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Conserved domains on  [gi|501350058|ref|WP_012381693|]
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MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Streptomyces]

Protein Classification

flavin monoamine oxidase family protein( domain architecture ID 11440890)

flavin monoamine oxidase family protein functions as an oxidoreductase that catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant

CATH:  3.50.50.60|1.10.405.10
EC:  1.-.-.-
Gene Ontology:  GO:0000166|GO:0016491
SCOP:  4000128

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
48-540 6.54e-117

Monoamine oxidase [Amino acid transport and metabolism];


:

Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 353.46  E-value: 6.54e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058  48 HGQEVAVIGGGLSGIIAAYELMKMGLKPVVYEA-DRIGGRLRTVGFDgcDPSLTAEMGAMRFPPSSTALQHYIDLVGLET 126
Cdd:COG1231    6 RGKDVVIVGAGLAGLAAARELRKAGLDVTVLEArDRVGGRVWTLRFG--DDGLYAELGAMRIPPSHTNLLALARELGLPL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058 127 RPFPNplspATPSTVVDLKGESHYAETIDDlpqVYRDVAEAWSACLEegadfsDMNRALRerdvprireIWSQLVERLDN 206
Cdd:COG1231   84 EPFPN----ENGNALLYLGGKRVRAGEIAA---DLRGVAELLAKLLR------ALAAALD---------PWAHPAAELDR 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058 207 QTFYGFLCDSDAftSFRHREIFGQVGFGTGGWDTDfPNSILEILRVVYT-EADDHHRGIVGGSQQLPLRLWDREPRKIVh 285
Cdd:COG1231  142 ESLAEWLRRNGA--SPSARRLLGLLGAGEYGADPD-ELSLLDLLRYAASaGGGAQQFRIVGGMDQLPRALAAELGDRIR- 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058 286 wpLGTslsslhggeprgAVTRLTRTaGNRITVTDATGDIRTFRAAVFTGQSWLLlSKIDCDDALfPIDHWTAMERTHYME 365
Cdd:COG1231  218 --LGA------------PVTRIRQD-GDGVTVTTDDGGTVRADAVIVTVPPSVL-RRIEFDPPL-PAAKRAAIQRLPYGA 280

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058 366 SSKLFVPVDRPFWLDKDATTGrdtmsMTLTDRMTRGTYLLDDGPDRPAVICLSYTWCDDSLKWLPLSSKERMEVMLKSLG 445
Cdd:COG1231  281 AIKVFLQFDRPFWEEDGLYGG-----ISLTDLPIRQTWYPSNGPDGGAGVLLGYVGGDDARALAALSPEERVAAALEQLA 355

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058 446 EIYPnvDVRSHIIgNPVTVSWENEPWFMGAFKANLPGHYRYQRRlfthfmqdRLPEDKRGLFLAGDDISW-TAGWAEGAV 524
Cdd:COG1231  356 RIFG--VYAAEPV-DYVSTDWGRDPWSRGAYAAAPPGQLTAAGP--------ALAEPDGRIHFAGEHTSDeWPGWVEGAL 424

                        490
                 ....*....|....*.
gi 501350058 525 QTALNAVWGVMHQFGG 540
Cdd:COG1231  425 ESGERAAAEILARLGG 440
 
Name Accession Description Interval E-value
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
48-540 6.54e-117

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 353.46  E-value: 6.54e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058  48 HGQEVAVIGGGLSGIIAAYELMKMGLKPVVYEA-DRIGGRLRTVGFDgcDPSLTAEMGAMRFPPSSTALQHYIDLVGLET 126
Cdd:COG1231    6 RGKDVVIVGAGLAGLAAARELRKAGLDVTVLEArDRVGGRVWTLRFG--DDGLYAELGAMRIPPSHTNLLALARELGLPL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058 127 RPFPNplspATPSTVVDLKGESHYAETIDDlpqVYRDVAEAWSACLEegadfsDMNRALRerdvprireIWSQLVERLDN 206
Cdd:COG1231   84 EPFPN----ENGNALLYLGGKRVRAGEIAA---DLRGVAELLAKLLR------ALAAALD---------PWAHPAAELDR 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058 207 QTFYGFLCDSDAftSFRHREIFGQVGFGTGGWDTDfPNSILEILRVVYT-EADDHHRGIVGGSQQLPLRLWDREPRKIVh 285
Cdd:COG1231  142 ESLAEWLRRNGA--SPSARRLLGLLGAGEYGADPD-ELSLLDLLRYAASaGGGAQQFRIVGGMDQLPRALAAELGDRIR- 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058 286 wpLGTslsslhggeprgAVTRLTRTaGNRITVTDATGDIRTFRAAVFTGQSWLLlSKIDCDDALfPIDHWTAMERTHYME 365
Cdd:COG1231  218 --LGA------------PVTRIRQD-GDGVTVTTDDGGTVRADAVIVTVPPSVL-RRIEFDPPL-PAAKRAAIQRLPYGA 280

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058 366 SSKLFVPVDRPFWLDKDATTGrdtmsMTLTDRMTRGTYLLDDGPDRPAVICLSYTWCDDSLKWLPLSSKERMEVMLKSLG 445
Cdd:COG1231  281 AIKVFLQFDRPFWEEDGLYGG-----ISLTDLPIRQTWYPSNGPDGGAGVLLGYVGGDDARALAALSPEERVAAALEQLA 355

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058 446 EIYPnvDVRSHIIgNPVTVSWENEPWFMGAFKANLPGHYRYQRRlfthfmqdRLPEDKRGLFLAGDDISW-TAGWAEGAV 524
Cdd:COG1231  356 RIFG--VYAAEPV-DYVSTDWGRDPWSRGAYAAAPPGQLTAAGP--------ALAEPDGRIHFAGEHTSDeWPGWVEGAL 424

                        490
                 ....*....|....*.
gi 501350058 525 QTALNAVWGVMHQFGG 540
Cdd:COG1231  425 ESGERAAAEILARLGG 440
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 59-535 1.05e-51

Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 183.08  E-value: 1.05e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058   59 LSGIIAAYELMKMGLKPVVYEA-DRIGGRLRTVGFDGcdpsLTAEMGAMRFPPSSTALQHYIDLVGLETRPFpnpLSPAT 137
Cdd:pfam01593   1 LAGLAAARELLRAGHDVTVLEArDRVGGRIRTVRDDG----FLIELGAMWFHGAQPPLLALLKELGLEDRLV---LPDPA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058  138 PSTVVDLKGESHYAETIDDLPQVYRDVAEA-----WSACLEEG-ADFSDMNRALRERDVPRIREIWSQLVERldnqtfyg 211
Cdd:pfam01593  74 PFYTVLFAGGRRYPGDFRRVPAGWEGLLEFgrllsIPEKLRLGlAALASDALDEFDLDDFSLAESLLFLGRR-------- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058  212 FLCDSDAFTSFRHREIFGQVGFGTGGWDTDFPNSIL---EILRVVYTEADDHHRGIVGGSQQLPLRLWDREPRKIVHwpL 288
Cdd:pfam01593 146 GPGDVEVWDRLIDPELFAALPFASGAFAGDPSELSAglaLPLLWALLGEGGSLLLPRGGLGALPDALAAQLLGGDVR--L 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058  289 GTSLSSLhggeprgavtrltRTAGNRITVTDATGDIRTFRAAVFTGQSWLLlsKIDCDDALFPIDHWTAMERTHYMESSK 368
Cdd:pfam01593 224 NTRVRSI-------------DREGDGVTVTLTDGEVIEADAVIVTVPLGVL--KRILFTPPLPPEKARAIRNLGYGPVNK 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058  369 LFVPVDRPFWLDKD-------ATTGRDTMSMTLTDRMTRgtyllddgPDRPAVICLSYTWCDDSL-KWLPLSSKERMEVM 440
Cdd:pfam01593 289 VHLEFDRKFWPDLGllgllseLLTGLGTAFSWLTFPNRA--------PPGKGLLLLVYVGPGDRArELEGLSDEELLQAV 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058  441 LKSLGEIYPNVDVRSHIIgnpVTVSWENEPWFMGAFKAN--LPGHYRYQRRLFTHFmqdrlpedkRGLFLAGDDISWT-A 517
Cdd:pfam01593 361 LRDLRKLFGEEAPEPLRV---LVSDWHTDPWPRGSYSLPqyGPGHDDYRPLARTPD---------PGLFFAGEHTSTGyP 428

                         490
                  ....*....|....*...
gi 501350058  518 GWAEGAVQTALNAVWGVM 535
Cdd:pfam01593 429 GTVEGAIESGRRAARAVL 446
PLN02576 PLN02576
protoporphyrinogen oxidase
 41-135 3.48e-09

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 59.26  E-value: 3.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058  41 GQIPATEHGQEVAVIGGGLSGIIAAYELM-KMGLKPVVYEA-DRIGGRLRTVGFDGcdpsLTAEMGAMRFPPSSTALQHY 118
Cdd:PLN02576   4 AEGSAAASSKDVAVVGAGVSGLAAAYALAsKHGVNVLVTEArDRVGGNITSVSEDG----FIWEEGPNSFQPSDPELTSA 79

                         90
                 ....*....|....*...
gi 501350058 119 IDLvGL-ETRPFPNPLSP 135
Cdd:PLN02576  80 VDS-GLrDDLVFPDPQAP 96
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 51-125 8.56e-06

protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 213540 [Multi-domain]  Cd Length: 462  Bit Score: 48.29  E-value: 8.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058   51 EVAVIGGGLSGIIAAYELMK----MGLKPVVYEA-DRIGGRLRTVGFDGcdpsLTAEMGAMRFPPSSTALQHYIDLVGLE 125
Cdd:TIGR00562   4 HVVIIGGGISGLCAAYYLEKeipeLPVELTLVEAsDRVGGKIQTVKEDG----YLIERGPDSFLERKKSAPDLVKDLGLE 79
 
Name Accession Description Interval E-value
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
48-540 6.54e-117

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 353.46  E-value: 6.54e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058  48 HGQEVAVIGGGLSGIIAAYELMKMGLKPVVYEA-DRIGGRLRTVGFDgcDPSLTAEMGAMRFPPSSTALQHYIDLVGLET 126
Cdd:COG1231    6 RGKDVVIVGAGLAGLAAARELRKAGLDVTVLEArDRVGGRVWTLRFG--DDGLYAELGAMRIPPSHTNLLALARELGLPL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058 127 RPFPNplspATPSTVVDLKGESHYAETIDDlpqVYRDVAEAWSACLEegadfsDMNRALRerdvprireIWSQLVERLDN 206
Cdd:COG1231   84 EPFPN----ENGNALLYLGGKRVRAGEIAA---DLRGVAELLAKLLR------ALAAALD---------PWAHPAAELDR 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058 207 QTFYGFLCDSDAftSFRHREIFGQVGFGTGGWDTDfPNSILEILRVVYT-EADDHHRGIVGGSQQLPLRLWDREPRKIVh 285
Cdd:COG1231  142 ESLAEWLRRNGA--SPSARRLLGLLGAGEYGADPD-ELSLLDLLRYAASaGGGAQQFRIVGGMDQLPRALAAELGDRIR- 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058 286 wpLGTslsslhggeprgAVTRLTRTaGNRITVTDATGDIRTFRAAVFTGQSWLLlSKIDCDDALfPIDHWTAMERTHYME 365
Cdd:COG1231  218 --LGA------------PVTRIRQD-GDGVTVTTDDGGTVRADAVIVTVPPSVL-RRIEFDPPL-PAAKRAAIQRLPYGA 280

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058 366 SSKLFVPVDRPFWLDKDATTGrdtmsMTLTDRMTRGTYLLDDGPDRPAVICLSYTWCDDSLKWLPLSSKERMEVMLKSLG 445
Cdd:COG1231  281 AIKVFLQFDRPFWEEDGLYGG-----ISLTDLPIRQTWYPSNGPDGGAGVLLGYVGGDDARALAALSPEERVAAALEQLA 355

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058 446 EIYPnvDVRSHIIgNPVTVSWENEPWFMGAFKANLPGHYRYQRRlfthfmqdRLPEDKRGLFLAGDDISW-TAGWAEGAV 524
Cdd:COG1231  356 RIFG--VYAAEPV-DYVSTDWGRDPWSRGAYAAAPPGQLTAAGP--------ALAEPDGRIHFAGEHTSDeWPGWVEGAL 424

                        490
                 ....*....|....*.
gi 501350058 525 QTALNAVWGVMHQFGG 540
Cdd:COG1231  425 ESGERAAAEILARLGG 440
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 59-535 1.05e-51

Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 183.08  E-value: 1.05e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058   59 LSGIIAAYELMKMGLKPVVYEA-DRIGGRLRTVGFDGcdpsLTAEMGAMRFPPSSTALQHYIDLVGLETRPFpnpLSPAT 137
Cdd:pfam01593   1 LAGLAAARELLRAGHDVTVLEArDRVGGRIRTVRDDG----FLIELGAMWFHGAQPPLLALLKELGLEDRLV---LPDPA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058  138 PSTVVDLKGESHYAETIDDLPQVYRDVAEA-----WSACLEEG-ADFSDMNRALRERDVPRIREIWSQLVERldnqtfyg 211
Cdd:pfam01593  74 PFYTVLFAGGRRYPGDFRRVPAGWEGLLEFgrllsIPEKLRLGlAALASDALDEFDLDDFSLAESLLFLGRR-------- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058  212 FLCDSDAFTSFRHREIFGQVGFGTGGWDTDFPNSIL---EILRVVYTEADDHHRGIVGGSQQLPLRLWDREPRKIVHwpL 288
Cdd:pfam01593 146 GPGDVEVWDRLIDPELFAALPFASGAFAGDPSELSAglaLPLLWALLGEGGSLLLPRGGLGALPDALAAQLLGGDVR--L 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058  289 GTSLSSLhggeprgavtrltRTAGNRITVTDATGDIRTFRAAVFTGQSWLLlsKIDCDDALFPIDHWTAMERTHYMESSK 368
Cdd:pfam01593 224 NTRVRSI-------------DREGDGVTVTLTDGEVIEADAVIVTVPLGVL--KRILFTPPLPPEKARAIRNLGYGPVNK 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058  369 LFVPVDRPFWLDKD-------ATTGRDTMSMTLTDRMTRgtyllddgPDRPAVICLSYTWCDDSL-KWLPLSSKERMEVM 440
Cdd:pfam01593 289 VHLEFDRKFWPDLGllgllseLLTGLGTAFSWLTFPNRA--------PPGKGLLLLVYVGPGDRArELEGLSDEELLQAV 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058  441 LKSLGEIYPNVDVRSHIIgnpVTVSWENEPWFMGAFKAN--LPGHYRYQRRLFTHFmqdrlpedkRGLFLAGDDISWT-A 517
Cdd:pfam01593 361 LRDLRKLFGEEAPEPLRV---LVSDWHTDPWPRGSYSLPqyGPGHDDYRPLARTPD---------PGLFFAGEHTSTGyP 428

                         490
                  ....*....|....*...
gi 501350058  518 GWAEGAVQTALNAVWGVM 535
Cdd:pfam01593 429 GTVEGAIESGRRAARAVL 446
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 52-127 2.19e-11

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 66.01  E-value: 2.19e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501350058  52 VAVIGGGLSGIIAAYELMKMGLKPVVYEA-DRIGGRLRTVGFDGcdpsLTAEMGAMRFPPSSTALQHYIDLVGLETR 127
Cdd:COG1232    4 VAVIGGGIAGLTAAYRLAKAGHEVTVLEAsDRVGGLIRTVEVDG----FRIDRGPHSFLTRDPEVLELLRELGLGDE 76
PLN02576 PLN02576
protoporphyrinogen oxidase
 41-135 3.48e-09

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 59.26  E-value: 3.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058  41 GQIPATEHGQEVAVIGGGLSGIIAAYELM-KMGLKPVVYEA-DRIGGRLRTVGFDGcdpsLTAEMGAMRFPPSSTALQHY 118
Cdd:PLN02576   4 AEGSAAASSKDVAVVGAGVSGLAAAYALAsKHGVNVLVTEArDRVGGNITSVSEDG----FIWEEGPNSFQPSDPELTSA 79

                         90
                 ....*....|....*...
gi 501350058 119 IDLvGL-ETRPFPNPLSP 135
Cdd:PLN02576  80 VDS-GLrDDLVFPDPQAP 96
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 28-88 1.37e-08

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 57.07  E-value: 1.37e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501350058  28 YAYDDFLAHPAGLGQIPATEHGQEVAVIGGGLSGIIAAYELMKMGLKPVVYEA-DRIGGRLR 88
Cdd:COG0493  100 FIADKAFEEGWVKPPPPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEAlDKPGGLLR 161
PRK07208 PRK07208
hypothetical protein; Provisional
 47-94 2.99e-08

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 56.44  E-value: 2.99e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 501350058  47 EHGQEVAVIGGGLSGIIAAYELMKMGLKPVVYEAD-RIGGRLRTVGFDG 94
Cdd:PRK07208   2 TNKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADpVVGGISRTVTYKG 50
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 52-130 9.83e-08

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 54.47  E-value: 9.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058  52 VAVIGGGLSGIIAAYELMKMGLKP--VVYEA-DRIGGRLRTVGFDGcdpsLTAEMGAMRF---PPSSTAL---------- 115
Cdd:PRK11883   3 VAIIGGGITGLSAAYRLHKKGPDAdiTLLEAsDRLGGKIQTVRKDG----FPIELGPESFlarKPSAPALvkelgledel 78

                         90       100
                 ....*....|....*....|.
gi 501350058 116 ------QHYIdLVGLETRPFP 130
Cdd:PRK11883  79 vanttgQSYI-YVNGKLHPIP 98
PRK07233 PRK07233
hypothetical protein; Provisional
 52-94 2.16e-07

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 53.35  E-value: 2.16e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 501350058  52 VAVIGGGLSGIIAAYELMKMGLKPVVYEAD-RIGGRLRTVGFDG 94
Cdd:PRK07233   2 IAIVGGGIAGLAAAYRLAKRGHEVTVFEADdQLGGLAASFEFGG 45
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 28-88 2.92e-07

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 52.87  E-value: 2.92e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501350058  28 YAYDDFLAHPAGLGQiPATEHGQEVAVIGGGLSGIIAAYELMKMGLKPVVYEA-DRIGGRLR 88
Cdd:PRK11749 120 YITDWAMETGWVLFK-RAPKTGKKVAVIGAGPAGLTAAHRLARKGYDVTIFEArDKAGGLLR 180
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
54-120 3.07e-07

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 47.53  E-value: 3.07e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501350058   54 VIGGGLSGIIAAYELMKMGLKPVVYEA-DRIGGRLRTVGFDGCdpslTAEMGAMRFPPSS-TALQHYID 120
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKrDRLGGNAYSYRVPGY----VFDYGAHIFHGSDePNVRDLLD 65
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 52-511 1.02e-06

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 51.39  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058  52 VAVIGGGLSGIIAAYELMKMGLKPVVYEA-DRIGGRLRTVGFDGcdpsLTAEMGAMRFPPsSTALQHYIDLVGLETRPfp 130
Cdd:COG1233    6 VVVIGAGIGGLAAAALLARAGYRVTVLEKnDTPGGRARTFERPG----FRFDVGPSVLTM-PGVLERLFRELGLEDYL-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058 131 nPLSPATPSTVVDLKGESHY------AETIDDLPQVYRDVAEAWSACLEEGADFSDM-NRALRERDVPRIREIWSQLVE- 202
Cdd:COG1233   79 -ELVPLDPAYRVPFPDGRALdlprdlERTAAELERLFPGDAEAYRRFLAELRRLYDAlLEDLLYRPLLSLRDLLRPLALa 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058 203 ---RLDNQTFYGFLcdSDAFTSFRHREIF-GQVGF-GTGGWDTDFPNSILeilrvVYTEaddHHRGI---VGGSQQLPLR 274
Cdd:COG1233  158 rllRLLLRSLRDLL--RRYFKDPRLRALLaGQALYlGLSPDRTPALYALI-----AYLE---YAGGVwypKGGMGALADA 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058 275 LWDReprkIVHwplgtslsslHGGEPR-GA-VTRLTrTAGNRIT-VTDATGDIRTFRAAVFTGQSWLLLSKIdCDDALFP 351
Cdd:COG1233  228 LARL----AEE----------LGGEIRtGAeVERIL-VEGGRATgVRLADGEEIRADAVVSNADPAHTYLRL-LGEEALP 291

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058 352 IDHWTAMERTHYMESS-KLFVPVDRP--------FWLDKD-ATTGRDTMSMTLTDRMTrgTYL-----LDDG---PDRPA 413
Cdd:COG1233  292 ARYRRRLERFRYSPSAfKLYLGLDGPlpglahhtIHLSEDyEAAFDDIFRGRLPEDPS--LYVsipslTDPSlapEGKHT 369

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058 414 VICLSYTWCDDSLKWLPLssKERM-EVMLKSLGEIYPnvDVRSHI----IGNPVTV------------SWENEPWFMGAF 476
Cdd:COG1233  370 LWVLVPVPYGLEDAWDEL--KEEYaERILARLERYAP--GLRDRIvareVLTPLDFerylnlvggaiyGGAHTLDQSAFF 445

                        490       500       510
                 ....*....|....*....|....*....|....*
gi 501350058 477 KanlPGHYRyqrrlfthfmqdrlpEDKRGLFLAGD 511
Cdd:COG1233  446 R---PSNYR---------------TPIPGLYLVGA 462
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 42-88 1.55e-06

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 50.93  E-value: 1.55e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 501350058  42 QIPATEHGQEVAVIGGGLSGIIAAYELMKMGLKPVVYE-ADRIGGRLR 88
Cdd:PRK12810 136 DPPVKRTGKKVAVVGSGPAGLAAADQLARAGHKVTVFErADRIGGLLR 183
PLN03000 PLN03000
amine oxidase
 28-104 3.52e-06

amine oxidase


Pssm-ID: 178578 [Multi-domain]  Cd Length: 881  Bit Score: 50.02  E-value: 3.52e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501350058  28 YAYDDFLAHPAGLGQIPATEHGQEVAVIGGGLSGIIAAYELMKMGLKPVVYEA-DRIGGRLRTVGFDGCDPSLTAEMG 104
Cdd:PLN03000 163 HGYINFGIAQAIKDKFPAQSSKSSVVIVGAGLSGLAAARQLMRFGFKVTVLEGrKRPGGRVYTKKMEANRVGAAADLG 240
PLN02328 PLN02328
lysine-specific histone demethylase 1 homolog
 29-104 4.97e-06

lysine-specific histone demethylase 1 homolog


Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 49.61  E-value: 4.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058  29 AYDDFLAHP-AGLGQIPATEHGQ----------EVAVIGGGLSGIIAAYELMKMGLKPVVYEA-DRIGGRLRTVGFDGCD 96
Cdd:PLN02328 207 AYNFLLEHGyINFGVAPVIKEAQlrsfegvepaNVVVVGAGLAGLVAARQLLSMGFKVVVLEGrARPGGRVKTMKMKGDG 286


                 ....*...
gi 501350058  97 PSLTAEMG 104
Cdd:PLN02328 287 VVAAADLG 294
PLN02676 PLN02676
polyamine oxidase
 52-105 7.10e-06

polyamine oxidase


Pssm-ID: 215362 [Multi-domain]  Cd Length: 487  Bit Score: 48.56  E-value: 7.10e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 501350058  52 VAVIGGGLSGIIAAYELMKMGLKPVV-YEA-DRIGGRLRTVGFDGcdpsLTAEMGA 105
Cdd:PLN02676  29 VIIVGAGMSGISAAKTLSEAGIEDILiLEAtDRIGGRMRKANFAG----VSVELGA 80
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 51-125 8.56e-06

protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 213540 [Multi-domain]  Cd Length: 462  Bit Score: 48.29  E-value: 8.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501350058   51 EVAVIGGGLSGIIAAYELMK----MGLKPVVYEA-DRIGGRLRTVGFDGcdpsLTAEMGAMRFPPSSTALQHYIDLVGLE 125
Cdd:TIGR00562   4 HVVIIGGGISGLCAAYYLEKeipeLPVELTLVEAsDRVGGKIQTVKEDG----YLIERGPDSFLERKKSAPDLVKDLGLE 79
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 51-85 9.14e-06

Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];


Pssm-ID: 441675 [Multi-domain]  Cd Length: 414  Bit Score: 48.32  E-value: 9.14e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 501350058  51 EVAVIGGGLSGIIAAYELMKMGLKPVVYE-ADRIGG 85
Cdd:COG2072    8 DVVVIGAGQAGLAAAYHLRRAGIDFVVLEkADDVGG 43
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 52-125 2.57e-05

Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];


Pssm-ID: 442577 [Multi-domain]  Cd Length: 445  Bit Score: 46.77  E-value: 2.57e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501350058  52 VAVIGGGLSGIIAAYELMKMGLKPVVYEA-DRIGGRLRTVGFDGCDpsLTAEMGAMRFPPSSTALQHYIDLVGLE 125
Cdd:COG3349    6 VVVVGGGLAGLAAAVELAEAGFRVTLLEArPRLGGRARSFPDPDTG--LPIDNGQHVLLGCYRNTLDLLRRIGAA 78
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
51-89 2.90e-05

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 46.27  E-value: 2.90e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 501350058  51 EVAVIGGGLSGIIAAYELMKMGLKPVVYEADRIGGRLRT 89
Cdd:COG0492    2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLAT 40
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
52-85 4.36e-05

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 46.05  E-value: 4.36e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 501350058  52 VAVIGGGLSGIIAAYELMKMGLKPVVYEADRIGG 85
Cdd:COG0665    5 VVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGS 38
PLN02268 PLN02268
probable polyamine oxidase
 52-89 8.32e-05

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 45.06  E-value: 8.32e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 501350058  52 VAVIGGGLSGIIAAYELMKMGLKPVVYEA-DRIGGRLRT 89
Cdd:PLN02268   3 VIVIGGGIAGIAAARALHDASFKVTLLESrDRIGGRVHT 41
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
50-98 8.57e-05

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 45.24  E-value: 8.57e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 501350058  50 QEVAVIGGGLSGIIAAYELMKMGLKPVVYE-ADRIGGRLRTVG--FDGCDPS 98
Cdd:COG1148  141 KRALVIGGGIAGMTAALELAEQGYEVYLVEkEPELGGRAAQLHktFPGLDCP 192
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 43-88 1.23e-04

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 44.87  E-value: 1.23e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 501350058  43 IPATEHGQEVAVIGGGLSGIIAAYELMKMGLKPVVYEA-DRIGGRLR 88
Cdd:PRK12771 131 APAPDTGKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAgPKLGGMMR 177
PRK13984 PRK13984
putative oxidoreductase; Provisional
 43-88 5.41e-04

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 42.83  E-value: 5.41e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 501350058  43 IPATEHGQEVAVIGGGLSGIIAAYELMKMGLKPVVYEA-DRIGGRLR 88
Cdd:PRK13984 277 DEPEKKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESlSKPGGVMR 323
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 51-85 1.05e-03

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 41.61  E-value: 1.05e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 501350058   51 EVAVIGGGLSGIIAAYELMKMGLKPVVYEADRIGG 85
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPG 35
PRK12831 PRK12831
putative oxidoreductase; Provisional
 44-80 1.23e-03

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 41.54  E-value: 1.23e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 501350058  44 PATEHGQEVAVIGGGLSGIIAAYELMKMGLKPVVYEA 80
Cdd:PRK12831 135 TEEKKGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEA 171
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
45-106 1.27e-03

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 41.28  E-value: 1.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501350058  45 ATEHGQEVAVIGGGLSGIIAAYELMKMGLKPVVYE-ADRIGGRLrtvgfdgcdpsLTAEMGAM 106
Cdd:COG1251  138 ALAPGKRVVVIGGGLIGLEAAAALRKRGLEVTVVErAPRLLPRQ-----------LDEEAGAL 189
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 44-88 2.14e-03

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 40.87  E-value: 2.14e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 501350058  44 PATEHGQEVAVIGGGLSGIIAAYELMKMGLKPVVYEA-DRIGGRLR 88
Cdd:PRK12814 188 RAPKSGKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDAnEQAGGMMR 233
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 52-98 2.91e-03

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 40.46  E-value: 2.91e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 501350058  52 VAVIGGGLSGIIAAYELMKMGLKPVVYEADRIGGR-LRTvgfdGCDPS 98
Cdd:COG1249    6 LVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGTcLNV----GCIPS 49
GIDA pfam01134
Glucose inhibited division protein A;
52-106 3.26e-03

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 39.84  E-value: 3.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501350058   52 VAVIGGGLSGIIAAYELMKMGLKPVVyeadrIGGRLRTVGFDGCDPS--------LTAEMGAM 106
Cdd:pfam01134   2 VIVIGGGHAGCEAALAAARMGAKVLL-----ITHNTDTIAELSCNPSiggiakghLVREIDAL 59
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 44-81 7.15e-03

bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;


Pssm-ID: 234978 [Multi-domain]  Cd Length: 662  Bit Score: 39.06  E-value: 7.15e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 501350058  44 PATEHGQEVAVIGGGLSGIIAAYELMKMGLKPVVYEAD 81
Cdd:PRK01747 255 PGSPKARDAAIIGGGIAGAALALALARRGWQVTLYEAD 292
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 50-79 7.55e-03

tRNA (uracil-5-)-methyltransferase Gid; Reviewed


Pssm-ID: 235416  Cd Length: 436  Bit Score: 38.97  E-value: 7.55e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 501350058  50 QEVAVIGGGLSGIIAAYELMKMGLKPVVYE 79
Cdd:PRK05335   3 KPVNVIGAGLAGSEAAWQLAKRGVPVELYE 32
 
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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