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Conserved domains on  [gi|1622824789|ref|XP_028689944|]
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pyrroline-5-carboxylate reductase 2 isoform X1 [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]; ...
 10-232 2.19e-90

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: 268.86  E-value: 2.19e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789  10 RKMGVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKklmAFQPAPKVIRCMTNTP 89
Cdd:COG0345    46 ERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVLEELAPLLDPDKLVISIAAGVTLATLEE---ALGGGAPVVRAMPNTP 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789  90 VVVREGATVYAMGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAFMALDALADGGVKMGLPRRLAVRL 169
Cdd:COG0345   123 ALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETAREL 202

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622824789 170 GAQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIHALHFLESGGFRSLLINAVEASCIRTREL 232
Cdd:COG0345   203 AAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTIAGLKVLEEGGLRAAVIEAVEAAAERSKEL 265
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 10-232 2.19e-90

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: 268.86  E-value: 2.19e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789  10 RKMGVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKklmAFQPAPKVIRCMTNTP 89
Cdd:COG0345    46 ERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVLEELAPLLDPDKLVISIAAGVTLATLEE---ALGGGAPVVRAMPNTP 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789  90 VVVREGATVYAMGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAFMALDALADGGVKMGLPRRLAVRL 169
Cdd:COG0345   123 ALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETAREL 202

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622824789 170 GAQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIHALHFLESGGFRSLLINAVEASCIRTREL 232
Cdd:COG0345   203 AAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTIAGLKVLEEGGLRAAVIEAVEAAAERSKEL 265
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 2-232 1.14e-84

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 254.50  E-value: 1.14e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789   2 NLPTVSALRKMGVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLmafqPAPKV 81
Cdd:PLN02688   37 NPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLTELRPLLSKDKLLVSVAAGITLADLQEWA----GGRRV 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789  82 IRCMTNTPVVVREGATVYAMGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAFMALDALADGGVKMGL 161
Cdd:PLN02688  113 VRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIWVVDEKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGL 192

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622824789 162 PRRLAVRLGAQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIHALHFLESGGFRSLLINAVEASCIRTREL 232
Cdd:PLN02688  193 PRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIAGVHELEKGGFRAALMNAVVAAAKRSREL 263
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 11-231 1.78e-82

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: 248.33  E-value: 1.78e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789  11 KMGVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLMAFQPapkVIRCMTNTPV 90
Cdd:TIGR00112  28 ELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLLGGTRR---VVRVMPNTPA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789  91 VVREGATVYAMGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAFMALDALADGGVKMGLPRRLAVRLG 170
Cdd:TIGR00112 105 KVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEALADAGVKQGLPRELALELA 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622824789 171 AQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIHALHFLESGGFRSLLINAVEASCIRTRE 231
Cdd:TIGR00112 185 AQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAVRRSRE 245
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 128-231 1.68e-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: 1.68e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789 128 EDLIDAVTGLSGSGPAYAFMALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIHALH 207
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80

                          90       100
                  ....*....|....*....|....
gi 1622824789 208 FLESGGFRSLLINAVEASCIRTRE 231
Cdd:pfam14748  81 VLEEGGFRGAVIEAVEAATKRAKE 104
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 10-232 2.19e-90

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: 268.86  E-value: 2.19e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789  10 RKMGVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKklmAFQPAPKVIRCMTNTP 89
Cdd:COG0345    46 ERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVLEELAPLLDPDKLVISIAAGVTLATLEE---ALGGGAPVVRAMPNTP 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789  90 VVVREGATVYAMGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAFMALDALADGGVKMGLPRRLAVRL 169
Cdd:COG0345   123 ALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETAREL 202

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622824789 170 GAQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIHALHFLESGGFRSLLINAVEASCIRTREL 232
Cdd:COG0345   203 AAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTIAGLKVLEEGGLRAAVIEAVEAAAERSKEL 265
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 2-232 1.14e-84

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 254.50  E-value: 1.14e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789   2 NLPTVSALRKMGVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLmafqPAPKV 81
Cdd:PLN02688   37 NPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLTELRPLLSKDKLLVSVAAGITLADLQEWA----GGRRV 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789  82 IRCMTNTPVVVREGATVYAMGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAFMALDALADGGVKMGL 161
Cdd:PLN02688  113 VRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIWVVDEKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGL 192

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622824789 162 PRRLAVRLGAQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIHALHFLESGGFRSLLINAVEASCIRTREL 232
Cdd:PLN02688  193 PRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIAGVHELEKGGFRAALMNAVVAAAKRSREL 263
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 11-231 1.78e-82

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: 248.33  E-value: 1.78e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789  11 KMGVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLMAFQPapkVIRCMTNTPV 90
Cdd:TIGR00112  28 ELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLLGGTRR---VVRVMPNTPA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789  91 VVREGATVYAMGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAFMALDALADGGVKMGLPRRLAVRLG 170
Cdd:TIGR00112 105 KVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEALADAGVKQGLPRELALELA 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622824789 171 AQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIHALHFLESGGFRSLLINAVEASCIRTRE 231
Cdd:TIGR00112 185 AQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAVRRSRE 245
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 8-232 1.47e-77

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 236.58  E-value: 1.47e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789   8 ALRKMGVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIGAdvQARHIVVSCAAGVTISSVEKKLMAFQPapkVIRCMTN 87
Cdd:PRK11880   44 LAEEYGVRAATDNQEAAQEADVVVLAVKPQVMEEVLSELKG--QLDKLVVSIAAGVTLARLERLLGADLP---VVRAMPN 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789  88 TPVVVREGATVYAMGTHALVEDGQLLEQLMSSVGFCTEVE-EDLIDAVTGLSGSGPAYAFMALDALADGGVKMGLPRRLA 166
Cdd:PRK11880  119 TPALVGAGMTALTANALVSAEDRELVENLLSAFGKVVWVDdEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQA 198

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622824789 167 VRLGAQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIHALHFLESGGFRSLLINAVEASCIRTREL 232
Cdd:PRK11880  199 RKLAAQTVLGAAKLLLESGEHPAELRDNVTSPGGTTIAALRVLEEKGLRAAVIEAVQAAAKRSKEL 264
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 128-231 1.68e-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: 1.68e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789 128 EDLIDAVTGLSGSGPAYAFMALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIHALH 207
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80

                          90       100
                  ....*....|....*....|....
gi 1622824789 208 FLESGGFRSLLINAVEASCIRTRE 231
Cdd:pfam14748  81 VLEEGGFRGAVIEAVEAATKRAKE 104
PTZ00431 PTZ00431
pyrroline carboxylate reductase; Provisional
 15-232 1.02e-45

pyrroline carboxylate reductase; Provisional


Pssm-ID: 173621 [Multi-domain]  Cd Length: 260  Bit Score: 154.72  E-value: 1.02e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789  15 NLTRSNKETVKHSDVLFLAVKPHIIPFILDEIgADVQARHIVVSCAAGVTISSVEKklMAFQPApKVIRCMTNTPVVVRE 94
Cdd:PTZ00431   46 VYLQSNEELAKTCDIIVLAVKPDLAGKVLLEI-KPYLGSKLLISICGGLNLKTLEE--MVGVEA-KIVRVMPNTPSLVGQ 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789  95 GATVYAMGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAFMALDALADGGVKMGLPRRLAVRLGAQAL 174
Cdd:PTZ00431  122 GSLVFCANNNVDSTDKKKVIDIFSACGIIQEIKEKDMDIATAISGCGPAYVFLFIESLIDAGVKNGLNRDVSKNLVLQTI 201

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622824789 175 LGAAKMLLDSEQHPCQLKDNVCSPGGATIHALHFLESGGFRSLLINAVEASCIRTREL 232
Cdd:PTZ00431  202 LGSVHMVKASDQPVQQLKDDVCSPGGITIVGLYTLEKHAFKYTVMDAVESACQKSKSM 259
PRK07679 PRK07679
pyrroline-5-carboxylate reductase; Reviewed
 10-238 8.40e-43

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 181079 [Multi-domain]  Cd Length: 279  Bit Score: 147.61  E-value: 8.40e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789  10 RKMGVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLMAFQPapkVIRCMTNTP 89
Cdd:PRK07679   49 QKYGVKGTHNKKELLTDANILFLAMKPKDVAEALIPFKEYIHNNQLIISLLAGVSTHSIRNLLQKDVP---IIRAMPNTS 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789  90 VVVREGATVYAMGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAFMALDALADGGVKMGLPRRLAVRL 169
Cdd:PRK07679  126 AAILKSATAISPSKHATAEHIQTAKALFETIGLVSVVEEEDMHAVTALSGSGPAYIYYVVEAMEKAAKKIGLKEDVAKSL 205

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622824789 170 GAQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIHALHFLESGGFRSLLINAVEASCIRTRELQSMADQ 238
Cdd:PRK07679  206 ILQTMIGAAEMLKASEKHPSILRKEITSPGGTTEAGIEVLQEHRFQQALISCITQATQRSHNLGKTLEQ 274
PRK07680 PRK07680
late competence protein ComER; Validated
 13-218 4.92e-19

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 84.25  E-value: 4.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789  13 GVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLmafqP--APKVIRCMTNTpv 90
Cdd:PRK07680   49 GIHVAKTIEEVISQSDLIFICVKPLDIYPLLQKLAPHLTDEHCLVSITSPISVEQLETLV----PcqVARIIPSITNR-- 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789  91 vVREGATVYAMGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAFMALDALADGGVKM-GLPRRLAVRL 169
Cdd:PRK07680  123 -ALSGASLFTFGSRCSEEDQQKLERLFSNISTPLVIEEDITRVSSDIVSCGPAFFSYLLQRFIDAAVEEtNISKEEATTL 201

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622824789 170 GAQALLGAAKmLLDSEQH-PCQLKDNVCSPGGATIHALHFLES---GGFRSLL 218
Cdd:PRK07680  202 ASEMLIGMGK-LLEKGLYtLPTLQEKVCVKGGITGEGIKVLEEevgDMFHRLF 253
PRK06928 PRK06928
pyrroline-5-carboxylate reductase; Reviewed
 14-202 6.20e-10

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235888 [Multi-domain]  Cd Length: 277  Bit Score: 58.63  E-value: 6.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789  14 VNLTRSNKETVKHSDVLFLAVKP-HIIPfILDEIGADVQARHIVVSCAAGVTISsvekKLMAFQPAPKVIRCMTNTPVVV 92
Cdd:PRK06928   52 VELADNEAEIFTKCDHSFICVPPlAVLP-LLKDCAPVLTPDRHVVSIAAGVSLD----DLLEITPGLQVSRLIPSLTSAV 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789  93 REGATVYAMGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAFMALDALADGGVKMG-LPRRLAVRLGA 171
Cdd:PRK06928  127 GVGTSLVAHAETVNEANKSRLEETLSHFSHVMTIREENMDIASNLTSSSPGFIAAIFEEFAEAAVRNSsLSDEEAFQFLN 206

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622824789 172 QALLGAAKMLLDSEQHPCQLKDNVCSPGGAT 202
Cdd:PRK06928  207 FALAGTGKLLVEEDYTFSGTIERVATKGGIT 237
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
7-62 1.99e-09

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 53.77  E-value: 1.99e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622824789   7 SALRKMGVNLT-RSNKETVKHSDVLFLAVKPHIIPFILDEIgADVQARHIVVSCAAG 62
Cdd:pfam03807  37 ELAEEYGVGATaVDNEEAAEEADVVFLAVKPEDAPDVLSEL-SDLLKGKIVISIAAG 92
PRK06476 PRK06476
pyrroline-5-carboxylate reductase; Reviewed
 14-230 3.68e-07

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235812 [Multi-domain]  Cd Length: 258  Bit Score: 50.02  E-value: 3.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789  14 VNLTRSNKETVKHSDVLFLAVKPhiipfildEIGADV------QARHIVVSCAAGVTISSVEKklmAFQPAPKVIRCMTN 87
Cdd:PRK06476   49 VRIAKDNQAVVDRSDVVFLAVRP--------QIAEEVlralrfRPGQTVISVIAATDRAALLE---WIGHDVKLVRAIPL 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824789  88 TPVVVREGAT-VYAmgTHALVEDgqLLEQLMSSVGFCTEVEEDLIDAVTGLsgSGPAYAFMalDALADGGVKMGLPRRLA 166
Cdd:PRK06476  118 PFVAERKGVTaIYP--PDPFVAA--LFDALGTAVECDSEEEYDLLAAASAL--MATYFGIL--ETATGWLEEQGLKRQKA 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622824789 167 VRLGAQALLGAAKMLLDSEQHP-CQLKDNVCSPGGATIHALHFLESGGFRSLLINAVEASCIRTR 230
Cdd:PRK06476  190 RAYLAPLFASLAQDAVRSTKTDfSALSREFSTKGGLNEQVLNDFSRQGGYAALTDALDRVLRRIN 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.
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