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Conserved domains on  [gi|2277090391|gb|KAI5596607|]
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hypothetical protein BDE02_02G013000 [Populus trichocarpa]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02328 PLN02328
lysine-specific histone demethylase 1 homolog
1-795 0e+00

lysine-specific histone demethylase 1 homolog


:

Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 1665.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391   1 METTAEPPQDPSDNANDVVSEDSSPETDL------------NDHQNSPETILPPSSETQSPL-PNTILDAPVSDSQDDSS 67
Cdd:PLN02328    1 METETKEPEDPADNVNDVVSEASSPETDLslspsqseqnieNDGQNSPETQSPLTELQPSPLpPNTTLDAPVSDSQGDES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391  68 DPIQPPQNPNSTFPAPPPKKRRRRKRFFTEINGNPPFRRHRIGGGLSKEVDVEALIAISVGFPVDSLTEEEIEANVVSTI 147
Cdd:PLN02328   81 SSEQQPQNPNSTEPAPPPKKRRRRKRFFTEINANPAFRRHRVRGGLGKEVDVEALIAISVGFPVDSLTEEEIEANVVSTI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 148 GGTEQANYIVVRNHILSRWRSSVSVWLTRDHALESIRAEHKALVDSAYNFLLQHGYINFGVALSIKEAQLKLNEGVERAN 227
Cdd:PLN02328  161 GGTEQANYIVVRNHILARWRSNVSNWLTRDHALESIRAEHKNLVDSAYNFLLEHGYINFGVAPVIKEAQLRSFEGVEPAN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 228 VVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGGRVKTMILKGEGVVAAADLGGSVLTGINGNPLGVLARQMGLPLHKV 307
Cdd:PLN02328  241 VVVVGAGLAGLVAARQLLSMGFKVVVLEGRARPGGRVKTMKMKGDGVVAAADLGGSVLTGINGNPLGVLARQLGLPLHKV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 308 RDICPLYLPDGKAVDSEIDSRIEASFNKLLDRVCKLRQAMIEEVKSVDVNLGTALEAFRHVYKVAEDPQELMLLNWHLAN 387
Cdd:PLN02328  321 RDICPLYLPDGKAVDAEIDSKIEASFNKLLDRVCKLRQAMIEEVKSVDVNLGTALEAFRHVYKVAEDPQERMLLNWHLAN 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 388 LEYANASLMSNLSMAYWDQDDPYEMGGDHCFIPGGNDTFVRELAKDLPIFYEKTVESIRYGVDGVIVYAGGQGFRGDMVL 467
Cdd:PLN02328  401 LEYANASLMSNLSMAYWDQDDPYEMGGDHCFIPGGNDTFVRELAKDLPIFYERTVESIRYGVDGVIVYAGGQEFHGDMVL 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 468 CTVPLGVLKKGSIEFVPELPQRKKDAIQRLGYGLLNKVALLFPYNFWGGEIDTFGHLTEDPSMRGEFFLFYSYSSVSGGA 547
Cdd:PLN02328  481 CTVPLGVLKKGSIEFYPELPQRKKDAIQRLGYGLLNKVALLFPYNFWGGEIDTFGHLTEDPSMRGEFFLFYSYSSVSGGP 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 548 LLIALVAGDAAVKFETMSPVESVKRVLGILRGIFHPKGIVVPDPVQSVCTRWGKDCFTYGSYSYVAVGSSGDDYDILAES 627
Cdd:PLN02328  561 LLIALVAGDAAVKFETLSPVESVKRVLQILRGIFHPKGIVVPDPVQAVCTRWGKDCFTYGSYSYVAVGSSGDDYDILAES 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 628 VGDGRVFFAGEATNKQYPATMHGAFLSGMREAANILRVANRRSLSVIDKVNNSLEEIDDLNELYDTPNLKFGSFSILFDP 707
Cdd:PLN02328  641 VGDGRVFFAGEATNKQYPATMHGAFLSGMREAANILRVARRRSLCIDDKVNNDEEEDDCLDQLFDTPDLTFGSFSILFDP 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 708 RSNDGESLSLLRVKFQGGESDSCFLCLYGLISRKQAVELSELQDDGKRMEMLYNNFQIRLVGRKGLPNAGESLLTYIKEA 787
Cdd:PLN02328  721 RSNDPESLSLLRVKFQGEKPDSCFLCLYGLVSRKQAIELGELDDDGKRNEYLYEKFQVVLVGRKGLSQEGESLISSIKEA 800

                  ....*...
gi 2277090391 788 RSKLNVGN 795
Cdd:PLN02328  801 RLNLQVFD 808
 
Name Accession Description Interval E-value
PLN02328 PLN02328
lysine-specific histone demethylase 1 homolog
1-795 0e+00

lysine-specific histone demethylase 1 homolog


Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 1665.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391   1 METTAEPPQDPSDNANDVVSEDSSPETDL------------NDHQNSPETILPPSSETQSPL-PNTILDAPVSDSQDDSS 67
Cdd:PLN02328    1 METETKEPEDPADNVNDVVSEASSPETDLslspsqseqnieNDGQNSPETQSPLTELQPSPLpPNTTLDAPVSDSQGDES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391  68 DPIQPPQNPNSTFPAPPPKKRRRRKRFFTEINGNPPFRRHRIGGGLSKEVDVEALIAISVGFPVDSLTEEEIEANVVSTI 147
Cdd:PLN02328   81 SSEQQPQNPNSTEPAPPPKKRRRRKRFFTEINANPAFRRHRVRGGLGKEVDVEALIAISVGFPVDSLTEEEIEANVVSTI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 148 GGTEQANYIVVRNHILSRWRSSVSVWLTRDHALESIRAEHKALVDSAYNFLLQHGYINFGVALSIKEAQLKLNEGVERAN 227
Cdd:PLN02328  161 GGTEQANYIVVRNHILARWRSNVSNWLTRDHALESIRAEHKNLVDSAYNFLLEHGYINFGVAPVIKEAQLRSFEGVEPAN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 228 VVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGGRVKTMILKGEGVVAAADLGGSVLTGINGNPLGVLARQMGLPLHKV 307
Cdd:PLN02328  241 VVVVGAGLAGLVAARQLLSMGFKVVVLEGRARPGGRVKTMKMKGDGVVAAADLGGSVLTGINGNPLGVLARQLGLPLHKV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 308 RDICPLYLPDGKAVDSEIDSRIEASFNKLLDRVCKLRQAMIEEVKSVDVNLGTALEAFRHVYKVAEDPQELMLLNWHLAN 387
Cdd:PLN02328  321 RDICPLYLPDGKAVDAEIDSKIEASFNKLLDRVCKLRQAMIEEVKSVDVNLGTALEAFRHVYKVAEDPQERMLLNWHLAN 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 388 LEYANASLMSNLSMAYWDQDDPYEMGGDHCFIPGGNDTFVRELAKDLPIFYEKTVESIRYGVDGVIVYAGGQGFRGDMVL 467
Cdd:PLN02328  401 LEYANASLMSNLSMAYWDQDDPYEMGGDHCFIPGGNDTFVRELAKDLPIFYERTVESIRYGVDGVIVYAGGQEFHGDMVL 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 468 CTVPLGVLKKGSIEFVPELPQRKKDAIQRLGYGLLNKVALLFPYNFWGGEIDTFGHLTEDPSMRGEFFLFYSYSSVSGGA 547
Cdd:PLN02328  481 CTVPLGVLKKGSIEFYPELPQRKKDAIQRLGYGLLNKVALLFPYNFWGGEIDTFGHLTEDPSMRGEFFLFYSYSSVSGGP 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 548 LLIALVAGDAAVKFETMSPVESVKRVLGILRGIFHPKGIVVPDPVQSVCTRWGKDCFTYGSYSYVAVGSSGDDYDILAES 627
Cdd:PLN02328  561 LLIALVAGDAAVKFETLSPVESVKRVLQILRGIFHPKGIVVPDPVQAVCTRWGKDCFTYGSYSYVAVGSSGDDYDILAES 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 628 VGDGRVFFAGEATNKQYPATMHGAFLSGMREAANILRVANRRSLSVIDKVNNSLEEIDDLNELYDTPNLKFGSFSILFDP 707
Cdd:PLN02328  641 VGDGRVFFAGEATNKQYPATMHGAFLSGMREAANILRVARRRSLCIDDKVNNDEEEDDCLDQLFDTPDLTFGSFSILFDP 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 708 RSNDGESLSLLRVKFQGGESDSCFLCLYGLISRKQAVELSELQDDGKRMEMLYNNFQIRLVGRKGLPNAGESLLTYIKEA 787
Cdd:PLN02328  721 RSNDPESLSLLRVKFQGEKPDSCFLCLYGLVSRKQAIELGELDDDGKRNEYLYEKFQVVLVGRKGLSQEGESLISSIKEA 800

                  ....*...
gi 2277090391 788 RSKLNVGN 795
Cdd:PLN02328  801 RLNLQVFD 808
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
219-664 1.31e-93

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 299.91  E-value: 1.31e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 219 LNEGVERANVVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGGRVKTMILKGEGVVaaADLGGSVLTGINGNPLGvLAR 298
Cdd:COG1231     1 MSRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGLY--AELGAMRIPPSHTNLLA-LAR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 299 QMGLPLHKVRDICP--LYLPDGKAVDSEIDSRIEASFNKLLDrvcKLRQAMIEEVKSVD--------VNLGTALEAFRhv 368
Cdd:COG1231    78 ELGLPLEPFPNENGnaLLYLGGKRVRAGEIAADLRGVAELLA---KLLRALAAALDPWAhpaaeldrESLAEWLRRNG-- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 369 ykVAEDPQELMLlnwHLANLEYANASlmSNLSMAYWDQD-DPYEMGGDHCFIPGGNDTFVRELAKDLP--IFYEKTVESI 445
Cdd:COG1231   153 --ASPSARRLLG---LLGAGEYGADP--DELSLLDLLRYaASAGGGAQQFRIVGGMDQLPRALAAELGdrIRLGAPVTRI 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 446 RYGVDGVIV-YAGGQGFRGDMVLCTVPLGVLKKgsIEFVPELPQRKKDAIQRLGYGLLNKVALLFPYNFWGGEIDTFGHL 524
Cdd:COG1231   226 RQDGDGVTVtTDDGGTVRADAVIVTVPPSVLRR--IEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEEDGLYGGIS 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 525 TEDPSMRGEFFLFYSYSsvSGGALLIALVAGDAAVKFETMSPVESVKRVLGILRGIFhpkGIVVPDPVQSVCTRWGKDCF 604
Cdd:COG1231   304 LTDLPIRQTWYPSNGPD--GGAGVLLGYVGGDDARALAALSPEERVAAALEQLARIF---GVYAAEPVDYVSTDWGRDPW 378
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 605 TYGSYSYVAVGSSGDDYDILAESvgDGRVFFAGEATNKQYPATMHGAFLSGMREAANILR 664
Cdd:COG1231   379 SRGAYAAAPPGQLTAAGPALAEP--DGRIHFAGEHTSDEWPGWVEGALESGERAAAEILA 436
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
235-663 1.64e-88

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: 286.69  E-value: 1.64e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 235 LAGLVAARQLMAMGFKVVVLEGRARPGGRVKTMILKGEGVvaaaDLGGSVLTGiNGNPLGVLARQMGLP----LHKVRDI 310
Cdd:pfam01593   1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVRDDGFLI----ELGAMWFHG-AQPPLLALLKELGLEdrlvLPDPAPF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 311 CPLYLPDGKAVDSEIdSRIEASFNKLLDRVC------KLR-------QAMIEEVKSVDVNLGTALEAFRHVYKVAEDPQE 377
Cdd:pfam01593  76 YTVLFAGGRRYPGDF-RRVPAGWEGLLEFGRllsipeKLRlglaalaSDALDEFDLDDFSLAESLLFLGRRGPGDVEVWD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 378 LMLLNWHLANLEYANASLMSNLS-----MAYWDQDDPYEMGGDHCFIPGGNDTFVRELAKDLP---IFYEKTVESIRYGV 449
Cdd:pfam01593 155 RLIDPELFAALPFASGAFAGDPSelsagLALPLLWALLGEGGSLLLPRGGLGALPDALAAQLLggdVRLNTRVRSIDREG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 450 DGVIV-YAGGQGFRGDMVLCTVPLGVLKKgsIEFVPELPQRKKDAIQRLGYGLLNKVALLFPYNFWGGEIDtFGHLTEDP 528
Cdd:pfam01593 235 DGVTVtLTDGEVIEADAVIVTVPLGVLKR--ILFTPPLPPEKARAIRNLGYGPVNKVHLEFDRKFWPDLGL-LGLLSELL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 529 SMRGEFFLFYSYSS--VSGGALLIA--LVAGDAAVKFETMSPVESVKRVLGILRGIFhpkGIVVPDPVQSVCTRWGKDCF 604
Cdd:pfam01593 312 TGLGTAFSWLTFPNraPPGKGLLLLvyVGPGDRARELEGLSDEELLQAVLRDLRKLF---GEEAPEPLRVLVSDWHTDPW 388
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2277090391 605 TYGSYSYVAVGSSGDDYDILAESVgDGRVFFAGEATNKQYPATMHGAFLSGMREAANIL 663
Cdd:pfam01593 389 PRGSYSLPQYGPGHDDYRPLARTP-DPGLFFAGEHTSTGYPGTVEGAIESGRRAARAVL 446
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
228-466 1.21e-07

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: 54.98  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 228 VVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGGRvkTMILKGEGVVaaADLGGSVLTgingNP--LGVLARQMGLPLH 305
Cdd:TIGR02734   1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGR--AGVLEDDGFR--FDTGPTVIT----MPeaLEELFALAGRDLA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 306 KVRDICPL------YLPDGKAVD-----SEIDSRIEaSFNKllDRVCKLRQAMI--EEVKSVD-VNLGT----------- 360
Cdd:TIGR02734  73 DYVELVPLdpfyrlCWEDGSQLDvdndqEELEAQIA-RFNP--GDVAGYRRFLDyaERVYREGyRKLGYvpflsprdllr 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 361 -------ALEAFRHVYKVA----EDPQELMLLNWH--LANLEYANASLMSNLsMAYWDQDDP--YEMGGDHCFIPGgndt 425
Cdd:TIGR02734 150 adapqllALLAWRSLYSKVarffSDERLRQAFSFHalFLGGNPFRTPSIYAL-ISALEREWGvwFPRGGTGALVAA---- 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2277090391 426 fVRELAKDLPIFYEKTVESIRYGVDGVIVYA----GGQGFRGDMV 466
Cdd:TIGR02734 225 -MAKLAEDLGGELRLNAEVIRIETEGGRATAvhlaDGERLDADAV 268
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
222-280 3.99e-06

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 47.12  E-value: 3.99e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391  222 GVERANVVVVGAGLAGLVAARQLMAMGFKVVVL--------EGRARPGGRVKTMILKG---EGVVAAADL 280
Cdd:smart01002  17 GVPPAKVVVIGAGVVGLGAAATAKGLGAEVTVLdvrparlrQLESLLGARFTTLYSQAellEEAVKEADL 86
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
222-285 1.57e-05

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 47.79  E-value: 1.57e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2277090391 222 GVERANVVVVGAGLAGLVAARQLMAMGFKVVVLE---GRARP-----GGRVKTMILKG---EGVVAAADLG-GSVL 285
Cdd:cd05305   165 GVPPAKVVILGAGVVGENAARVALGLGAEVTVLDinlERLRYlddifGGRVTTLYSNPanlEEALKEADLViGAVL 240
 
Name Accession Description Interval E-value
PLN02328 PLN02328
lysine-specific histone demethylase 1 homolog
1-795 0e+00

lysine-specific histone demethylase 1 homolog


Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 1665.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391   1 METTAEPPQDPSDNANDVVSEDSSPETDL------------NDHQNSPETILPPSSETQSPL-PNTILDAPVSDSQDDSS 67
Cdd:PLN02328    1 METETKEPEDPADNVNDVVSEASSPETDLslspsqseqnieNDGQNSPETQSPLTELQPSPLpPNTTLDAPVSDSQGDES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391  68 DPIQPPQNPNSTFPAPPPKKRRRRKRFFTEINGNPPFRRHRIGGGLSKEVDVEALIAISVGFPVDSLTEEEIEANVVSTI 147
Cdd:PLN02328   81 SSEQQPQNPNSTEPAPPPKKRRRRKRFFTEINANPAFRRHRVRGGLGKEVDVEALIAISVGFPVDSLTEEEIEANVVSTI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 148 GGTEQANYIVVRNHILSRWRSSVSVWLTRDHALESIRAEHKALVDSAYNFLLQHGYINFGVALSIKEAQLKLNEGVERAN 227
Cdd:PLN02328  161 GGTEQANYIVVRNHILARWRSNVSNWLTRDHALESIRAEHKNLVDSAYNFLLEHGYINFGVAPVIKEAQLRSFEGVEPAN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 228 VVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGGRVKTMILKGEGVVAAADLGGSVLTGINGNPLGVLARQMGLPLHKV 307
Cdd:PLN02328  241 VVVVGAGLAGLVAARQLLSMGFKVVVLEGRARPGGRVKTMKMKGDGVVAAADLGGSVLTGINGNPLGVLARQLGLPLHKV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 308 RDICPLYLPDGKAVDSEIDSRIEASFNKLLDRVCKLRQAMIEEVKSVDVNLGTALEAFRHVYKVAEDPQELMLLNWHLAN 387
Cdd:PLN02328  321 RDICPLYLPDGKAVDAEIDSKIEASFNKLLDRVCKLRQAMIEEVKSVDVNLGTALEAFRHVYKVAEDPQERMLLNWHLAN 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 388 LEYANASLMSNLSMAYWDQDDPYEMGGDHCFIPGGNDTFVRELAKDLPIFYEKTVESIRYGVDGVIVYAGGQGFRGDMVL 467
Cdd:PLN02328  401 LEYANASLMSNLSMAYWDQDDPYEMGGDHCFIPGGNDTFVRELAKDLPIFYERTVESIRYGVDGVIVYAGGQEFHGDMVL 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 468 CTVPLGVLKKGSIEFVPELPQRKKDAIQRLGYGLLNKVALLFPYNFWGGEIDTFGHLTEDPSMRGEFFLFYSYSSVSGGA 547
Cdd:PLN02328  481 CTVPLGVLKKGSIEFYPELPQRKKDAIQRLGYGLLNKVALLFPYNFWGGEIDTFGHLTEDPSMRGEFFLFYSYSSVSGGP 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 548 LLIALVAGDAAVKFETMSPVESVKRVLGILRGIFHPKGIVVPDPVQSVCTRWGKDCFTYGSYSYVAVGSSGDDYDILAES 627
Cdd:PLN02328  561 LLIALVAGDAAVKFETLSPVESVKRVLQILRGIFHPKGIVVPDPVQAVCTRWGKDCFTYGSYSYVAVGSSGDDYDILAES 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 628 VGDGRVFFAGEATNKQYPATMHGAFLSGMREAANILRVANRRSLSVIDKVNNSLEEIDDLNELYDTPNLKFGSFSILFDP 707
Cdd:PLN02328  641 VGDGRVFFAGEATNKQYPATMHGAFLSGMREAANILRVARRRSLCIDDKVNNDEEEDDCLDQLFDTPDLTFGSFSILFDP 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 708 RSNDGESLSLLRVKFQGGESDSCFLCLYGLISRKQAVELSELQDDGKRMEMLYNNFQIRLVGRKGLPNAGESLLTYIKEA 787
Cdd:PLN02328  721 RSNDPESLSLLRVKFQGEKPDSCFLCLYGLVSRKQAIELGELDDDGKRNEYLYEKFQVVLVGRKGLSQEGESLISSIKEA 800

                  ....*...
gi 2277090391 788 RSKLNVGN 795
Cdd:PLN02328  801 RLNLQVFD 808
PLN03000 PLN03000
amine oxidase
113-789 0e+00

amine oxidase


Pssm-ID: 178578 [Multi-domain]  Cd Length: 881  Bit Score: 924.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 113 LSKEVDVEALIAISVGFPVDSLTEEEIEANVVSTIGGTEQANYIVVRNHILSRWRSSVSVWLTRDHALESIRAEHKALVD 192
Cdd:PLN03000   75 INKEATTEALLALTAGFPADSLTEEEIEFGVVPIVGGIEQVNYILIRNHIISKWRENISSWVTKEMFLGSIPKHCSSLLD 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 193 SAYNFLLQHGYINFGVALSIKEaqlKLNEGVERANVVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGGRVKTMILKGE 272
Cdd:PLN03000  155 SAYNYLVTHGYINFGIAQAIKD---KFPAQSSKSSVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGGRVYTKKMEAN 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 273 GVVAAADLGGSVLTGINGNPLGVLARQMGLPLHKVRDICPLYLPDGKAVDSEIDSRIEASFNKLLDRVCKLRQAMIEevK 352
Cdd:PLN03000  232 RVGAAADLGGSVLTGTLGNPLGIIARQLGSSLYKVRDKCPLYRVDGKPVDPDVDLKVEVAFNQLLDKASKLRQLMGD--V 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 353 SVDVNLGTALEAFRHVYKVAEDPQELMLLNWHLANLEYANASLMSNLSMAYWDQDDPYEMGGDHCFIPGGNDTFVRELAK 432
Cdd:PLN03000  310 SMDVSLGAALETFRQVSGNDVATEEMGLFNWHLANLEYANAGLVSKLSLAFWDQDDPYDMGGDHCFLPGGNGRLVQALAE 389
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 433 DLPIFYEKTVESIRYGVDGVIVYAGGQGFRGDMVLCTVPLGVLKKGSIEFVPELPQRKKDAIQRLGYGLLNKVALLFPYN 512
Cdd:PLN03000  390 NVPILYEKTVQTIRYGSNGVKVIAGNQVYEGDMVLCTVPLGVLKNGSIKFVPELPQRKLDCIKRLGFGLLNKVAMLFPYV 469
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 513 FWGGEIDTFGHLTEDPSMRGEFFLFYSYSSVSGGALLIALVAGDAAVKFETMSPVESVKRVLGILRGIFHPKGIVVPDPV 592
Cdd:PLN03000  470 FWSTDLDTFGHLTEDPNYRGEFFLFYSYAPVAGGPLLIALVAGEAAHKFETMPPTDAVTRVLHILRGIYEPQGINVPDPL 549
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 593 QSVCTRWGKDCFTYGSYSYVAVGSSGDDYDILAESVGDGRVFFAGEATNKQYPATMHGAFLSGMREAANILRVANRRSLS 672
Cdd:PLN03000  550 QTVCTRWGGDPFSLGSYSNVAVGASGDDYDILAESVGDGRLFFAGEATTRRYPATMHGAFVTGLREAANMAQSAKARGIR 629
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 673 V-IDK--VNNSLEEIDDLNELYDTPNLKFGSFSILFDPRSNDGESLSLLRVKFQG---GESD----------------SC 730
Cdd:PLN03000  630 KrIDRnpSKNAHSCAILLADLFRDPDLEFGSFAIIFSRRNPDPKSPAILRVTLSEprkRNEDpkadqhsnkilfqqlqSH 709
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2277090391 731 F-----LCLYGLISRKQAVELSELQD-DGKRMEMLYNNFQIRLVGRKGLPNAGESLLTYIKEARS 789
Cdd:PLN03000  710 FnqqqqIQVYTLLTRQQALDLREVRGgDEKRLNYLCETLGVKLVGRKGLGPGADSVIASIKAERT 774
PLN02529 PLN02529
lysine-specific histone demethylase 1
105-788 0e+00

lysine-specific histone demethylase 1


Pssm-ID: 178144 [Multi-domain]  Cd Length: 738  Bit Score: 829.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 105 RRHRIGGGLSKEVDVEALIAISVGFPVDSLTEEEIEANVVSTIGGTEQANYIVVRNHILSRWRSSVSVWLTRDHALESIR 184
Cdd:PLN02529   43 KKNRTKQDLEKETETEAMIALSVGFPIDALLEEEIRAGVVRELGGKEQNDYIVVRNHILARWRSNVGIWLSKGQIKETVS 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 185 AEHKALVDSAYNFLLQHGYINFGVALSIKEAQLKL-NEGveraNVVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGGR 263
Cdd:PLN02529  123 SEYEHLISAAYDFLLYNGYINFGVSPSFASPIPEEgTEG----SVIIVGAGLAGLAAARQLLSFGFKVVVLEGRNRPGGR 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 264 VKTMILKGEGVVAAADLGGSVLTGINGNPLGVLARQMGLPLHKVRDICPLYLPDGKAVDSEIDSRIEASFNKLLDRVCKL 343
Cdd:PLN02529  199 VYTQKMGRKGQFAAVDLGGSVITGIHANPLGVLARQLSIPLHKVRDNCPLYKPDGALVDKEIDSNIEFIFNKLLDKVTEL 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 344 RQAMieEVKSVDVNLGTALEAFRHVYKVAEDPQELMLLNWHLANLEYANASLMSNLSMAYWDQDDPYEMGGDHCFIPGGN 423
Cdd:PLN02529  279 RQIM--GGFANDISLGSVLERLRQLYGVARSTEERQLLDWHLANLEYANAGCLSDLSAAYWDQDDPYEMGGDHCFLAGGN 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 424 DTFVRELAKDLPIFYEKTVESIRYGVDGVIVYAGGQGFRGDMVLCTVPLGVLKKGSIEFVPELPQRKKDAIQRLGYGLLN 503
Cdd:PLN02529  357 WRLINALCEGVPIFYGKTVDTIKYGNDGVEVIAGSQVFQADMVLCTVPLGVLKKRTIRFEPELPRRKLAAIDRLGFGLLN 436
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 504 KVALLFPYNFWGGEIDTFGHLTEDPSMRGEFFLFYSYSSVSGGALLIALVAGDAAVKFETMSPVESVKRVLGILRGIFHP 583
Cdd:PLN02529  437 KVAMVFPSVFWGEELDTFGCLNESSNKRGEFFLFYGYHTVSGGPALVALVAGEAAQRFENTDPSTLLHRVLSVLRGIYNP 516
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 584 KGIVVPDPVQSVCTRWGKDCFTYGSYSYVAVGSSGDDYDILAESVGdGRVFFAGEATNKQYPATMHGAFLSGMREAANIL 663
Cdd:PLN02529  517 KGINVPDPIQTICTRWGSDPLSYGSYSHVRVQSSGSDYDILAESVS-GRLFFAGEATTRQYPATMHGAFLSGLREASRIL 595
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 664 RVAN------RRSLSVIDKVNNsleeiDDLNELYDTPNLKFGSFSILFDPRSNDGESLSLLRVKFQGGESDSCF-LCLYG 736
Cdd:PLN02529  596 HVARsqqsnsRKSMQRNSGVSN-----DVLIDLFKRPDLAFGKFSFIFNPLTEDPKSMGIMRVTFDNSGDDLNLpLQLYT 670
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2277090391 737 LISRKQA--VELSELQDDGKrMEMLYNNFQIRLVGRKGLPNAGESLLTYIKEAR 788
Cdd:PLN02529  671 VLSREQAhkLQLDEGSNESK-LSCLMKNLGLKLMGPSSLVNTGGSLISTIANAR 723
PLN02976 PLN02976
amine oxidase
219-693 1.00e-115

amine oxidase


Pssm-ID: 215527 [Multi-domain]  Cd Length: 1713  Bit Score: 384.99  E-value: 1.00e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391  219 LNEGVERANVVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGGRVKTmilKGEGVVAAADLGGSVLTGINGN------- 291
Cdd:PLN02976   687 LCDSVDRKKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGRVYT---DRSSLSVPVDLGASIITGVEADvaterrp 763
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391  292 -PLGVLARQMGLPLHKVRDICPLY-LPDGKAVDSEIDSRIEASFNKLLDRVCKL----------------------RQAM 347
Cdd:PLN02976   764 dPSSLICAQLGLELTVLNSDCPLYdVVTGEKVPADLDEALEAEYNSLLDDMVLLvaqkgehamkmsledgleyalkRRRM 843
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391  348 IEEVKSVDVN-LGTALEAFRHVYKVAED--------------PQELMLLNWHLANLEYANASLMSNLSMAYWDQDDPYE- 411
Cdd:PLN02976   844 PRPGVDIDETeLGNAADDLYDSASTGVDgghcekeskedvlsPLERRVMNWHFAHLEYGCAALLKEVSLPYWNQDDVYGg 923
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391  412 MGGDHCFIPGGNDTFVRELAKDLPIFYEKTVESIRYGVDGV-----------IVYAGGQGFRGDMVLCTVPLGVLKKGSI 480
Cdd:PLN02976   924 FGGAHCMIKGGYSNVVESLAEGLDIHLNHVVTDVSYGSKDAgasgssrkkvkVSTSNGSEFLGDAVLITVPLGCLKAETI 1003
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391  481 EFVPELPQRKKDAIQRLGYGLLNKVALLFPYNFWGGEIDTFGHLTEDPSMRGEFFLFYSYSSVSGGALLIALVAGDAAVK 560
Cdd:PLN02976  1004 KFSPPLPDWKYSSIQRLGFGVLNKVVLEFPEVFWDDSVDYFGATAEETDLRGQCFMFWNVKKTVGAPVLIALVVGKAAID 1083
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391  561 FETMSPVESVKRVLGILRGIFhpKGIVVPDPVQSVCTRWGKDCFTYGSYSYVAVGSSGDDYDILAESVGDGrVFFAGEAT 640
Cdd:PLN02976  1084 GQSMSSSDHVNHALMVLRKLF--GEALVPDPVASVVTDWGRDPFSYGAYSYVAIGASGEDYDILGRPVENC-LFFAGEAT 1160
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2277090391  641 NKQYPATMHGAFLSGMREAANI----------------LRVANRRSLSVIDKVN---NSLEEIDDLNELYDT 693
Cdd:PLN02976  1161 CKEHPDTVGGAMMSGLREAVRIidilntgndytaeveaLETAQRHSESERDEVRditKRLEAVELSNVLYKN 1232
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
219-664 1.31e-93

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 299.91  E-value: 1.31e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 219 LNEGVERANVVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGGRVKTMILKGEGVVaaADLGGSVLTGINGNPLGvLAR 298
Cdd:COG1231     1 MSRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGLY--AELGAMRIPPSHTNLLA-LAR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 299 QMGLPLHKVRDICP--LYLPDGKAVDSEIDSRIEASFNKLLDrvcKLRQAMIEEVKSVD--------VNLGTALEAFRhv 368
Cdd:COG1231    78 ELGLPLEPFPNENGnaLLYLGGKRVRAGEIAADLRGVAELLA---KLLRALAAALDPWAhpaaeldrESLAEWLRRNG-- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 369 ykVAEDPQELMLlnwHLANLEYANASlmSNLSMAYWDQD-DPYEMGGDHCFIPGGNDTFVRELAKDLP--IFYEKTVESI 445
Cdd:COG1231   153 --ASPSARRLLG---LLGAGEYGADP--DELSLLDLLRYaASAGGGAQQFRIVGGMDQLPRALAAELGdrIRLGAPVTRI 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 446 RYGVDGVIV-YAGGQGFRGDMVLCTVPLGVLKKgsIEFVPELPQRKKDAIQRLGYGLLNKVALLFPYNFWGGEIDTFGHL 524
Cdd:COG1231   226 RQDGDGVTVtTDDGGTVRADAVIVTVPPSVLRR--IEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEEDGLYGGIS 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 525 TEDPSMRGEFFLFYSYSsvSGGALLIALVAGDAAVKFETMSPVESVKRVLGILRGIFhpkGIVVPDPVQSVCTRWGKDCF 604
Cdd:COG1231   304 LTDLPIRQTWYPSNGPD--GGAGVLLGYVGGDDARALAALSPEERVAAALEQLARIF---GVYAAEPVDYVSTDWGRDPW 378
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 605 TYGSYSYVAVGSSGDDYDILAESvgDGRVFFAGEATNKQYPATMHGAFLSGMREAANILR 664
Cdd:COG1231   379 SRGAYAAAPPGQLTAAGPALAEP--DGRIHFAGEHTSDEWPGWVEGALESGERAAAEILA 436
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
235-663 1.64e-88

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: 286.69  E-value: 1.64e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 235 LAGLVAARQLMAMGFKVVVLEGRARPGGRVKTMILKGEGVvaaaDLGGSVLTGiNGNPLGVLARQMGLP----LHKVRDI 310
Cdd:pfam01593   1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVRDDGFLI----ELGAMWFHG-AQPPLLALLKELGLEdrlvLPDPAPF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 311 CPLYLPDGKAVDSEIdSRIEASFNKLLDRVC------KLR-------QAMIEEVKSVDVNLGTALEAFRHVYKVAEDPQE 377
Cdd:pfam01593  76 YTVLFAGGRRYPGDF-RRVPAGWEGLLEFGRllsipeKLRlglaalaSDALDEFDLDDFSLAESLLFLGRRGPGDVEVWD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 378 LMLLNWHLANLEYANASLMSNLS-----MAYWDQDDPYEMGGDHCFIPGGNDTFVRELAKDLP---IFYEKTVESIRYGV 449
Cdd:pfam01593 155 RLIDPELFAALPFASGAFAGDPSelsagLALPLLWALLGEGGSLLLPRGGLGALPDALAAQLLggdVRLNTRVRSIDREG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 450 DGVIV-YAGGQGFRGDMVLCTVPLGVLKKgsIEFVPELPQRKKDAIQRLGYGLLNKVALLFPYNFWGGEIDtFGHLTEDP 528
Cdd:pfam01593 235 DGVTVtLTDGEVIEADAVIVTVPLGVLKR--ILFTPPLPPEKARAIRNLGYGPVNKVHLEFDRKFWPDLGL-LGLLSELL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 529 SMRGEFFLFYSYSS--VSGGALLIA--LVAGDAAVKFETMSPVESVKRVLGILRGIFhpkGIVVPDPVQSVCTRWGKDCF 604
Cdd:pfam01593 312 TGLGTAFSWLTFPNraPPGKGLLLLvyVGPGDRARELEGLSDEELLQAVLRDLRKLF---GEEAPEPLRVLVSDWHTDPW 388
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2277090391 605 TYGSYSYVAVGSSGDDYDILAESVgDGRVFFAGEATNKQYPATMHGAFLSGMREAANIL 663
Cdd:pfam01593 389 PRGSYSLPQYGPGHDDYRPLARTP-DPGLFFAGEHTSTGYPGTVEGAIESGRRAARAVL 446
PLN02268 PLN02268
probable polyamine oxidase
228-664 4.39e-75

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 250.37  E-value: 4.39e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 228 VVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGGRVKTMILKGEGVvaaaDLGGSVLTGI-NGNPLGVLARQMGLPLHK 306
Cdd:PLN02268    3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIGGRVHTDYSFGFPV----DMGASWLHGVcNENPLAPLIGRLGLPLYR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 307 V---------RDI--CPLYLPDGKAVDSEIDSRIEASFNKLLDRVCKLRQAMIEevksvDVNLgtaLEAFRHVykVAEDP 375
Cdd:PLN02268   79 TsgdnsvlydHDLesYALFDMDGNQVPQELVTKVGETFERILEETEKVRDEHEE-----DMSL---LQAISIV--LERHP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 376 ---QELM---LLNWHLANLEYANASLMSNLSMAYWDQDDPYEmgGDHCFIPGGNDTFVRELAKDLPIFYEKTVESIRYGV 449
Cdd:PLN02268  149 elrLEGLaheVLQWYLCRMEGWFAADADTISLKSWDQEELLE--GGHGLMVRGYDPVINTLAKGLDIRLNHRVTKIVRRY 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 450 DGVIVYA-GGQGFRGDMVLCTVPLGVLKKGSIEFVPELPQRKKDAIQRLGYGLLNKVALLFPYNFWgGEIDTFGHLTEDP 528
Cdd:PLN02268  227 NGVKVTVeDGTTFVADAAIIAVPLGVLKANIIKFEPELPEWKEEAISDLGVGIENKIALHFDSVFW-PNVEFLGVVAPTS 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 529 SMRGEFFLFYsysSVSGGALLIALVAGDAAVKFETMSPVESVKRVLGILRGIFhPKGivvPDPVQSVCTRWGKDCFTYGS 608
Cdd:PLN02268  306 YGCSYFLNLH---KATGHPVLVYMPAGRLARDIEKLSDEAAANFAMSQLKKML-PDA---TEPVQYLVSRWGSDPNSLGC 378
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2277090391 609 YSYVAVGSSGDDYDILAESVGDgrVFFAGEATNKQYPATMHGAFLSGMREAANILR 664
Cdd:PLN02268  379 YSYDLVGKPHDLYERLRAPVDN--LFFAGEATSSDFPGSVHGAYSTGVMAAEECRM 432
PLN02568 PLN02568
polyamine oxidase
225-664 2.10e-49

polyamine oxidase


Pssm-ID: 215308 [Multi-domain]  Cd Length: 539  Bit Score: 182.72  E-value: 2.10e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 225 RANVVVVGAGLAGLVAARQLMAMG-----FKVVVLEGRARPGGRVKTMILKGEGVvaaaDLGGSVLTGINGNPLGVLARQ 299
Cdd:PLN02568    5 KPRIVIIGAGMAGLTAANKLYTSSaandmFELTVVEGGDRIGGRINTSEFGGERI----EMGATWIHGIGGSPVYKIAQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 300 MGLPLHKVRDICPLYLPD--------GKAVDSEIDSRIEASFNKLLDRVCKLRQAMIEEVKSVDVNL------------G 359
Cdd:PLN02568   81 AGSLESDEPWECMDGFPDrpktvaegGFEVDPSIVESISTLFRGLMDDAQGKLIEPSEVDEVDFVKLaakaarvcesggG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 360 TALEAFRH----VY--KVAEDPQELMLLNWHLANLEYANASLMSNLSMAYWDQDD----------PYEM-GGDHCFIPGG 422
Cdd:PLN02568  161 GSVGSFLRrgldAYwdSVSADEQIKGYGGWSRKLLEEAIFTMHENTQRTYTSADDlstldlaaesEYRMfPGEEITIAKG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 423 NDTFVRELAKDLP---IFYEKTVESIRYGVDGV-IVYAGGQGFRGDMVLCTVPLGVLKKGSIE----FVPELPQRKKDAI 494
Cdd:PLN02568  241 YLSVIEALASVLPpgtIQLGRKVTRIEWQDEPVkLHFADGSTMTADHVIVTVSLGVLKAGIGEdsglFSPPLPDFKTDAI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 495 QRLGYGLLNKVALLF--PYNFWGGEIDTF--------GHLTEDPS------MRGEFFLF--YSYSSVsggalLIALVAGD 556
Cdd:PLN02568  321 SRLGFGVVNKLFVELspRPDGSPEDVAKFpflqmafhRSDSEARHdkipwwMRRTASICpiHKNSSV-----LLSWFAGK 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 557 AAVKFETMSPVEsvkrvlgILRGI------FHPKGIVVPDPVQSVC--------------------TRWGKDCFTYGSYS 610
Cdd:PLN02568  396 EALELEKLSDEE-------IIRGVqttlssFLKRRVAGLGSQSHPLcnggassndgsrwkfvkvlkSKWGTDPLFLGSYS 468
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2277090391 611 YVAVGSSGDDYDILAESVGDG-----------RVFFAGEATNKQYPATMHGAFLSGMREAANILR 664
Cdd:PLN02568  469 YVAVGSSGDDLDRMAEPLPRIsdhdqaggpplQLLFAGEATHRTHYSTTHGAYFSGLREANRLLQ 533
PLN02676 PLN02676
polyamine oxidase
208-663 9.67e-41

polyamine oxidase


Pssm-ID: 215362 [Multi-domain]  Cd Length: 487  Bit Score: 156.80  E-value: 9.67e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 208 VALSIKEAQLKLNEGVERANVVVVGAGLAGLVAARQLMAMGFK-VVVLEGRARPGGRVKTMILKGEGVvaaaDLGGSVLT 286
Cdd:PLN02676    9 VLLAVHLFAVAAMDAKPSPSVIIVGAGMSGISAAKTLSEAGIEdILILEATDRIGGRMRKANFAGVSV----ELGANWVE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 287 GING---NPLGVLARQMGLPLHkVRDICPL----YLPDGKAVDSEIdsrIEASFNKLLDRV--CKLRQAMIEEVKSVDVN 357
Cdd:PLN02676   85 GVGGpesNPIWELANKLKLRTF-YSDFDNLssniYKQDGGLYPKKV---VQKSMKVADASDefGENLSISLSAKKAVDIS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 358 LGTALEAFRHVYKVaedPQElMLLNWHLANLEYANASLMSNLSMAYwdqddP----YEMGGDHCFI--PGGNDTFVRELA 431
Cdd:PLN02676  161 ILTAQRLFGQVPKT---PLE-MVIDYYNYDYEFAEPPRVTSLKNTE-----PnptfVDFGEDEYFVadPRGYESLVYYLA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 432 K-----------DLPIFYEKTVESIRYGVDGVIVYA-GGQGFRGDMVLCTVPLGVLKKGSIEFVPELPQRKKDAIQRLGY 499
Cdd:PLN02676  232 EqflstksgkitDPRLKLNKVVREISYSKNGVTVKTeDGSVYRAKYVIVSVSLGVLQSDLIKFKPPLPDWKIEAIYQFDM 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 500 GLLNKVALLFPYNFWggeidtfghltedPSMRG-EFFLFYS----YSSV--------SGGALLIALVAGDAAVKFETMSP 566
Cdd:PLN02676  312 AVYTKIFLKFPYKFW-------------PSGPGtEFFLYAHerrgYYPFwqhleneyPGSNVLFVTVTDEESRRIEQQPD 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 567 VESVKRVLGILRGIFHPKgivVPDPVQSVCTRWGKDCFTYGSYSYVAVGSSGDDYDILAESVgdGRVFFAGEATNKQYPA 646
Cdd:PLN02676  379 SETKAEIMEVLRKMFGPN---IPEATDILVPRWWSNRFFKGSYSNWPIGVSRYEFDQIRAPV--GRVYFTGEHTSEKYNG 453
                         490
                  ....*....|....*..
gi 2277090391 647 TMHGAFLSGMrEAANIL 663
Cdd:PLN02676  454 YVHGAYLAGI-DTANDL 469
SWIRM pfam04433
SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid ...
132-206 2.91e-17

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: 76.83  E-value: 2.91e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2277090391 132 DSLTEEE--IEANVVSTIGGTeQANYIVVRNHILSRWRSSVSVWLTRDHALESIRAEHkALVDSAYNFLLQHGYINF 206
Cdd:pfam04433   4 DKLHPIEkrLLPEFFNGKSKT-PEVYLEIRNFILNLWRENPKEYLTKTDARRALKGDV-NLISRIHEFLERWGLINF 78
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
225-601 4.36e-15

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: 78.34  E-value: 4.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 225 RANVVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGGRVKTmiLKGEGVVaaADLGG-SVLTgiNGNPLGVLARQMGL- 302
Cdd:COG1232     1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRT--VEVDGFR--IDRGPhSFLT--RDPEVLELLRELGLg 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 303 -----PLHKVRDIcplyLPDGKAVDseI-DSRIEASFNKLLDRVCKLRQAMIEEVKSVDVNLGTALEAF------RHVYK 370
Cdd:COG1232    75 delvwPNTRKSYI----YYGGKLHP--LpQGPLALLRSPLLSLAGKLRALLELLAPRRPPGEDESLAEFvrrrfgREVYE 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 371 V----------AEDPQELmLLNW---HLANLEYANASLMSNLsMAYWDQDDPYEMggdhcFIP--GGNDTFVRELAKDLP 435
Cdd:COG1232   149 RlvepllegvyAGDPDEL-SADWafpRLKRLELEHGSLIKGA-LALRKGAKAGEV-----FGYlrGGLGTLVEALAEALE 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 436 ---IFYEKTVESIRYGVDGVIV-YAGGQGFRGDMVLCTVPLGVLkkgsIEFVPELPQRKKDAIQRLGYGLLNKVALLFPy 511
Cdd:COG1232   222 ageIRLGTRVTAIEREGGGWRVtTSDGETIEADAVVSATPAPAL----ARLLAPLPPEVAAALAGIPYASVAVVALGFD- 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 512 nfwGGEI---DTFG---HLTEDPSMRGefFLFYS----YSSVSGGALLIALVAGDAAVKFETMSPVESVKRVLGILRGIF 581
Cdd:COG1232   297 ---RPDLpppDGFGwlvPRDEGVPILA--VTFSSnkwpHRAPDGKVLLRLEVGGAGDPELWQLSDEELVALALADLRKLL 371
                         410       420
                  ....*....|....*....|
gi 2277090391 582 HPKGivvpDPVQSVCTRWGK 601
Cdd:COG1232   372 GIDA----EPVDTRVVRWPK 387
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
228-530 6.33e-13

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 71.80  E-value: 6.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 228 VVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGGRVKTMILKGegvvAAADLGGSVLTgiNGNPLGVLARQMG----LP 303
Cdd:COG1233     6 VVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTFERPG----FRFDVGPSVLT--MPGVLERLFRELGledyLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 304 LHKVRDICPLYLPDGKAVDSEID-SRIEASFNK-----------LLDRVCKLRQAMIE-----------EVKSVDVNLGT 360
Cdd:COG1233    80 LVPLDPAYRVPFPDGRALDLPRDlERTAAELERlfpgdaeayrrFLAELRRLYDALLEdllyrpllslrDLLRPLALARL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 361 ALEAFRHVYKVA----EDPQELMLLNWHLANL---EYANASLMSNLSMAYwdqddpYEMGGDHCfiPGGNDTFVRELAKD 433
Cdd:COG1233   160 LRLLLRSLRDLLrryfKDPRLRALLAGQALYLglsPDRTPALYALIAYLE------YAGGVWYP--KGGMGALADALARL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 434 L-----PIFYEKTVESIRY---GVDGVIVyAGGQGFRGDMVLCTVPLGVLKKgsiEFVPE--LPQRKKDAIQRLGYGL-- 501
Cdd:COG1233   232 AeelggEIRTGAEVERILVeggRATGVRL-ADGEEIRADAVVSNADPAHTYL---RLLGEeaLPARYRRRLERFRYSPsa 307
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 2277090391 502 -------------LNKVALLFPYNFWGGEIDTF-GHLTEDPSM 530
Cdd:COG1233   308 fklylgldgplpgLAHHTIHLSEDYEAAFDDIFrGRLPEDPSL 350
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
230-293 1.73e-10

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 57.16  E-value: 1.73e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2277090391 230 VVGAGLAGLVAARQLMAMGFKVVVLEGRARPGGRVKTMILKGEGVvaaaDLGGSVLTGINGNPL 293
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYSYRVPGYVF----DYGAHIFHGSDEPNV 60
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
224-266 2.43e-09

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


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 59.51  E-value: 2.43e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2277090391 224 ERANVVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGGRVKT 266
Cdd:COG3380     2 SMPDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGGRMAT 44
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
228-670 2.55e-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: 60.25  E-value: 2.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 228 VVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGGRVKTMILKGEGVVaaADLGGSVLTGINGNPLGvLARQMGLPLHKV 307
Cdd:COG3349     6 VVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGGRARSFPDPDTGLP--IDNGQHVLLGCYRNTLD-LLRRIGAADNLV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 308 -RDICPLYLPDGKAVDSEiDSRIEASFN-----------KLLDRV--------CKLRQAMIEEvksvDVNLGTALEAFR- 366
Cdd:COG3349    83 gPEPLQFPLPGGRRWTLR-APRLPAPLHllrallrapglSLADRLallrlltaCRERRWRELD----DISVADWLRRHGq 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 367 --HVYKVAEDPQELMLLNwhlANLEYANASLMSN-LSMAYWDQDDPYEMGgdhcfIPGG--NDTFVRELAKDL-----PI 436
Cdd:COG3349   158 spRLIRRLWEPLLLAALN---TPPEQASARLALTvLRETLLAGPAASDLL-----VPRGplSELFVDPALAYLearggEV 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 437 FYEKTVESIRY---GVDGVIVyAGGQGFRGDMVLCTVPLGVLKKgsieFVPELPQRK-KDAIQRLGYGLLNKVALLFPYN 512
Cdd:COG3349   230 RLGTRVRALEFdggRVTGLVL-ADGETVPADAVVLAVPPEVAAR----LLPELARLPeLGLLAPLEYSPIVNVHLWLDRP 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 513 FWGGEIDTFGhLTEDPSMrgefFLFYSYSSVSGGALLIALVAGdAAVKFETMSPVESVKRVLGILRGIFhpkGIVVPDPV 592
Cdd:COG3349   305 VTLGPPPFAG-LVGSTSQ----WVFDRGAGDGGQGGVLSVVIS-AADRLLDLSREELAAEVWAELAALL---PAAREALP 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 593 qsvctRWGKD--------CFTYGSYSY---VAVGSSGddydilaesvgdgrVFFAGEATNKQYPATMHGAFLSGMREAAN 661
Cdd:COG3349   376 -----VWSRVvrekratfAATPGSDRLrpgARTPIPN--------------LFLAGDWTATGLPATMEGAVRSGRRAANA 436

                  ....*....
gi 2277090391 662 ILRVANRRS 670
Cdd:COG3349   437 ILARLGRPA 445
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
220-262 5.61e-08

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: 56.02  E-value: 5.61e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2277090391 220 NEGVERANVVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGG 262
Cdd:COG2072     1 TAATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGG 43
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
228-466 1.21e-07

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: 54.98  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 228 VVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGGRvkTMILKGEGVVaaADLGGSVLTgingNP--LGVLARQMGLPLH 305
Cdd:TIGR02734   1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGR--AGVLEDDGFR--FDTGPTVIT----MPeaLEELFALAGRDLA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 306 KVRDICPL------YLPDGKAVD-----SEIDSRIEaSFNKllDRVCKLRQAMI--EEVKSVD-VNLGT----------- 360
Cdd:TIGR02734  73 DYVELVPLdpfyrlCWEDGSQLDvdndqEELEAQIA-RFNP--GDVAGYRRFLDyaERVYREGyRKLGYvpflsprdllr 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 361 -------ALEAFRHVYKVA----EDPQELMLLNWH--LANLEYANASLMSNLsMAYWDQDDP--YEMGGDHCFIPGgndt 425
Cdd:TIGR02734 150 adapqllALLAWRSLYSKVarffSDERLRQAFSFHalFLGGNPFRTPSIYAL-ISALEREWGvwFPRGGTGALVAA---- 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2277090391 426 fVRELAKDLPIFYEKTVESIRYGVDGVIVYA----GGQGFRGDMV 466
Cdd:TIGR02734 225 -MAKLAEDLGGELRLNAEVIRIETEGGRATAvhlaDGERLDADAV 268
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
228-262 6.19e-07

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: 52.44  E-value: 6.19e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2277090391 228 VVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGG 262
Cdd:COG0493   124 VAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG 158
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
224-262 7.95e-07

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 52.49  E-value: 7.95e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2277090391 224 ERANVVVVGAGLAGLVAARQLMAMGFKVVVL--EGRARPGG 262
Cdd:COG3573     4 MDADVIVVGAGLAGLVAAAELADAGRRVLLLdqEPEANLGG 44
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
224-281 1.33e-06

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: 51.09  E-value: 1.33e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2277090391 224 ERANVVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGGRVKTMILKGEGVVAAADLG 281
Cdd:COG0654     2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSPRSLELLRRLG 59
PRK07233 PRK07233
hypothetical protein; Provisional
227-262 1.85e-06

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 51.04  E-value: 1.85e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2277090391 227 NVVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGG 262
Cdd:PRK07233    1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGG 36
PRK12834 PRK12834
putative FAD-binding dehydrogenase; Reviewed
224-262 2.07e-06

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 183782 [Multi-domain]  Cd Length: 549  Bit Score: 51.05  E-value: 2.07e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2277090391 224 ERANVVVVGAGLAGLVAARQLMAMGFKVVVL--EGRARPGG 262
Cdd:PRK12834    3 MDADVIVVGAGLAGLVAAAELADAGKRVLLLdqENEANLGG 43
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
222-280 3.99e-06

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 47.12  E-value: 3.99e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391  222 GVERANVVVVGAGLAGLVAARQLMAMGFKVVVL--------EGRARPGGRVKTMILKG---EGVVAAADL 280
Cdd:smart01002  17 GVPPAKVVVIGAGVVGLGAAATAKGLGAEVTVLdvrparlrQLESLLGARFTTLYSQAellEEAVKEADL 86
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
224-262 4.66e-06

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 49.52  E-value: 4.66e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2277090391 224 ERANVVVVGAGLAGLVAARQLMAMGFKVVVLEgRARPGG 262
Cdd:COG0665     1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLE-RGRPGS 38
Ald COG0686
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ...
222-285 5.64e-06

Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and metabolism]; Alanine dehydrogenase (includes sporulation protein SpoVN) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440450 [Multi-domain]  Cd Length: 372  Bit Score: 49.24  E-value: 5.64e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2277090391 222 GVERANVVVVGAGLAGLVAARQLMAMGFKVVVLE---GRAR-----PGGRVKTMILKG---EGVVAAADLG-GSVL 285
Cdd:COG0686   165 GVPPAKVVILGGGVVGTNAARMALGLGADVTVLDinlDRLRrlddiFGGRVTTLYSNPaniEEALKEADLViGAVL 240
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
228-262 1.03e-05

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 48.64  E-value: 1.03e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2277090391 228 VVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGG 262
Cdd:PRK11749  143 VAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG 177
gltD PRK12810
glutamate synthase subunit beta; Reviewed
228-275 1.23e-05

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 48.62  E-value: 1.23e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2277090391 228 VVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGG------------------RVKtmILKGEGVV 275
Cdd:PRK12810  146 VAVVGSGPAGLAAADQLARAGHKVTVFERADRIGGllrygipdfklekevidrRIE--LMEAEGIE 209
PLN02576 PLN02576
protoporphyrinogen oxidase
226-267 1.39e-05

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 48.47  E-value: 1.39e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2277090391 226 ANVVVVGAGLAGLVAARQLMA-MGFKVVVLEGRARPGGRVKTM 267
Cdd:PLN02576   13 KDVAVVGAGVSGLAAAYALASkHGVNVLVTEARDRVGGNITSV 55
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
222-285 1.57e-05

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 47.79  E-value: 1.57e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2277090391 222 GVERANVVVVGAGLAGLVAARQLMAMGFKVVVLE---GRARP-----GGRVKTMILKG---EGVVAAADLG-GSVL 285
Cdd:cd05305   165 GVPPAKVVILGAGVVGENAARVALGLGAEVTVLDinlERLRYlddifGGRVTTLYSNPanlEEALKEADLViGAVL 240
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
228-262 2.70e-05

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: 47.52  E-value: 2.70e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2277090391 228 VVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGG 262
Cdd:COG1053     6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
228-262 4.24e-05

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: 46.62  E-value: 4.24e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2277090391 228 VVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGG 262
Cdd:pfam01266   2 VVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGS 36
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
233-361 5.70e-05

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 45.73  E-value: 5.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 233 AGLAGLVAARQLMAMGFKVVVLEGRARPGGRVktmilKGEGVVAAA--DLGgsvltgingnPLGVLArQMGLPLHKVRdi 310
Cdd:COG0644     1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDKI-----CGGGLLPRAleELE----------PLGLDE-PLERPVRGAR-- 62
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2277090391 311 cpLYLPDGKAVdsEIDSRIEASFnkLLDRVcKLRQAMIEEVKS--VDVNLGTA 361
Cdd:COG0644    63 --FYSPGGKSV--ELPPGRGGGY--VVDRA-RFDRWLAEQAEEagAEVRTGTR 108
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
227-267 5.91e-05

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 46.39  E-value: 5.91e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2277090391 227 NVVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGGRVKTM 267
Cdd:COG1148   142 RALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQL 182
PRK13984 PRK13984
putative oxidoreductase; Provisional
219-262 6.33e-05

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 46.30  E-value: 6.33e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2277090391 219 LNEGVERAN--VVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGG 262
Cdd:PRK13984  275 LDDEPEKKNkkVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGG 320
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
222-257 1.05e-04

Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.


Pssm-ID: 426165 [Multi-domain]  Cd Length: 213  Bit Score: 44.41  E-value: 1.05e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2277090391 222 GVERANVVVVGAGLAGLVAARQLMAMGFKVVVLEGR 257
Cdd:pfam01262  25 GVAPAKVLVIGGGVAGLNAAATAKGLGAIVTILDVR 60
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
226-264 2.43e-04

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 44.36  E-value: 2.43e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2277090391 226 ANVVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGGRV 264
Cdd:COG1251   143 KRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQ 181
PRK07208 PRK07208
hypothetical protein; Provisional
224-271 2.76e-04

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 44.11  E-value: 2.76e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2277090391 224 ERANVVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGGRVKTMILKG 271
Cdd:PRK07208    3 NKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGISRTVTYKG 50
Thi4 pfam01946
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
226-262 4.21e-04

Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.


Pssm-ID: 460393  Cd Length: 232  Bit Score: 42.84  E-value: 4.21e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2277090391 226 ANVVVVGAGLAGLVAARQLM-AMGFKVVVLEGRARPGG 262
Cdd:pfam01946  18 SDVVIVGAGSSGLTAAYYLAkNRGLKVAIIERSVSPGG 55
GdhA COG0334
Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism]; Glutamate ...
206-252 4.55e-04

Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism]; Glutamate dehydrogenase/leucine dehydrogenase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440103 [Multi-domain]  Cd Length: 411  Bit Score: 43.51  E-value: 4.55e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2277090391 206 FGVALSIKEAQLKLNEGVERANVVVVGAGLAGLVAARQLMAMGFKVV 252
Cdd:COG0334   189 RGVVYFAREALKKLGLSLEGKTVAVQGFGNVGSYAAELLHELGAKVV 235
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
228-262 6.30e-04

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 43.18  E-value: 6.30e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2277090391 228 VVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGG 262
Cdd:PRK12814  196 VAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGG 230
PLN02172 PLN02172
flavin-containing monooxygenase FMO GS-OX
227-262 9.07e-04

flavin-containing monooxygenase FMO GS-OX


Pssm-ID: 215116 [Multi-domain]  Cd Length: 461  Bit Score: 42.54  E-value: 9.07e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2277090391 227 NVVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGG 262
Cdd:PLN02172   12 HVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGG 47
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
228-262 9.60e-04

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 42.55  E-value: 9.60e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2277090391 228 VVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGG 262
Cdd:PRK12771  140 VAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGG 174
PLN02612 PLN02612
phytoene desaturase
227-264 1.18e-03

phytoene desaturase


Pssm-ID: 215330 [Multi-domain]  Cd Length: 567  Bit Score: 42.14  E-value: 1.18e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2277090391 227 NVVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGGRV 264
Cdd:PLN02612   95 KVVIAGAGLAGLSTAKYLADAGHKPILLEARDVLGGKV 132
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
227-263 1.26e-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: 41.53  E-value: 1.26e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2277090391 227 NVVVVGAGLAGLVAARQLMAMGFKVVVLE-GRARPGGR 263
Cdd:pfam07992   2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEdEGTCPYGG 39
PRK07804 PRK07804
L-aspartate oxidase; Provisional
223-254 1.54e-03

L-aspartate oxidase; Provisional


Pssm-ID: 236102 [Multi-domain]  Cd Length: 541  Bit Score: 41.88  E-value: 1.54e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2277090391 223 VERANVVVVGAGLAGLVAARQLMAMGFKVVVL 254
Cdd:PRK07804   14 RDAADVVVVGSGVAGLTAALAARRAGRRVLVV 45
PRK12831 PRK12831
putative oxidoreductase; Provisional
228-262 2.09e-03

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 41.54  E-value: 2.09e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2277090391 228 VVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGG 262
Cdd:PRK12831  143 VAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGG 177
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
226-262 2.14e-03

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 41.69  E-value: 2.14e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2277090391  226 ANVVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGG 262
Cdd:PTZ00306   410 ARVIVVGGGLAGCSAAIEAASCGAQVILLEKEAKLGG 446
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
227-303 2.17e-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: 41.22  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 227 NVVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGGRVKTmiLKGEGV-VAAADLGGSVLTGIN------G----NPLGV 295
Cdd:COG0771     6 KVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPAPELAAAE--LEAPGVeVVLGEHPEELLDGADlvvkspGippdHPLLK 83

                  ....*...
gi 2277090391 296 LARQMGLP 303
Cdd:COG0771    84 AARAAGIP 91
PLN02487 PLN02487
zeta-carotene desaturase
224-264 2.60e-03

zeta-carotene desaturase


Pssm-ID: 215268 [Multi-domain]  Cd Length: 569  Bit Score: 41.32  E-value: 2.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2277090391 224 ERANVVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGGRV 264
Cdd:PLN02487   74 PKLKVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGGKV 114
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
228-262 3.17e-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: 40.84  E-value: 3.17e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2277090391 228 VVVVGAGLAGLVAARQLMAMGFKVVVLEgRARPGG 262
Cdd:COG1249     6 LVVIGAGPGGYVAAIRAAQLGLKVALVE-KGRLGG 39
PRK06370 PRK06370
FAD-containing oxidoreductase;
224-262 3.63e-03

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 40.57  E-value: 3.63e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2277090391 224 ERANVVVVGAGLAGLVAARQLMAMGFKVVVLEgRARPGG 262
Cdd:PRK06370    4 QRYDAIVIGAGQAGPPLAARAAGLGMKVALIE-RGLLGG 41
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
228-262 3.94e-03

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: 40.35  E-value: 3.94e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2277090391 228 VVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGG 262
Cdd:pfam00890   2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGG 36
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
228-261 3.97e-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: 40.60  E-value: 3.97e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2277090391 228 VVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPG 261
Cdd:PRK01747  263 AAIIGGGIAGAALALALARRGWQVTLYEADEAPA 296
PRK07843 PRK07843
3-oxosteroid 1-dehydrogenase;
227-290 4.75e-03

3-oxosteroid 1-dehydrogenase;


Pssm-ID: 236111 [Multi-domain]  Cd Length: 557  Bit Score: 40.40  E-value: 4.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2277090391 227 NVVVVGAGLAGLVAARQLMAMGFKVVVLE-------GRARPGGRV---KTMILKGEGVVAAADLGGSVLTGING 290
Cdd:PRK07843    9 DVVVVGSGAAGMVAALTAAHRGLSTVVVEkaphyggSTARSGGGVwipNNEVLKRAGVPDTPEAARTYLHSIVG 82
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
228-262 5.15e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 40.16  E-value: 5.15e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2277090391 228 VVVVGAGLAGLVAARQLMAMGFKVVVLEGrARPGG 262
Cdd:PRK06292    6 VIVIGAGPAGYVAARRAAKLGKKVALIEK-GPLGG 39
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
205-264 5.45e-03

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 39.79  E-value: 5.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2277090391 205 NFGVALSIKEAqLKLNEGverANVVVVGAGLAGLVAARQLMAMGFKVVVLEGRARPGGRV 264
Cdd:COG0446   108 TLDDADALREA-LKEFKG---KRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGVL 163
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
228-267 5.98e-03

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 39.72  E-value: 5.98e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2277090391 228 VVVVGAGLAGLVAARQLMAMGFKVVVLEGRArPGGRVKTM 267
Cdd:COG0492     3 VVIIGAGPAGLTAAIYAARAGLKTLVIEGGE-PGGQLATT 41
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
228-271 6.41e-03

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 39.83  E-value: 6.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2277090391 228 VVVVGAGLAGLVAARQL--MAMGFKVVVLEGRARPGGRVKTMILKG 271
Cdd:PRK11883    3 VAIIGGGITGLSAAYRLhkKGPDADITLLEASDRLGGKIQTVRKDG 48
NAD_bind_1_Glu_DH cd01076
NAD(P) binding domain of glutamate dehydrogenase, subgroup 1; Amino acid dehydrogenase (DH) is ...
206-252 7.77e-03

NAD(P) binding domain of glutamate dehydrogenase, subgroup 1; Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. Glutamate DH is a multidomain enzyme that catalyzes the reaction from glutamate to 2-oxyoglutarate and ammonia in the presence of NAD or NADP. It is present in all organisms. Enzymes involved in ammonia assimilation are typically NADP+-dependent, while those involved in glutamate catabolism are generally NAD+-dependent. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha -beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133445 [Multi-domain]  Cd Length: 227  Bit Score: 38.67  E-value: 7.77e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2277090391 206 FGVALSIKEAQLKLNEGVERANVVVVGAGLAGLVAARQLMAMGFKVV 252
Cdd:cd01076    12 RGVAYATREALKKLGIGLAGARVAIQGFGNVGSHAARFLHEAGAKVV 58
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
220-260 8.63e-03

bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 39.50  E-value: 8.63e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2277090391 220 NEGVERANVVVVGAGLAGLVAARQLMAMGFKVVVLEGRARP 260
Cdd:PRK06183    5 HPDAHDTDVVIVGAGPVGLTLANLLGQYGVRVLVLERWPTL 45
YhiN COG2081
Predicted flavoprotein YhiN [General function prediction only];
229-261 8.65e-03

Predicted flavoprotein YhiN [General function prediction only];


Pssm-ID: 441684 [Multi-domain]  Cd Length: 402  Bit Score: 39.26  E-value: 8.65e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2277090391 229 VVVGAGLAGLVAARQLMAMGFKVVVLEGRARPG 261
Cdd:COG2081     1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVG 33
 
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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