partial [Homo sapiens]

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]; ...
 19-260 1.46e-92

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: 274.25  E-value: 1.46e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929  19 SPRRVGFVGAGRMAGAIAQGLIRAGkVEAQHILASAPTDRNLCHFQA-LGCRTTHSNQEVLQSCLLVIFATKPHVLPAVL 97
Cdd:COG0345   1 MSMKIGFIGAGNMGSAIIKGLLKSG-VPPEDIIVSDRSPERLEALAErYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929  98 AEVAPVVTTEHILVSVAAGVSLSTLEELLPPNTRVLRVLPNLPCVVQEGAIVMARGRHVGSSETNLLQHLLEACGRCEEV 177
Cdd:COG0345  80 EELAPLLDPDKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWV 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929 178 PEAYVDIHTGLSGSGVAFVCAFSEALAEGAVKMGMPSSLAHRIAAQTLLGTAKMLLHEGQHPAQLRSDVCTPGGTTIYGL 257
Cdd:COG0345 160 DEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTIAGL 239


                ...
gi 62896929 258 HAL 260
Cdd:COG0345 240 KVL 242
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 19-260 1.46e-92

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: 274.25  E-value: 1.46e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929  19 SPRRVGFVGAGRMAGAIAQGLIRAGkVEAQHILASAPTDRNLCHFQA-LGCRTTHSNQEVLQSCLLVIFATKPHVLPAVL 97
Cdd:COG0345   1 MSMKIGFIGAGNMGSAIIKGLLKSG-VPPEDIIVSDRSPERLEALAErYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929  98 AEVAPVVTTEHILVSVAAGVSLSTLEELLPPNTRVLRVLPNLPCVVQEGAIVMARGRHVGSSETNLLQHLLEACGRCEEV 177
Cdd:COG0345  80 EELAPLLDPDKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWV 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929 178 PEAYVDIHTGLSGSGVAFVCAFSEALAEGAVKMGMPSSLAHRIAAQTLLGTAKMLLHEGQHPAQLRSDVCTPGGTTIYGL 257
Cdd:COG0345 160 DEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTIAGL 239


                ...
gi 62896929 258 HAL 260
Cdd:COG0345 240 KVL 242
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 22-260 8.42e-81

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 244.48  E-value: 8.42e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929   22 RVGFVGAGRMAGAIAQGLIRAGKVEAQHILASAPTDRNLC-HFQALGCRTTHSNQEVLQSCLLVIFATKPHVLPAVLAEV 100
Cdd:PLN02688   2 RVGFIGAGKMAEAIARGLVASGVVPPSRISTADDSNPARRdVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLTEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929  101 APVVTTEHILVSVAAGVSLSTLEELLPPNtRVLRVLPNLPCVVQEGAIVMARGRHVGSSETNLLQHLLEACGRCEEVPEA 180
Cdd:PLN02688  82 RPLLSKDKLLVSVAAGITLADLQEWAGGR-RVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIWVVDEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929  181 YVDIHTGLSGSGVAFVCAFSEALAEGAVKMGMPSSLAHRIAAQTLLGTAKMLLHEGQHPAQLRSDVCTPGGTTIYGLHAL 260
Cdd:PLN02688 161 LLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIAGVHEL 240
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 39-260 4.79e-70

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: 216.36  E-value: 4.79e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929    39 LIRAGKVEAQHILASAP-TDRNLCHFQALGCRTTHSNQEVLQSCLLVIFATKPHVLPAVLAEVAPVVTTEHILVSVAAGV 117
Cdd:TIGR00112   1 LLKAGALAPYDIYVINRsPEKLAALAKELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929   118 SLSTLEELLPPNTRVLRVLPNLPCVVQEGAIVMARGRHVGSSETNLLQHLLEACGRCEEVPEAYVDIHTGLSGSGVAFVC 197
Cdd:TIGR00112  81 TLEKLSQLLGGTRRVVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVF 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62896929   198 AFSEALAEGAVKMGMPSSLAHRIAAQTLLGTAKMLLHEGQHPAQLRSDVCTPGGTTIYGLHAL 260
Cdd:TIGR00112 161 LFIEALADAGVKQGLPRELALELAAQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVL 223
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 179-260 1.44e-34

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: 120.58  E-value: 1.44e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929   179 EAYVDIHTGLSGSGVAFVCAFSEALAEGAVKMGMPSSLAHRIAAQTLLGTAKMLLHEGQHPAQLRSDVCTPGGTTIYGLH 258
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80


                  ..
gi 62896929   259 AL 260
Cdd:pfam14748  81 VL 82
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 19-260 1.46e-92

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: 274.25  E-value: 1.46e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929  19 SPRRVGFVGAGRMAGAIAQGLIRAGkVEAQHILASAPTDRNLCHFQA-LGCRTTHSNQEVLQSCLLVIFATKPHVLPAVL 97
Cdd:COG0345   1 MSMKIGFIGAGNMGSAIIKGLLKSG-VPPEDIIVSDRSPERLEALAErYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929  98 AEVAPVVTTEHILVSVAAGVSLSTLEELLPPNTRVLRVLPNLPCVVQEGAIVMARGRHVGSSETNLLQHLLEACGRCEEV 177
Cdd:COG0345  80 EELAPLLDPDKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWV 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929 178 PEAYVDIHTGLSGSGVAFVCAFSEALAEGAVKMGMPSSLAHRIAAQTLLGTAKMLLHEGQHPAQLRSDVCTPGGTTIYGL 257
Cdd:COG0345 160 DEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTIAGL 239


                ...
gi 62896929 258 HAL 260
Cdd:COG0345 240 KVL 242
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 22-260 8.42e-81

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 244.48  E-value: 8.42e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929   22 RVGFVGAGRMAGAIAQGLIRAGKVEAQHILASAPTDRNLC-HFQALGCRTTHSNQEVLQSCLLVIFATKPHVLPAVLAEV 100
Cdd:PLN02688   2 RVGFIGAGKMAEAIARGLVASGVVPPSRISTADDSNPARRdVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLTEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929  101 APVVTTEHILVSVAAGVSLSTLEELLPPNtRVLRVLPNLPCVVQEGAIVMARGRHVGSSETNLLQHLLEACGRCEEVPEA 180
Cdd:PLN02688  82 RPLLSKDKLLVSVAAGITLADLQEWAGGR-RVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIWVVDEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929  181 YVDIHTGLSGSGVAFVCAFSEALAEGAVKMGMPSSLAHRIAAQTLLGTAKMLLHEGQHPAQLRSDVCTPGGTTIYGLHAL 260
Cdd:PLN02688 161 LLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIAGVHEL 240
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 21-260 2.23e-73

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 225.41  E-value: 2.23e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929   21 RRVGFVGAGRMAGAIAQGLIRAGkVEAQHILASAPTDRNLCHF-QALGCRTTHSNQEVLQSCLLVIFATKPHVLPAVLAE 99
Cdd:PRK11880   3 KKIGFIGGGNMASAIIGGLLASG-VPAKDIIVSDPSPEKRAALaEEYGVRAATDNQEAAQEADVVVLAVKPQVMEEVLSE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929  100 VAPVVTTehILVSVAAGVSLSTLEELLPPNTRVLRVLPNLPCVVQEGAIVMARGRHVGSSETNLLQHLLEACGRCEEVP- 178
Cdd:PRK11880  82 LKGQLDK--LVVSIAAGVTLARLERLLGADLPVVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGKVVWVDd 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929  179 EAYVDIHTGLSGSGVAFVCAFSEALAEGAVKMGMPSSLAHRIAAQTLLGTAKMLLHEGQHPAQLRSDVCTPGGTTIYGLH 258
Cdd:PRK11880 160 EKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESGEHPAELRDNVTSPGGTTIAALR 239


                 ..
gi 62896929  259 AL 260
Cdd:PRK11880 240 VL 241
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 39-260 4.79e-70

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: 216.36  E-value: 4.79e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929    39 LIRAGKVEAQHILASAP-TDRNLCHFQALGCRTTHSNQEVLQSCLLVIFATKPHVLPAVLAEVAPVVTTEHILVSVAAGV 117
Cdd:TIGR00112   1 LLKAGALAPYDIYVINRsPEKLAALAKELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929   118 SLSTLEELLPPNTRVLRVLPNLPCVVQEGAIVMARGRHVGSSETNLLQHLLEACGRCEEVPEAYVDIHTGLSGSGVAFVC 197
Cdd:TIGR00112  81 TLEKLSQLLGGTRRVVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVF 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62896929   198 AFSEALAEGAVKMGMPSSLAHRIAAQTLLGTAKMLLHEGQHPAQLRSDVCTPGGTTIYGLHAL 260
Cdd:TIGR00112 161 LFIEALADAGVKQGLPRELALELAAQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVL 223
PTZ00431 PTZ00431
pyrroline carboxylate reductase; Provisional
 22-260 1.75e-51

pyrroline carboxylate reductase; Provisional


Pssm-ID: 173621 [Multi-domain]  Cd Length: 260  Bit Score: 169.36  E-value: 1.75e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929   22 RVGFVGAGRMAGAIAQGLIRAGKVEAQHILASAPTDRN--LCHFQalgcrtthSNQEVLQSCLLVIFATKPHVLPAVLAE 99
Cdd:PTZ00431   5 RVGFIGLGKMGSALAYGIENSNIIGKENIYYHTPSKKNtpFVYLQ--------SNEELAKTCDIIVLAVKPDLAGKVLLE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929  100 VAPVVTTEhILVSVAAGVSLSTLEELLPPNTRVLRVLPNLPCVVQEGAIVMARGRHVGSSETNLLQHLLEACGRCEEVPE 179
Cdd:PTZ00431  77 IKPYLGSK-LLISICGGLNLKTLEEMVGVEAKIVRVMPNTPSLVGQGSLVFCANNNVDSTDKKKVIDIFSACGIIQEIKE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929  180 AYVDIHTGLSGSGVAFVCAFSEALAEGAVKMGMPSSLAHRIAAQTLLGTAKMLLHEGQHPAQLRSDVCTPGGTTIYGLHA 259
Cdd:PTZ00431 156 KDMDIATAISGCGPAYVFLFIESLIDAGVKNGLNRDVSKNLVLQTILGSVHMVKASDQPVQQLKDDVCSPGGITIVGLYT 235


                 .
gi 62896929  260 L 260
Cdd:PTZ00431 236 L 236
PRK07679 PRK07679
pyrroline-5-carboxylate reductase; Reviewed
 19-260 7.58e-41

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 181079 [Multi-domain]  Cd Length: 279  Bit Score: 142.22  E-value: 7.58e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929   19 SPRRVGFVGAGRMAGAIAQGLIRAGKVEAQHILASAPTDRNLCHF--QALGCRTTHSNQEVLQSCLLVIFATKPHVLPAV 96
Cdd:PRK07679   2 SIQNISFLGAGSIAEAIIGGLLHANVVKGEQITVSNRSNETRLQElhQKYGVKGTHNKKELLTDANILFLAMKPKDVAEA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929   97 LAEVAPVVTTEHILVSVAAGVSLSTLEELLPPNTRVLRVLPNLPCVVQEGAIVMARGRHVGSSETNLLQHLLEACGRCEE 176
Cdd:PRK07679  82 LIPFKEYIHNNQLIISLLAGVSTHSIRNLLQKDVPIIRAMPNTSAAILKSATAISPSKHATAEHIQTAKALFETIGLVSV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929  177 VPEAyvDIH--TGLSGSGVAFVCAFSEALAEGAVKMGMPSSLAHRIAAQTLLGTAKMLLHEGQHPAQLRSDVCTPGGTTI 254
Cdd:PRK07679 162 VEEE--DMHavTALSGSGPAYIYYVVEAMEKAAKKIGLKEDVAKSLILQTMIGAAEMLKASEKHPSILRKEITSPGGTTE 239


                 ....*.
gi 62896929  255 YGLHAL 260
Cdd:PRK07679 240 AGIEVL 245
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 179-260 1.44e-34

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: 120.58  E-value: 1.44e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929   179 EAYVDIHTGLSGSGVAFVCAFSEALAEGAVKMGMPSSLAHRIAAQTLLGTAKMLLHEGQHPAQLRSDVCTPGGTTIYGLH 258
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80


                  ..
gi 62896929   259 AL 260
Cdd:pfam14748  81 VL 82
PRK06928 PRK06928
pyrroline-5-carboxylate reductase; Reviewed
 22-270 4.89e-29

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235888 [Multi-domain]  Cd Length: 277  Bit Score: 111.40  E-value: 4.89e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929   22 RVGFVGAGRMAGAIAQGLIRAGKVEAQHILASapTDRNLCHFQALGCRTTH-----SNQEVLQSCLLvIFATKP--HVLP 94
Cdd:PRK06928   3 KIGFIGYGSMADMIATKLLETEVATPEEIILY--SSSKNEHFNQLYDKYPTveladNEAEIFTKCDH-SFICVPplAVLP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929   95 aVLAEVAPVVTTEHILVSVAAGVSLSTLEELlPPNTRVLRVLPNLPCVVQEGAIVMARGRHVGSSETNLLQHLLEACGRC 174
Cdd:PRK06928  80 -LLKDCAPVLTPDRHVVSIAAGVSLDDLLEI-TPGLQVSRLIPSLTSAVGVGTSLVAHAETVNEANKSRLEETLSHFSHV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929  175 EEVPEAYVDIHTGLSGSGVAFVCAFSEALAEGAVKMgmpSSLAHRIAAQ----TLLGTAKMLLHEGQHPAQLRSDVCTPG 250
Cdd:PRK06928 158 MTIREENMDIASNLTSSSPGFIAAIFEEFAEAAVRN---SSLSDEEAFQflnfALAGTGKLLVEEDYTFSGTIERVATKG 234

                        250       260
                 ....*....|....*....|
gi 62896929  251 GTTIYGLHalaLVWIQAPSF 270
Cdd:PRK06928 235 GITAEGAE---VIQAQLPQF 251
PRK07680 PRK07680
late competence protein ComER; Validated
 22-260 7.70e-23

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 94.65  E-value: 7.70e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929   22 RVGFVGAGRMAGAIAQGLIRAGKVEAQHILAsapTDRNLCHFQAL-----GCRTTHSNQEVLQSCLLVIFATKPHVLPAV 96
Cdd:PRK07680   2 NIGFIGTGNMGTILIEAFLESGAVKPSQLTI---TNRTPAKAYHIkerypGIHVAKTIEEVISQSDLIFICVKPLDIYPL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929   97 LAEVAPVVTTEHILVSVAAGVSLSTLEELLPpnTRVLRVLPNLPCVVQEGAIVMARGRHVGSSETNLLQHLLEACGRCEE 176
Cdd:PRK07680  79 LQKLAPHLTDEHCLVSITSPISVEQLETLVP--CQVARIIPSITNRALSGASLFTFGSRCSEEDQQKLERLFSNISTPLV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929  177 VPEAYVDIHTGLSGSGVAFVCAFSEALAEGAVKM-GMPSSLAHRIAAQTLLGTAKMLLHEGQHPAQLRSDVCTPGGTTIY 255
Cdd:PRK07680 157 IEEDITRVSSDIVSCGPAFFSYLLQRFIDAAVEEtNISKEEATTLASEMLIGMGKLLEKGLYTLPTLQEKVCVKGGITGE 236


                 ....*
gi 62896929  256 GLHAL 260
Cdd:PRK07680 237 GIKVL 241
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
24-116 2.78e-11

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 58.78  E-value: 2.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929    24 GFVGAGRMAGAIAQGLIRAGKVEAqhILASAPTDRNLCHF-QALGCRTTH-SNQEVLQSCLLVIFATKPHVLPAVLAEVA 101
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAGPHEV--VVANSRNPEKAEELaEEYGVGATAvDNEEAAEEADVVFLAVKPEDAPDVLSELS 78

                          90
                  ....*....|....*
gi 62896929   102 PVVtTEHILVSVAAG 116
Cdd:pfam03807  79 DLL-KGKIVISIAAG 92
PRK06476 PRK06476
pyrroline-5-carboxylate reductase; Reviewed
 22-144 1.15e-07

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235812 [Multi-domain]  Cd Length: 258  Bit Score: 51.56  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929   22 RVGFVGAGRMAGAIAQGLIRAGkVEAQHILAS---APTDRNLCH-FQALgcRTTHSNQEVLQSCLLVIFAtkphVLPAVL 97
Cdd:PRK06476   2 KIGFIGTGAITEAMVTGLLTSP-ADVSEIIVSprnAQIAARLAErFPKV--RIAKDNQAVVDRSDVVFLA----VRPQIA 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 62896929   98 AEVAPVVT--TEHILVSVAAGVSLSTLEELLPPNTRVLRVLPnLPCVVQ 144
Cdd:PRK06476  75 EEVLRALRfrPGQTVISVIAATDRAALLEWIGHDVKLVRAIP-LPFVAE 122
GpsA COG0240
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
 22-132 2.97e-04

Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440010 [Multi-domain]  Cd Length: 327  Bit Score: 41.56  E-value: 2.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929  22 RVGFVGAGRMAGAIAQGLIRAG---------KVEAQHI---------LASAPTDRNLchfqalgcRTTHSNQEVLQSCLL 83
Cdd:COG0240   2 KIAVLGAGSWGTALAKVLARNGhevtlwgrdPEVAEEInetrenpryLPGVKLPENL--------RATSDLEEALAGADL 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 62896929  84 VIFATKPHVLPAVLAEVAPVVTTEHILVSVAAGVSLST-------LEELLPPNTRV 132
Cdd:COG0240  74 VLLAVPSQALREVLEQLAPLLPPGAPVVSATKGIEPGTgllmsevIAEELPGALRI 129
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 22-123 6.74e-04

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


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 40.18  E-value: 6.74e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62896929  22 RVGFVGAGRMAGAIAQGLIRAGKVEAQhilASAPTDRNLCHFQA-LGCRTTHSNQEVLQSCLLVIFATKPHVLPAVLAEV 100
Cdd:COG5495   5 KIGIIGAGRVGTALAAALRAAGHEVVG---VYSRSPASAERAAAlLGAVPALDLEELAAEADLVLLAVPDDAIAEVAAGL 81

                        90       100
                ....*....|....*....|....*
gi 62896929 101 A--PVVTTEHILVSVAAGVSLSTLE 123
Cdd:COG5495  82 AaaGALRPGQLVVHTSGALGSDVLA 106
 
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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