|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02328 |
PLN02328 |
lysine-specific histone demethylase 1 homolog |
203-849 |
7.93e-125 |
|
lysine-specific histone demethylase 1 homolog
Pssm-ID: 215187 [Multi-domain] Cd Length: 808 Bit Score: 395.90 E-value: 7.93e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 203 LPHDRMTSQE-AACFPDIISGPQQTQkvFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSdtvLVHRVHSYLERHGL 281
Cdd:PLN02328 142 FPVDSLTEEEiEANVVSTIGGTEQAN--YIVVRNHILARWRSNVSNWLTRDHALESIRAEHKN---LVDSAYNFLLEHGY 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 282 INFGIYKRIKPLPTK-----KTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFR-KGNYV---ADLGAM 352
Cdd:PLN02328 217 INFGVAPVIKEAQLRsfegvEPANVVVVGAGLAGLVAARQLLSMGFKVVVLEGRARPGGRVKTMKmKGDGVvaaADLGGS 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 353 VVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAdtvkVPKEKDEMVEQEFNRLLEAtsylshqldfnvlnnkpvsl 432
Cdd:PLN02328 297 VLTGINGNPLGVLARQLGLPLHKVRDICPLYLPDGKA----VDAEIDSKIEASFNKLLDR-------------------- 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 433 gqalevVIQLQEKHVkdeqiehwkkivktqEELKELlnkMVNLKEKIKELHQQYKeasevkpprditaeflvkskhrdlt 512
Cdd:PLN02328 353 ------VCKLRQAMI---------------EEVKSV---DVNLGTALEAFRHVYK------------------------- 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 513 alckeydeLAETQgkleeklqeleanppsdvylssRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVR 592
Cdd:PLN02328 384 --------VAEDP----------------------QERMLLNWHLANLEYANASLMSNLSMAYWDQDDPYEMGGDHCFIP 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 593 NGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRstsqtfiYKCDAVLCTLPLGVLKQQppAVQFVPPLPEWKT 672
Cdd:PLN02328 434 GGNDTFVRELAKDLPIFYERTVESIRYGVDGVIVYAGGQE-------FHGDMVLCTVPLGVLKKG--SIEFYPELPQRKK 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 673 SAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFW---NLYKAPILLALVAGEAAGIMENISDDVIVG 749
Cdd:PLN02328 505 DAIQRLGYGLLNKVALLFPYNFWGGEIDTFGHLTEDPSMRGEFFLFYsysSVSGGPLLIALVAGDAAVKFETLSPVESVK 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 750 RCLAILKGIFGSS--AVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGpsipgapqpipRLFFAGEHT 827
Cdd:PLN02328 585 RVLQILRGIFHPKgiVVPDPVQAVCTRWGKDCFTYGSYSYVAVGSSGDDYDILAESVGDG-----------RVFFAGEAT 653
|
650 660
....*....|....*....|..
gi 58761544 828 IRNYPATVHGALLSGLREAGRI 849
Cdd:PLN02328 654 NKQYPATMHGAFLSGMREAANI 675
|
|
| PLN03000 |
PLN03000 |
amine oxidase |
198-850 |
2.73e-123 |
|
amine oxidase
Pssm-ID: 178578 [Multi-domain] Cd Length: 881 Bit Score: 394.00 E-value: 2.73e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 198 AFQSRLPHDRMTSQE--AACFPdIISGPQQTQkvFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSdtvLVHRVHSY 275
Cdd:PLN03000 86 ALTAGFPADSLTEEEieFGVVP-IVGGIEQVN--YILIRNHIISKWRENISSWVTKEMFLGSIPKHCSS---LLDSAYNY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 276 LERHGLINFGIYKRIK-PLPTKKT-GKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFR-KGNYV---ADL 349
Cdd:PLN03000 160 LVTHGYINFGIAQAIKdKFPAQSSkSSVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGGRVYTKKmEANRVgaaADL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 350 GAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAdtvkVPKEKDEMVEQEFNRLLEATSYLsHQLDFNVlnNKP 429
Cdd:PLN03000 240 GGSVLTGTLGNPLGIIARQLGSSLYKVRDKCPLYRVDGKP----VDPDVDLKVEVAFNQLLDKASKL-RQLMGDV--SMD 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 430 VSLGQALEVVIQLQEKHVKDEQIehwkkivktqeelkellnkmvnlkekikelhqqykeasevkpprditaeflvkskhr 509
Cdd:PLN03000 313 VSLGAALETFRQVSGNDVATEEM--------------------------------------------------------- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 510 dltalckeydelaetqgkleeklqeleanppsdvylssrdrQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHL 589
Cdd:PLN03000 336 -----------------------------------------GLFNWHLANLEYANAGLVSKLSLAFWDQDDPYDMGGDHC 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 590 TVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTrstsqtfIYKCDAVLCTLPLGVLKQQppAVQFVPPLPE 669
Cdd:PLN03000 375 FLPGGNGRLVQALAENVPILYEKTVQTIRYGSNGVKVIAGNQ-------VYEGDMVLCTVPLGVLKNG--SIKFVPELPQ 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 670 WKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWN---LYKAPILLALVAGEAAGIMENISDDV 746
Cdd:PLN03000 446 RKLDCIKRLGFGLLNKVAMLFPYVFWSTDLDTFGHLTEDPNYRGEFFLFYSyapVAGGPLLIALVAGEAAHKFETMPPTD 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 747 IVGRCLAILKGIFGSSA--VPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGpsipgapqpipRLFFAG 824
Cdd:PLN03000 526 AVTRVLHILRGIYEPQGinVPDPLQTVCTRWGGDPFSLGSYSNVAVGASGDDYDILAESVGDG-----------RLFFAG 594
|
650 660
....*....|....*....|....*.
gi 58761544 825 EHTIRNYPATVHGALLSGLREAGRIA 850
Cdd:PLN03000 595 EATTRRYPATMHGAFVTGLREAANMA 620
|
|
| PLN02529 |
PLN02529 |
lysine-specific histone demethylase 1 |
227-849 |
1.10e-114 |
|
lysine-specific histone demethylase 1
Pssm-ID: 178144 [Multi-domain] Cd Length: 738 Bit Score: 366.91 E-value: 1.10e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 227 QKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSdtvLVHRVHSYLERHGLINFGIYKRI-KPLPTKKT-GKVIII 304
Cdd:PLN02529 90 QNDYIVVRNHILARWRSNVGIWLSKGQIKETVSSEYEH---LISAAYDFLLYNGYINFGVSPSFaSPIPEEGTeGSVIIV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 305 GSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVAT---FRKGNYVA-DLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKC 380
Cdd:PLN02529 167 GAGLAGLAAARQLLSFGFKVVVLEGRNRPGGRVYTqkmGRKGQFAAvDLGGSVITGIHANPLGVLARQLSIPLHKVRDNC 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 381 PLYEANGqadtVKVPKEKDEMVEQEFNRLLEATSylshqldfnvlnnkpvslgqalevviqlqekhvkdeqiehwkkivk 460
Cdd:PLN02529 247 PLYKPDG----ALVDKEIDSNIEFIFNKLLDKVT---------------------------------------------- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 461 tqeELKELLNKMVNlkekikelhqqykeasevkpprDITAeflvkskhrdltalckeydelaetqGKLEEKLQELEAnpp 540
Cdd:PLN02529 277 ---ELRQIMGGFAN----------------------DISL-------------------------GSVLERLRQLYG--- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 541 sdVYLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYT 620
Cdd:PLN02529 304 --VARSTEERQLLDWHLANLEYANAGCLSDLSAAYWDQDDPYEMGGDHCFLAGGNWRLINALCEGVPIFYGKTVDTIKYG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 621 ASGCEVIAvntrsTSQtfIYKCDAVLCTLPLGVLKQQppAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVN 700
Cdd:PLN02529 382 NDGVEVIA-----GSQ--VFQADMVLCTVPLGVLKKR--TIRFEPELPRRKLAAIDRLGFGLLNKVAMVFPSVFWGEELD 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 701 LFGHVGSTTASRGELFLFWNLYK---APILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSA--VPQPKETVVSRW 775
Cdd:PLN02529 453 TFGCLNESSNKRGEFFLFYGYHTvsgGPALVALVAGEAAQRFENTDPSTLLHRVLSVLRGIYNPKGinVPDPIQTICTRW 532
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58761544 776 RADPWARGSYSYVAAGSSGNDYDLMAQpitpgpSIPGapqpipRLFFAGEHTIRNYPATVHGALLSGLREAGRI 849
Cdd:PLN02529 533 GSDPLSYGSYSHVRVQSSGSDYDILAE------SVSG------RLFFAGEATTRQYPATMHGAFLSGLREASRI 594
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
300-851 |
1.74e-112 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 378.44 E-value: 1.74e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYV-ADLGAMVVTGLGGN--------PMAVVSKQVN 370
Cdd:PLN02976 695 KIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGRVYTDRSSLSVpVDLGASIITGVEADvaterrpdPSSLICAQLG 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 371 MELAKIKQKCPLYeangqaDTV---KVPKEKDEMVEQEFNRLLEatsylshQLDFNVLNNKPVSLGQALEvviqlqekhv 447
Cdd:PLN02976 775 LELTVLNSDCPLY------DVVtgeKVPADLDEALEAEYNSLLD-------DMVLLVAQKGEHAMKMSLE---------- 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 448 kdEQIEHwkkivktqeELKEllNKMVNLKEKIKElhqqykeasevkpprditaeflvkskhrdlTALCKEYDELAETQgK 527
Cdd:PLN02976 832 --DGLEY---------ALKR--RRMPRPGVDIDE------------------------------TELGNAADDLYDSA-S 867
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 528 LEEKLQELEANPPSDVyLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFE-FTGSHLTVRNGYSCVPVALAEGL 606
Cdd:PLN02976 868 TGVDGGHCEKESKEDV-LSPLERRVMNWHFAHLEYGCAALLKEVSLPYWNQDDVYGgFGGAHCMIKGGYSNVVESLAEGL 946
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 607 DIKLNTAVRQVRY-------TASGCEVIAVNTRSTSQtfiYKCDAVLCTLPLGVLKQQppAVQFVPPLPEWKTSAVQRMG 679
Cdd:PLN02976 947 DIHLNHVVTDVSYgskdagaSGSSRKKVKVSTSNGSE---FLGDAVLITVPLGCLKAE--TIKFSPPLPDWKYSSIQRLG 1021
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 680 FGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYK---APILLALVAGEAAGIMENISDDVIVGRCLAILK 756
Cdd:PLN02976 1022 FGVLNKVVLEFPEVFWDDSVDYFGATAEETDLRGQCFMFWNVKKtvgAPVLIALVVGKAAIDGQSMSSSDHVNHALMVLR 1101
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 757 GIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGpsipgapqpiprLFFAGEHTIRNYPATVH 836
Cdd:PLN02976 1102 KLFGEALVPDPVASVVTDWGRDPFSYGAYSYVAIGASGEDYDILGRPVENC------------LFFAGEATCKEHPDTVG 1169
|
570
....*....|....*
gi 58761544 837 GALLSGLREAGRIAD 851
Cdd:PLN02976 1170 GAMMSGLREAVRIID 1184
|
|
| Amino_oxidase |
pfam01593 |
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ... |
308-849 |
7.76e-99 |
|
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: 315.97 E-value: 7.76e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 308 VSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGgNPMAVVSKQVNMELakiKQKCPLYEANG 387
Cdd:pfam01593 1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVRDDGFLIELGAMWFHGAQ-PPLLALLKELGLED---RLVLPDPAPFY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 388 QADTV--KVPKEKDEMVEQEFNRLLEAtsylshqldfnvlnnkpvslgqalevviqlqekhvkdeqiehwkkivktqeel 465
Cdd:pfam01593 77 TVLFAggRRYPGDFRRVPAGWEGLLEF----------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 466 kellNKMVNLKEKIKELHqqykeasevkpprditaeFLVKSKHRDLTALCKeydelaetqGKLEEKLQELEANPPSDVYL 545
Cdd:pfam01593 104 ----GRLLSIPEKLRLGL------------------AALASDALDEFDLDD---------FSLAESLLFLGRRGPGDVEV 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 546 SsrDRQILDWHFANLEFANAT-----PLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAE---GLDIKLNTAVRQV 617
Cdd:pfam01593 153 W--DRLIDPELFAALPFASGAfagdpSELSAGLALPLLWALLGEGGSLLLPRGGLGALPDALAAqllGGDVRLNTRVRSI 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 618 RYTASGCEVIAVNTRStsqtfiYKCDAVLCTLPLGVLKqqppAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDP 697
Cdd:pfam01593 231 DREGDGVTVTLTDGEV------IEADAVIVTVPLGVLK----RILFTPPLPPEKARAIRNLGYGPVNKVHLEFDRKFWPD 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 698 SvNLFGHVGSTTASRGELFLF--WNLY----KAPILLALV-AGEAAGIMENISDDVIVGRCLAILKGIFGSsAVPQPKET 770
Cdd:pfam01593 301 L-GLLGLLSELLTGLGTAFSWltFPNRappgKGLLLLVYVgPGDRARELEGLSDEELLQAVLRDLRKLFGE-EAPEPLRV 378
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58761544 771 VVSRWRADPWARGSYSYVAAGSSGNDYDlmaqpitpgpsiPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRI 849
Cdd:pfam01593 379 LVSDWHTDPWPRGSYSLPQYGPGHDDYR------------PLARTPDPGLFFAGEHTSTGYPGTVEGAIESGRRAARAV 445
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
300-855 |
1.75e-71 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 242.52 E-value: 1.75e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKG--NYVADLGAMVVtglGGNPMAVvskqvnMELAKiK 377
Cdd:COG1231 9 DVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGddGLYAELGAMRI---PPSHTNL------LALAR-E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 378 QKCPLYEANGQADtvkvpkekdemveqefNRLLeatsylshqldfnVLNNKPVSLGQalevviqlqekhvkdeqiehwkk 457
Cdd:COG1231 79 LGLPLEPFPNENG----------------NALL-------------YLGGKRVRAGE----------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 458 IVKTQEELKELLNKMVnlkekikelhqqykeasevkppRDITAEFlvkskhRDLTALCKEYDElaetqgkleEKLQE-LE 536
Cdd:COG1231 107 IAADLRGVAELLAKLL----------------------RALAAAL------DPWAHPAAELDR---------ESLAEwLR 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 537 ANPpsdvyLSSRDRQILDwhfANLEFANATPLSTLSLKHWDQD-DDFEFTGSHLTVRNGYSCVPVALAEGL--DIKLNTA 613
Cdd:COG1231 150 RNG-----ASPSARRLLG---LLGAGEYGADPDELSLLDLLRYaASAGGGAQQFRIVGGMDQLPRALAAELgdRIRLGAP 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 614 VRQVRYTASGCEVIavntrsTSQTFIYKCDAVLCTLPLGVLKQqppaVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRV 693
Cdd:COG1231 222 VTRIRQDGDGVTVT------TDDGGTVRADAVIVTVPPSVLRR----IEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRP 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 694 FWDPSvnlfGHVGSTTASRGELFL-FWNLY----KAPILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAvPQPK 768
Cdd:COG1231 292 FWEED----GLYGGISLTDLPIRQtWYPSNgpdgGAGVLLGYVGGDDARALAALSPEERVAAALEQLARIFGVYA-AEPV 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 769 ETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPItpgpsipgapqpiPRLFFAGEHTIRNYPATVHGALLSGLREAGR 848
Cdd:COG1231 367 DYVSTDWGRDPWSRGAYAAAPPGQLTAAGPALAEPD-------------GRIHFAGEHTSDEWPGWVEGALESGERAAAE 433
|
....*..
gi 58761544 849 IADQFLG 855
Cdd:COG1231 434 ILARLGG 440
|
|
| PLN02268 |
PLN02268 |
probable polyamine oxidase |
301-846 |
4.90e-70 |
|
probable polyamine oxidase
Pssm-ID: 177909 [Multi-domain] Cd Length: 435 Bit Score: 238.43 E-value: 4.90e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 301 VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGG-NPMAVVSKQVNMELAKIK-- 377
Cdd:PLN02268 3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIGGRVHTDYSFGFPVDMGASWLHGVCNeNPLAPLIGRLGLPLYRTSgd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 378 ---------QKCPLYEANGqadtVKVPKEKDEMVEQEFNRLLEATsylshqldfnvlnnkpvslgqalevviqlqeKHVK 448
Cdd:PLN02268 83 nsvlydhdlESYALFDMDG----NQVPQELVTKVGETFERILEET-------------------------------EKVR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 449 DEQIEHwkkivktqeelkellnkmVNLKEKIKelhqqykeasevkpprditaefLVKSKHRDLtalckeydelaetqgkl 528
Cdd:PLN02268 128 DEHEED------------------MSLLQAIS----------------------IVLERHPEL----------------- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 529 eeKLQELeanppsdvylssrDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEftGSHLTVRNGYSCVPVALAEGLDI 608
Cdd:PLN02268 151 --RLEGL-------------AHEVLQWYLCRMEGWFAADADTISLKSWDQEELLE--GGHGLMVRGYDPVINTLAKGLDI 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 609 KLNTAVRQVRYTASGCEViavnTRSTSQTFIykCDAVLCTLPLGVLKQQppAVQFVPPLPEWKTSAVQRMGFGNLNKVVL 688
Cdd:PLN02268 214 RLNHRVTKIVRRYNGVKV----TVEDGTTFV--ADAAIIAVPLGVLKAN--IIKFEPELPEWKEEAISDLGVGIENKIAL 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 689 CFDRVFWdPSVNLFGHVGSTTASRGelfLFWNLYKA---PILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSavP 765
Cdd:PLN02268 286 HFDSVFW-PNVEFLGVVAPTSYGCS---YFLNLHKAtghPVLVYMPAGRLARDIEKLSDEAAANFAMSQLKKMLPDA--T 359
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 766 QPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITpgpsipgapqpipRLFFAGEHTIRNYPATVHGALLSGLRE 845
Cdd:PLN02268 360 EPVQYLVSRWGSDPNSLGCYSYDLVGKPHDLYERLRAPVD-------------NLFFAGEATSSDFPGSVHGAYSTGVMA 426
|
.
gi 58761544 846 A 846
Cdd:PLN02268 427 A 427
|
|
| PLN02568 |
PLN02568 |
polyamine oxidase |
297-849 |
4.02e-43 |
|
polyamine oxidase
Pssm-ID: 215308 [Multi-domain] Cd Length: 539 Bit Score: 165.00 E-value: 4.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 297 KTGKVIIIGSGVSGLAAARQLQSFG-----MDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKqvnm 371
Cdd:PLN02568 4 KKPRIVIIGAGMAGLTAANKLYTSSaandmFELTVVEGGDRIGGRINTSEFGGERIEMGATWIHGIGGSPVYKIAQ---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 372 ELAKIKQKCPLYEANGQADTVKVPKEKDEMVEQefnRLLEATSYLSHQL-DFnvlnnkpvslgqalevviqLQEKHVKDE 450
Cdd:PLN02568 80 EAGSLESDEPWECMDGFPDRPKTVAEGGFEVDP---SIVESISTLFRGLmDD-------------------AQGKLIEPS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 451 QIEhwkkivktqeelkelLNKMVNLKEKikelhqqykeASEVKPPRDITA--EFLvKSKHRDLTALCKEYDELAETQGKL 528
Cdd:PLN02568 138 EVD---------------EVDFVKLAAK----------AARVCESGGGGSvgSFL-RRGLDAYWDSVSADEQIKGYGGWS 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 529 EEKLQEleanppsdvylssrdrQILDWHfANLE--FANATPLSTLSLkhwDQDDDF-EFTGSHLTVRNGYSCVPVALAEG 605
Cdd:PLN02568 192 RKLLEE----------------AIFTMH-ENTQrtYTSADDLSTLDL---AAESEYrMFPGEEITIAKGYLSVIEALASV 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 606 LD---IKLNTAVRQVRYTAsgcEVIAVNTRSTSqtfIYKCDAVLCTLPLGVLKQQ--PPAVQFVPPLPEWKTSAVQRMGF 680
Cdd:PLN02568 252 LPpgtIQLGRKVTRIEWQD---EPVKLHFADGS---TMTADHVIVTVSLGVLKAGigEDSGLFSPPLPDFKTDAISRLGF 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 681 GNLNKVVLCF----DRVFWD----PSVNLFGHvGSTTASRGELFLFW-----NLY----KAPILLALVAGEAAGIMENIS 743
Cdd:PLN02568 326 GVVNKLFVELsprpDGSPEDvakfPFLQMAFH-RSDSEARHDKIPWWmrrtaSICpihkNSSVLLSWFAGKEALELEKLS 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 744 DDVIV-------------------GRCLAILKGIFGSSAVPQPKETVV--SRWRADPWARGSYSYVAAGSSGNDYDLMAQ 802
Cdd:PLN02568 405 DEEIIrgvqttlssflkrrvaglgSQSHPLCNGGASSNDGSRWKFVKVlkSKWGTDPLFLGSYSYVAVGSSGDDLDRMAE 484
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 58761544 803 PITPGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRI 849
Cdd:PLN02568 485 PLPRISDHDQAGGPPLQLLFAGEATHRTHYSTTHGAYFSGLREANRL 531
|
|
| PLN02676 |
PLN02676 |
polyamine oxidase |
296-846 |
3.33e-36 |
|
polyamine oxidase
Pssm-ID: 215362 [Multi-domain] Cd Length: 487 Bit Score: 143.70 E-value: 3.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 296 KKTGKVIIIGSGVSGLAAARQLQSFGM-DVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGnpmavvsKQVNmela 374
Cdd:PLN02676 24 KPSPSVIIVGAGMSGISAAKTLSEAGIeDILILEATDRIGGRMRKANFAGVSVELGANWVEGVGG-------PESN---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 375 kikqkcPLYEangqadtvkvpkekdeMVEQefnrlLEATSYLShqlDF-NVLNNkpvslgqalevvIQLQEKHVKDEqie 453
Cdd:PLN02676 93 ------PIWE----------------LANK-----LKLRTFYS---DFdNLSSN------------IYKQDGGLYPK--- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 454 hwkkivktqeelkellnkmvnlkekiKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALckeydelaetqgkleeKLQ 533
Cdd:PLN02676 128 --------------------------KVVQKSMKVADASDEFGENLSISLSAKKAVDISIL----------------TAQ 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 534 ELEANPPSdvylsSRDRQILDWHFANLEFA---------NATPLSTLSlkhwDQDDDFEFTGShltvRNGYSCVPVALAE 604
Cdd:PLN02676 166 RLFGQVPK-----TPLEMVIDYYNYDYEFAepprvtslkNTEPNPTFV----DFGEDEYFVAD----PRGYESLVYYLAE 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 605 G---------LD--IKLNTAVRQVRYTASGcevIAVNTRSTSqtfIYKCDAVLCTLPLGVLkqQPPAVQFVPPLPEWKTS 673
Cdd:PLN02676 233 QflstksgkiTDprLKLNKVVREISYSKNG---VTVKTEDGS---VYRAKYVIVSVSLGVL--QSDLIKFKPPLPDWKIE 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 674 AVQRMGFGNLNKVVLCFDRVFWdPSVN-----LFGHVgsttaSRGeLFLFW----NLYK-APILLALVAGEAAGIMENIS 743
Cdd:PLN02676 305 AIYQFDMAVYTKIFLKFPYKFW-PSGPgteffLYAHE-----RRG-YYPFWqhleNEYPgSNVLFVTVTDEESRRIEQQP 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 744 DDVIVGRCLAILKGIFGSSaVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITpgpsipgapqpipRLFFA 823
Cdd:PLN02676 378 DSETKAEIMEVLRKMFGPN-IPEATDILVPRWWSNRFFKGSYSNWPIGVSRYEFDQIRAPVG-------------RVYFT 443
|
570 580
....*....|....*....|...
gi 58761544 824 GEHTIRNYPATVHGALLSGLREA 846
Cdd:PLN02676 444 GEHTSEKYNGYVHGAYLAGIDTA 466
|
|
| SWIRM |
pfam04433 |
SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid ... |
206-284 |
3.65e-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: 3.65e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58761544 206 DRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEapynSDTVLVHRVHSYLERHGLINF 284
Cdd:pfam04433 4 DKLHPIEKRLLPEFFNGKSKTPEVYLEIRNFILNLWRENPKEYLTKTDARRALK----GDVNLISRIHEFLERWGLINF 78
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
300-351 |
1.64e-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: 1.64e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 58761544 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGA 351
Cdd:COG1232 3 RVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRTVEVDGFRIDRGP 54
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
303-362 |
2.39e-14 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 68.33 E-value: 2.39e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 303 IIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPM 362
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYSYRVPGYVFDYGAHIFHGSDEPNV 60
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
300-355 |
6.60e-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: 6.60e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 58761544 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVT 355
Cdd:COG1233 5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTFERPGFRFDVGPSVLT 60
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
300-351 |
4.79e-13 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 71.06 E-value: 4.79e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 58761544 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGA 351
Cdd:COG3380 5 DIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGGRMATRRLDGGRFDHGA 56
|
|
| crtI_fam |
TIGR02734 |
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ... |
301-355 |
1.05e-10 |
|
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two symmetrical pairs of) sites. This is achieved by two enzymes (crtP and crtQ) in cyanobacteria (Gloeobacter being an exception) and plants, but by a single enzyme in most other bacteria and in fungi. This single enzyme is called the bacterial-type phytoene desaturase, or CrtI. Most members of this family, part of the larger pfam01593, which also contains amino oxidases, are CrtI itself; it is likely that all members act on either phytoene or on related compounds such as dehydrosqualene, for carotenoid biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 274273 [Multi-domain] Cd Length: 495 Bit Score: 64.99 E-value: 1.05e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 58761544 301 VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVT 355
Cdd:TIGR02734 1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGRAGVLEDDGFRFDTGPTVIT 55
|
|
| PRK11883 |
PRK11883 |
protoporphyrinogen oxidase; Reviewed |
300-351 |
1.53e-09 |
|
protoporphyrinogen oxidase; Reviewed
Pssm-ID: 237009 [Multi-domain] Cd Length: 451 Bit Score: 61.02 E-value: 1.53e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 58761544 300 KVIIIGSGVSGLAAARQLQSFG--MDVTLLEARDRVGGRVATFRKGNYVADLGA 351
Cdd:PRK11883 2 KVAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKIQTVRKDGFPIELGP 55
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
298-350 |
2.54e-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: 2.54e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 58761544 298 TGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRkgnyVADLG 350
Cdd:COG3349 3 PPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGGRARSFP----DPDTG 51
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
300-345 |
4.35e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 59.52 E-value: 4.35e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 58761544 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNY 345
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAASFEFGGL 46
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
288-335 |
4.39e-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: 59.76 E-value: 4.39e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 58761544 288 KRIKPLPTKKTGK-VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 335
Cdd:COG0493 110 WVKPPPPAPRTGKkVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG 158
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
290-335 |
6.92e-09 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 59.02 E-value: 6.92e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 58761544 290 IKPL-PTKKTGK-VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 335
Cdd:PRK12810 133 VKPDpPVKRTGKkVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGG 180
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
301-345 |
2.61e-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: 57.18 E-value: 2.61e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 58761544 301 VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGrvaTFRKGNY 345
Cdd:COG2072 9 VVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGG---TWRDNRY 50
|
|
| PLN02576 |
PLN02576 |
protoporphyrinogen oxidase |
301-351 |
3.04e-08 |
|
protoporphyrinogen oxidase
Pssm-ID: 215314 [Multi-domain] Cd Length: 496 Bit Score: 57.33 E-value: 3.04e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 58761544 301 VIIIGSGVSGLAAARQLQS-FGMDVTLLEARDRVGGRVATFRKGNYVADLGA 351
Cdd:PLN02576 15 VAVVGAGVSGLAAAYALASkHGVNVLVTEARDRVGGNITSVSEDGFIWEEGP 66
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
274-335 |
7.88e-08 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 55.57 E-value: 7.88e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58761544 274 SYLERHG---LINFGIYKRIKPLPTKKtgKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 335
Cdd:PRK11749 115 GRLERYItdwAMETGWVLFKRAPKTGK--KVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG 177
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
300-339 |
2.36e-07 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 53.97 E-value: 2.36e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 58761544 300 KVIIIGSGVSGLAAARQLQSfGMDVTLLEARDRVGGRVAT 339
Cdd:COG2907 5 RIAVIGSGISGLTAAWLLSR-RHDVTLFEANDRLGGHTHT 43
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
367-537 |
2.57e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 53.38 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 367 KQVNMELAKIKQKcpLYEANGQADTV--KVPKEKDEMVEQEFNRLLEATsyLSHQLD--FNVLNNKPVSLGQALEVVIQL 442
Cdd:COG1340 67 DELNEKVKELKEE--RDELNEKLNELreELDELRKELAELNKAGGSIDK--LRKEIErlEWRQQTEVLSPEEEKELVEKI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 443 QEKhvkDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQ------------------YKEASEVKPPRD-ITAEFL 503
Cdd:COG1340 143 KEL---EKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKikelaeeaqelheemielYKEADELRKEADeLHKEIV 219
|
170 180 190
....*....|....*....|....*....|....
gi 58761544 504 VKSKHRDltALCKEYDELAETQGKLEEKLQELEA 537
Cdd:COG1340 220 EAQEKAD--ELHEEIIELQKELRELRKELKKLRK 251
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
300-341 |
5.48e-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: 52.40 E-value: 5.48e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 58761544 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRvATFR 341
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSG-ASGR 41
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
292-335 |
1.46e-06 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 51.80 E-value: 1.46e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 58761544 292 PLPTKKTGK-VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 335
Cdd:PRK12771 130 PAPAPDTGKrVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGG 174
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
281-342 |
2.25e-06 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 51.40 E-value: 2.25e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 58761544 281 LINFGIYK--RIKPLPTKK---TGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRK 342
Cdd:COG1148 118 LVRMAVAKakLLEPLEPIKvpvNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQLHK 184
|
|
| proto_IX_ox |
TIGR00562 |
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ... |
298-351 |
3.88e-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: 50.22 E-value: 3.88e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 58761544 298 TGKVIIIGSGVSGLAAARQLQ----SFGMDVTLLEARDRVGGRVATFRKGNYVADLGA 351
Cdd:TIGR00562 2 KKHVVIIGGGISGLCAAYYLEkeipELPVELTLVEASDRVGGKIQTVKEDGYLIERGP 59
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
300-341 |
4.23e-06 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 49.90 E-value: 4.23e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 58761544 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEaRDRVGGRvATFR 341
Cdd:COG0665 4 DVVVIGGGIAGLSTAYHLARRGLDVTVLE-RGRPGSG-ASGR 43
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
367-537 |
1.28e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 367 KQVNMELAKIKQKCPLYEANGQADTV-----KVPKEKDEMVEQEFNRLLEatsylshqlDFNVLNNKPVSLGQALEvviq 441
Cdd:PRK03918 483 RELEKVLKKESELIKLKELAEQLKELeeklkKYNLEELEKKAEEYEKLKE---------KLIKLKGEIKSLKKELE---- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 442 lQEKHVKDEQIEHWKKIVKTQEELKELLNKMVN--------LKEKIKELHQQYKEASEVKP-PRDItaEFLVKSKHRDLT 512
Cdd:PRK03918 550 -KLEELKKKLAELEKKLDELEEELAELLKELEElgfesveeLEERLKELEPFYNEYLELKDaEKEL--EREEKELKKLEE 626
|
170 180
....*....|....*....|....*
gi 58761544 513 ALCKEYDELAETQGKLEEKLQELEA 537
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEE 651
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
288-335 |
1.59e-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: 1.59e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 58761544 288 KRIKPLP-TKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 335
Cdd:PRK12775 419 KPVKPPRfSKKLGKVAICGSGPAGLAAAADLVKYGVDVTVYEALHVVGG 467
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
289-335 |
1.83e-05 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 48.57 E-value: 1.83e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 58761544 289 RIKPLPTKKTGK-VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 335
Cdd:PRK12814 183 RYIPERAPKSGKkVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGG 230
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
434-537 |
1.84e-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: 46.84 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 434 QALEVVIQLQEKHVKDEQIEHWKK-----IVKTQEELKELLNKMVNLKEKIKELHQQYKEA-SEVKpprdiTAEFLVK-- 505
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKelpaeLAELEDELAALEARLEAAKTELEDLEKEIKRLeLEIE-----EVEARIKky 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 58761544 506 -------SKHRDLTALCKEYDELAETQGKLEEKLQELEA 537
Cdd:COG1579 79 eeqlgnvRNNKEYEALQKEIESLKRRISDLEDEILELME 117
|
|
| PLN02487 |
PLN02487 |
zeta-carotene desaturase |
292-346 |
2.91e-05 |
|
zeta-carotene desaturase
Pssm-ID: 215268 [Multi-domain] Cd Length: 569 Bit Score: 47.87 E-value: 2.91e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 292 PLPTKKTG---KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATF--RKGNYV 346
Cdd:PLN02487 66 PEPEAYKGpklKVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGGKVGSFvdKNGNHI 125
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
300-350 |
3.17e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 47.58 E-value: 3.17e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 58761544 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG--RVATFrKGNYVaDLG 350
Cdd:PRK07208 6 SVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGisRTVTY-KGNRF-DIG 56
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
287-335 |
4.03e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 47.45 E-value: 4.03e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 58761544 287 YKRIKPLPT-KKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 335
Cdd:PRK13984 271 YSEILDDEPeKKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGG 320
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
300-336 |
5.40e-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: 46.08 E-value: 5.40e-05
10 20 30
....*....|....*....|....*....|....*..
gi 58761544 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGR 336
Cdd:COG0654 5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPD 41
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
371-549 |
7.01e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 371 MELAKIKQKCP-----LYE-------ANGQADTVKVPKEKDEMVEQE---FNRLLEATSYLSHQldfnvlnNKPVSLGQA 435
Cdd:PRK03918 429 EELKKAKGKCPvcgreLTEehrkellEEYTAELKRIEKELKEIEEKErklRKELRELEKVLKKE-------SELIKLKEL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 436 LEVVIQLQEK---HVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVkpprditaEFLVKSKHRDLT 512
Cdd:PRK03918 502 AEQLKELEEKlkkYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL--------EKKLDELEEELA 573
|
170 180 190
....*....|....*....|....*....|....*...
gi 58761544 513 ALCKEYDELA-ETQGKLEEKLQELEanPPSDVYLSSRD 549
Cdd:PRK03918 574 ELLKELEELGfESVEELEERLKELE--PFYNEYLELKD 609
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
300-339 |
8.45e-05 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 45.50 E-value: 8.45e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 58761544 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEaRDRVGGRVAT 339
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIE-GGEPGGQLAT 40
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
287-356 |
8.49e-05 |
|
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 45.44 E-value: 8.49e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58761544 287 YKRIKPLPTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEA-RDRVggrvatfrkgNYVADLGAMVVTG 356
Cdd:COG0569 84 RRRMERGIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVIDKdPERV----------ERLAEEDVLVIVG 144
|
|
| PLN02612 |
PLN02612 |
phytoene desaturase |
289-341 |
1.08e-04 |
|
phytoene desaturase
Pssm-ID: 215330 [Multi-domain] Cd Length: 567 Bit Score: 45.99 E-value: 1.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 58761544 289 RIKPLPTKKTgKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFR 341
Cdd:PLN02612 85 RSAPRPAKPL-KVVIAGAGLAGLSTAKYLADAGHKPILLEARDVLGGKVAAWK 136
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
299-333 |
1.13e-04 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 45.00 E-value: 1.13e-04
10 20 30
....*....|....*....|....*....|....*
gi 58761544 299 GKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRV 333
Cdd:pfam07992 153 KRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRL 187
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
290-335 |
1.71e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 45.01 E-value: 1.71e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 58761544 290 IKPLPT--KKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 335
Cdd:PRK12831 130 IDLSETeeKKGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGG 177
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
300-333 |
1.85e-04 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 40.65 E-value: 1.85e-04
10 20 30
....*....|....*....|....*....|....
gi 58761544 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRV 333
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRL 34
|
|
| LhgO |
COG0579 |
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism]; |
301-334 |
2.64e-04 |
|
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
Pssm-ID: 440344 [Multi-domain] Cd Length: 418 Bit Score: 44.37 E-value: 2.64e-04
10 20 30
....*....|....*....|....*....|....*
gi 58761544 301 VIIIGSGVSGLAAARQL-QSFGMDVTLLEARDRVG 334
Cdd:COG0579 7 VVIIGAGIVGLALARELsRYEDLKVLVLEKEDDVA 41
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
440-552 |
3.70e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 440 IQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKppRDITAEFLVKSK-----HRDLTAL 514
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL--AQAQEELESLQEeaeelQEELEEL 120
|
90 100 110
....*....|....*....|....*....|....*...
gi 58761544 515 CKEYDELAETQGKLEEKLQELEANppsdvyLSSRDRQI 552
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSE------IAEREEEL 152
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
301-335 |
3.93e-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: 3.93e-04
10 20 30
....*....|....*....|....*....|....*
gi 58761544 301 VIIIGSGVSGLAAARQLQSFGMDVTLLEaRDRVGG 335
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVE-KGRLGG 39
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
367-536 |
4.09e-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: 44.24 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 367 KQVNMELAKIK-QKcplyeangQADTVKvpKEKDEMVEQEfNRLLEATSYLSHqldfnvlNNKPVSlgqALEVVIQLQEK 445
Cdd:TIGR04523 291 NQLKSEISDLNnQK--------EQDWNK--ELKSELKNQE-KKLEEIQNQISQ-------NNKIIS---QLNEQISQLKK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 446 HV---------KDEQI-EHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPPRDITaeflVKSKHRDLTALC 515
Cdd:TIGR04523 350 ELtnsesenseKQRELeEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQ----IKKLQQEKELLE 425
|
170 180
....*....|....*....|.
gi 58761544 516 KEYDELAETQGKLEEKLQELE 536
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLT 446
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
396-552 |
4.27e-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: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 396 KEKDEMVEQEFNRLLEATSYLSHQL-----DFNVLNNKPVSLGQALEVVIQLQEKhVKDEQIEHWKKIVKTQEELKELLN 470
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIekkqqEINEKTTEISNTQTQLNQLKDEQNK-IKKQLSEKQKELEQNNKKIKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 471 KMVNLKEKIKELHQQyKEA---SEVKpprditaEFLvKSKHRDLTALCKEYD-------ELAETQGKLEEKLQELEANPp 540
Cdd:TIGR04523 289 QLNQLKSEISDLNNQ-KEQdwnKELK-------SEL-KNQEKKLEEIQNQISqnnkiisQLNEQISQLKKELTNSESEN- 358
|
170
....*....|..
gi 58761544 541 sdvylSSRDRQI 552
Cdd:TIGR04523 359 -----SEKQREL 365
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
300-336 |
1.00e-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: 42.31 E-value: 1.00e-03
10 20 30
....*....|....*....|....*....|....*...
gi 58761544 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEA-RDRVGGR 336
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDeGTCPYGG 39
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
23-98 |
1.33e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 42.36 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 23 AGPGTAGGSENGSEVAAQPAGLSGPAEVGPGAVGERTPRKKEPPRASPP----GGLAEPPGSAGPQAGPTVVPGSATPME 98
Cdd:PHA03378 699 RAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPaaapGRARPPAAAPGRARPPAAAPGAPTPQP 778
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
296-337 |
1.38e-03 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 42.05 E-value: 1.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 58761544 296 KKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRV 337
Cdd:COG1251 140 APGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQ 181
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
300-356 |
1.48e-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: 1.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 58761544 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKgnyvadLGAMVVTG 356
Cdd:COG0771 6 KVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPAPELAAAELEA------PGVEVVLG 56
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
296-335 |
1.58e-03 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 42.04 E-value: 1.58e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 58761544 296 KKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 335
Cdd:PRK12778 429 KNGKKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGG 468
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
368-538 |
1.65e-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: 42.35 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 368 QVNMELAKIKQKCPLYEA--NGQADTVKVPKEKDEMVEQEFNRLLEATSYLSHQLDF--NVLNNKPVSLGQALEVVIQLQ 443
Cdd:TIGR02168 751 QLSKELTELEAEIEELEErlEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElrAELTLLNEEAANLRERLESLE 830
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 444 -EKHVKDEQIEHWKKIVKTQEELKELLNK-MVNLKEKIKELHQQYKEASEVKpprditaeflvKSKHRDLTALCKEYDEL 521
Cdd:TIGR02168 831 rRIAATERRLEDLEEQIEELSEDIESLAAeIEELEELIEELESELEALLNER-----------ASLEEALALLRSELEEL 899
|
170
....*....|....*..
gi 58761544 522 AETQGKLEEKLQELEAN 538
Cdd:TIGR02168 900 SEELRELESKRSELRRE 916
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
396-536 |
1.79e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 396 KEKDEMVEQEFNRLLEATSYLSHQLDFNVLNN-KPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLN---- 470
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDlSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAeagv 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 471 --------------KMVNLKEKIKELHQQYKE-ASEVKPPRDITAEFLVKSKHRDLT----ALCKEYDELAETQGKLEEK 531
Cdd:COG4717 382 edeeelraaleqaeEYQELKEELEELEEQLEElLGELEELLEALDEEELEEELEELEeeleELEEELEELREELAELEAE 461
|
....*
gi 58761544 532 LQELE 536
Cdd:COG4717 462 LEQLE 466
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
442-537 |
2.02e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 442 LQEKHVKDEQIEhwKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPprditaeflVKSKHRDLTALCKEY--- 518
Cdd:PRK03918 240 IEELEKELESLE--GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKE---------KAEEYIKLSEFYEEYlde 308
|
90 100
....*....|....*....|
gi 58761544 519 -DELAETQGKLEEKLQELEA 537
Cdd:PRK03918 309 lREIEKRLSRLEEEINGIEE 328
|
|
| MRPL52 |
pfam18699 |
Mitoribosomal protein mL52; Members of this family include the mamalian mitoribosomal proteins ... |
421-494 |
2.13e-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: 2.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58761544 421 DFNVLNNKPVSLGQalevviqLQEKHvKDEQIEHWKKIVKTQEELKELLnKMVNLKEKIKELHQQYKEASEVKP 494
Cdd:pfam18699 25 DFSFADGRPAPVTS-------GQLKR-KLKQIELAKKIVKLSSEVDEAE-ERYKRKQEEEEEEIQKIIDNKLKP 89
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
367-566 |
2.25e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 367 KQVNMELAKIKQKcpLYEANGQADTVKvpkEKDEMVEQEFNRLLEATSYLSHQLdfNVLNNKPVSLgqalevviQLQEKH 446
Cdd:COG4372 69 EQARSELEQLEEE--LEELNEQLQAAQ---AELAQAQEELESLQEEAEELQEEL--EELQKERQDL--------EQQRKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 447 VKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPPRDITAefLVKSKHRdlTALCKEYDELAETQG 526
Cdd:COG4372 134 LEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE--LLKEANR--NAEKEEELAEAEKLI 209
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 58761544 527 KLEEKLQELEANPPSDVYLSSRDRQILDWHFANLEFANAT 566
Cdd:COG4372 210 ESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
393-538 |
2.41e-03 |
|
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: 41.54 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 393 KVPKEKDEMvEQEFNRLLEATSYLSHQLDfnvlNNKPVSlgQALEVVIQL--QEKHVKDEQIEHWKK-IVKTQEELKEL- 468
Cdd:TIGR04523 374 KLKKENQSY-KQEIKNLESQINDLESKIQ----NQEKLN--QQKDEQIKKlqQEKELLEKEIERLKEtIIKNNSEIKDLt 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 469 -----LNKMVN--------LKEKIKELHQQYKEA-SEVKpprDITAEFlvKSKHRDLTALCKEYDELAETQGKLEEKLQE 534
Cdd:TIGR04523 447 nqdsvKELIIKnldntresLETQLKVLSRSINKIkQNLE---QKQKEL--KSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
....
gi 58761544 535 LEAN 538
Cdd:TIGR04523 522 LKEK 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
368-537 |
2.47e-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: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 368 QVNMELAKIKQKCPLYEANGQADTVKVPKEKDEMVEQEfNRLLEATS-YLSHQLDFNVLNNKPVSLGQALEVVIQLQEKh 446
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE-EEIEELQKeLYALANEISRLEQQKQILRERLANLERQLEE- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 447 vKDEQIEHWK-KIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPprdiTAEFLVKSKHRDLTALCKEYDELAETQ 525
Cdd:TIGR02168 321 -LEAQLEELEsKLDELAEELAELEEKLEELKEELESLEAELEELEAELE----ELESRLEELEEQLETLRSKVAQLELQI 395
|
170
....*....|..
gi 58761544 526 GKLEEKLQELEA 537
Cdd:TIGR02168 396 ASLNNEIERLEA 407
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
294-339 |
2.63e-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: 2.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 58761544 294 PTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLL--------EARDRVGGRVAT 339
Cdd:smart01002 16 GGVPPAKVVVIGAGVVGLGAAATAKGLGAEVTVLdvrparlrQLESLLGARFTT 69
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
403-537 |
2.77e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 403 EQEFNRLLEATSYLSHQLDfnvlnnkpvSLGQALEVVIQLQEKHVKDEQI-EHWKKIVKTQEELKELLNKMVNLKEKIKE 481
Cdd:COG4717 87 EEEYAELQEELEELEEELE---------ELEAELEELREELEKLEKLLQLlPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58761544 482 LHQQY-------KEASEVKppRDITAEFLVKS--KHRDLTALCKEYDELAETQGKLEEKLQELEA 537
Cdd:COG4717 158 LRELEeeleeleAELAELQ--EELEELLEQLSlaTEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
301-359 |
3.44e-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: 40.67 E-value: 3.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58761544 301 VIIIGSGVSG----LAAARQlqsfGMDVTLLEARDRVGGR-----VATFRkGNYVADlgAMVVTGLGG 359
Cdd:pfam12831 2 VVVVGGGPAGvaaaIAAARA----GAKVLLVERRGFLGGMltsglVGPDM-GFYLNK--EQVVGGIAR 62
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
440-536 |
3.69e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 440 IQLQEKHVKDEQIEhwkkIVKTQEELKELLNKMVNLKEKIKELHQQYKEasevKPPRDITAEFLVKSKH-----RDLTAL 514
Cdd:PRK03918 614 LEREEKELKKLEEE----LDKAFEELAETEKRLEELRKELEELEKKYSE----EEYEELREEYLELSRElaglrAELEEL 685
|
90 100
....*....|....*....|..
gi 58761544 515 CKEYDELAETQGKLEEKLQELE 536
Cdd:PRK03918 686 EKRREEIKKTLEKLKEELEERE 707
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
286-339 |
4.02e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 40.88 E-value: 4.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 58761544 286 IYKRIKPLPTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVAT 339
Cdd:PRK12843 4 VVSELSPERWDAEFDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGTTAT 57
|
|
| PRK06847 |
PRK06847 |
hypothetical protein; Provisional |
300-335 |
4.10e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235874 [Multi-domain] Cd Length: 375 Bit Score: 40.63 E-value: 4.10e-03
10 20 30
....*....|....*....|....*....|....*...
gi 58761544 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARD--RVGG 335
Cdd:PRK06847 6 KVLIVGGGIGGLSAAIALRRAGIAVDLVEIDPewRVYG 43
|
|
| Ald |
COG0686 |
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ... |
299-339 |
4.21e-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: 4.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 58761544 299 GKVIIIGSGVSGLAAARQLQSFGMDVTLL--------EARDRVGGRVAT 339
Cdd:COG0686 169 AKVVILGGGVVGTNAARMALGLGADVTVLdinldrlrRLDDIFGGRVTT 217
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
299-339 |
4.22e-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: 4.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 58761544 299 GKVIIIGSGVSGLAAARQLQSFGMDVTLL--------EARDRVGGRVAT 339
Cdd:cd05305 169 AKVVILGAGVVGENAARVALGLGAEVTVLdinlerlrYLDDIFGGRVTT 217
|
|
| AlaDh_PNT_C |
pfam01262 |
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
294-333 |
5.48e-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: 39.02 E-value: 5.48e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 58761544 294 PTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRV 333
Cdd:pfam01262 24 PGVAPAKVLVIGGGVAGLNAAATAKGLGAIVTILDVRPAR 63
|
|
| mnmC |
PRK01747 |
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ... |
300-334 |
5.53e-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: 5.53e-03
10 20 30
....*....|....*....|....*....|....*
gi 58761544 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVG 334
Cdd:PRK01747 262 DAAIIGGGIAGAALALALARRGWQVTLYEADEAPA 296
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
22-110 |
6.19e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 40.35 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 22 EAGPGTAGGSENGSEVAAQPAGLSGPAEVGPGAVGERTPRKKEPPRASPPgglAEPPGSAGPQAGPTVVPGSATPMETGI 101
Cdd:PRK07764 382 ERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQP---APAPAPAPAPPSPAGNAPAGGAPSPPP 458
|
....*....
gi 58761544 102 AETPEGRRT 110
Cdd:PRK07764 459 AAAPSAQPA 467
|
|
| PTZ00306 |
PTZ00306 |
NADH-dependent fumarate reductase; Provisional |
288-338 |
6.61e-03 |
|
NADH-dependent fumarate reductase; Provisional
Pssm-ID: 140327 [Multi-domain] Cd Length: 1167 Bit Score: 40.15 E-value: 6.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 58761544 288 KRIK-PLPTKktgkVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVA 338
Cdd:PTZ00306 402 KRIAgSLPAR----VIVVGGGLAGCSAAIEAASCGAQVILLEKEAKLGGNSA 449
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
289-335 |
8.03e-03 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 39.78 E-value: 8.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 58761544 289 RIKPLPtkktGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 335
Cdd:PRK06292 164 ELDKLP----KSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILP 206
|
|
| murD |
PRK14106 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional |
300-378 |
8.71e-03 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
Pssm-ID: 184511 [Multi-domain] Cd Length: 450 Bit Score: 39.57 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLE--ARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIK 377
Cdd:PRK14106 7 KVLVVGAGVSGLALAKFLKKLGAKVILTDekEEDQLKEALEELGELGIELVLGEYPEEFLEGVDLVVVSPGVPLDSPPVV 86
|
.
gi 58761544 378 Q 378
Cdd:PRK14106 87 Q 87
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
301-335 |
9.11e-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: 39.43 E-value: 9.11e-03
10 20 30
....*....|....*....|....*....|....*
gi 58761544 301 VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 335
Cdd:COG1053 6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
20-105 |
9.66e-03 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 39.63 E-value: 9.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58761544 20 GTEAGPGTAGG--SENGSEVAAQPAGLSGPAEVG---PGAVGERTPrkkEPPRASPPGGLAEPPGSAGpQAGPTVVPGSA 94
Cdd:COG5164 99 TTPAGDGGATGppDDGGATGPPDDGGSTTPPSGGsttPPGDGGSTP---PGPGSTGPGGSTTPPGDGG-STTPPGPGGST 174
|
90
....*....|.
gi 58761544 95 TPMETGIAETP 105
Cdd:COG5164 175 TPPDDGGSTTP 185
|
|
| |
