|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02328 |
PLN02328 |
lysine-specific histone demethylase 1 homolog |
210-852 |
2.16e-127 |
|
lysine-specific histone demethylase 1 homolog
Pssm-ID: 215187 [Multi-domain] Cd Length: 808 Bit Score: 402.83 E-value: 2.16e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 210 LPHDRMTSQE-AACFPDIISGPQQTQkvFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSdtvLVHRVHSYLERHGL 288
Cdd:PLN02328 142 FPVDSLTEEEiEANVVSTIGGTEQAN--YIVVRNHILARWRSNVSNWLTRDHALESIRAEHKN---LVDSAYNFLLEHGY 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 289 INFGIYKRIKPLPIK-----KTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFR-KGNYV---ADLGAM 359
Cdd:PLN02328 217 INFGVAPVIKEAQLRsfegvEPANVVVVGAGLAGLVAARQLLSMGFKVVVLEGRARPGGRVKTMKmKGDGVvaaADLGGS 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 360 VVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEFNRLLEAtsylshqldfnvlnnkpvslgqal 439
Cdd:PLN02328 297 VLTGINGNPLGVLARQLGLPLHKVRDICPLYLPDGKAVDAEIDSKIEASFNKLLDR------------------------ 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 440 evVIQLQEKHVkdeqiehwkkivktqEELKELlnkMVNLKEKIKELHQQYKeasevkpprditaeflvkskhrdltalck 519
Cdd:PLN02328 353 --VCKLRQAMI---------------EEVKSV---DVNLGTALEAFRHVYK----------------------------- 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 520 eydeLAETQgkleeklqeleanppsdvylssRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYS 599
Cdd:PLN02328 384 ----VAEDP----------------------QERMLLNWHLANLEYANASLMSNLSMAYWDQDDPYEMGGDHCFIPGGND 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 600 CVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRstsqtfiYKCDAVLCTLPLGVLKQQppAVQFVPPLPEWKTSAVQ 679
Cdd:PLN02328 438 TFVRELAKDLPIFYERTVESIRYGVDGVIVYAGGQE-------FHGDMVLCTVPLGVLKKG--SIEFYPELPQRKKDAIQ 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 680 RMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFW---NLYKAPILLALVAGEAAGIMENISDDVIVGRCLA 756
Cdd:PLN02328 509 RLGYGLLNKVALLFPYNFWGGEIDTFGHLTEDPSMRGEFFLFYsysSVSGGPLLIALVAGDAAVKFETLSPVESVKRVLQ 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 757 ILKGIFGSS--AVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGpsipgapqpipRLFFAGEHTIRNY 834
Cdd:PLN02328 589 ILRGIFHPKgiVVPDPVQAVCTRWGKDCFTYGSYSYVAVGSSGDDYDILAESVGDG-----------RVFFAGEATNKQY 657
|
650
....*....|....*...
gi 37360004 835 PATVHGALLSGLREAGRI 852
Cdd:PLN02328 658 PATMHGAFLSGMREAANI 675
|
|
| PLN03000 |
PLN03000 |
amine oxidase |
205-853 |
8.95e-125 |
|
amine oxidase
Pssm-ID: 178578 [Multi-domain] Cd Length: 881 Bit Score: 397.85 E-value: 8.95e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 205 AFQSRLPHDRMTSQE--AACFPdIISGPQQTQkvFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSdtvLVHRVHSY 282
Cdd:PLN03000 86 ALTAGFPADSLTEEEieFGVVP-IVGGIEQVN--YILIRNHIISKWRENISSWVTKEMFLGSIPKHCSS---LLDSAYNY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 283 LERHGLINFGIYKRIK-PLPIKKT-GKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFR-KGNYV---ADL 356
Cdd:PLN03000 160 LVTHGYINFGIAQAIKdKFPAQSSkSSVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGGRVYTKKmEANRVgaaADL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 357 GAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEFNRLLEATSYLsHQLDFNVlnNKPVSLG 436
Cdd:PLN03000 240 GGSVLTGTLGNPLGIIARQLGSSLYKVRDKCPLYRVDGKPVDPDVDLKVEVAFNQLLDKASKL-RQLMGDV--SMDVSLG 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 437 QALEVVIQLQEKHVKDEQIehwkkivktqeelkellnkmvnlkekikelhqqykeasevkpprditaeflvkskhrdlta 516
Cdd:PLN03000 317 AALETFRQVSGNDVATEEM------------------------------------------------------------- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 517 lckeydelaetqgkleeklqeleanppsdvylssrdrQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRN 596
Cdd:PLN03000 336 -------------------------------------GLFNWHLANLEYANAGLVSKLSLAFWDQDDPYDMGGDHCFLPG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 597 GYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTrstsqtfIYKCDAVLCTLPLGVLKQQppAVQFVPPLPEWKTS 676
Cdd:PLN03000 379 GNGRLVQALAENVPILYEKTVQTIRYGSNGVKVIAGNQ-------VYEGDMVLCTVPLGVLKNG--SIKFVPELPQRKLD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 677 AVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWN---LYKAPILLALVAGEAAGIMENISDDVIVGR 753
Cdd:PLN03000 450 CIKRLGFGLLNKVAMLFPYVFWSTDLDTFGHLTEDPNYRGEFFLFYSyapVAGGPLLIALVAGEAAHKFETMPPTDAVTR 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 754 CLAILKGIFGSSA--VPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGpsipgapqpipRLFFAGEHTI 831
Cdd:PLN03000 530 VLHILRGIYEPQGinVPDPLQTVCTRWGGDPFSLGSYSNVAVGASGDDYDILAESVGDG-----------RLFFAGEATT 598
|
650 660
....*....|....*....|..
gi 37360004 832 RNYPATVHGALLSGLREAGRIA 853
Cdd:PLN03000 599 RRYPATMHGAFVTGLREAANMA 620
|
|
| PLN02529 |
PLN02529 |
lysine-specific histone demethylase 1 |
234-852 |
5.17e-117 |
|
lysine-specific histone demethylase 1
Pssm-ID: 178144 [Multi-domain] Cd Length: 738 Bit Score: 373.07 E-value: 5.17e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 234 QKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSdtvLVHRVHSYLERHGLINFGIYKRI-KPLPIKKT-GKVIII 311
Cdd:PLN02529 90 QNDYIVVRNHILARWRSNVGIWLSKGQIKETVSSEYEH---LISAAYDFLLYNGYINFGVSPSFaSPIPEEGTeGSVIIV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 312 GSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVAT---FRKGNYVA-DLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKC 387
Cdd:PLN02529 167 GAGLAGLAAARQLLSFGFKVVVLEGRNRPGGRVYTqkmGRKGQFAAvDLGGSVITGIHANPLGVLARQLSIPLHKVRDNC 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 388 PLYEANGQAVPKEKDEMVEQEFNRLLEATSylshqldfnvlnnkpvslgqalevviqlqekhvkdeqiehwkkivktqeE 467
Cdd:PLN02529 247 PLYKPDGALVDKEIDSNIEFIFNKLLDKVT-------------------------------------------------E 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 468 LKELLNKMVNlkekikelhqqykeasevkpprDITAeflvkskhrdltalckeydelaetqGKLEEKLQELEAnppsdVY 547
Cdd:PLN02529 278 LRQIMGGFAN----------------------DISL-------------------------GSVLERLRQLYG-----VA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 548 LSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGC 627
Cdd:PLN02529 306 RSTEERQLLDWHLANLEYANAGCLSDLSAAYWDQDDPYEMGGDHCFLAGGNWRLINALCEGVPIFYGKTVDTIKYGNDGV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 628 EVIAvntrsTSQtfIYKCDAVLCTLPLGVLKQQppAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGH 707
Cdd:PLN02529 386 EVIA-----GSQ--VFQADMVLCTVPLGVLKKR--TIRFEPELPRRKLAAIDRLGFGLLNKVAMVFPSVFWGEELDTFGC 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 708 VGSTTASRGELFLFWNLYK---APILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSA--VPQPKETVVSRWRADP 782
Cdd:PLN02529 457 LNESSNKRGEFFLFYGYHTvsgGPALVALVAGEAAQRFENTDPSTLLHRVLSVLRGIYNPKGinVPDPIQTICTRWGSDP 536
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 783 WARGSYSYVAAGSSGNDYDLMAQpitpgpSIPGapqpipRLFFAGEHTIRNYPATVHGALLSGLREAGRI 852
Cdd:PLN02529 537 LSYGSYSHVRVQSSGSDYDILAE------SVSG------RLFFAGEATTRQYPATMHGAFLSGLREASRI 594
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
307-854 |
8.53e-113 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 379.60 E-value: 8.53e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 307 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYV-ADLGAMVVTGLGGN--------PMAVVSKQVN 377
Cdd:PLN02976 695 KIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGRVYTDRSSLSVpVDLGASIITGVEADvaterrpdPSSLICAQLG 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 378 MELAKIKQKCPLYE-ANGQAVPKEKDEMVEQEFNRLLEatsylshQLDFNVLNNKPVSLGQALEvviqlqekhvkdEQIE 456
Cdd:PLN02976 775 LELTVLNSDCPLYDvVTGEKVPADLDEALEAEYNSLLD-------DMVLLVAQKGEHAMKMSLE------------DGLE 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 457 HwkkivktqeELKEllNKMVNLKEKIKElhqqykeasevkpprditaeflvkskhrdlTALCKEYDELAETQgKLEEKLQ 536
Cdd:PLN02976 836 Y---------ALKR--RRMPRPGVDIDE------------------------------TELGNAADDLYDSA-STGVDGG 873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 537 ELEANPPSDVyLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFE-FTGSHLTVRNGYSCVPVALAEGLDIKLNT 615
Cdd:PLN02976 874 HCEKESKEDV-LSPLERRVMNWHFAHLEYGCAALLKEVSLPYWNQDDVYGgFGGAHCMIKGGYSNVVESLAEGLDIHLNH 952
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 616 AVRQVRY-------TASGCEVIAVNTRSTSQtfiYKCDAVLCTLPLGVLKQQppAVQFVPPLPEWKTSAVQRMGFGNLNK 688
Cdd:PLN02976 953 VVTDVSYgskdagaSGSSRKKVKVSTSNGSE---FLGDAVLITVPLGCLKAE--TIKFSPPLPDWKYSSIQRLGFGVLNK 1027
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 689 VVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYK---APILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSS 765
Cdd:PLN02976 1028 VVLEFPEVFWDDSVDYFGATAEETDLRGQCFMFWNVKKtvgAPVLIALVVGKAAIDGQSMSSSDHVNHALMVLRKLFGEA 1107
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 766 AVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGpsipgapqpiprLFFAGEHTIRNYPATVHGALLSG 845
Cdd:PLN02976 1108 LVPDPVASVVTDWGRDPFSYGAYSYVAIGASGEDYDILGRPVENC------------LFFAGEATCKEHPDTVGGAMMSG 1175
|
....*....
gi 37360004 846 LREAGRIAD 854
Cdd:PLN02976 1176 LREAVRIID 1184
|
|
| Amino_oxidase |
pfam01593 |
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ... |
315-852 |
2.08e-98 |
|
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: 314.81 E-value: 2.08e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 315 VSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGgNPMAVVSKQVNMELakiKQKCPLYEA-- 392
Cdd:pfam01593 1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVRDDGFLIELGAMWFHGAQ-PPLLALLKELGLED---RLVLPDPAPfy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 393 -----NGQAVPKEKdEMVEQEFNRLLEAtsylshqldfnvlnnkpvslgqalevviqlqekhvkdeqiehwkkivktqee 467
Cdd:pfam01593 77 tvlfaGGRRYPGDF-RRVPAGWEGLLEF---------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 468 lkellNKMVNLKEKIKELHqqykeasevkpprditaeFLVKSKHRDLTALCKeydelaetqGKLEEKLQELEANPPSDVY 547
Cdd:pfam01593 104 -----GRLLSIPEKLRLGL------------------AALASDALDEFDLDD---------FSLAESLLFLGRRGPGDVE 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 548 LSsrDRQILDWHFANLEFANAT-----PLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAE---GLDIKLNTAVRQ 619
Cdd:pfam01593 152 VW--DRLIDPELFAALPFASGAfagdpSELSAGLALPLLWALLGEGGSLLLPRGGLGALPDALAAqllGGDVRLNTRVRS 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 620 VRYTASGCEVIAVNTRStsqtfiYKCDAVLCTLPLGVLKqqppAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWD 699
Cdd:pfam01593 230 IDREGDGVTVTLTDGEV------IEADAVIVTVPLGVLK----RILFTPPLPPEKARAIRNLGYGPVNKVHLEFDRKFWP 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 700 PSvNLFGHVGSTTASRGELFLF--WNLY----KAPILLALV-AGEAAGIMENISDDVIVGRCLAILKGIFGSsAVPQPKE 772
Cdd:pfam01593 300 DL-GLLGLLSELLTGLGTAFSWltFPNRappgKGLLLLVYVgPGDRARELEGLSDEELLQAVLRDLRKLFGE-EAPEPLR 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 773 TVVSRWRADPWARGSYSYVAAGSSGNDYDlmaqpitpgpsiPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRI 852
Cdd:pfam01593 378 VLVSDWHTDPWPRGSYSLPQYGPGHDDYR------------PLARTPDPGLFFAGEHTSTGYPGTVEGAIESGRRAARAV 445
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
307-858 |
1.30e-72 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 245.60 E-value: 1.30e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 307 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKG--NYVADLGAMVVTGLGGNPMAVVsKQVNMELakik 384
Cdd:COG1231 9 DVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGddGLYAELGAMRIPPSHTNLLALA-RELGLPL---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 385 qkCPLYEANGQAVpkekdemveqefnrlleatsYlshqldfnVLNNKPVSLGQalevviqlqekhvkdeqiehwkkIVKT 464
Cdd:COG1231 84 --EPFPNENGNAL--------------------L--------YLGGKRVRAGE-----------------------IAAD 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 465 QEELKELLNKMVnlkekikelhqqykeasevkppRDITAEFlvkskhRDLTALCKEYDElaetqgkleEKLQE-LEANPp 543
Cdd:COG1231 111 LRGVAELLAKLL----------------------RALAAAL------DPWAHPAAELDR---------ESLAEwLRRNG- 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 544 sdvyLSSRDRQILDwhfANLEFANATPLSTLSLKHWDQD-DDFEFTGSHLTVRNGYSCVPVALAEGL--DIKLNTAVRQV 620
Cdd:COG1231 153 ----ASPSARRLLG---LLGAGEYGADPDELSLLDLLRYaASAGGGAQQFRIVGGMDQLPRALAAELgdRIRLGAPVTRI 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 621 RYTASGCEVIavntrsTSQTFIYKCDAVLCTLPLGVLKQqppaVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDP 700
Cdd:COG1231 226 RQDGDGVTVT------TDDGGTVRADAVIVTVPPSVLRR----IEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEE 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 701 SvnlfGHVGSTTASRGELFL-FWNLY----KAPILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAvPQPKETVV 775
Cdd:COG1231 296 D----GLYGGISLTDLPIRQtWYPSNgpdgGAGVLLGYVGGDDARALAALSPEERVAAALEQLARIFGVYA-AEPVDYVS 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 776 SRWRADPWARGSYSYVAAGSSGNDYDLMAQPItpgpsipgapqpiPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQ 855
Cdd:COG1231 371 TDWGRDPWSRGAYAAAPPGQLTAAGPALAEPD-------------GRIHFAGEHTSDEWPGWVEGALESGERAAAEILAR 437
|
...
gi 37360004 856 FLG 858
Cdd:COG1231 438 LGG 440
|
|
| PLN02268 |
PLN02268 |
probable polyamine oxidase |
308-849 |
1.65e-71 |
|
probable polyamine oxidase
Pssm-ID: 177909 [Multi-domain] Cd Length: 435 Bit Score: 242.29 E-value: 1.65e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 308 VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGG-NPMAVVSKQVNMELAKIK-- 384
Cdd:PLN02268 3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIGGRVHTDYSFGFPVDMGASWLHGVCNeNPLAPLIGRLGLPLYRTSgd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 385 ---------QKCPLYEANGQAVPKEKDEMVEQEFNRLLEATsylshqldfnvlnnkpvslgqalevviqlqeKHVKDEQI 455
Cdd:PLN02268 83 nsvlydhdlESYALFDMDGNQVPQELVTKVGETFERILEET-------------------------------EKVRDEHE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 456 EHwkkivktqeelkellnkmVNLKEKIKelhqqykeasevkpprditaefLVKSKHRDLtalckeydelaetqgkleeKL 535
Cdd:PLN02268 132 ED------------------MSLLQAIS----------------------IVLERHPEL-------------------RL 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 536 QELeanppsdvylssrDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEftGSHLTVRNGYSCVPVALAEGLDIKLNT 615
Cdd:PLN02268 153 EGL-------------AHEVLQWYLCRMEGWFAADADTISLKSWDQEELLE--GGHGLMVRGYDPVINTLAKGLDIRLNH 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 616 AVRQVRYTASGCEViavnTRSTSQTFIykCDAVLCTLPLGVLKQQppAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDR 695
Cdd:PLN02268 218 RVTKIVRRYNGVKV----TVEDGTTFV--ADAAIIAVPLGVLKAN--IIKFEPELPEWKEEAISDLGVGIENKIALHFDS 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 696 VFWdPSVNLFGHVGSTTASRGelfLFWNLYKA---PILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSavPQPKE 772
Cdd:PLN02268 290 VFW-PNVEFLGVVAPTSYGCS---YFLNLHKAtghPVLVYMPAGRLARDIEKLSDEAAANFAMSQLKKMLPDA--TEPVQ 363
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37360004 773 TVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITpgpsipgapqpipRLFFAGEHTIRNYPATVHGALLSGLREA 849
Cdd:PLN02268 364 YLVSRWGSDPNSLGCYSYDLVGKPHDLYERLRAPVD-------------NLFFAGEATSSDFPGSVHGAYSTGVMAA 427
|
|
| PLN02568 |
PLN02568 |
polyamine oxidase |
304-852 |
1.02e-41 |
|
polyamine oxidase
Pssm-ID: 215308 [Multi-domain] Cd Length: 539 Bit Score: 161.15 E-value: 1.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 304 KTGKVIIIGSGVSGLAAARQLQSFG-----MDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNm 378
Cdd:PLN02568 4 KKPRIVIIGAGMAGLTAANKLYTSSaandmFELTVVEGGDRIGGRINTSEFGGERIEMGATWIHGIGGSPVYKIAQEAG- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 379 elakikqkcplyeANGQAVPKEKdemveqefnrlleatsylshqldFNVLNNKPVSLGQALEVViqlqekhvkDEQIEHw 458
Cdd:PLN02568 83 -------------SLESDEPWEC-----------------------MDGFPDRPKTVAEGGFEV---------DPSIVE- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 459 kkivktqeELKELLNKMVNLKEKiKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALCKeydelaetQGkLEEKLQEL 538
Cdd:PLN02568 117 --------SISTLFRGLMDDAQG-KLIEPSEVDEVDFVKLAAKAARVCESGGGGSVGSFLR--------RG-LDAYWDSV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 539 EANPPSDVYLSSRDRQILDWHFA---NLE--FANATPLSTLSLkhwDQDDDF-EFTGSHLTVRNGYSCVPVALAEGLD-- 610
Cdd:PLN02568 179 SADEQIKGYGGWSRKLLEEAIFTmheNTQrtYTSADDLSTLDL---AAESEYrMFPGEEITIAKGYLSVIEALASVLPpg 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 611 -IKLNTAVRQVRYTAsgcEVIAVNTRSTSqtfIYKCDAVLCTLPLGVLKQQ--PPAVQFVPPLPEWKTSAVQRMGFGNLN 687
Cdd:PLN02568 256 tIQLGRKVTRIEWQD---EPVKLHFADGS---TMTADHVIVTVSLGVLKAGigEDSGLFSPPLPDFKTDAISRLGFGVVN 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 688 KVVLCF----DRVFWD----PSVNLFGHvGSTTASRGELFLFW-----NLY----KAPILLALVAGEAAGIMENISDDVI 750
Cdd:PLN02568 330 KLFVELsprpDGSPEDvakfPFLQMAFH-RSDSEARHDKIPWWmrrtaSICpihkNSSVLLSWFAGKEALELEKLSDEEI 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 751 V-------------------GRCLAILKGIFGSSAVPQPKETVV--SRWRADPWARGSYSYVAAGSSGNDYDLMAQPITP 809
Cdd:PLN02568 409 IrgvqttlssflkrrvaglgSQSHPLCNGGASSNDGSRWKFVKVlkSKWGTDPLFLGSYSYVAVGSSGDDLDRMAEPLPR 488
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 37360004 810 GPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRI 852
Cdd:PLN02568 489 ISDHDQAGGPPLQLLFAGEATHRTHYSTTHGAYFSGLREANRL 531
|
|
| PLN02676 |
PLN02676 |
polyamine oxidase |
303-849 |
1.02e-36 |
|
polyamine oxidase
Pssm-ID: 215362 [Multi-domain] Cd Length: 487 Bit Score: 145.24 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 303 KKTGKVIIIGSGVSGLAAARQLQSFGM-DVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGnpmavvsKQVNmela 381
Cdd:PLN02676 24 KPSPSVIIVGAGMSGISAAKTLSEAGIeDILILEATDRIGGRMRKANFAGVSVELGANWVEGVGG-------PESN---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 382 kikqkcPLYEangqavpkekdeMVEQefnrlLEATSYLShqlDF-NVLNNkpvslgqalevvIQLQEKHVKDEqiehwkk 460
Cdd:PLN02676 93 ------PIWE------------LANK-----LKLRTFYS---DFdNLSSN------------IYKQDGGLYPK------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 461 ivktqeelkellnkmvnlkekiKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALckeydelaetqgkleeKLQELEA 540
Cdd:PLN02676 128 ----------------------KVVQKSMKVADASDEFGENLSISLSAKKAVDISIL----------------TAQRLFG 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 541 NPPSdvylsSRDRQILDWHFANLEFA---------NATPLSTLSlkhwDQDDDFEFTGShltvRNGYSCVPVALAEG--- 608
Cdd:PLN02676 170 QVPK-----TPLEMVIDYYNYDYEFAepprvtslkNTEPNPTFV----DFGEDEYFVAD----PRGYESLVYYLAEQfls 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 609 ------LD--IKLNTAVRQVRYTASGcevIAVNTRSTSqtfIYKCDAVLCTLPLGVLkqQPPAVQFVPPLPEWKTSAVQR 680
Cdd:PLN02676 237 tksgkiTDprLKLNKVVREISYSKNG---VTVKTEDGS---VYRAKYVIVSVSLGVL--QSDLIKFKPPLPDWKIEAIYQ 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 681 MGFGNLNKVVLCFDRVFWdPSVN-----LFGHVgsttaSRGeLFLFW----NLYK-APILLALVAGEAAGIMENISDDVI 750
Cdd:PLN02676 309 FDMAVYTKIFLKFPYKFW-PSGPgteffLYAHE-----RRG-YYPFWqhleNEYPgSNVLFVTVTDEESRRIEQQPDSET 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 751 VGRCLAILKGIFGSSaVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITpgpsipgapqpipRLFFAGEHT 830
Cdd:PLN02676 382 KAEIMEVLRKMFGPN-IPEATDILVPRWWSNRFFKGSYSNWPIGVSRYEFDQIRAPVG-------------RVYFTGEHT 447
|
570
....*....|....*....
gi 37360004 831 IRNYPATVHGALLSGLREA 849
Cdd:PLN02676 448 SEKYNGYVHGAYLAGIDTA 466
|
|
| SWIRM |
pfam04433 |
SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid ... |
213-291 |
3.66e-23 |
|
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: 93.78 E-value: 3.66e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37360004 213 DRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEapynSDTVLVHRVHSYLERHGLINF 291
Cdd:pfam04433 4 DKLHPIEKRLLPEFFNGKSKTPEVYLEIRNFILNLWRENPKEYLTKTDARRALK----GDVNLISRIHEFLERWGLINF 78
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
307-358 |
1.54e-14 |
|
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: 76.79 E-value: 1.54e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 37360004 307 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGA 358
Cdd:COG1232 3 RVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRTVEVDGFRIDRGP 54
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
310-369 |
2.40e-14 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 68.33 E-value: 2.40e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 310 IIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPM 369
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYSYRVPGYVFDYGAHIFHGSDEPNV 60
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
307-362 |
6.35e-14 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 75.27 E-value: 6.35e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 37360004 307 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVT 362
Cdd:COG1233 5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTFERPGFRFDVGPSVLT 60
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
307-358 |
4.59e-13 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 71.45 E-value: 4.59e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 37360004 307 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGA 358
Cdd:COG3380 5 DIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGGRMATRRLDGGRFDHGA 56
|
|
| crtI_fam |
TIGR02734 |
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ... |
308-362 |
9.28e-11 |
|
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: 65.38 E-value: 9.28e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 37360004 308 VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVT 362
Cdd:TIGR02734 1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGRAGVLEDDGFRFDTGPTVIT 55
|
|
| PRK11883 |
PRK11883 |
protoporphyrinogen oxidase; Reviewed |
307-358 |
1.34e-09 |
|
protoporphyrinogen oxidase; Reviewed
Pssm-ID: 237009 [Multi-domain] Cd Length: 451 Bit Score: 61.40 E-value: 1.34e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 37360004 307 KVIIIGSGVSGLAAARQLQSFG--MDVTLLEARDRVGGRVATFRKGNYVADLGA 358
Cdd:PRK11883 2 KVAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKIQTVRKDGFPIELGP 55
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
305-357 |
2.71e-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: 2.71e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 37360004 305 TGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRkgnyVADLG 357
Cdd:COG3349 3 PPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGGRARSFP----DPDTG 51
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
295-342 |
3.08e-09 |
|
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: 60.15 E-value: 3.08e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 37360004 295 KRIKPLPIKKTGK-VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 342
Cdd:COG0493 110 WVKPPPPAPRTGKkVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG 158
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
307-352 |
4.37e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 59.52 E-value: 4.37e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 37360004 307 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNY 352
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAASFEFGGL 46
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
297-342 |
1.58e-08 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 57.87 E-value: 1.58e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 37360004 297 IKPL-PIKKTGK-VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 342
Cdd:PRK12810 133 VKPDpPVKRTGKkVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGG 180
|
|
| PLN02576 |
PLN02576 |
protoporphyrinogen oxidase |
308-358 |
2.34e-08 |
|
protoporphyrinogen oxidase
Pssm-ID: 215314 [Multi-domain] Cd Length: 496 Bit Score: 57.72 E-value: 2.34e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 37360004 308 VIIIGSGVSGLAAARQLQS-FGMDVTLLEARDRVGGRVATFRKGNYVADLGA 358
Cdd:PLN02576 15 VAVVGAGVSGLAAAYALASkHGVNVLVTEARDRVGGNITSVSEDGFIWEEGP 66
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
308-352 |
2.41e-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: 57.18 E-value: 2.41e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 37360004 308 VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGrvaTFRKGNY 352
Cdd:COG2072 9 VVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGG---TWRDNRY 50
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
307-346 |
2.37e-07 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 53.97 E-value: 2.37e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 37360004 307 KVIIIGSGVSGLAAARQLQSfGMDVTLLEARDRVGGRVAT 346
Cdd:COG2907 5 RIAVIGSGISGLTAAWLLSR-RHDVTLFEANDRLGGHTHT 43
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
297-342 |
2.58e-07 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 54.03 E-value: 2.58e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 37360004 297 IKPLPIKKTGK-VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 342
Cdd:PRK11749 131 VLFKRAPKTGKkVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG 177
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
307-348 |
4.65e-07 |
|
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: 52.79 E-value: 4.65e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 37360004 307 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRvATFR 348
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSG-ASGR 41
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
374-540 |
1.49e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.06 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 374 KQVNMELAKIKQKcpLYEANGQAvpKEKDEMVEQ------EFNRLLEATSYLSHQLD--FNVLNNKPVSLGQALEVVIQL 445
Cdd:COG1340 67 DELNEKVKELKEE--RDELNEKL--NELREELDElrkelaELNKAGGSIDKLRKEIErlEWRQQTEVLSPEEEKELVEKI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 446 QEKhvkDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQ------------------YKEASEVKPPRD-ITAEFL 506
Cdd:COG1340 143 KEL---EKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKikelaeeaqelheemielYKEADELRKEADeLHKEIV 219
|
170 180 190
....*....|....*....|....*....|....
gi 37360004 507 VKSKHRDltALCKEYDELAETQGKLEEKLQELEA 540
Cdd:COG1340 220 EAQEKAD--ELHEEIIELQKELRELRKELKKLRK 251
|
|
| proto_IX_ox |
TIGR00562 |
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ... |
305-358 |
3.28e-06 |
|
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 213540 [Multi-domain] Cd Length: 462 Bit Score: 50.60 E-value: 3.28e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 37360004 305 TGKVIIIGSGVSGLAAARQLQ----SFGMDVTLLEARDRVGGRVATFRKGNYVADLGA 358
Cdd:TIGR00562 2 KKHVVIIGGGISGLCAAYYLEkeipELPVELTLVEASDRVGGKIQTVKEDGYLIERGP 59
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
307-348 |
3.57e-06 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 50.29 E-value: 3.57e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 37360004 307 KVIIIGSGVSGLAAARQLQSFGMDVTLLEaRDRVGGRvATFR 348
Cdd:COG0665 4 DVVVIGGGIAGLSTAYHLARRGLDVTVLE-RGRPGSG-ASGR 43
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
299-342 |
4.34e-06 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 50.26 E-value: 4.34e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 37360004 299 PLPIKKTGK-VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 342
Cdd:PRK12771 130 PAPAPDTGKrVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGG 174
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
288-349 |
5.11e-06 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 50.24 E-value: 5.11e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37360004 288 LINFGIYK--RIKPL---PIKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRK 349
Cdd:COG1148 118 LVRMAVAKakLLEPLepiKVPVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQLHK 184
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
295-342 |
1.46e-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: 48.78 E-value: 1.46e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 37360004 295 KRIKPLPI-KKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 342
Cdd:PRK12775 419 KPVKPPRFsKKLGKVAICGSGPAGLAAAADLVKYGVDVTVYEALHVVGG 467
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
301-342 |
1.60e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 48.61 E-value: 1.60e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 37360004 301 PIKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 342
Cdd:PRK13984 279 PEKKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGG 320
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
307-357 |
3.19e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 47.58 E-value: 3.19e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 37360004 307 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG--RVATFrKGNYVaDLG 357
Cdd:PRK07208 6 SVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGisRTVTY-KGNRF-DIG 56
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
437-540 |
3.54e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 437 QALEVVIQLQEKHVKDEQIEHWKK-----IVKTQEELKELLNKMVNLKEKIKELHQQYKEA-SEVKpprdiTAEFLVK-- 508
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKelpaeLAELEDELAALEARLEAAKTELEDLEKEIKRLeLEIE-----EVEARIKky 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 37360004 509 -------SKHRDLTALCKEYDELAETQGKLEEKLQELEA 540
Cdd:COG1579 79 eeqlgnvRNNKEYEALQKEIESLKRRISDLEDEILELME 117
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
296-342 |
3.58e-05 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 47.42 E-value: 3.58e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 37360004 296 RIKPLPIKKTGK-VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 342
Cdd:PRK12814 183 RYIPERAPKSGKkVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGG 230
|
|
| PLN02487 |
PLN02487 |
zeta-carotene desaturase |
299-353 |
4.05e-05 |
|
zeta-carotene desaturase
Pssm-ID: 215268 [Multi-domain] Cd Length: 569 Bit Score: 47.10 E-value: 4.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 299 PLPIKKTG---KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATF--RKGNYV 353
Cdd:PLN02487 66 PEPEAYKGpklKVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGGKVGSFvdKNGNHI 125
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
378-552 |
4.12e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 378 MELAKIKQKCPL----------------YEANGQAVPKEKDEMVEQE---FNRLLEATSYLSHQldfnvlnNKPVSLGQA 438
Cdd:PRK03918 429 EELKKAKGKCPVcgrelteehrkelleeYTAELKRIEKELKEIEEKErklRKELRELEKVLKKE-------SELIKLKEL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 439 LEVVIQLQEK---HVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVkpprditaEFLVKSKHRDLT 515
Cdd:PRK03918 502 AEQLKELEEKlkkYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL--------EKKLDELEEELA 573
|
170 180 190
....*....|....*....|....*....|....*...
gi 37360004 516 ALCKEYDELA-ETQGKLEEKLQELEanPPSDVYLSSRD 552
Cdd:PRK03918 574 ELLKELEELGfESVEELEERLKELE--PFYNEYLELKD 609
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
447-540 |
4.41e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 447 EKHVKDEQIEHWKKIVKTQEELKELLNKMVN--------LKEKIKELHQQYKEASEVKP-PRDItaEFLVKSKHRDLTAL 517
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEELAELLKELEElgfesveeLEERLKELEPFYNEYLELKDaEKEL--EREEKELKKLEEEL 628
|
90 100
....*....|....*....|...
gi 37360004 518 CKEYDELAETQGKLEEKLQELEA 540
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEE 651
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
307-343 |
5.19e-05 |
|
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: 46.47 E-value: 5.19e-05
10 20 30
....*....|....*....|....*....|....*..
gi 37360004 307 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGR 343
Cdd:COG0654 5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPD 41
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
307-346 |
7.23e-05 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 45.88 E-value: 7.23e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 37360004 307 KVIIIGSGVSGLAAARQLQSFGMDVTLLEaRDRVGGRVAT 346
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIE-GGEPGGQLAT 40
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
306-340 |
9.39e-05 |
|
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: 45.39 E-value: 9.39e-05
10 20 30
....*....|....*....|....*....|....*
gi 37360004 306 GKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRV 340
Cdd:pfam07992 153 KRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRL 187
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
294-363 |
1.33e-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: 44.67 E-value: 1.33e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37360004 294 YKRIKPLPIKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEA-RDRVggrvatfrkgNYVADLGAMVVTG 363
Cdd:COG0569 84 RRRMERGIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVIDKdPERV----------ERLAEEDVLVIVG 144
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
298-342 |
1.68e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 45.01 E-value: 1.68e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 37360004 298 KPLPIKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 342
Cdd:PRK12831 133 SETEEKKGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGG 177
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
307-340 |
1.69e-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: 41.04 E-value: 1.69e-04
10 20 30
....*....|....*....|....*....|....
gi 37360004 307 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRV 340
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRL 34
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
65-125 |
2.15e-04 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 45.06 E-value: 2.15e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37360004 65 AAPPAGLTGPTDMATGAAGERTPRKKEPPRASPP----GGLAEPPGSAGPQAGPTAGPGSATPME 125
Cdd:PHA03378 714 AQRPAAATGRARPPAAAPGRARPPAAAPGRARPPaaapGRARPPAAAPGRARPPAAAPGAPTPQP 778
|
|
| PLN02612 |
PLN02612 |
phytoene desaturase |
296-348 |
2.48e-04 |
|
phytoene desaturase
Pssm-ID: 215330 [Multi-domain] Cd Length: 567 Bit Score: 44.83 E-value: 2.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 37360004 296 RIKPLPIKKTgKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFR 348
Cdd:PLN02612 85 RSAPRPAKPL-KVVIAGAGLAGLSTAKYLADAGHKPILLEARDVLGGKVAAWK 136
|
|
| LhgO |
COG0579 |
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism]; |
308-341 |
2.58e-04 |
|
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
Pssm-ID: 440344 [Multi-domain] Cd Length: 418 Bit Score: 44.37 E-value: 2.58e-04
10 20 30
....*....|....*....|....*....|....*
gi 37360004 308 VIIIGSGVSGLAAARQL-QSFGMDVTLLEARDRVG 341
Cdd:COG0579 7 VVIIGAGIVGLALARELsRYEDLKVLVLEKEDDVA 41
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
308-342 |
3.50e-04 |
|
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: 43.92 E-value: 3.50e-04
10 20 30
....*....|....*....|....*....|....*
gi 37360004 308 VIIIGSGVSGLAAARQLQSFGMDVTLLEaRDRVGG 342
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVE-KGRLGG 39
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
399-555 |
4.29e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 399 KEKDEMVEQEFNRLLEATSYLSHQL-----DFNVLNNKPVSLGQALEVVIQLQEKhVKDEQIEHWKKIVKTQEELKELLN 473
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIekkqqEINEKTTEISNTQTQLNQLKDEQNK-IKKQLSEKQKELEQNNKKIKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 474 KMVNLKEKIKELHQQyKEA---SEVKpprditaEFLvKSKHRDLTALCKEYD-------ELAETQGKLEEKLQELEANPp 543
Cdd:TIGR04523 289 QLNQLKSEISDLNNQ-KEQdwnKELK-------SEL-KNQEKKLEEIQNQISqnnkiisQLNEQISQLKKELTNSESEN- 358
|
170
....*....|..
gi 37360004 544 sdvylSSRDRQI 555
Cdd:TIGR04523 359 -----SEKQREL 365
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
443-555 |
5.78e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 443 IQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKppRDITAEFLVKSK-----HRDLTAL 517
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL--AQAQEELESLQEeaeelQEELEEL 120
|
90 100 110
....*....|....*....|....*....|....*...
gi 37360004 518 CKEYDELAETQGKLEEKLQELEANppsdvyLSSRDRQI 555
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSE------IAEREEEL 152
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
294-344 |
6.94e-04 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 42.82 E-value: 6.94e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 37360004 294 YKRIKPLpIKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRV 344
Cdd:COG1251 132 ADALRAA-LAPGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQ 181
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
307-343 |
7.91e-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: 42.31 E-value: 7.91e-04
10 20 30
....*....|....*....|....*....|....*...
gi 37360004 307 KVIIIGSGVSGLAAARQLQSFGMDVTLLEA-RDRVGGR 343
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDeGTCPYGG 39
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
299-342 |
1.27e-03 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 42.42 E-value: 1.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 37360004 299 PLPIKKTG-KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 342
Cdd:PRK12778 424 PEVAEKNGkKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGG 468
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
307-363 |
1.38e-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: 41.99 E-value: 1.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 37360004 307 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKgnyvadLGAMVVTG 363
Cdd:COG0771 6 KVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPAPELAAAELEA------PGVEVVLG 56
|
|
| MRPL52 |
pfam18699 |
Mitoribosomal protein mL52; Members of this family include the mamalian mitoribosomal proteins ... |
424-497 |
2.68e-03 |
|
Mitoribosomal protein mL52; Members of this family include the mamalian mitoribosomal proteins mL52 which is found in the 39S subunit. The mL52 has no homologs in yeast.
Pssm-ID: 465836 Cd Length: 91 Bit Score: 37.95 E-value: 2.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37360004 424 DFNVLNNKPVSLGQalevviqLQEKHvKDEQIEHWKKIVKTQEELKELLnKMVNLKEKIKELHQQYKEASEVKP 497
Cdd:pfam18699 25 DFSFADGRPAPVTS-------GQLKR-KLKQIELAKKIVKLSSEVDEAE-ERYKRKQEEEEEEIQKIIDNKLKP 89
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
306-346 |
2.77e-03 |
|
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: 39.03 E-value: 2.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 37360004 306 GKVIIIGSGVSGLAAARQLQSFGMDVTLL--------EARDRVGGRVAT 346
Cdd:smart01002 21 AKVVVIGAGVVGLGAAATAKGLGAEVTVLdvrparlrQLESLLGARFTT 69
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
399-541 |
2.87e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 399 KEKDEMVEQEFNRLLEATSYLSHQLDF--NVLNNKPVSLGQALEVVIQLQ-EKHVKDEQIEHWKKIVKTQEELKELLNK- 474
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDElrAELTLLNEEAANLRERLESLErRIAATERRLEDLEEQIEELSEDIESLAAe 860
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37360004 475 MVNLKEKIKELHQQYKEASEVKpprditaeflvKSKHRDLTALCKEYDELAETQGKLEEKLQELEAN 541
Cdd:TIGR02168 861 IEELEELIEELESELEALLNER-----------ASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
308-366 |
2.98e-03 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 41.06 E-value: 2.98e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37360004 308 VIIIGSGVSG----LAAARQlqsfGMDVTLLEARDRVGGR-----VATFRkGNYVADlgAMVVTGLGG 366
Cdd:pfam12831 2 VVVVGGGPAGvaaaIAAARA----GAKVLLVERRGFLGGMltsglVGPDM-GFYLNK--EQVVGGIAR 62
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
399-539 |
3.08e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 399 KEKDEMVEQEFNRLLEATSYLSHQLDFNVLNN-KPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLN---- 473
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDlSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAeagv 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 474 --------------KMVNLKEKIKELHQQYKE-ASEVKPPRDITAEFLVKSKHRDLT----ALCKEYDELAETQGKLEEK 534
Cdd:COG4717 382 edeeelraaleqaeEYQELKEELEELEEQLEElLGELEELLEALDEEELEEELEELEeeleELEEELEELREELAELEAE 461
|
....*
gi 37360004 535 LQELE 539
Cdd:COG4717 462 LEQLE 466
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
445-540 |
3.15e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 445 LQEKHVKDEQIEhwKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPprditaeflVKSKHRDLTALCKEY--- 521
Cdd:PRK03918 240 IEELEKELESLE--GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKE---------KAEEYIKLSEFYEEYlde 308
|
90 100
....*....|....*....|
gi 37360004 522 -DELAETQGKLEEKLQELEA 540
Cdd:PRK03918 309 lREIEKRLSRLEEEINGIEE 328
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
306-346 |
3.75e-03 |
|
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: 40.47 E-value: 3.75e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 37360004 306 GKVIIIGSGVSGLAAARQLQSFGMDVTLL--------EARDRVGGRVAT 346
Cdd:cd05305 169 AKVVILGAGVVGENAARVALGLGAEVTVLdinlerlrYLDDIFGGRVTT 217
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
374-539 |
3.77e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 374 KQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEfNRLLEATSYLSH-QLDFNVLNNKPVSLGQALEVVIQLQ--EKHV 450
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKE-ERLEELKKKLKElEKRLEELEERHELYEEAKAKKEELErlKKRL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 451 KDEQIEHWKKIVKT--------QEELKELLNKMVNLKEKIKELHQ---QYKEASEVKP--PRDITAEF---LVKSKHRDL 514
Cdd:PRK03918 382 TGLTPEKLEKELEElekakeeiEEEISKITARIGELKKEIKELKKaieELKKAKGKCPvcGRELTEEHrkeLLEEYTAEL 461
|
170 180
....*....|....*....|....*
gi 37360004 515 TALCKEYDELAETQGKLEEKLQELE 539
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELE 486
|
|
| PRK06847 |
PRK06847 |
hypothetical protein; Provisional |
307-342 |
3.77e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235874 [Multi-domain] Cd Length: 375 Bit Score: 40.63 E-value: 3.77e-03
10 20 30
....*....|....*....|....*....|....*...
gi 37360004 307 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARD--RVGG 342
Cdd:PRK06847 6 KVLIVGGGIGGLSAAIALRRAGIAVDLVEIDPewRVYG 43
|
|
| Ald |
COG0686 |
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ... |
306-346 |
3.78e-03 |
|
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: 40.38 E-value: 3.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 37360004 306 GKVIIIGSGVSGLAAARQLQSFGMDVTLL--------EARDRVGGRVAT 346
Cdd:COG0686 169 AKVVILGGGVVGTNAARMALGLGADVTVLdinldrlrRLDDIFGGRVTT 217
|
|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
307-467 |
4.25e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 168661 [Multi-domain] Cd Length: 373 Bit Score: 40.44 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 307 KVIIIGSGVSGLAAARQLQSFGMDVTLLEardrvggrvatfrKGNYVADLGAMVvtGLGGNpmaVVSKQVNMELAK-IKQ 385
Cdd:PRK06753 2 KIAIIGAGIGGLTAAALLQEQGHEVKVFE-------------KNESVKEVGAGI--GIGDN---VIKKLGNHDLAKgIKN 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 386 kcplyeaNGQAVPkekdemveqEFNRLLEATSYLSH-QLDFNVLNnkpVSLGQalEVVIQLQEKHVKDEQIEHWKKIVKT 464
Cdd:PRK06753 64 -------AGQILS---------TMNLLDDKGTLLNKvKLKSNTLN---VTLHR--QTLIDIIKSYVKEDAIFTGKEVTKI 122
|
...
gi 37360004 465 QEE 467
Cdd:PRK06753 123 ENE 125
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
406-540 |
5.14e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 406 EQEFNRLLEATSYLSHQLDfnvlnnkpvSLGQALEVVIQLQEKHVKDEQI-EHWKKIVKTQEELKELLNKMVNLKEKIKE 484
Cdd:COG4717 87 EEEYAELQEELEELEEELE---------ELEAELEELREELEKLEKLLQLlPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37360004 485 LHQQY-------KEASEVKppRDITAEFLVKS--KHRDLTALCKEYDELAETQGKLEEKLQELEA 540
Cdd:COG4717 158 LRELEeeleeleAELAELQ--EELEELLEQLSlaTEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
65-125 |
5.21e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 40.44 E-value: 5.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37360004 65 AAPPAGLTGPTDMATGAAGERTPRKKEPPRASPPGGlaePPGSAGPQAGPTAGP-------GSATPME 125
Cdd:PHA03378 734 ARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAA---APGAPTPQPPPQAPPapqqrprGAPTPQP 798
|
|
| AlaDh_PNT_C |
pfam01262 |
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
306-340 |
5.40e-03 |
|
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: 39.40 E-value: 5.40e-03
10 20 30
....*....|....*....|....*....|....*
gi 37360004 306 GKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRV 340
Cdd:pfam01262 29 AKVLVIGGGVAGLNAAATAKGLGAIVTILDVRPAR 63
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
443-539 |
5.44e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 443 IQLQEKHVKDEQIEhwkkIVKTQEELKELLNKMVNLKEKIKELHQQY-KEASEVKPPRDITAEFLVKSKHRDLTALCKEY 521
Cdd:PRK03918 614 LEREEKELKKLEEE----LDKAFEELAETEKRLEELRKELEELEKKYsEEEYEELREEYLELSRELAGLRAELEELEKRR 689
|
90
....*....|....*...
gi 37360004 522 DELAETQGKLEEKLQELE 539
Cdd:PRK03918 690 EEIKKTLEKLKEELEERE 707
|
|
| mnmC |
PRK01747 |
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ... |
307-341 |
5.65e-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: 40.21 E-value: 5.65e-03
10 20 30
....*....|....*....|....*....|....*
gi 37360004 307 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVG 341
Cdd:PRK01747 262 DAAIIGGGIAGAALALALARRGWQVTLYEADEAPA 296
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
63-155 |
5.86e-03 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 40.64 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 63 EVAAPPAGLTGPTDMATGAAGERTPRKKEPPRASPPGGLAE--PPGSAGPQAGPTA--GPGSATPMETGIAETPEGRRTS 138
Cdd:PRK12270 40 STAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPaaPPKPAAAAAAAAApaAPPAAAAAAAPAAAAVEDEVTP 119
|
90
....*....|....*..
gi 37360004 139 RRKRAKVEYREMDESLA 155
Cdd:PRK12270 120 LRGAAAAVAKNMDASLE 136
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
293-346 |
5.93e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 40.10 E-value: 5.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 37360004 293 IYKRIKPLPIKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVAT 346
Cdd:PRK12843 4 VVSELSPERWDAEFDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGTTAT 57
|
|
| PTZ00306 |
PTZ00306 |
NADH-dependent fumarate reductase; Provisional |
295-345 |
6.58e-03 |
|
NADH-dependent fumarate reductase; Provisional
Pssm-ID: 140327 [Multi-domain] Cd Length: 1167 Bit Score: 40.15 E-value: 6.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 37360004 295 KRIK-PLPikktGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVA 345
Cdd:PTZ00306 402 KRIAgSLP----ARVIVVGGGLAGCSAAIEAASCGAQVILLEKEAKLGGNSA 449
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
296-342 |
7.27e-03 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 39.78 E-value: 7.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 37360004 296 RIKPLPikktGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 342
Cdd:PRK06292 164 ELDKLP----KSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILP 206
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
308-342 |
7.83e-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: 39.82 E-value: 7.83e-03
10 20 30
....*....|....*....|....*....|....*
gi 37360004 308 VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 342
Cdd:COG1053 6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
|
|
| murD |
PRK14106 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional |
307-385 |
8.67e-03 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
Pssm-ID: 184511 [Multi-domain] Cd Length: 450 Bit Score: 39.57 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 307 KVIIIGSGVSGLAAARQLQSFGMDVTLLE--ARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIK 384
Cdd:PRK14106 7 KVLVVGAGVSGLALAKFLKKLGAKVILTDekEEDQLKEALEELGELGIELVLGEYPEEFLEGVDLVVVSPGVPLDSPPVV 86
|
.
gi 37360004 385 Q 385
Cdd:PRK14106 87 Q 87
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
61-145 |
8.87e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 39.92 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37360004 61 GSEVAAPPAGLTGPTDMATGAAGERTPRKKEPPRASPPGGLAePPGSAGPQAGPTAGPGSATPMETGIAETPEG----RR 136
Cdd:PHA03247 2788 VASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLP-PPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGdvrrRP 2866
|
....*....
gi 37360004 137 TSRRKRAKV 145
Cdd:PHA03247 2867 PSRSPAAKP 2875
|
|
| |
