|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02328 |
PLN02328 |
lysine-specific histone demethylase 1 homolog |
204-850 |
3.22e-125 |
|
lysine-specific histone demethylase 1 homolog
Pssm-ID: 215187 [Multi-domain] Cd Length: 808 Bit Score: 397.06 E-value: 3.22e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 204 LPHDRMTSQE-AACFPDIISGPQQTQkvFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSdtvLVHRVHSYLERHGL 282
Cdd:PLN02328 142 FPVDSLTEEEiEANVVSTIGGTEQAN--YIVVRNHILARWRSNVSNWLTRDHALESIRAEHKN---LVDSAYNFLLEHGY 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 283 INFGIYKRIKPLPIK-----KTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFR-KGNYV---ADLGAM 353
Cdd:PLN02328 217 INFGVAPVIKEAQLRsfegvEPANVVVVGAGLAGLVAARQLLSMGFKVVVLEGRARPGGRVKTMKmKGDGVvaaADLGGS 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 354 VVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAdtvkVPKEKDEMVEQEFNRLLEAtsylshqldfnvlnnkpvsl 433
Cdd:PLN02328 297 VLTGINGNPLGVLARQLGLPLHKVRDICPLYLPDGKA----VDAEIDSKIEASFNKLLDR-------------------- 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 434 gqalevVIQLQEKHVkdeqiehwkkivktqEELKELlnkMVNLKEKIKELHQQYKeasevkpprditaeflvkskhrdlt 513
Cdd:PLN02328 353 ------VCKLRQAMI---------------EEVKSV---DVNLGTALEAFRHVYK------------------------- 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 514 alckeydeLAETQgkleeklqeleanppsdvylssRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVR 593
Cdd:PLN02328 384 --------VAEDP----------------------QERMLLNWHLANLEYANASLMSNLSMAYWDQDDPYEMGGDHCFIP 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 594 NGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRstsqtfiYKCDAVLCTLPLGVLKQQppAVQFVPPLPEWKT 673
Cdd:PLN02328 434 GGNDTFVRELAKDLPIFYERTVESIRYGVDGVIVYAGGQE-------FHGDMVLCTVPLGVLKKG--SIEFYPELPQRKK 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 674 SAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFW---NLYKAPILLALVAGEAAGIMENISDDVIVG 750
Cdd:PLN02328 505 DAIQRLGYGLLNKVALLFPYNFWGGEIDTFGHLTEDPSMRGEFFLFYsysSVSGGPLLIALVAGDAAVKFETLSPVESVK 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 751 RCLAILKGIFGSS--AVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGpsipgapqpipRLFFAGEHT 828
Cdd:PLN02328 585 RVLQILRGIFHPKgiVVPDPVQAVCTRWGKDCFTYGSYSYVAVGSSGDDYDILAESVGDG-----------RVFFAGEAT 653
|
650 660
....*....|....*....|..
gi 568932208 829 IRNYPATVHGALLSGLREAGRI 850
Cdd:PLN02328 654 NKQYPATMHGAFLSGMREAANI 675
|
|
| PLN03000 |
PLN03000 |
amine oxidase |
199-851 |
1.30e-122 |
|
amine oxidase
Pssm-ID: 178578 [Multi-domain] Cd Length: 881 Bit Score: 392.08 E-value: 1.30e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 199 AFQSRLPHDRMTSQE--AACFPdIISGPQQTQkvFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSdtvLVHRVHSY 276
Cdd:PLN03000 86 ALTAGFPADSLTEEEieFGVVP-IVGGIEQVN--YILIRNHIISKWRENISSWVTKEMFLGSIPKHCSS---LLDSAYNY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 277 LERHGLINFGIYKRIK-PLPIKKT-GKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFR-KGNYV---ADL 350
Cdd:PLN03000 160 LVTHGYINFGIAQAIKdKFPAQSSkSSVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGGRVYTKKmEANRVgaaADL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 351 GAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAdtvkVPKEKDEMVEQEFNRLLEATSYLsHQLDFNVlnNKP 430
Cdd:PLN03000 240 GGSVLTGTLGNPLGIIARQLGSSLYKVRDKCPLYRVDGKP----VDPDVDLKVEVAFNQLLDKASKL-RQLMGDV--SMD 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 431 VSLGQALEVVIQLQEKHVKDEQIehwkkivktqeelkellnkmvnlkekikelhqqykeasevkpprditaeflvkskhr 510
Cdd:PLN03000 313 VSLGAALETFRQVSGNDVATEEM--------------------------------------------------------- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 511 dltalckeydelaetqgkleeklqeleanppsdvylssrdrQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHL 590
Cdd:PLN03000 336 -----------------------------------------GLFNWHLANLEYANAGLVSKLSLAFWDQDDPYDMGGDHC 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 591 TVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTrstsqtfIYKCDAVLCTLPLGVLKQQppAVQFVPPLPE 670
Cdd:PLN03000 375 FLPGGNGRLVQALAENVPILYEKTVQTIRYGSNGVKVIAGNQ-------VYEGDMVLCTVPLGVLKNG--SIKFVPELPQ 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 671 WKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWN---LYKAPILLALVAGEAAGIMENISDDV 747
Cdd:PLN03000 446 RKLDCIKRLGFGLLNKVAMLFPYVFWSTDLDTFGHLTEDPNYRGEFFLFYSyapVAGGPLLIALVAGEAAHKFETMPPTD 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 748 IVGRCLAILKGIFGSSA--VPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGpsipgapqpipRLFFAG 825
Cdd:PLN03000 526 AVTRVLHILRGIYEPQGinVPDPLQTVCTRWGGDPFSLGSYSNVAVGASGDDYDILAESVGDG-----------RLFFAG 594
|
650 660
....*....|....*....|....*.
gi 568932208 826 EHTIRNYPATVHGALLSGLREAGRIA 851
Cdd:PLN03000 595 EATTRRYPATMHGAFVTGLREAANMA 620
|
|
| PLN02529 |
PLN02529 |
lysine-specific histone demethylase 1 |
228-850 |
2.07e-114 |
|
lysine-specific histone demethylase 1
Pssm-ID: 178144 [Multi-domain] Cd Length: 738 Bit Score: 366.14 E-value: 2.07e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 228 QKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSdtvLVHRVHSYLERHGLINFGIYKRI-KPLPIKKT-GKVIII 305
Cdd:PLN02529 90 QNDYIVVRNHILARWRSNVGIWLSKGQIKETVSSEYEH---LISAAYDFLLYNGYINFGVSPSFaSPIPEEGTeGSVIIV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 306 GSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVAT---FRKGNYVA-DLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKC 381
Cdd:PLN02529 167 GAGLAGLAAARQLLSFGFKVVVLEGRNRPGGRVYTqkmGRKGQFAAvDLGGSVITGIHANPLGVLARQLSIPLHKVRDNC 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 382 PLYEANGqadtVKVPKEKDEMVEQEFNRLLEATSylshqldfnvlnnkpvslgqalevviqlqekhvkdeqiehwkkivk 461
Cdd:PLN02529 247 PLYKPDG----ALVDKEIDSNIEFIFNKLLDKVT---------------------------------------------- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 462 tqeELKELLNKMVNlkekikelhqqykeasevkpprDITAeflvkskhrdltalckeydelaetqGKLEEKLQELEAnpp 541
Cdd:PLN02529 277 ---ELRQIMGGFAN----------------------DISL-------------------------GSVLERLRQLYG--- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 542 sdVYLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYT 621
Cdd:PLN02529 304 --VARSTEERQLLDWHLANLEYANAGCLSDLSAAYWDQDDPYEMGGDHCFLAGGNWRLINALCEGVPIFYGKTVDTIKYG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 622 ASGCEVIAvntrsTSQtfIYKCDAVLCTLPLGVLKQQppAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVN 701
Cdd:PLN02529 382 NDGVEVIA-----GSQ--VFQADMVLCTVPLGVLKKR--TIRFEPELPRRKLAAIDRLGFGLLNKVAMVFPSVFWGEELD 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 702 LFGHVGSTTASRGELFLFWNLYK---APILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSA--VPQPKETVVSRW 776
Cdd:PLN02529 453 TFGCLNESSNKRGEFFLFYGYHTvsgGPALVALVAGEAAQRFENTDPSTLLHRVLSVLRGIYNPKGinVPDPIQTICTRW 532
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932208 777 RADPWARGSYSYVAAGSSGNDYDLMAQpitpgpSIPGapqpipRLFFAGEHTIRNYPATVHGALLSGLREAGRI 850
Cdd:PLN02529 533 GSDPLSYGSYSHVRVQSSGSDYDILAE------SVSG------RLFFAGEATTRQYPATMHGAFLSGLREASRI 594
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
301-852 |
1.79e-112 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 378.44 E-value: 1.79e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYV-ADLGAMVVTGLGGN--------PMAVVSKQVN 371
Cdd:PLN02976 695 KIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGRVYTDRSSLSVpVDLGASIITGVEADvaterrpdPSSLICAQLG 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 372 MELAKIKQKCPLYeangqaDTV---KVPKEKDEMVEQEFNRLLEatsylshQLDFNVLNNKPVSLGQALEvviqlqekhv 448
Cdd:PLN02976 775 LELTVLNSDCPLY------DVVtgeKVPADLDEALEAEYNSLLD-------DMVLLVAQKGEHAMKMSLE---------- 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 449 kdEQIEHwkkivktqeELKEllNKMVNLKEKIKElhqqykeasevkpprditaeflvkskhrdlTALCKEYDELAETQgK 528
Cdd:PLN02976 832 --DGLEY---------ALKR--RRMPRPGVDIDE------------------------------TELGNAADDLYDSA-S 867
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 529 LEEKLQELEANPPSDVyLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFE-FTGSHLTVRNGYSCVPVALAEGL 607
Cdd:PLN02976 868 TGVDGGHCEKESKEDV-LSPLERRVMNWHFAHLEYGCAALLKEVSLPYWNQDDVYGgFGGAHCMIKGGYSNVVESLAEGL 946
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 608 DIKLNTAVRQVRY-------TASGCEVIAVNTRSTSQtfiYKCDAVLCTLPLGVLKQQppAVQFVPPLPEWKTSAVQRMG 680
Cdd:PLN02976 947 DIHLNHVVTDVSYgskdagaSGSSRKKVKVSTSNGSE---FLGDAVLITVPLGCLKAE--TIKFSPPLPDWKYSSIQRLG 1021
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 681 FGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYK---APILLALVAGEAAGIMENISDDVIVGRCLAILK 757
Cdd:PLN02976 1022 FGVLNKVVLEFPEVFWDDSVDYFGATAEETDLRGQCFMFWNVKKtvgAPVLIALVVGKAAIDGQSMSSSDHVNHALMVLR 1101
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 758 GIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGpsipgapqpiprLFFAGEHTIRNYPATVH 837
Cdd:PLN02976 1102 KLFGEALVPDPVASVVTDWGRDPFSYGAYSYVAIGASGEDYDILGRPVENC------------LFFAGEATCKEHPDTVG 1169
|
570
....*....|....*
gi 568932208 838 GALLSGLREAGRIAD 852
Cdd:PLN02976 1170 GAMMSGLREAVRIID 1184
|
|
| Amino_oxidase |
pfam01593 |
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ... |
309-850 |
7.92e-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: 7.92e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 309 VSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGgNPMAVVSKQVNMELakiKQKCPLYEANG 388
Cdd:pfam01593 1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVRDDGFLIELGAMWFHGAQ-PPLLALLKELGLED---RLVLPDPAPFY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 389 QADTV--KVPKEKDEMVEQEFNRLLEAtsylshqldfnvlnnkpvslgqalevviqlqekhvkdeqiehwkkivktqeel 466
Cdd:pfam01593 77 TVLFAggRRYPGDFRRVPAGWEGLLEF----------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 467 kellNKMVNLKEKIKELHqqykeasevkpprditaeFLVKSKHRDLTALCKeydelaetqGKLEEKLQELEANPPSDVYL 546
Cdd:pfam01593 104 ----GRLLSIPEKLRLGL------------------AALASDALDEFDLDD---------FSLAESLLFLGRRGPGDVEV 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 547 SsrDRQILDWHFANLEFANAT-----PLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAE---GLDIKLNTAVRQV 618
Cdd:pfam01593 153 W--DRLIDPELFAALPFASGAfagdpSELSAGLALPLLWALLGEGGSLLLPRGGLGALPDALAAqllGGDVRLNTRVRSI 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 619 RYTASGCEVIAVNTRStsqtfiYKCDAVLCTLPLGVLKqqppAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDP 698
Cdd:pfam01593 231 DREGDGVTVTLTDGEV------IEADAVIVTVPLGVLK----RILFTPPLPPEKARAIRNLGYGPVNKVHLEFDRKFWPD 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 699 SvNLFGHVGSTTASRGELFLF--WNLY----KAPILLALV-AGEAAGIMENISDDVIVGRCLAILKGIFGSsAVPQPKET 771
Cdd:pfam01593 301 L-GLLGLLSELLTGLGTAFSWltFPNRappgKGLLLLVYVgPGDRARELEGLSDEELLQAVLRDLRKLFGE-EAPEPLRV 378
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568932208 772 VVSRWRADPWARGSYSYVAAGSSGNDYDlmaqpitpgpsiPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRI 850
Cdd:pfam01593 379 LVSDWHTDPWPRGSYSLPQYGPGHDDYR------------PLARTPDPGLFFAGEHTSTGYPGTVEGAIESGRRAARAV 445
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
301-856 |
1.24e-71 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 242.90 E-value: 1.24e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKG--NYVADLGAMVVtglGGNPMAVvskqvnMELAKiK 378
Cdd:COG1231 9 DVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGddGLYAELGAMRI---PPSHTNL------LALAR-E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 379 QKCPLYEANGQADtvkvpkekdemveqefNRLLeatsylshqldfnVLNNKPVSLGQalevviqlqekhvkdeqiehwkk 458
Cdd:COG1231 79 LGLPLEPFPNENG----------------NALL-------------YLGGKRVRAGE----------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 459 IVKTQEELKELLNKMVnlkekikelhqqykeasevkppRDITAEFlvkskhRDLTALCKEYDElaetqgkleEKLQE-LE 537
Cdd:COG1231 107 IAADLRGVAELLAKLL----------------------RALAAAL------DPWAHPAAELDR---------ESLAEwLR 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 538 ANPpsdvyLSSRDRQILDwhfANLEFANATPLSTLSLKHWDQD-DDFEFTGSHLTVRNGYSCVPVALAEGL--DIKLNTA 614
Cdd:COG1231 150 RNG-----ASPSARRLLG---LLGAGEYGADPDELSLLDLLRYaASAGGGAQQFRIVGGMDQLPRALAAELgdRIRLGAP 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 615 VRQVRYTASGCEVIavntrsTSQTFIYKCDAVLCTLPLGVLKQqppaVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRV 694
Cdd:COG1231 222 VTRIRQDGDGVTVT------TDDGGTVRADAVIVTVPPSVLRR----IEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRP 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 695 FWDPSvnlfGHVGSTTASRGELFL-FWNLY----KAPILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAvPQPK 769
Cdd:COG1231 292 FWEED----GLYGGISLTDLPIRQtWYPSNgpdgGAGVLLGYVGGDDARALAALSPEERVAAALEQLARIFGVYA-AEPV 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 770 ETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPItpgpsipgapqpiPRLFFAGEHTIRNYPATVHGALLSGLREAGR 849
Cdd:COG1231 367 DYVSTDWGRDPWSRGAYAAAPPGQLTAAGPALAEPD-------------GRIHFAGEHTSDEWPGWVEGALESGERAAAE 433
|
....*..
gi 568932208 850 IADQFLG 856
Cdd:COG1231 434 ILARLGG 440
|
|
| PLN02268 |
PLN02268 |
probable polyamine oxidase |
302-847 |
4.96e-70 |
|
probable polyamine oxidase
Pssm-ID: 177909 [Multi-domain] Cd Length: 435 Bit Score: 238.43 E-value: 4.96e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 302 VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGG-NPMAVVSKQVNMELAKIK-- 378
Cdd:PLN02268 3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIGGRVHTDYSFGFPVDMGASWLHGVCNeNPLAPLIGRLGLPLYRTSgd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 379 ---------QKCPLYEANGqadtVKVPKEKDEMVEQEFNRLLEATsylshqldfnvlnnkpvslgqalevviqlqeKHVK 449
Cdd:PLN02268 83 nsvlydhdlESYALFDMDG----NQVPQELVTKVGETFERILEET-------------------------------EKVR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 450 DEQIEHwkkivktqeelkellnkmVNLKEKIKelhqqykeasevkpprditaefLVKSKHRDLtalckeydelaetqgkl 529
Cdd:PLN02268 128 DEHEED------------------MSLLQAIS----------------------IVLERHPEL----------------- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 530 eeKLQELeanppsdvylssrDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEftGSHLTVRNGYSCVPVALAEGLDI 609
Cdd:PLN02268 151 --RLEGL-------------AHEVLQWYLCRMEGWFAADADTISLKSWDQEELLE--GGHGLMVRGYDPVINTLAKGLDI 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 610 KLNTAVRQVRYTASGCEViavnTRSTSQTFIykCDAVLCTLPLGVLKQQppAVQFVPPLPEWKTSAVQRMGFGNLNKVVL 689
Cdd:PLN02268 214 RLNHRVTKIVRRYNGVKV----TVEDGTTFV--ADAAIIAVPLGVLKAN--IIKFEPELPEWKEEAISDLGVGIENKIAL 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 690 CFDRVFWdPSVNLFGHVGSTTASRGelfLFWNLYKA---PILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSavP 766
Cdd:PLN02268 286 HFDSVFW-PNVEFLGVVAPTSYGCS---YFLNLHKAtghPVLVYMPAGRLARDIEKLSDEAAANFAMSQLKKMLPDA--T 359
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 767 QPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITpgpsipgapqpipRLFFAGEHTIRNYPATVHGALLSGLRE 846
Cdd:PLN02268 360 EPVQYLVSRWGSDPNSLGCYSYDLVGKPHDLYERLRAPVD-------------NLFFAGEATSSDFPGSVHGAYSTGVMA 426
|
.
gi 568932208 847 A 847
Cdd:PLN02268 427 A 427
|
|
| PLN02568 |
PLN02568 |
polyamine oxidase |
298-850 |
2.32e-43 |
|
polyamine oxidase
Pssm-ID: 215308 [Multi-domain] Cd Length: 539 Bit Score: 165.77 E-value: 2.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 298 KTGKVIIIGSGVSGLAAARQLQSFG-----MDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKqvnm 372
Cdd:PLN02568 4 KKPRIVIIGAGMAGLTAANKLYTSSaandmFELTVVEGGDRIGGRINTSEFGGERIEMGATWIHGIGGSPVYKIAQ---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 373 ELAKIKQKCPLYEANGQADTVKVPKEKDEMVEQefnRLLEATSYLSHQL-DFnvlnnkpvslgqalevviqLQEKHVKDE 451
Cdd:PLN02568 80 EAGSLESDEPWECMDGFPDRPKTVAEGGFEVDP---SIVESISTLFRGLmDD-------------------AQGKLIEPS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 452 QIEhwkkivktqeelkelLNKMVNLKEKikelhqqykeASEVKPPRDITA--EFLvKSKHRDLTALCKEYDELAETQGKL 529
Cdd:PLN02568 138 EVD---------------EVDFVKLAAK----------AARVCESGGGGSvgSFL-RRGLDAYWDSVSADEQIKGYGGWS 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 530 EEKLQEleanppsdvylssrdrQILDWHfANLE--FANATPLSTLSLkhwDQDDDF-EFTGSHLTVRNGYSCVPVALAEG 606
Cdd:PLN02568 192 RKLLEE----------------AIFTMH-ENTQrtYTSADDLSTLDL---AAESEYrMFPGEEITIAKGYLSVIEALASV 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 607 LD---IKLNTAVRQVRYTAsgcEVIAVNTRSTSqtfIYKCDAVLCTLPLGVLKQQ--PPAVQFVPPLPEWKTSAVQRMGF 681
Cdd:PLN02568 252 LPpgtIQLGRKVTRIEWQD---EPVKLHFADGS---TMTADHVIVTVSLGVLKAGigEDSGLFSPPLPDFKTDAISRLGF 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 682 GNLNKVVLCF----DRVFWD----PSVNLFGHvGSTTASRGELFLFW-----NLY----KAPILLALVAGEAAGIMENIS 744
Cdd:PLN02568 326 GVVNKLFVELsprpDGSPEDvakfPFLQMAFH-RSDSEARHDKIPWWmrrtaSICpihkNSSVLLSWFAGKEALELEKLS 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 745 DDVIV-------------------GRCLAILKGIFGSSAVPQPKETVV--SRWRADPWARGSYSYVAAGSSGNDYDLMAQ 803
Cdd:PLN02568 405 DEEIIrgvqttlssflkrrvaglgSQSHPLCNGGASSNDGSRWKFVKVlkSKWGTDPLFLGSYSYVAVGSSGDDLDRMAE 484
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 568932208 804 PITPGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRI 850
Cdd:PLN02568 485 PLPRISDHDQAGGPPLQLLFAGEATHRTHYSTTHGAYFSGLREANRL 531
|
|
| PLN02676 |
PLN02676 |
polyamine oxidase |
297-847 |
3.34e-36 |
|
polyamine oxidase
Pssm-ID: 215362 [Multi-domain] Cd Length: 487 Bit Score: 143.70 E-value: 3.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 297 KKTGKVIIIGSGVSGLAAARQLQSFGM-DVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGnpmavvsKQVNmela 375
Cdd:PLN02676 24 KPSPSVIIVGAGMSGISAAKTLSEAGIeDILILEATDRIGGRMRKANFAGVSVELGANWVEGVGG-------PESN---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 376 kikqkcPLYEangqadtvkvpkekdeMVEQefnrlLEATSYLShqlDF-NVLNNkpvslgqalevvIQLQEKHVKDEqie 454
Cdd:PLN02676 93 ------PIWE----------------LANK-----LKLRTFYS---DFdNLSSN------------IYKQDGGLYPK--- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 455 hwkkivktqeelkellnkmvnlkekiKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALckeydelaetqgkleeKLQ 534
Cdd:PLN02676 128 --------------------------KVVQKSMKVADASDEFGENLSISLSAKKAVDISIL----------------TAQ 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 535 ELEANPPSdvylsSRDRQILDWHFANLEFA---------NATPLSTLSlkhwDQDDDFEFTGShltvRNGYSCVPVALAE 605
Cdd:PLN02676 166 RLFGQVPK-----TPLEMVIDYYNYDYEFAepprvtslkNTEPNPTFV----DFGEDEYFVAD----PRGYESLVYYLAE 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 606 G---------LD--IKLNTAVRQVRYTASGcevIAVNTRSTSqtfIYKCDAVLCTLPLGVLkqQPPAVQFVPPLPEWKTS 674
Cdd:PLN02676 233 QflstksgkiTDprLKLNKVVREISYSKNG---VTVKTEDGS---VYRAKYVIVSVSLGVL--QSDLIKFKPPLPDWKIE 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 675 AVQRMGFGNLNKVVLCFDRVFWdPSVN-----LFGHVgsttaSRGeLFLFW----NLYK-APILLALVAGEAAGIMENIS 744
Cdd:PLN02676 305 AIYQFDMAVYTKIFLKFPYKFW-PSGPgteffLYAHE-----RRG-YYPFWqhleNEYPgSNVLFVTVTDEESRRIEQQP 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 745 DDVIVGRCLAILKGIFGSSaVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITpgpsipgapqpipRLFFA 824
Cdd:PLN02676 378 DSETKAEIMEVLRKMFGPN-IPEATDILVPRWWSNRFFKGSYSNWPIGVSRYEFDQIRAPVG-------------RVYFT 443
|
570 580
....*....|....*....|...
gi 568932208 825 GEHTIRNYPATVHGALLSGLREA 847
Cdd:PLN02676 444 GEHTSEKYNGYVHGAYLAGIDTA 466
|
|
| SWIRM |
pfam04433 |
SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid ... |
207-285 |
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 568932208 207 DRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEapynSDTVLVHRVHSYLERHGLINF 285
Cdd:pfam04433 4 DKLHPIEKRLLPEFFNGKSKTPEVYLEIRNFILNLWRENPKEYLTKTDARRALK----GDVNLISRIHEFLERWGLINF 78
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
301-352 |
1.53e-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: 1.53e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 568932208 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGA 352
Cdd:COG1232 3 RVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRTVEVDGFRIDRGP 54
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
304-363 |
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 568932208 304 IIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPM 363
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYSYRVPGYVFDYGAHIFHGSDEPNV 60
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
301-356 |
6.38e-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: 6.38e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568932208 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVT 356
Cdd:COG1233 5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTFERPGFRFDVGPSVLT 60
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
301-352 |
4.62e-13 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 71.06 E-value: 4.62e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 568932208 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGA 352
Cdd:COG3380 5 DIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGGRMATRRLDGGRFDHGA 56
|
|
| crtI_fam |
TIGR02734 |
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ... |
302-356 |
9.34e-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: 9.34e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 568932208 302 VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVT 356
Cdd:TIGR02734 1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGRAGVLEDDGFRFDTGPTVIT 55
|
|
| PRK11883 |
PRK11883 |
protoporphyrinogen oxidase; Reviewed |
301-352 |
1.42e-09 |
|
protoporphyrinogen oxidase; Reviewed
Pssm-ID: 237009 [Multi-domain] Cd Length: 451 Bit Score: 61.40 E-value: 1.42e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568932208 301 KVIIIGSGVSGLAAARQLQSFG--MDVTLLEARDRVGGRVATFRKGNYVADLGA 352
Cdd:PRK11883 2 KVAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKIQTVRKDGFPIELGP 55
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
299-351 |
2.52e-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: 60.64 E-value: 2.52e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568932208 299 TGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRkgnyVADLG 351
Cdd:COG3349 3 PPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGGRARSFP----DPDTG 51
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
289-336 |
2.89e-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: 2.89e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568932208 289 KRIKPLPIKKTGK-VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 336
Cdd:COG0493 110 WVKPPPPAPRTGKkVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG 158
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
301-346 |
4.36e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 59.52 E-value: 4.36e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 568932208 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNY 346
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAASFEFGGL 46
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
291-336 |
1.51e-08 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 57.87 E-value: 1.51e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 568932208 291 IKPL-PIKKTGK-VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 336
Cdd:PRK12810 133 VKPDpPVKRTGKkVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGG 180
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
302-346 |
2.44e-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: 2.44e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 568932208 302 VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGrvaTFRKGNY 346
Cdd:COG2072 9 VVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGG---TWRDNRY 50
|
|
| PLN02576 |
PLN02576 |
protoporphyrinogen oxidase |
302-352 |
2.61e-08 |
|
protoporphyrinogen oxidase
Pssm-ID: 215314 [Multi-domain] Cd Length: 496 Bit Score: 57.33 E-value: 2.61e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 568932208 302 VIIIGSGVSGLAAARQLQS-FGMDVTLLEARDRVGGRVATFRKGNYVADLGA 352
Cdd:PLN02576 15 VAVVGAGVSGLAAAYALASkHGVNVLVTEARDRVGGNITSVSEDGFIWEEGP 66
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
301-340 |
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 568932208 301 KVIIIGSGVSGLAAARQLQSfGMDVTLLEARDRVGGRVAT 340
Cdd:COG2907 5 RIAVIGSGISGLTAAWLLSR-RHDVTLFEANDRLGGHTHT 43
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
291-336 |
2.40e-07 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 54.03 E-value: 2.40e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 568932208 291 IKPLPIKKTGK-VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 336
Cdd:PRK11749 131 VLFKRAPKTGKkVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG 177
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
368-538 |
4.34e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.61 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 368 KQVNMELAKIKQKcpLYEANGQADTV--KVPKEKDEMVEQEFNRLLEATsyLSHQLD--FNVLNNKPVSLGQALEVVIQL 443
Cdd:COG1340 67 DELNEKVKELKEE--RDELNEKLNELreELDELRKELAELNKAGGSIDK--LRKEIErlEWRQQTEVLSPEEEKELVEKI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 444 QEKhvkDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQ------------------YKEASEVKPPRD-ITAEFL 504
Cdd:COG1340 143 KEL---EKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKikelaeeaqelheemielYKEADELRKEADeLHKEIV 219
|
170 180 190
....*....|....*....|....*....|....
gi 568932208 505 VKSKHRDltALCKEYDELAETQGKLEEKLQELEA 538
Cdd:COG1340 220 EAQEKAD--ELHEEIIELQKELRELRKELKKLRK 251
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
301-342 |
4.89e-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: 4.89e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 568932208 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRvATFR 342
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSG-ASGR 41
|
|
| proto_IX_ox |
TIGR00562 |
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ... |
299-352 |
3.66e-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: 3.66e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568932208 299 TGKVIIIGSGVSGLAAARQLQ----SFGMDVTLLEARDRVGGRVATFRKGNYVADLGA 352
Cdd:TIGR00562 2 KKHVVIIGGGISGLCAAYYLEkeipELPVELTLVEASDRVGGKIQTVKEDGYLIERGP 59
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
301-342 |
3.75e-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: 3.75e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 568932208 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEaRDRVGGRvATFR 342
Cdd:COG0665 4 DVVVIGGGIAGLSTAYHLARRGLDVTVLE-RGRPGSG-ASGR 43
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
293-336 |
3.90e-06 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 50.64 E-value: 3.90e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 568932208 293 PLPIKKTGK-VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 336
Cdd:PRK12771 130 PAPAPDTGKrVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGG 174
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
282-343 |
5.09e-06 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 50.24 E-value: 5.09e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568932208 282 LINFGIYK--RIKPL---PIKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRK 343
Cdd:COG1148 118 LVRMAVAKakLLEPLepiKVPVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQLHK 184
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
368-538 |
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 568932208 368 KQVNMELAKIKQKCPLYEANGQADTV-----KVPKEKDEMVEQEFNRLLEatsylshqlDFNVLNNKPVSLGQALEvviq 442
Cdd:PRK03918 483 RELEKVLKKESELIKLKELAEQLKELeeklkKYNLEELEKKAEEYEKLKE---------KLIKLKGEIKSLKKELE---- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 443 lQEKHVKDEQIEHWKKIVKTQEELKELLNKMVN--------LKEKIKELHQQYKEASEVKP-PRDItaEFLVKSKHRDLT 513
Cdd:PRK03918 550 -KLEELKKKLAELEKKLDELEEELAELLKELEElgfesveeLEERLKELEPFYNEYLELKDaEKEL--EREEKELKKLEE 626
|
170 180
....*....|....*....|....*
gi 568932208 514 ALCKEYDELAETQGKLEEKLQELEA 538
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEE 651
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
289-336 |
1.39e-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: 49.17 E-value: 1.39e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568932208 289 KRIKPLPI-KKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 336
Cdd:PRK12775 419 KPVKPPRFsKKLGKVAICGSGPAGLAAAADLVKYGVDVTVYEALHVVGG 467
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
295-336 |
1.51e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 48.61 E-value: 1.51e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 568932208 295 PIKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 336
Cdd:PRK13984 279 PEKKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGG 320
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
435-538 |
2.28e-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: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 435 QALEVVIQLQEKHVKDEQIEHWKK-----IVKTQEELKELLNKMVNLKEKIKELHQQYKEA-SEVKpprdiTAEFLVK-- 506
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKelpaeLAELEDELAALEARLEAAKTELEDLEKEIKRLeLEIE-----EVEARIKky 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 568932208 507 -------SKHRDLTALCKEYDELAETQGKLEEKLQELEA 538
Cdd:COG1579 79 eeqlgnvRNNKEYEALQKEIESLKRRISDLEDEILELME 117
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
301-351 |
3.18e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 47.58 E-value: 3.18e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568932208 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG--RVATFrKGNYVaDLG 351
Cdd:PRK07208 6 SVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGisRTVTY-KGNRF-DIG 56
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
290-336 |
3.20e-05 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 47.80 E-value: 3.20e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 568932208 290 RIKPLPIKKTGK-VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 336
Cdd:PRK12814 183 RYIPERAPKSGKkVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGG 230
|
|
| PLN02487 |
PLN02487 |
zeta-carotene desaturase |
293-347 |
4.18e-05 |
|
zeta-carotene desaturase
Pssm-ID: 215268 [Multi-domain] Cd Length: 569 Bit Score: 47.10 E-value: 4.18e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 293 PLPIKKTG---KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATF--RKGNYV 347
Cdd:PLN02487 66 PEPEAYKGpklKVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGGKVGSFvdKNGNHI 125
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
301-337 |
5.22e-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: 5.22e-05
10 20 30
....*....|....*....|....*....|....*..
gi 568932208 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGR 337
Cdd:COG0654 5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPD 41
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
372-550 |
7.38e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 372 MELAKIKQKCP-----LYE-------ANGQADTVKVPKEKDEMVEQE---FNRLLEATSYLSHQldfnvlnNKPVSLGQA 436
Cdd:PRK03918 429 EELKKAKGKCPvcgreLTEehrkellEEYTAELKRIEKELKEIEEKErklRKELRELEKVLKKE-------SELIKLKEL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 437 LEVVIQLQEK---HVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVkpprditaEFLVKSKHRDLT 513
Cdd:PRK03918 502 AEQLKELEEKlkkYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL--------EKKLDELEEELA 573
|
170 180 190
....*....|....*....|....*....|....*...
gi 568932208 514 ALCKEYDELA-ETQGKLEEKLQELEanPPSDVYLSSRD 550
Cdd:PRK03918 574 ELLKELEELGfESVEELEERLKELE--PFYNEYLELKD 609
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
301-340 |
7.74e-05 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 45.50 E-value: 7.74e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 568932208 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEaRDRVGGRVAT 340
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIE-GGEPGGQLAT 40
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
300-334 |
1.01e-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: 45.39 E-value: 1.01e-04
10 20 30
....*....|....*....|....*....|....*
gi 568932208 300 GKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRV 334
Cdd:pfam07992 153 KRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRL 187
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
288-357 |
1.32e-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: 1.32e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568932208 288 YKRIKPLPIKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEA-RDRVggrvatfrkgNYVADLGAMVVTG 357
Cdd:COG0569 84 RRRMERGIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVIDKdPERV----------ERLAEEDVLVIVG 144
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
292-336 |
1.66e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 45.01 E-value: 1.66e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 568932208 292 KPLPIKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 336
Cdd:PRK12831 133 SETEEKKGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGG 177
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
301-334 |
1.68e-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: 1.68e-04
10 20 30
....*....|....*....|....*....|....
gi 568932208 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRV 334
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRL 34
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
39-99 |
1.72e-04 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 45.44 E-value: 1.72e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932208 39 AAPPAGLTGPTDMATGAAGERTPRKKEPPRASPP----GGLAEPPGSAGPQAGPTAGPGSATPME 99
Cdd:PHA03378 714 AQRPAAATGRARPPAAAPGRARPPAAAPGRARPPaaapGRARPPAAAPGRARPPAAAPGAPTPQP 778
|
|
| PLN02612 |
PLN02612 |
phytoene desaturase |
290-342 |
2.43e-04 |
|
phytoene desaturase
Pssm-ID: 215330 [Multi-domain] Cd Length: 567 Bit Score: 44.83 E-value: 2.43e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568932208 290 RIKPLPIKKTgKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFR 342
Cdd:PLN02612 85 RSAPRPAKPL-KVVIAGAGLAGLSTAKYLADAGHKPILLEARDVLGGKVAAWK 136
|
|
| LhgO |
COG0579 |
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism]; |
302-335 |
2.57e-04 |
|
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
Pssm-ID: 440344 [Multi-domain] Cd Length: 418 Bit Score: 44.37 E-value: 2.57e-04
10 20 30
....*....|....*....|....*....|....*
gi 568932208 302 VIIIGSGVSGLAAARQL-QSFGMDVTLLEARDRVG 335
Cdd:COG0579 7 VVIIGAGIVGLALARELsRYEDLKVLVLEKEDDVA 41
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
302-336 |
3.64e-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: 3.64e-04
10 20 30
....*....|....*....|....*....|....*
gi 568932208 302 VIIIGSGVSGLAAARQLQSFGMDVTLLEaRDRVGG 336
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVE-KGRLGG 39
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
368-537 |
4.10e-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: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 368 KQVNMELAKIK-QKcplyeangQADTVKvpKEKDEMVEQEfNRLLEATSYLSHqldfnvlNNKPVSlgqALEVVIQLQEK 446
Cdd:TIGR04523 291 NQLKSEISDLNnQK--------EQDWNK--ELKSELKNQE-KKLEEIQNQISQ-------NNKIIS---QLNEQISQLKK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 447 HV---------KDEQI-EHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPPRDITaeflVKSKHRDLTALC 516
Cdd:TIGR04523 350 ELtnsesenseKQRELeEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQ----IKKLQQEKELLE 425
|
170 180
....*....|....*....|.
gi 568932208 517 KEYDELAETQGKLEEKLQELE 537
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLT 446
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
397-553 |
4.28e-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: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 397 KEKDEMVEQEFNRLLEATSYLSHQL-----DFNVLNNKPVSLGQALEVVIQLQEKhVKDEQIEHWKKIVKTQEELKELLN 471
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIekkqqEINEKTTEISNTQTQLNQLKDEQNK-IKKQLSEKQKELEQNNKKIKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 472 KMVNLKEKIKELHQQyKEA---SEVKpprditaEFLvKSKHRDLTALCKEYD-------ELAETQGKLEEKLQELEANPp 541
Cdd:TIGR04523 289 QLNQLKSEISDLNNQ-KEQdwnKELK-------SEL-KNQEKKLEEIQNQISqnnkiisQLNEQISQLKKELTNSESEN- 358
|
170
....*....|..
gi 568932208 542 sdvylSSRDRQI 553
Cdd:TIGR04523 359 -----SEKQREL 365
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
441-553 |
4.60e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 441 IQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKppRDITAEFLVKSK-----HRDLTAL 515
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL--AQAQEELESLQEeaeelQEELEEL 120
|
90 100 110
....*....|....*....|....*....|....*...
gi 568932208 516 CKEYDELAETQGKLEEKLQELEANppsdvyLSSRDRQI 553
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSE------IAEREEEL 152
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
288-338 |
7.17e-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: 7.17e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568932208 288 YKRIKPLpIKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRV 338
Cdd:COG1251 132 ADALRAA-LAPGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQ 181
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
301-337 |
8.62e-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: 8.62e-04
10 20 30
....*....|....*....|....*....|....*...
gi 568932208 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEA-RDRVGGR 337
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDeGTCPYGG 39
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
293-336 |
1.24e-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: 1.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 568932208 293 PLPIKKTG-KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 336
Cdd:PRK12778 424 PEVAEKNGkKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGG 468
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
301-357 |
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 568932208 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKgnyvadLGAMVVTG 357
Cdd:COG0771 6 KVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPAPELAAAELEA------PGVEVVLG 56
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
369-539 |
1.81e-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: 41.97 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 369 QVNMELAKIKQKCPLYEA--NGQADTVKVPKEKDEMVEQEFNRLLEATSYLSHQLDF--NVLNNKPVSLGQALEVVIQLQ 444
Cdd:TIGR02168 751 QLSKELTELEAEIEELEErlEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElrAELTLLNEEAANLRERLESLE 830
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 445 -EKHVKDEQIEHWKKIVKTQEELKELLNK-MVNLKEKIKELHQQYKEASEVKpprditaeflvKSKHRDLTALCKEYDEL 522
Cdd:TIGR02168 831 rRIAATERRLEDLEEQIEELSEDIESLAAeIEELEELIEELESELEALLNER-----------ASLEEALALLRSELEEL 899
|
170
....*....|....*..
gi 568932208 523 AETQGKLEEKLQELEAN 539
Cdd:TIGR02168 900 SEELRELESKRSELRRE 916
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
443-538 |
2.11e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 443 LQEKHVKDEQIEhwKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPprditaeflVKSKHRDLTALCKEY--- 519
Cdd:PRK03918 240 IEELEKELESLE--GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKE---------KAEEYIKLSEFYEEYlde 308
|
90 100
....*....|....*....|
gi 568932208 520 -DELAETQGKLEEKLQELEA 538
Cdd:PRK03918 309 lREIEKRLSRLEEEINGIEE 328
|
|
| MRPL52 |
pfam18699 |
Mitoribosomal protein mL52; Members of this family include the mamalian mitoribosomal proteins ... |
422-495 |
2.24e-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: 2.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568932208 422 DFNVLNNKPVSLGQalevviqLQEKHvKDEQIEHWKKIVKTQEELKELLnKMVNLKEKIKELHQQYKEASEVKP 495
Cdd:pfam18699 25 DFSFADGRPAPVTS-------GQLKR-KLKQIELAKKIVKLSSEVDEAE-ERYKRKQEEEEEEIQKIIDNKLKP 89
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
397-537 |
2.36e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 397 KEKDEMVEQEFNRLLEATSYLSHQLDFNVLNN-KPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLN---- 471
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDlSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAeagv 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 472 --------------KMVNLKEKIKELHQQYKE-ASEVKPPRDITAEFLVKSKHRDLT----ALCKEYDELAETQGKLEEK 532
Cdd:COG4717 382 edeeelraaleqaeEYQELKEELEELEEQLEElLGELEELLEALDEEELEEELEELEeeleELEEELEELREELAELEAE 461
|
....*
gi 568932208 533 LQELE 537
Cdd:COG4717 462 LEQLE 466
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
394-539 |
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 568932208 394 KVPKEKDEMvEQEFNRLLEATSYLSHQLDfnvlNNKPVSlgQALEVVIQL--QEKHVKDEQIEHWKK-IVKTQEELKEL- 469
Cdd:TIGR04523 374 KLKKENQSY-KQEIKNLESQINDLESKIQ----NQEKLN--QQKDEQIKKlqQEKELLEKEIERLKEtIIKNNSEIKDLt 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 470 -----LNKMVN--------LKEKIKELHQQYKEA-SEVKpprDITAEFlvKSKHRDLTALCKEYDELAETQGKLEEKLQE 535
Cdd:TIGR04523 447 nqdsvKELIIKnldntresLETQLKVLSRSINKIkQNLE---QKQKEL--KSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
....
gi 568932208 536 LEAN 539
Cdd:TIGR04523 522 LKEK 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
369-538 |
2.65e-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: 41.58 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 369 QVNMELAKIKQKCPLYEANGQADTVKVPKEKDEMVEQEfNRLLEATS-YLSHQLDFNVLNNKPVSLGQALEVVIQLQEKh 447
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE-EEIEELQKeLYALANEISRLEQQKQILRERLANLERQLEE- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 448 vKDEQIEHWK-KIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPprdiTAEFLVKSKHRDLTALCKEYDELAETQ 526
Cdd:TIGR02168 321 -LEAQLEELEsKLDELAEELAELEEKLEELKEELESLEAELEELEAELE----ELESRLEELEEQLETLRSKVAQLELQI 395
|
170
....*....|..
gi 568932208 527 GKLEEKLQELEA 538
Cdd:TIGR02168 396 ASLNNEIERLEA 407
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
300-340 |
2.93e-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: 2.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568932208 300 GKVIIIGSGVSGLAAARQLQSFGMDVTLL--------EARDRVGGRVAT 340
Cdd:smart01002 21 AKVVVIGAGVVGLGAAATAKGLGAEVTVLdvrparlrQLESLLGARFTT 69
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
368-567 |
2.98e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 368 KQVNMELAKIKQKcpLYEANGQADTVKvpkEKDEMVEQEFNRLLEATSYLSHQLdfNVLNNKPVSLgqalevviQLQEKH 447
Cdd:COG4372 69 EQARSELEQLEEE--LEELNEQLQAAQ---AELAQAQEELESLQEEAEELQEEL--EELQKERQDL--------EQQRKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 448 VKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPPRDITAefLVKSKHRdlTALCKEYDELAETQG 527
Cdd:COG4372 134 LEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE--LLKEANR--NAEKEEELAEAEKLI 209
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568932208 528 KLEEKLQELEANPPSDVYLSSRDRQILDWHFANLEFANAT 567
Cdd:COG4372 210 ESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
302-360 |
3.02e-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: 3.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568932208 302 VIIIGSGVSG----LAAARQlqsfGMDVTLLEARDRVGGR-----VATFRkGNYVADlgAMVVTGLGG 360
Cdd:pfam12831 2 VVVVGGGPAGvaaaIAAARA----GAKVLLVERRGFLGGMltsglVGPDM-GFYLNK--EQVVGGIAR 62
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
404-538 |
3.67e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 404 EQEFNRLLEATSYLSHQLDfnvlnnkpvSLGQALEVVIQLQEKHVKDEQI-EHWKKIVKTQEELKELLNKMVNLKEKIKE 482
Cdd:COG4717 87 EEEYAELQEELEELEEELE---------ELEAELEELREELEKLEKLLQLlPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568932208 483 LHQQY-------KEASEVKppRDITAEFLVKS--KHRDLTALCKEYDELAETQGKLEEKLQELEA 538
Cdd:COG4717 158 LRELEeeleeleAELAELQ--EELEELLEQLSlaTEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
441-537 |
3.76e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 441 IQLQEKHVKDEQIEhwkkIVKTQEELKELLNKMVNLKEKIKELHQQYKEasevKPPRDITAEFLVKSKH-----RDLTAL 515
Cdd:PRK03918 614 LEREEKELKKLEEE----LDKAFEELAETEKRLEELRKELEELEKKYSE----EEYEELREEYLELSRElaglrAELEEL 685
|
90 100
....*....|....*....|..
gi 568932208 516 CKEYDELAETQGKLEEKLQELE 537
Cdd:PRK03918 686 EKRREEIKKTLEKLKEELEERE 707
|
|
| PRK06847 |
PRK06847 |
hypothetical protein; Provisional |
301-336 |
3.76e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235874 [Multi-domain] Cd Length: 375 Bit Score: 40.63 E-value: 3.76e-03
10 20 30
....*....|....*....|....*....|....*...
gi 568932208 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARD--RVGG 336
Cdd:PRK06847 6 KVLIVGGGIGGLSAAIALRRAGIAVDLVEIDPewRVYG 43
|
|
| Ald |
COG0686 |
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ... |
300-340 |
3.80e-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: 3.80e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568932208 300 GKVIIIGSGVSGLAAARQLQSFGMDVTLL--------EARDRVGGRVAT 340
Cdd:COG0686 169 AKVVILGGGVVGTNAARMALGLGADVTVLdinldrlrRLDDIFGGRVTT 217
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
300-340 |
3.81e-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: 3.81e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568932208 300 GKVIIIGSGVSGLAAARQLQSFGMDVTLL--------EARDRVGGRVAT 340
Cdd:cd05305 169 AKVVILGAGVVGENAARVALGLGAEVTVLdinlerlrYLDDIFGGRVTT 217
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
39-99 |
4.35e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 40.82 E-value: 4.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568932208 39 AAPPAGLTGPTDMATGAAGERTPRKKEPPRASPPGGlaePPGSAGPQAGPTAGP-------GSATPME 99
Cdd:PHA03378 734 ARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAA---APGAPTPQPPPQAPPapqqrprGAPTPQP 798
|
|
| mnmC |
PRK01747 |
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ... |
301-335 |
5.68e-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: 5.68e-03
10 20 30
....*....|....*....|....*....|....*
gi 568932208 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVG 335
Cdd:PRK01747 262 DAAIIGGGIAGAALALALARRGWQVTLYEADEAPA 296
|
|
| AlaDh_PNT_C |
pfam01262 |
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
300-334 |
5.74e-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: 5.74e-03
10 20 30
....*....|....*....|....*....|....*
gi 568932208 300 GKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRV 334
Cdd:pfam01262 29 AKVLVIGGGVAGLNAAATAKGLGAIVTILDVRPAR 63
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
287-340 |
6.17e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 40.10 E-value: 6.17e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 568932208 287 IYKRIKPLPIKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVAT 340
Cdd:PRK12843 4 VVSELSPERWDAEFDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGTTAT 57
|
|
| PTZ00306 |
PTZ00306 |
NADH-dependent fumarate reductase; Provisional |
289-339 |
6.68e-03 |
|
NADH-dependent fumarate reductase; Provisional
Pssm-ID: 140327 [Multi-domain] Cd Length: 1167 Bit Score: 40.15 E-value: 6.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 568932208 289 KRIK-PLPikktGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVA 339
Cdd:PTZ00306 402 KRIAgSLP----ARVIVVGGGLAGCSAAIEAASCGAQVILLEKEAKLGGNSA 449
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
39-119 |
7.16e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 39.86 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 39 AAPPAGLTGPTDMATGAAgeRTPRKKEPPRASPPGGLAEPPGSAGPQAGPTAGPGSATPmetGIAETPEGRRTSRRKRAK 118
Cdd:PRK12323 372 AGPATAAAAPVAQPAPAA--AAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSP---APEALAAARQASARGPGG 446
|
.
gi 568932208 119 V 119
Cdd:PRK12323 447 A 447
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
290-336 |
7.64e-03 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 39.78 E-value: 7.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 568932208 290 RIKPLPikktGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 336
Cdd:PRK06292 164 ELDKLP----KSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILP 206
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
35-119 |
8.20e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 40.31 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 35 GSEVAAPPAGLTGPTDMATGAAGERTPRKKEPPRASPPGGLAePPGSAGPQAGPTAGPGSATPMETGIAETPEG----RR 110
Cdd:PHA03247 2788 VASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLP-PPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGdvrrRP 2866
|
....*....
gi 568932208 111 TSRRKRAKV 119
Cdd:PHA03247 2867 PSRSPAAKP 2875
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
302-336 |
8.22e-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: 8.22e-03
10 20 30
....*....|....*....|....*....|....*
gi 568932208 302 VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 336
Cdd:COG1053 6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
|
|
| murD |
PRK14106 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional |
301-379 |
8.64e-03 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
Pssm-ID: 184511 [Multi-domain] Cd Length: 450 Bit Score: 39.57 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLE--ARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIK 378
Cdd:PRK14106 7 KVLVVGAGVSGLALAKFLKKLGAKVILTDekEEDQLKEALEELGELGIELVLGEYPEEFLEGVDLVVVSPGVPLDSPPVV 86
|
.
gi 568932208 379 Q 379
Cdd:PRK14106 87 Q 87
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
40-127 |
9.79e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 39.92 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568932208 40 APPAGLTGPTDMATGAagerTPRKKEPPRASPPGGLAEPPGSAGPQAGPTAGPG---SATPMETGIAETPEGRRTSRRKR 116
Cdd:PHA03247 2591 APPQSARPRAPVDDRG----DPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPhppPTVPPPERPRDDPAPGRVSRPRR 2666
|
90
....*....|.
gi 568932208 117 AKVEYREMDES 127
Cdd:PHA03247 2667 ARRLGRAAQAS 2677
|
|
| |
