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Conserved domains on  [gi|21356479|ref|NP_649194|]
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suppressor of variegation 3-3, isoform A [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN03000 super family cl31963
amine oxidase
74-827 3.25e-114

amine oxidase


The actual alignment was detected with superfamily member PLN03000:

Pssm-ID: 178578 [Multi-domain]  Cd Length: 881  Bit Score: 370.12  E-value: 3.25e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   74 RRNRPKVDYSNRPS------GSGDTASNDKSGSASmgpnnqqaerRSQSQTRKSEANATSSSVSGPSAGNSRPSQNgdsk 147
Cdd:PLN03000  11 RRGRSQRSASSLNSlpvpnvGTLPGNTNFVSSSAS----------SSGRFNVESVNGSNQTTKSYPGIGDEIITIN---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  148 dRDAGTPTVLSGQEGavfqsrLPFNKMTpNEEACFPDISRSGILGHRVFLNIRNSLLHMWVDNPKIQLSFEIALKNLPPP 227
Cdd:PLN03000  77 -KEATTEALLALTAG------FPADSLT-EEEIEFGVVPIVGGIEQVNYILIRNHIISKWRENISSWVTKEMFLGSIPKH 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  228 FDSepsLVRRVHSFLERHGFINFGIFKRLK-PIPAK-KLGKVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRIST 305
Cdd:PLN03000 149 CSS---LLDSAYNYLVTHGYINFGIAQAIKdKFPAQsSKSSVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGGRVYT 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  306 FR----KNSYIADVGAMVVTGVYGNPMTILSKQIGMDLVPIQQTCPLYGPDGKPVPKEKDDVIEREFNRLLESASYLSHR 381
Cdd:PLN03000 226 KKmeanRVGAAADLGGSVLTGTLGNPLGIIARQLGSSLYKVRDKCPLYRVDGKPVDPDVDLKVEVAFNQLLDKASKLRQL 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  382 LdfnyaGDCP--VSLGDALEwiismqemqvmhkrgqhmqeiiatqtkiieqrrrlkTLRDTIGklknehlaminqrkpkg 459
Cdd:PLN03000 306 M-----GDVSmdVSLGAALE------------------------------------TFRQVSG----------------- 327
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  460 tdgdlkycyqefnirntqikmeetistfHDLHAEEKQMLaklheleqnrpsdvylssrdrlilDWHFANLEFANATRLNN 539
Cdd:PLN03000 328 ----------------------------NDVATEEMGLF------------------------NWHLANLEYANAGLVSK 355
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  540 LSLKHWDQDDDFEFIGHHTTVRNGYSCVPVALTENLDIRVNSAVKEIKYGTKGVEVVAENlktsnsqMTYKADLVVCTLT 619
Cdd:PLN03000 356 LSLAFWDQDDPYDMGGDHCFLPGGNGRLVQALAENVPILYEKTVQTIRYGSNGVKVIAGN-------QVYEGDMVLCTVP 428
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  620 LGVLKvavahkesqqSNTVKFDPPLPDWKQQAIKRLGFGNLNKVVLCFDRIFWDPNANLFGHVGSTTASRGEMFLFWS-- 697
Cdd:PLN03000 429 LGVLK----------NGSIKFVPELPQRKLDCIKRLGFGLLNKVAMLFPYVFWSTDLDTFGHLTEDPNYRGEFFLFYSya 498
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  698 -ISSSPVLLALVAGMAANLVESVTDDIIIGRCMSVLKNIF--GNTSVPQPKETVVTRWRSDPWARGSYSYVSVGSSGSDY 774
Cdd:PLN03000 499 pVAGGPLLIALVAGEAAHKFETMPPTDAVTRVLHILRGIYepQGINVPDPLQTVCTRWGGDPFSLGSYSNVAVGASGDDY 578
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|...
gi 21356479  775 DLLAAPVippsskdaeGLPRLFFAGEHTIRNYPATVHGAYLSGLREAGRIADY 827
Cdd:PLN03000 579 DILAESV---------GDGRLFFAGEATTRRYPATMHGAFVTGLREAANMAQS 622
 
Name Accession Description Interval E-value
PLN03000 PLN03000
amine oxidase
74-827 3.25e-114

amine oxidase


Pssm-ID: 178578 [Multi-domain]  Cd Length: 881  Bit Score: 370.12  E-value: 3.25e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   74 RRNRPKVDYSNRPS------GSGDTASNDKSGSASmgpnnqqaerRSQSQTRKSEANATSSSVSGPSAGNSRPSQNgdsk 147
Cdd:PLN03000  11 RRGRSQRSASSLNSlpvpnvGTLPGNTNFVSSSAS----------SSGRFNVESVNGSNQTTKSYPGIGDEIITIN---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  148 dRDAGTPTVLSGQEGavfqsrLPFNKMTpNEEACFPDISRSGILGHRVFLNIRNSLLHMWVDNPKIQLSFEIALKNLPPP 227
Cdd:PLN03000  77 -KEATTEALLALTAG------FPADSLT-EEEIEFGVVPIVGGIEQVNYILIRNHIISKWRENISSWVTKEMFLGSIPKH 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  228 FDSepsLVRRVHSFLERHGFINFGIFKRLK-PIPAK-KLGKVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRIST 305
Cdd:PLN03000 149 CSS---LLDSAYNYLVTHGYINFGIAQAIKdKFPAQsSKSSVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGGRVYT 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  306 FR----KNSYIADVGAMVVTGVYGNPMTILSKQIGMDLVPIQQTCPLYGPDGKPVPKEKDDVIEREFNRLLESASYLSHR 381
Cdd:PLN03000 226 KKmeanRVGAAADLGGSVLTGTLGNPLGIIARQLGSSLYKVRDKCPLYRVDGKPVDPDVDLKVEVAFNQLLDKASKLRQL 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  382 LdfnyaGDCP--VSLGDALEwiismqemqvmhkrgqhmqeiiatqtkiieqrrrlkTLRDTIGklknehlaminqrkpkg 459
Cdd:PLN03000 306 M-----GDVSmdVSLGAALE------------------------------------TFRQVSG----------------- 327
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  460 tdgdlkycyqefnirntqikmeetistfHDLHAEEKQMLaklheleqnrpsdvylssrdrlilDWHFANLEFANATRLNN 539
Cdd:PLN03000 328 ----------------------------NDVATEEMGLF------------------------NWHLANLEYANAGLVSK 355
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  540 LSLKHWDQDDDFEFIGHHTTVRNGYSCVPVALTENLDIRVNSAVKEIKYGTKGVEVVAENlktsnsqMTYKADLVVCTLT 619
Cdd:PLN03000 356 LSLAFWDQDDPYDMGGDHCFLPGGNGRLVQALAENVPILYEKTVQTIRYGSNGVKVIAGN-------QVYEGDMVLCTVP 428
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  620 LGVLKvavahkesqqSNTVKFDPPLPDWKQQAIKRLGFGNLNKVVLCFDRIFWDPNANLFGHVGSTTASRGEMFLFWS-- 697
Cdd:PLN03000 429 LGVLK----------NGSIKFVPELPQRKLDCIKRLGFGLLNKVAMLFPYVFWSTDLDTFGHLTEDPNYRGEFFLFYSya 498
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  698 -ISSSPVLLALVAGMAANLVESVTDDIIIGRCMSVLKNIF--GNTSVPQPKETVVTRWRSDPWARGSYSYVSVGSSGSDY 774
Cdd:PLN03000 499 pVAGGPLLIALVAGEAAHKFETMPPTDAVTRVLHILRGIYepQGINVPDPLQTVCTRWGGDPFSLGSYSNVAVGASGDDY 578
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|...
gi 21356479  775 DLLAAPVippsskdaeGLPRLFFAGEHTIRNYPATVHGAYLSGLREAGRIADY 827
Cdd:PLN03000 579 DILAESV---------GDGRLFFAGEATTRRYPATMHGAFVTGLREAANMAQS 622
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
274-824 3.84e-86

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: 282.46  E-value: 3.84e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   274 ISGLAVAHQLQQFGMDVIVLEARDRVGGRISTFRKNSYIADVGAMVVTGvYGNPMTILSKQIGMDLvpiQQTCPLYGP-- 351
Cdd:pfam01593   1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVRDDGFLIELGAMWFHG-AQPPLLALLKELGLED---RLVLPDPAPfy 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   352 -----DGKPVPKEKDDViEREFNRLLESASYLShrldfnyagdcpvslgdalewiismqemqvmhkrgqhmqeiiatqtk 426
Cdd:pfam01593  77 tvlfaGGRRYPGDFRRV-PAGWEGLLEFGRLLS----------------------------------------------- 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   427 iIEQRRRLKTLRDTIGKLKNEHLAMINqrkpkgtdgdlkycyqefnirntqikmeetistfhdlHAEEkqmlakLHELEQ 506
Cdd:pfam01593 109 -IPEKLRLGLAALASDALDEFDLDDFS-------------------------------------LAES------LLFLGR 144
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   507 NRPSDVYLSsrDRLILDWHFANLEFANAT-----RLNNLSLKHWDQDDDFEFIGHHTTVRNGYSCVPVALTENL---DIR 578
Cdd:pfam01593 145 RGPGDVEVW--DRLIDPELFAALPFASGAfagdpSELSAGLALPLLWALLGEGGSLLLPRGGLGALPDALAAQLlggDVR 222
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   579 VNSAVKEIKYGTKGVEVVAENlktsnsQMTYKADLVVCTLTLGVLKvavahkesqqsnTVKFDPPLPDWKQQAIKRLGFG 658
Cdd:pfam01593 223 LNTRVRSIDREGDGVTVTLTD------GEVIEADAVIVTVPLGVLK------------RILFTPPLPPEKARAIRNLGYG 284
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   659 NLNKVVLCFDRIFWDPNAnLFGHVGSTTASRGEMFlFWSI-------SSSPVLLALV-AGMAANLVESVTDDIIIGRCMS 730
Cdd:pfam01593 285 PVNKVHLEFDRKFWPDLG-LLGLLSELLTGLGTAF-SWLTfpnrappGKGLLLLVYVgPGDRARELEGLSDEELLQAVLR 362
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   731 VLKNIFGNtSVPQPKETVVTRWRSDPWARGSYSYVSVGSSGSDYDLLAAPVIPpsskdaeglpRLFFAGEHTIRNYPATV 810
Cdd:pfam01593 363 DLRKLFGE-EAPEPLRVLVSDWHTDPWPRGSYSLPQYGPGHDDYRPLARTPDP----------GLFFAGEHTSTGYPGTV 431
                         570
                  ....*....|....
gi 21356479   811 HGAYLSGLREAGRI 824
Cdd:pfam01593 432 EGAIESGRRAARAV 445
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
266-825 2.53e-59

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 209.01  E-value: 2.53e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479 266 KVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRISTFRK--NSYIADVGAMVVTGVYGNpMTILSKQIGMDLVPIQ 343
Cdd:COG1231   9 DVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFgdDGLYAELGAMRIPPSHTN-LLALARELGLPLEPFP 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479 344 QTCP--LYGPDGKPVPKEKDDVIEREFNRLLesasylsHRLDFNYAGDCPVSLGDALEW-IISMQEMqvmhkrgqhmqei 420
Cdd:COG1231  88 NENGnaLLYLGGKRVRAGEIAADLRGVAELL-------AKLLRALAAALDPWAHPAAELdRESLAEW------------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479 421 iatqtkiIEQRRRLKTLRDTIGklknehlAMINQRKPKGTDgdlkycyqefnirntqikmeeTISTFHdlhaeekqmlak 500
Cdd:COG1231 148 -------LRRNGASPSARRLLG-------LLGAGEYGADPD---------------------ELSLLD------------ 180
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479 501 lheleqnrpsdvylssrdrlILDWHFANLefanatrlnnlslkhwDQDDDFEFIGhhttvrnGYSCVPVALTENL--DIR 578
Cdd:COG1231 181 --------------------LLRYAASAG----------------GGAQQFRIVG-------GMDQLPRALAAELgdRIR 217
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479 579 VNSAVKEIKYGTKGVEVvaenlkTSNSQMTYKADLVVCTLTLGVLKvavahkesqqsnTVKFDPPLPDWKQQAIKRLGFG 658
Cdd:COG1231 218 LGAPVTRIRQDGDGVTV------TTDDGGTVRADAVIVTVPPSVLR------------RIEFDPPLPAAKRAAIQRLPYG 279
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479 659 NLNKVVLCFDRIFWDPNanlfGHVGSTTASRGEMFLFW-----SISSSPVLLALVAGMAANLVESVTDDIIIGRCMSVLK 733
Cdd:COG1231 280 AAIKVFLQFDRPFWEED----GLYGGISLTDLPIRQTWypsngPDGGAGVLLGYVGGDDARALAALSPEERVAAALEQLA 355
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479 734 NIFGNTSvPQPKETVVTRWRSDPWARGSYSYVSVGSSGSDYDLLAAPVippsskdaeglPRLFFAGEHTIRNYPATVHGA 813
Cdd:COG1231 356 RIFGVYA-AEPVDYVSTDWGRDPWSRGAYAAAPPGQLTAAGPALAEPD-----------GRIHFAGEHTSDEWPGWVEGA 423
                       570
                ....*....|..
gi 21356479 814 YLSGLREAGRIA 825
Cdd:COG1231 424 LESGERAAAEIL 435
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
267-321 3.27e-10

phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two symmetrical pairs of) sites. This is achieved by two enzymes (crtP and crtQ) in cyanobacteria (Gloeobacter being an exception) and plants, but by a single enzyme in most other bacteria and in fungi. This single enzyme is called the bacterial-type phytoene desaturase, or CrtI. Most members of this family, part of the larger pfam01593, which also contains amino oxidases, are CrtI itself; it is likely that all members act on either phytoene or on related compounds such as dehydrosqualene, for carotenoid biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 274273 [Multi-domain]  Cd Length: 495  Bit Score: 63.45  E-value: 3.27e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 21356479   267 VIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRISTFRKNSYIADVGAMVVT 321
Cdd:TIGR02734   1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGRAGVLEDDGFRFDTGPTVIT 55
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
233-292 6.10e-03

Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family; Formate dehydrogenase, D-specific 2-hydroxy acid dehydrogenase, Phosphoglycerate Dehydrogenase, Lactate dehydrogenase, Thermostable Phosphite Dehydrogenase, and Hydroxy(phenyl)pyruvate reductase, among others, share a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase, among others. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240622 [Multi-domain]  Cd Length: 302  Bit Score: 39.53  E-value: 6.10e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21356479 233 SLVRRvhsFLERHGFINFGIFKRLKPIPAKKL-GKVI-VIGAGISGLAVAHQLQQFGMDVIV 292
Cdd:cd05198 110 ALLRR---LPRADAAVRRGWGWLWAGFPGYELeGKTVgIVGLGRIGQRVAKRLQAFGMKVLY 168
 
Name Accession Description Interval E-value
PLN03000 PLN03000
amine oxidase
74-827 3.25e-114

amine oxidase


Pssm-ID: 178578 [Multi-domain]  Cd Length: 881  Bit Score: 370.12  E-value: 3.25e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   74 RRNRPKVDYSNRPS------GSGDTASNDKSGSASmgpnnqqaerRSQSQTRKSEANATSSSVSGPSAGNSRPSQNgdsk 147
Cdd:PLN03000  11 RRGRSQRSASSLNSlpvpnvGTLPGNTNFVSSSAS----------SSGRFNVESVNGSNQTTKSYPGIGDEIITIN---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  148 dRDAGTPTVLSGQEGavfqsrLPFNKMTpNEEACFPDISRSGILGHRVFLNIRNSLLHMWVDNPKIQLSFEIALKNLPPP 227
Cdd:PLN03000  77 -KEATTEALLALTAG------FPADSLT-EEEIEFGVVPIVGGIEQVNYILIRNHIISKWRENISSWVTKEMFLGSIPKH 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  228 FDSepsLVRRVHSFLERHGFINFGIFKRLK-PIPAK-KLGKVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRIST 305
Cdd:PLN03000 149 CSS---LLDSAYNYLVTHGYINFGIAQAIKdKFPAQsSKSSVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGGRVYT 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  306 FR----KNSYIADVGAMVVTGVYGNPMTILSKQIGMDLVPIQQTCPLYGPDGKPVPKEKDDVIEREFNRLLESASYLSHR 381
Cdd:PLN03000 226 KKmeanRVGAAADLGGSVLTGTLGNPLGIIARQLGSSLYKVRDKCPLYRVDGKPVDPDVDLKVEVAFNQLLDKASKLRQL 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  382 LdfnyaGDCP--VSLGDALEwiismqemqvmhkrgqhmqeiiatqtkiieqrrrlkTLRDTIGklknehlaminqrkpkg 459
Cdd:PLN03000 306 M-----GDVSmdVSLGAALE------------------------------------TFRQVSG----------------- 327
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  460 tdgdlkycyqefnirntqikmeetistfHDLHAEEKQMLaklheleqnrpsdvylssrdrlilDWHFANLEFANATRLNN 539
Cdd:PLN03000 328 ----------------------------NDVATEEMGLF------------------------NWHLANLEYANAGLVSK 355
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  540 LSLKHWDQDDDFEFIGHHTTVRNGYSCVPVALTENLDIRVNSAVKEIKYGTKGVEVVAENlktsnsqMTYKADLVVCTLT 619
Cdd:PLN03000 356 LSLAFWDQDDPYDMGGDHCFLPGGNGRLVQALAENVPILYEKTVQTIRYGSNGVKVIAGN-------QVYEGDMVLCTVP 428
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  620 LGVLKvavahkesqqSNTVKFDPPLPDWKQQAIKRLGFGNLNKVVLCFDRIFWDPNANLFGHVGSTTASRGEMFLFWS-- 697
Cdd:PLN03000 429 LGVLK----------NGSIKFVPELPQRKLDCIKRLGFGLLNKVAMLFPYVFWSTDLDTFGHLTEDPNYRGEFFLFYSya 498
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  698 -ISSSPVLLALVAGMAANLVESVTDDIIIGRCMSVLKNIF--GNTSVPQPKETVVTRWRSDPWARGSYSYVSVGSSGSDY 774
Cdd:PLN03000 499 pVAGGPLLIALVAGEAAHKFETMPPTDAVTRVLHILRGIYepQGINVPDPLQTVCTRWGGDPFSLGSYSNVAVGASGDDY 578
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|...
gi 21356479  775 DLLAAPVippsskdaeGLPRLFFAGEHTIRNYPATVHGAYLSGLREAGRIADY 827
Cdd:PLN03000 579 DILAESV---------GDGRLFFAGEATTRRYPATMHGAFVTGLREAANMAQS 622
PLN02328 PLN02328
lysine-specific histone demethylase 1 homolog
23-824 1.33e-110

lysine-specific histone demethylase 1 homolog


Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 358.54  E-value: 1.33e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   23 ISDDSDGEPTPKRNVNHPPSALSAP------NPGQKQKHPDEDSNDAPATSD--ERRTSRRNRPKVDYSNRPSGSGDTAS 94
Cdd:PLN02328   1 METETKEPEDPADNVNDVVSEASSPetdlslSPSQSEQNIENDGQNSPETQSplTELQPSPLPPNTTLDAPVSDSQGDES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   95 NdkSGSASMGPNNQQAERRSQSQTRK----SEANATsssvsgPSAGNSRPSqNGDSKDRDAGTPTVLSgqegavfqSRLP 170
Cdd:PLN02328  81 S--SEQQPQNPNSTEPAPPPKKRRRRkrffTEINAN------PAFRRHRVR-GGLGKEVDVEALIAIS--------VGFP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  171 FNKMTPNE-EACFpdISRSGILGHRVFLNIRNSLLHMWVDNPKIQLSFEIALKNLPPpfdSEPSLVRRVHSFLERHGFIN 249
Cdd:PLN02328 144 VDSLTEEEiEANV--VSTIGGTEQANYIVVRNHILARWRSNVSNWLTRDHALESIRA---EHKNLVDSAYNFLLEHGYIN 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  250 FGIfkrLKPIPAKKLGK--------VIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRISTFRKNS----YIADVGA 317
Cdd:PLN02328 219 FGV---APVIKEAQLRSfegvepanVVVVGAGLAGLVAARQLLSMGFKVVVLEGRARPGGRVKTMKMKGdgvvAAADLGG 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  318 MVVTGVYGNPMTILSKQIGMDLVPIQQTCPLYGPDGKPVPKEKDDVIEREFNRLLesasylshrldfnyagdcpvslgda 397
Cdd:PLN02328 296 SVLTGINGNPLGVLARQLGLPLHKVRDICPLYLPDGKAVDAEIDSKIEASFNKLL------------------------- 350
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  398 lewiismqemqvmhkrgqhmqeiiatqtkiieqrrrlktlrDTIGKLKNehlAMINQRKpkgtdgdlkycyqefnirNTQ 477
Cdd:PLN02328 351 -----------------------------------------DRVCKLRQ---AMIEEVK------------------SVD 368
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  478 IKMEETISTFHDLH--AEEKQmlaklheleqnrpsdvylssrDRLILDWHFANLEFANATRLNNLSLKHWDQDDDFEFIG 555
Cdd:PLN02328 369 VNLGTALEAFRHVYkvAEDPQ---------------------ERMLLNWHLANLEYANASLMSNLSMAYWDQDDPYEMGG 427
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  556 HHTTVRNGYSCVPVALTENLDIRVNSAVKEIKYGTKGVEVVAENlktsnsqMTYKADLVVCTLTLGVLKvavahkesqqS 635
Cdd:PLN02328 428 DHCFIPGGNDTFVRELAKDLPIFYERTVESIRYGVDGVIVYAGG-------QEFHGDMVLCTVPLGVLK----------K 490
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  636 NTVKFDPPLPDWKQQAIKRLGFGNLNKVVLCFDRIFWDPNANLFGHVGSTTASRGEMFLFWSISS---SPVLLALVAGMA 712
Cdd:PLN02328 491 GSIEFYPELPQRKKDAIQRLGYGLLNKVALLFPYNFWGGEIDTFGHLTEDPSMRGEFFLFYSYSSvsgGPLLIALVAGDA 570
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  713 ANLVESVTDDIIIGRCMSVLKNIF--GNTSVPQPKETVVTRWRSDPWARGSYSYVSVGSSGSDYDLLAAPVippsskdae 790
Cdd:PLN02328 571 AVKFETLSPVESVKRVLQILRGIFhpKGIVVPDPVQAVCTRWGKDCFTYGSYSYVAVGSSGDDYDILAESV--------- 641
                        810       820       830
                 ....*....|....*....|....*....|....
gi 21356479  791 GLPRLFFAGEHTIRNYPATVHGAYLSGLREAGRI 824
Cdd:PLN02328 642 GDGRVFFAGEATNKQYPATMHGAFLSGMREAANI 675
PLN02529 PLN02529
lysine-specific histone demethylase 1
196-824 1.59e-103

lysine-specific histone demethylase 1


Pssm-ID: 178144 [Multi-domain]  Cd Length: 738  Bit Score: 337.63  E-value: 1.59e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  196 FLNIRNSLLHMWVDNPKIQLSFEIALKNLPPPFDSepsLVRRVHSFLERHGFINFGIFKRL-KPIPAKKL-GKVIVIGAG 273
Cdd:PLN02529  93 YIVVRNHILARWRSNVGIWLSKGQIKETVSSEYEH---LISAAYDFLLYNGYINFGVSPSFaSPIPEEGTeGSVIIVGAG 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  274 ISGLAVAHQLQQFGMDVIVLEARDRVGGRIST---FRKNSYIA-DVGAMVVTGVYGNPMTILSKQIGMDLVPIQQTCPLY 349
Cdd:PLN02529 170 LAGLAAARQLLSFGFKVVVLEGRNRPGGRVYTqkmGRKGQFAAvDLGGSVITGIHANPLGVLARQLSIPLHKVRDNCPLY 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  350 GPDGKPVPKEKDDVIEREFNRLLESASYLSHRLDfNYAGDcpVSLGDALEwiismqemqvmhkrgqhmqeiiatqtkiie 429
Cdd:PLN02529 250 KPDGALVDKEIDSNIEFIFNKLLDKVTELRQIMG-GFAND--ISLGSVLE------------------------------ 296
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  430 QRRRLKTlrdtigklknehlaminqrkpkgtdgdlkycyqefnirntqikmeetistfhdlhaeekqmlaklheleqnrp 509
Cdd:PLN02529 297 RLRQLYG------------------------------------------------------------------------- 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  510 sdVYLSSRDRLILDWHFANLEFANATRLNNLSLKHWDQDDDFEFIGHHTTVRNGYSCVPVALTENLDIRVNSAVKEIKYG 589
Cdd:PLN02529 304 --VARSTEERQLLDWHLANLEYANAGCLSDLSAAYWDQDDPYEMGGDHCFLAGGNWRLINALCEGVPIFYGKTVDTIKYG 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  590 TKGVEVVAenlktsNSQMtYKADLVVCTLTLGVLKvavahkesqqSNTVKFDPPLPDWKQQAIKRLGFGNLNKVVLCFDR 669
Cdd:PLN02529 382 NDGVEVIA------GSQV-FQADMVLCTVPLGVLK----------KRTIRFEPELPRRKLAAIDRLGFGLLNKVAMVFPS 444
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  670 IFWDPNANLFGHVGSTTASRGEMFLFWS---ISSSPVLLALVAGMAANLVESVTDDIIIGRCMSVLKNIFG--NTSVPQP 744
Cdd:PLN02529 445 VFWGEELDTFGCLNESSNKRGEFFLFYGyhtVSGGPALVALVAGEAAQRFENTDPSTLLHRVLSVLRGIYNpkGINVPDP 524
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  745 KETVVTRWRSDPWARGSYSYVSVGSSGSDYDLLAAPVippsskdaegLPRLFFAGEHTIRNYPATVHGAYLSGLREAGRI 824
Cdd:PLN02529 525 IQTICTRWGSDPLSYGSYSHVRVQSSGSDYDILAESV----------SGRLFFAGEATTRQYPATMHGAFLSGLREASRI 594
PLN02976 PLN02976
amine oxidase
266-826 1.77e-95

amine oxidase


Pssm-ID: 215527 [Multi-domain]  Cd Length: 1713  Bit Score: 329.91  E-value: 1.77e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   266 KVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRISTFRKN-SYIADVGAMVVTGVYGN--------PMTILSKQIG 336
Cdd:PLN02976  695 KIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGRVYTDRSSlSVPVDLGASIITGVEADvaterrpdPSSLICAQLG 774
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   337 MDLVPIQQTCPLYgpD---GKPVPKEKDDVIEREFNRLLESASYLshrldFNYAGDCPV--SLGDALEWIIsmqemqvmh 411
Cdd:PLN02976  775 LELTVLNSDCPLY--DvvtGEKVPADLDEALEAEYNSLLDDMVLL-----VAQKGEHAMkmSLEDGLEYAL--------- 838
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   412 krgqhmqeiiatqtkiieQRRRLKTLRDTIGKLKNEHLAM-INQRKPKGTDGDLkycyqefnirntqikmeetistfhdl 490
Cdd:PLN02976  839 ------------------KRRRMPRPGVDIDETELGNAADdLYDSASTGVDGGH-------------------------- 874
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   491 haeekqmlaklheLEQNRPSDVyLSSRDRLILDWHFANLEFANATRLNNLSLKHWDQDDDFE-FIGHHTTVRNGYSCVPV 569
Cdd:PLN02976  875 -------------CEKESKEDV-LSPLERRVMNWHFAHLEYGCAALLKEVSLPYWNQDDVYGgFGGAHCMIKGGYSNVVE 940
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   570 ALTENLDIRVNSAVKEIKYGTKGVEVVAENLK-----TSNSQmTYKADLVVCTLTLGVLKvavahkesqqSNTVKFDPPL 644
Cdd:PLN02976  941 SLAEGLDIHLNHVVTDVSYGSKDAGASGSSRKkvkvsTSNGS-EFLGDAVLITVPLGCLK----------AETIKFSPPL 1009
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   645 PDWKQQAIKRLGFGNLNKVVLCFDRIFWDPNANLFGHVGSTTASRGEMFLFWSISSS---PVLLALVAGMAANLVESVTD 721
Cdd:PLN02976 1010 PDWKYSSIQRLGFGVLNKVVLEFPEVFWDDSVDYFGATAEETDLRGQCFMFWNVKKTvgaPVLIALVVGKAAIDGQSMSS 1089
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   722 DIIIGRCMSVLKNIFGNTSVPQPKETVVTRWRSDPWARGSYSYVSVGSSGSDYDLLAAPVippssKDAeglprLFFAGEH 801
Cdd:PLN02976 1090 SDHVNHALMVLRKLFGEALVPDPVASVVTDWGRDPFSYGAYSYVAIGASGEDYDILGRPV-----ENC-----LFFAGEA 1159
                         570       580
                  ....*....|....*....|....*
gi 21356479   802 TIRNYPATVHGAYLSGLREAGRIAD 826
Cdd:PLN02976 1160 TCKEHPDTVGGAMMSGLREAVRIID 1184
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
274-824 3.84e-86

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: 282.46  E-value: 3.84e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   274 ISGLAVAHQLQQFGMDVIVLEARDRVGGRISTFRKNSYIADVGAMVVTGvYGNPMTILSKQIGMDLvpiQQTCPLYGP-- 351
Cdd:pfam01593   1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVRDDGFLIELGAMWFHG-AQPPLLALLKELGLED---RLVLPDPAPfy 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   352 -----DGKPVPKEKDDViEREFNRLLESASYLShrldfnyagdcpvslgdalewiismqemqvmhkrgqhmqeiiatqtk 426
Cdd:pfam01593  77 tvlfaGGRRYPGDFRRV-PAGWEGLLEFGRLLS----------------------------------------------- 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   427 iIEQRRRLKTLRDTIGKLKNEHLAMINqrkpkgtdgdlkycyqefnirntqikmeetistfhdlHAEEkqmlakLHELEQ 506
Cdd:pfam01593 109 -IPEKLRLGLAALASDALDEFDLDDFS-------------------------------------LAES------LLFLGR 144
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   507 NRPSDVYLSsrDRLILDWHFANLEFANAT-----RLNNLSLKHWDQDDDFEFIGHHTTVRNGYSCVPVALTENL---DIR 578
Cdd:pfam01593 145 RGPGDVEVW--DRLIDPELFAALPFASGAfagdpSELSAGLALPLLWALLGEGGSLLLPRGGLGALPDALAAQLlggDVR 222
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   579 VNSAVKEIKYGTKGVEVVAENlktsnsQMTYKADLVVCTLTLGVLKvavahkesqqsnTVKFDPPLPDWKQQAIKRLGFG 658
Cdd:pfam01593 223 LNTRVRSIDREGDGVTVTLTD------GEVIEADAVIVTVPLGVLK------------RILFTPPLPPEKARAIRNLGYG 284
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   659 NLNKVVLCFDRIFWDPNAnLFGHVGSTTASRGEMFlFWSI-------SSSPVLLALV-AGMAANLVESVTDDIIIGRCMS 730
Cdd:pfam01593 285 PVNKVHLEFDRKFWPDLG-LLGLLSELLTGLGTAF-SWLTfpnrappGKGLLLLVYVgPGDRARELEGLSDEELLQAVLR 362
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   731 VLKNIFGNtSVPQPKETVVTRWRSDPWARGSYSYVSVGSSGSDYDLLAAPVIPpsskdaeglpRLFFAGEHTIRNYPATV 810
Cdd:pfam01593 363 DLRKLFGE-EAPEPLRVLVSDWHTDPWPRGSYSLPQYGPGHDDYRPLARTPDP----------GLFFAGEHTSTGYPGTV 431
                         570
                  ....*....|....
gi 21356479   811 HGAYLSGLREAGRI 824
Cdd:pfam01593 432 EGAIESGRRAARAV 445
PLN02268 PLN02268
probable polyamine oxidase
267-821 7.77e-66

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 226.88  E-value: 7.77e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  267 VIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRISTFRKNSYIADVGAMVVTGVYG-NPmtiLSKQIGMDLVPIQQT 345
Cdd:PLN02268   3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIGGRVHTDYSFGFPVDMGASWLHGVCNeNP---LAPLIGRLGLPLYRT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  346 --------------CPLYGPDGKPVPKEKDDVIEREFNRLLESasylSHRLDFNYAGDCPVslgdalewiisMQEMQVMH 411
Cdd:PLN02268  80 sgdnsvlydhdlesYALFDMDGNQVPQELVTKVGETFERILEE----TEKVRDEHEEDMSL-----------LQAISIVL 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  412 KRGQHmqeiiatqtkiieqrrrlktlrdtigkLKNEHLAminqrkpkgtdgdlkycyqefnirntqikmeetistfhdlh 491
Cdd:PLN02268 145 ERHPE---------------------------LRLEGLA----------------------------------------- 156
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  492 aeekqmlaklHEleqnrpsdvylssrdrlILDWHFANLEFANATRLNNLSLKHWDQDDDFEfiGHHTTVRNGYSCVPVAL 571
Cdd:PLN02268 157 ----------HE-----------------VLQWYLCRMEGWFAADADTISLKSWDQEELLE--GGHGLMVRGYDPVINTL 207
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  572 TENLDIRVNSAVKEIKYGTKGVEVVAENLKTsnsqmtYKADLVVCTLTLGVLKvavahkesqqSNTVKFDPPLPDWKQQA 651
Cdd:PLN02268 208 AKGLDIRLNHRVTKIVRRYNGVKVTVEDGTT------FVADAAIIAVPLGVLK----------ANIIKFEPELPEWKEEA 271
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  652 IKRLGFGNLNKVVLCFDRIFWdPNANLFGHVGSTTASRGEMFLFWSISSSPVLLALVAGMAANLVESVTDDIIIGRCMSV 731
Cdd:PLN02268 272 ISDLGVGIENKIALHFDSVFW-PNVEFLGVVAPTSYGCSYFLNLHKATGHPVLVYMPAGRLARDIEKLSDEAAANFAMSQ 350
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  732 LKNIFGNTsvPQPKETVVTRWRSDPWARGSYSYVSVGSSGSDYDLLAAPVippsskdaeglPRLFFAGEHTIRNYPATVH 811
Cdd:PLN02268 351 LKKMLPDA--TEPVQYLVSRWGSDPNSLGCYSYDLVGKPHDLYERLRAPV-----------DNLFFAGEATSSDFPGSVH 417
                        570
                 ....*....|
gi 21356479  812 GAYLSGLREA 821
Cdd:PLN02268 418 GAYSTGVMAA 427
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
266-825 2.53e-59

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 209.01  E-value: 2.53e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479 266 KVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRISTFRK--NSYIADVGAMVVTGVYGNpMTILSKQIGMDLVPIQ 343
Cdd:COG1231   9 DVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFgdDGLYAELGAMRIPPSHTN-LLALARELGLPLEPFP 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479 344 QTCP--LYGPDGKPVPKEKDDVIEREFNRLLesasylsHRLDFNYAGDCPVSLGDALEW-IISMQEMqvmhkrgqhmqei 420
Cdd:COG1231  88 NENGnaLLYLGGKRVRAGEIAADLRGVAELL-------AKLLRALAAALDPWAHPAAELdRESLAEW------------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479 421 iatqtkiIEQRRRLKTLRDTIGklknehlAMINQRKPKGTDgdlkycyqefnirntqikmeeTISTFHdlhaeekqmlak 500
Cdd:COG1231 148 -------LRRNGASPSARRLLG-------LLGAGEYGADPD---------------------ELSLLD------------ 180
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479 501 lheleqnrpsdvylssrdrlILDWHFANLefanatrlnnlslkhwDQDDDFEFIGhhttvrnGYSCVPVALTENL--DIR 578
Cdd:COG1231 181 --------------------LLRYAASAG----------------GGAQQFRIVG-------GMDQLPRALAAELgdRIR 217
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479 579 VNSAVKEIKYGTKGVEVvaenlkTSNSQMTYKADLVVCTLTLGVLKvavahkesqqsnTVKFDPPLPDWKQQAIKRLGFG 658
Cdd:COG1231 218 LGAPVTRIRQDGDGVTV------TTDDGGTVRADAVIVTVPPSVLR------------RIEFDPPLPAAKRAAIQRLPYG 279
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479 659 NLNKVVLCFDRIFWDPNanlfGHVGSTTASRGEMFLFW-----SISSSPVLLALVAGMAANLVESVTDDIIIGRCMSVLK 733
Cdd:COG1231 280 AAIKVFLQFDRPFWEED----GLYGGISLTDLPIRQTWypsngPDGGAGVLLGYVGGDDARALAALSPEERVAAALEQLA 355
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479 734 NIFGNTSvPQPKETVVTRWRSDPWARGSYSYVSVGSSGSDYDLLAAPVippsskdaeglPRLFFAGEHTIRNYPATVHGA 813
Cdd:COG1231 356 RIFGVYA-AEPVDYVSTDWGRDPWSRGAYAAAPPGQLTAAGPALAEPD-----------GRIHFAGEHTSDEWPGWVEGA 423
                       570
                ....*....|..
gi 21356479 814 YLSGLREAGRIA 825
Cdd:COG1231 424 LESGERAAAEIL 435
PLN02676 PLN02676
polyamine oxidase
261-821 8.47e-39

polyamine oxidase


Pssm-ID: 215362 [Multi-domain]  Cd Length: 487  Bit Score: 151.41  E-value: 8.47e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  261 AKKLGKVIVIGAGISGLAVAHQLQQFGM-DVIVLEARDRVGGRISTFRKNSYIADVGAMVVTGVYG---NPMTILSKQIG 336
Cdd:PLN02676  23 AKPSPSVIIVGAGMSGISAAKTLSEAGIeDILILEATDRIGGRMRKANFAGVSVELGANWVEGVGGpesNPIWELANKLK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  337 M-----DLVPIQQTcpLYGPDGKPVPKekdDVIEREFNRLLESAsylshrldfnyagdcpvslgdalEWIISMQemQVMH 411
Cdd:PLN02676 103 LrtfysDFDNLSSN--IYKQDGGLYPK---KVVQKSMKVADASD-----------------------EFGENLS--ISLS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  412 KRGQHMQEIIATQtkiieqrrRLKtlrdtiGKLKNEHLAMInqrkpkgtdgdLKYCYQEFNI----RNTQIKMEETISTF 487
Cdd:PLN02676 153 AKKAVDISILTAQ--------RLF------GQVPKTPLEMV-----------IDYYNYDYEFaeppRVTSLKNTEPNPTF 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  488 HD------LHAEEKQMLAKLHELEQNrpsdvYLSSRDRLILDwhfanlefanaTRLnnlslkhwdqdddfefighhttvr 561
Cdd:PLN02676 208 VDfgedeyFVADPRGYESLVYYLAEQ-----FLSTKSGKITD-----------PRL------------------------ 247
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  562 ngyscvpvaltenldiRVNSAVKEIKYGTKGVEVVAENlktsNSqmTYKADLVVCTLTLGVLkvavahkesqQSNTVKFD 641
Cdd:PLN02676 248 ----------------KLNKVVREISYSKNGVTVKTED----GS--VYRAKYVIVSVSLGVL----------QSDLIKFK 295
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  642 PPLPDWKQQAIKRLGFGNLNKVVLCFDRIFWdPNAN-----LFGHVgsttaSRGeMFLFW-----SISSSPVLLALVAGM 711
Cdd:PLN02676 296 PPLPDWKIEAIYQFDMAVYTKIFLKFPYKFW-PSGPgteffLYAHE-----RRG-YYPFWqhlenEYPGSNVLFVTVTDE 368
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  712 AANLVESVTDDIIIGRCMSVLKNIFGNtSVPQPKETVVTRWRSDPWARGSYSYVSVGSSGSDYDLLAAPVippsskdaeg 791
Cdd:PLN02676 369 ESRRIEQQPDSETKAEIMEVLRKMFGP-NIPEATDILVPRWWSNRFFKGSYSNWPIGVSRYEFDQIRAPV---------- 437
                        570       580       590
                 ....*....|....*....|....*....|
gi 21356479  792 lPRLFFAGEHTIRNYPATVHGAYLSGLREA 821
Cdd:PLN02676 438 -GRVYFTGEHTSEKYNGYVHGAYLAGIDTA 466
PLN02568 PLN02568
polyamine oxidase
261-828 6.39e-35

polyamine oxidase


Pssm-ID: 215308 [Multi-domain]  Cd Length: 539  Bit Score: 140.73  E-value: 6.39e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  261 AKKlGKVIVIGAGISGLAVAHQLQQFG-----MDVIVLEARDRVGGRISTFRKNSYIADVGAMVVTGVYGNPMTILSKQI 335
Cdd:PLN02568   3 AKK-PRIVIIGAGMAGLTAANKLYTSSaandmFELTVVEGGDRIGGRINTSEFGGERIEMGATWIHGIGGSPVYKIAQEA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  336 GmdlvPIQQTCPLYGPDGKP-VPKEKDDVIEREFNRLLESASYLSHRLdFNYAGDCPVSLGDALEwiismqemqvmhkrg 414
Cdd:PLN02568  82 G----SLESDEPWECMDGFPdRPKTVAEGGFEVDPSIVESISTLFRGL-MDDAQGKLIEPSEVDE--------------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  415 QHMQEIIATQTKIIEqrrrlktlrdtigklknehlaminqrkpKGTDGDL-KYCYQEFNIRNTQIKMEETISTF--HDLH 491
Cdd:PLN02568 142 VDFVKLAAKAARVCE----------------------------SGGGGSVgSFLRRGLDAYWDSVSADEQIKGYggWSRK 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  492 AEEKQMLAkLHELEQNrpsdVYLSSRDRLILDWHFANlefanatrlnnlslKHWDqdddfeFIGHHTTVRNGYSCVPVAL 571
Cdd:PLN02568 194 LLEEAIFT-MHENTQR----TYTSADDLSTLDLAAES--------------EYRM------FPGEEITIAKGYLSVIEAL 248
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  572 TENLD---IRVNSAVKEIKYGTKGVEVVAENlktsNSQMTykADLVVCTLTLGVLKvAVAHKESQQsntvkFDPPLPDWK 648
Cdd:PLN02568 249 ASVLPpgtIQLGRKVTRIEWQDEPVKLHFAD----GSTMT--ADHVIVTVSLGVLK-AGIGEDSGL-----FSPPLPDFK 316
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  649 QQAIKRLGFGNLNKVVLCF----DRIFWD----PNANLFGHvGSTTASRGEMFLFW-----SIS----SSPVLLALVAGM 711
Cdd:PLN02568 317 TDAISRLGFGVVNKLFVELsprpDGSPEDvakfPFLQMAFH-RSDSEARHDKIPWWmrrtaSICpihkNSSVLLSWFAGK 395
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  712 AANLVESVTDDIII-----------------GRCMSVLKNIFGNTSVPQPKETVV----TRWRSDPWARGSYSYVSVGSS 770
Cdd:PLN02568 396 EALELEKLSDEEIIrgvqttlssflkrrvagLGSQSHPLCNGGASSNDGSRWKFVkvlkSKWGTDPLFLGSYSYVAVGSS 475
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  771 GSDYDLLAAPVIPPSSKDAEGLP--RLFFAGEHTIRNYPATVHGAYLSGLREAGRIADYY 828
Cdd:PLN02568 476 GDDLDRMAEPLPRISDHDQAGGPplQLLFAGEATHRTHYSTTHGAYFSGLREANRLLQHY 535
SWIRM pfam04433
SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid ...
171-250 1.24e-21

SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid residues found in chromosomal proteins. It contains a helix-turn helix motif and binds to DNA.


Pssm-ID: 461307 [Multi-domain]  Cd Length: 78  Bit Score: 89.54  E-value: 1.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   171 FNKMTPNEEACFPDISRSGILGHRVFLNIRNSLLHMWVDNPKIQLSFEIALKNLpppfDSEPSLVRRVHSFLERHGFINF 250
Cdd:pfam04433   3 PDKLHPIEKRLLPEFFNGKSKTPEVYLEIRNFILNLWRENPKEYLTKTDARRAL----KGDVNLISRIHEFLERWGLINF 78
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
266-317 2.82e-16

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: 82.19  E-value: 2.82e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 21356479 266 KVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRISTFRKNSYIADVGA 317
Cdd:COG1232   3 RVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRTVEVDGFRIDRGP 54
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
266-371 3.47e-14

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 76.04  E-value: 3.47e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479 266 KVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRISTFRKNSYIADVGAMVVTgvYGNPMTILSKQIG-MDLVPIQQ 344
Cdd:COG1233   5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTFERPGFRFDVGPSVLT--MPGVLERLFRELGlEDYLELVP 82
                        90       100       110
                ....*....|....*....|....*....|.
gi 21356479 345 TCPLYG---PDGKPVPKEKD-DVIEREFNRL 371
Cdd:COG1233  83 LDPAYRvpfPDGRALDLPRDlERTAAELERL 113
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
269-328 4.67e-14

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 67.56  E-value: 4.67e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   269 VIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRISTFRKNSYIADVGAMVVTGVYGNPM 328
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYSYRVPGYVFDYGAHIFHGSDEPNV 60
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
266-317 1.68e-12

Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 69.52  E-value: 1.68e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 21356479 266 KVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRISTFRKNSYIADVGA 317
Cdd:COG3380   5 DIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGGRMATRRLDGGRFDHGA 56
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
267-311 2.57e-12

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: 69.89  E-value: 2.57e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 21356479 267 VIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGrisTFRKNSY 311
Cdd:COG2072   9 VVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGG---TWRDNRY 50
PLN02576 PLN02576
protoporphyrinogen oxidase
267-317 9.51e-11

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 65.03  E-value: 9.51e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 21356479  267 VIVIGAGISGLAVAHQLQ-QFGMDVIVLEARDRVGGRISTFRKNSYIADVGA 317
Cdd:PLN02576  15 VAVVGAGVSGLAAAYALAsKHGVNVLVTEARDRVGGNITSVSEDGFIWEEGP 66
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
266-317 1.95e-10

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 64.10  E-value: 1.95e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 21356479  266 KVIVIGAGISGLAVAHQLQQFG--MDVIVLEARDRVGGRISTFRKNSYIADVGA 317
Cdd:PRK11883   2 KVAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKIQTVRKDGFPIELGP 55
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
267-321 3.27e-10

phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two symmetrical pairs of) sites. This is achieved by two enzymes (crtP and crtQ) in cyanobacteria (Gloeobacter being an exception) and plants, but by a single enzyme in most other bacteria and in fungi. This single enzyme is called the bacterial-type phytoene desaturase, or CrtI. Most members of this family, part of the larger pfam01593, which also contains amino oxidases, are CrtI itself; it is likely that all members act on either phytoene or on related compounds such as dehydrosqualene, for carotenoid biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 274273 [Multi-domain]  Cd Length: 495  Bit Score: 63.45  E-value: 3.27e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 21356479   267 VIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRISTFRKNSYIADVGAMVVT 321
Cdd:TIGR02734   1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGRAGVLEDDGFRFDTGPTVIT 55
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
266-357 1.54e-09

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: 61.39  E-value: 1.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   266 KVIVIGAGISGLAVAHQLQ----QFGMDVIVLEARDRVGGRISTFRKNSYIADVGAMVVTGVYGNPMTILsKQIGM-DLV 340
Cdd:TIGR00562   4 HVVIIGGGISGLCAAYYLEkeipELPVELTLVEASDRVGGKIQTVKEDGYLIERGPDSFLERKKSAPDLV-KDLGLeHVL 82
                          90       100
                  ....*....|....*....|.
gi 21356479   341 PIQQTCP--LYGPDGK--PVP 357
Cdd:TIGR00562  83 VSDATGQryVLVNRGKlmPVP 103
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
265-307 3.64e-09

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: 59.87  E-value: 3.64e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 21356479 265 GKVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRISTFR 307
Cdd:COG3349   4 PRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGGRARSFP 46
PRK07233 PRK07233
hypothetical protein; Provisional
266-314 9.84e-09

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 58.74  E-value: 9.84e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 21356479  266 KVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRISTFRKNSYIAD 314
Cdd:PRK07233   1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAASFEFGGLPIE 49
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
254-301 1.92e-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: 57.45  E-value: 1.92e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 21356479 254 KRLKPIPAKKLGK-VIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGG 301
Cdd:COG0493 110 WVKPPPPAPRTGKkVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG 158
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
266-301 2.89e-08

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: 56.64  E-value: 2.89e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 21356479   266 KVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGG 301
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGS 36
gltD PRK12810
glutamate synthase subunit beta; Reviewed
257-301 1.09e-07

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 55.17  E-value: 1.09e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 21356479  257 KP-IPAKKLGK-VIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGG 301
Cdd:PRK12810 134 KPdPPVKRTGKkVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGG 180
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
258-301 1.29e-07

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 55.19  E-value: 1.29e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 21356479  258 PIPAKKLGK-VIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGG 301
Cdd:PRK11749 133 FKRAPKTGKkVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG 177
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
266-307 2.30e-07

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 53.76  E-value: 2.30e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 21356479 266 KVIVIGAGISGLAVAHQLQQFGMDVIVLEaRDRVGGRiSTFR 307
Cdd:COG0665   4 DVVVIGGGIAGLSTAYHLARRGLDVTVLE-RGRPGSG-ASGR 43
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
266-310 3.11e-07

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 53.40  E-value: 3.11e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 21356479 266 KVIVIGAGISGLAVAHQLQQFGMDVIVLEARD--RVGGRISTFRKNS 310
Cdd:COG0654   5 DVLIVGGGPAGLALALALARAGIRVTVVERAPppRPDGRGIALSPRS 51
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
267-300 3.49e-06

L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 50.53  E-value: 3.49e-06
                        10        20        30
                ....*....|....*....|....*....|....*
gi 21356479 267 VIVIGAGISGLAVAHQLQQF-GMDVIVLEARDRVG 300
Cdd:COG0579   7 VVIIGAGIVGLALARELSRYeDLKVLVLEKEDDVA 41
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
242-301 8.03e-06

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 49.49  E-value: 8.03e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356479  242 LERhgFI-NFGIFKRLK-PIPAKKLGK-VIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGG 301
Cdd:PRK12771 114 VER--FLgDYAIANGWKfPAPAPDTGKrVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGG 174
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
266-301 8.80e-06

Predicted flavin-containing amine oxidase [General function prediction only];


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 48.96  E-value: 8.80e-06
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 21356479 266 KVIVIGAGISGLAVAHQLQQfGMDVIVLEARDRVGG 301
Cdd:COG2907   5 RIAVIGSGISGLTAAWLLSR-RHDVTLFEANDRLGG 39
PRK12775 PRK12775
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ...
254-314 1.92e-05

putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional


Pssm-ID: 183738 [Multi-domain]  Cd Length: 1006  Bit Score: 48.40  E-value: 1.92e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21356479   254 KRLKPIP-AKKLGKVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGG----RISTFRKNSYIAD 314
Cdd:PRK12775  419 KPVKPPRfSKKLGKVAICGSGPAGLAAAADLVKYGVDVTVYEALHVVGGvlqyGIPSFRLPRDIID 484
PLN02612 PLN02612
phytoene desaturase
255-330 3.25e-05

phytoene desaturase


Pssm-ID: 215330 [Multi-domain]  Cd Length: 567  Bit Score: 47.53  E-value: 3.25e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21356479  255 RLKPIPAKKLgKVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRISTFR-KNSYIADVGAMVVTGVYGNPMTI 330
Cdd:PLN02612  85 RSAPRPAKPL-KVVIAGAGLAGLSTAKYLADAGHKPILLEARDVLGGKVAAWKdEDGDWYETGLHIFFGAYPNVQNL 160
PRK07208 PRK07208
hypothetical protein; Provisional
266-316 5.38e-05

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 46.81  E-value: 5.38e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 21356479  266 KVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGrIS-TFRKNSYIADVG 316
Cdd:PRK07208   6 SVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGG-ISrTVTYKGNRFDIG 56
PRK12416 PRK12416
protoporphyrinogen oxidase; Provisional
267-317 8.19e-05

protoporphyrinogen oxidase; Provisional


Pssm-ID: 183516  Cd Length: 463  Bit Score: 45.97  E-value: 8.19e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 21356479  267 VIVIGAGISGLAVAHQLQQ------FGMDVIVLEARDRVGGRISTFRKNSYIADVGA 317
Cdd:PRK12416   4 VVVIGGGITGLSTMFYLEKlkkdynIDLNLILVEKEEYLGGKIHSVEEKDFIMESGA 60
PLN02487 PLN02487
zeta-carotene desaturase
258-338 9.21e-05

zeta-carotene desaturase


Pssm-ID: 215268 [Multi-domain]  Cd Length: 569  Bit Score: 45.95  E-value: 9.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  258 PIPAKKLG---KVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRISTF--RKNSYIaDVGAMVVTGVYGNPMTILS 332
Cdd:PLN02487  66 PEPEAYKGpklKVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGGKVGSFvdKNGNHI-EMGLHVFFGCYNNLFRLMK 144

                 ....*.
gi 21356479  333 KqIGMD 338
Cdd:PLN02487 145 K-VGAD 149
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
254-308 1.15e-04

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 45.62  E-value: 1.15e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21356479 254 KRLKPIPAKKLG---KVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRISTFRK 308
Cdd:COG1148 127 KLLEPLEPIKVPvnkRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQLHK 184
PRK08243 PRK08243
4-hydroxybenzoate 3-monooxygenase; Validated
266-303 1.21e-04

4-hydroxybenzoate 3-monooxygenase; Validated


Pssm-ID: 236198 [Multi-domain]  Cd Length: 392  Bit Score: 45.56  E-value: 1.21e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 21356479  266 KVIVIGAGISGLAVAHQLQQFGMDVIVLEARDR--VGGRI 303
Cdd:PRK08243   4 QVAIIGAGPAGLLLGQLLHLAGIDSVVLERRSReyVEGRI 43
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
261-299 1.27e-04

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 45.00  E-value: 1.27e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 21356479   261 AKKLGKVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRV 299
Cdd:pfam07992 149 KLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRL 187
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
246-322 1.28e-04

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 45.06  E-value: 1.28e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21356479 246 GFINFGIFKRLKPIPAKKL-GKVIVIGAGISGLAVAHQLQQFGMDVIVLEA-RDRVggristfrknSYIADVGAMVVTG 322
Cdd:COG0569  76 GGLLEALRRRRMERGIKKLkMHVIIIGAGRVGRSLARELEEEGHDVVVIDKdPERV----------ERLAEEDVLVIVG 144
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
266-299 2.27e-04

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 40.65  E-value: 2.27e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 21356479   266 KVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRV 299
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRL 34
PRK07538 PRK07538
hypothetical protein; Provisional
266-295 2.45e-04

hypothetical protein; Provisional


Pssm-ID: 236046 [Multi-domain]  Cd Length: 413  Bit Score: 44.50  E-value: 2.45e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 21356479  266 KVIVIGAGISGLAVAHQLQQFGMDVIVLEA 295
Cdd:PRK07538   2 KVLIAGGGIGGLTLALTLHQRGIEVVVFEA 31
PRK08132 PRK08132
FAD-dependent oxidoreductase; Provisional
266-323 4.57e-04

FAD-dependent oxidoreductase; Provisional


Pssm-ID: 236158 [Multi-domain]  Cd Length: 547  Bit Score: 43.70  E-value: 4.57e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21356479  266 KVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRV--GGRISTFRKNSY-IAD-VGA---MVVTGV 323
Cdd:PRK08132  25 PVVVVGAGPVGLALAIDLAQQGVPVVLLDDDDTLstGSRAICFAKRSLeIFDrLGCgerMVDKGV 89
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
255-338 4.69e-04

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 43.95  E-value: 4.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  255 RLKPIPAKKLGK-VIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGR----ISTFRK-----NSYIADVGAMVVTGVY 324
Cdd:PRK12814 183 RYIPERAPKSGKkVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMmrygIPRFRLpesviDADIAPLRAMGAEFRF 262
                         90
                 ....*....|....
gi 21356479  325 GnpmTILSKQIGMD 338
Cdd:PRK12814 263 N---TVFGRDITLE 273
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
267-301 7.19e-04

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 43.05  E-value: 7.19e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 21356479   267 VIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGG 301
Cdd:pfam00890   2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGG 36
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
258-315 1.02e-03

bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 42.81  E-value: 1.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21356479  258 PIPAKKLG-KVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGG----RISTFRKNSYIADV 315
Cdd:PRK12778 424 PEVAEKNGkKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGGvlkyGIPEFRLPKKIVDV 486
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
266-297 1.08e-03

UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440534 [Multi-domain]  Cd Length: 445  Bit Score: 42.38  E-value: 1.08e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 21356479 266 KVIVIGAGISGLAVAHQLQQFGMDVIVLEARD 297
Cdd:COG0771   6 KVLVLGLGKSGLAAARLLAKLGAEVTVSDDRP 37
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
267-301 1.14e-03

Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 42.51  E-value: 1.14e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 21356479 267 VIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGG 301
Cdd:COG1053   6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
PRK12678 PRK12678
transcription termination factor Rho; Provisional
24-152 1.22e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 42.58  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479   24 SDDSDGEPTPKRNVNHPPSALSAPNPGQKQKHPDEDSNDAPATSDERRTSRRNRPKVDYSNRPSGSGDTASNDKSGSASM 103
Cdd:PRK12678 120 SAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRD 199
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 21356479  104 GPNNQQAERRSQSQTRKSEANATSSSVSGPSAGNSRPSQNGDSKDRDAG 152
Cdd:PRK12678 200 GDDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRG 248
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
24-156 1.25e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.85  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479    24 SDDSDGEPTPKRNVNHP--PSALSAPNPGQKQKHPDEDSNDAPATSDERRTSRRNRPKVDYS-----NRPSGSGDTASND 96
Cdd:PHA03307  287 SSSSPRERSPSPSPSSPgsGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSrspspSRPPPPADPSSPR 366
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21356479    97 KSGSASMGPNNQQAE--RRSQSQTRKSEANATSSSVSGPSAGNSRPSQNGDSKDRDAGTPTV 156
Cdd:PHA03307  367 KRPRPSRAPSSPAASagRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYA 428
PRK12831 PRK12831
putative oxidoreductase; Provisional
255-301 1.47e-03

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 41.93  E-value: 1.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 21356479  255 RLKPIPAKKLGKVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGG 301
Cdd:PRK12831 131 DLSETEEKKGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGG 177
PRK11728 PRK11728
L-2-hydroxyglutarate oxidase;
267-300 1.50e-03

L-2-hydroxyglutarate oxidase;


Pssm-ID: 183292 [Multi-domain]  Cd Length: 393  Bit Score: 41.73  E-value: 1.50e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 21356479  267 VIVIGAGISGLAVAHQLQQF--GMDVIVLEARDRVG 300
Cdd:PRK11728   5 FVIIGGGIVGLSTAMQLQERypGARIAVLEKESGPA 40
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
266-305 1.52e-03

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 41.64  E-value: 1.52e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 21356479 266 KVIVIGAGISGLAVAHQLQQFGMDVIVLEaRDRVGGRIST 305
Cdd:COG0492   2 DVVIIGAGPAGLTAAIYAARAGLKTLVIE-GGEPGGQLAT 40
PRK06847 PRK06847
hypothetical protein; Provisional
266-301 1.58e-03

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 41.78  E-value: 1.58e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 21356479  266 KVIVIGAGISGLAVAHQLQQFGMDVIVLEARD--RVGG 301
Cdd:PRK06847   6 KVLIVGGGIGGLSAAIALRRAGIAVDLVEIDPewRVYG 43
PRK12843 PRK12843
FAD-dependent oxidoreductase;
252-305 1.65e-03

FAD-dependent oxidoreductase;


Pssm-ID: 237225 [Multi-domain]  Cd Length: 578  Bit Score: 42.03  E-value: 1.65e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 21356479  252 IFKRLKPIPAKKLGKVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRIST 305
Cdd:PRK12843   4 VVSELSPERWDAEFDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGTTAT 57
PRK12834 PRK12834
putative FAD-binding dehydrogenase; Reviewed
267-301 1.72e-03

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 183782 [Multi-domain]  Cd Length: 549  Bit Score: 41.81  E-value: 1.72e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 21356479  267 VIVIGAGISGLAVAHQLQQFGMDVIVL--EARDRVGG 301
Cdd:PRK12834   7 VIVVGAGLAGLVAAAELADAGKRVLLLdqENEANLGG 43
murD PRK14106
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
266-344 2.09e-03

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional


Pssm-ID: 184511 [Multi-domain]  Cd Length: 450  Bit Score: 41.49  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356479  266 KVIVIGAGISGLAVAHQLQQFGMDVIVLE--ARDRVGGRISTFRKNSYIADVGAMVVTGVYGNPMTILSKQIGMDLVPIQ 343
Cdd:PRK14106   7 KVLVVGAGVSGLALAKFLKKLGAKVILTDekEEDQLKEALEELGELGIELVLGEYPEEFLEGVDLVVVSPGVPLDSPPVV 86

                 .
gi 21356479  344 Q 344
Cdd:PRK14106  87 Q 87
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
253-304 2.09e-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: 41.76  E-value: 2.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 21356479  253 FKRLKPIPAKKlgkVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRIS 304
Cdd:PRK01747 252 FARPGSPKARD---AAIIGGGIAGAALALALARRGWQVTLYEADEAPAQGAS 300
PRK13984 PRK13984
putative oxidoreductase; Provisional
260-301 2.24e-03

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 41.68  E-value: 2.24e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 21356479  260 PAKKLGKVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGG 301
Cdd:PRK13984 279 PEKKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGG 320
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
267-301 2.58e-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: 41.23  E-value: 2.58e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 21356479 267 VIVIGAGISGLAVAHQLQQFGMDVIVLEaRDRVGG 301
Cdd:COG1249   6 LVVIGAGPGGYVAAIRAAQLGLKVALVE-KGRLGG 39
PRK06753 PRK06753
hypothetical protein; Provisional
266-333 3.75e-03

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 40.44  E-value: 3.75e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21356479  266 KVIVIGAGISGLAVAHQLQQFGMDVIVLEardrvggristfrKNSYIADVGAMVvtGVYGNPMTILSK 333
Cdd:PRK06753   2 KIAIIGAGIGGLTAAALLQEQGHEVKVFE-------------KNESVKEVGAGI--GIGDNVIKKLGN 54
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
233-292 6.10e-03

Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family; Formate dehydrogenase, D-specific 2-hydroxy acid dehydrogenase, Phosphoglycerate Dehydrogenase, Lactate dehydrogenase, Thermostable Phosphite Dehydrogenase, and Hydroxy(phenyl)pyruvate reductase, among others, share a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase, among others. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240622 [Multi-domain]  Cd Length: 302  Bit Score: 39.53  E-value: 6.10e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21356479 233 SLVRRvhsFLERHGFINFGIFKRLKPIPAKKL-GKVI-VIGAGISGLAVAHQLQQFGMDVIV 292
Cdd:cd05198 110 ALLRR---LPRADAAVRRGWGWLWAGFPGYELeGKTVgIVGLGRIGQRVAKRLQAFGMKVLY 168
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
255-301 6.11e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 40.16  E-value: 6.11e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 21356479  255 RLKPIPakklGKVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGG 301
Cdd:PRK06292 164 ELDKLP----KSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILP 206
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
272-303 6.17e-03

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 39.57  E-value: 6.17e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 21356479 272 AGISGLAVAHQLQQFGMDVIVLEARDRVGGRI 303
Cdd:COG0644   1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDKI 32
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
266-303 7.78e-03

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 39.22  E-value: 7.78e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 21356479   266 KVIVIGAGISGLAVAHQLQQFGMDVIVLEA-RDRVGGRI 303
Cdd:pfam07992   2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDeGTCPYGGC 40
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
267-301 9.43e-03

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 39.39  E-value: 9.43e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 21356479 267 VIVIGAGISGLAVAHQLQQFGMDVIVL--EARDRVGG 301
Cdd:COG3573   8 VIVVGAGLAGLVAAAELADAGRRVLLLdqEPEANLGG 44
 
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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