|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02328 |
PLN02328 |
lysine-specific histone demethylase 1 homolog |
203-845 |
4.56e-127 |
|
lysine-specific histone demethylase 1 homolog
Pssm-ID: 215187 [Multi-domain] Cd Length: 808 Bit Score: 401.68 E-value: 4.56e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 203 LPHDRMTSQE-AACFPDIISGPQQTQkvFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSdtvLVHRVHSYLERHGL 281
Cdd:PLN02328 142 FPVDSLTEEEiEANVVSTIGGTEQAN--YIVVRNHILARWRSNVSNWLTRDHALESIRAEHKN---LVDSAYNFLLEHGY 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 282 INFGIYKRIKPLPTK-----KTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFR-KGNYV---ADLGAM 352
Cdd:PLN02328 217 INFGVAPVIKEAQLRsfegvEPANVVVVGAGLAGLVAARQLLSMGFKVVVLEGRARPGGRVKTMKmKGDGVvaaADLGGS 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 353 VVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEFNRLLEAtsylshqldfnvlnnkpvslgqal 432
Cdd:PLN02328 297 VLTGINGNPLGVLARQLGLPLHKVRDICPLYLPDGKAVDAEIDSKIEASFNKLLDR------------------------ 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 433 evVIQLQEKHVkdeqiehwkkivktqEELKELlnkMVNLKEKIKELHQQYKeasevkpprditaeflvkskhrdltalck 512
Cdd:PLN02328 353 --VCKLRQAMI---------------EEVKSV---DVNLGTALEAFRHVYK----------------------------- 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 513 eydeLAETQgkleeklqeleanppsdvylssRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYS 592
Cdd:PLN02328 384 ----VAEDP----------------------QERMLLNWHLANLEYANASLMSNLSMAYWDQDDPYEMGGDHCFIPGGND 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 593 CVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRstsqtfiYKCDAVLCTLPLGVLKQQppAVQFVPPLPEWKTSAVQ 672
Cdd:PLN02328 438 TFVRELAKDLPIFYERTVESIRYGVDGVIVYAGGQE-------FHGDMVLCTVPLGVLKKG--SIEFYPELPQRKKDAIQ 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 673 RMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFW---NLYKAPILLALVAGEAAGIMENISDDVIVGRCLA 749
Cdd:PLN02328 509 RLGYGLLNKVALLFPYNFWGGEIDTFGHLTEDPSMRGEFFLFYsysSVSGGPLLIALVAGDAAVKFETLSPVESVKRVLQ 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 750 ILKGIFGSS--AVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGpsipgapqpipRLFFAGEHTIRNY 827
Cdd:PLN02328 589 ILRGIFHPKgiVVPDPVQAVCTRWGKDCFTYGSYSYVAVGSSGDDYDILAESVGDG-----------RVFFAGEATNKQY 657
|
650
....*....|....*...
gi 530360925 828 PATVHGALLSGLREAGRI 845
Cdd:PLN02328 658 PATMHGAFLSGMREAANI 675
|
|
| PLN03000 |
PLN03000 |
amine oxidase |
198-846 |
1.60e-125 |
|
amine oxidase
Pssm-ID: 178578 [Multi-domain] Cd Length: 881 Bit Score: 399.78 E-value: 1.60e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 198 AFQSRLPHDRMTSQE--AACFPdIISGPQQTQkvFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSdtvLVHRVHSY 275
Cdd:PLN03000 86 ALTAGFPADSLTEEEieFGVVP-IVGGIEQVN--YILIRNHIISKWRENISSWVTKEMFLGSIPKHCSS---LLDSAYNY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 276 LERHGLINFGIYKRIK-PLPTKKT-GKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFR-KGNYV---ADL 349
Cdd:PLN03000 160 LVTHGYINFGIAQAIKdKFPAQSSkSSVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGGRVYTKKmEANRVgaaADL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 350 GAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEFNRLLEATSYLsHQLDFNVlnNKPVSLG 429
Cdd:PLN03000 240 GGSVLTGTLGNPLGIIARQLGSSLYKVRDKCPLYRVDGKPVDPDVDLKVEVAFNQLLDKASKL-RQLMGDV--SMDVSLG 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 430 QALEVVIQLQEKHVKDEQIehwkkivktqeelkellnkmvnlkekikelhqqykeasevkpprditaeflvkskhrdlta 509
Cdd:PLN03000 317 AALETFRQVSGNDVATEEM------------------------------------------------------------- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 510 lckeydelaetqgkleeklqeleanppsdvylssrdrQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRN 589
Cdd:PLN03000 336 -------------------------------------GLFNWHLANLEYANAGLVSKLSLAFWDQDDPYDMGGDHCFLPG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 590 GYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTrstsqtfIYKCDAVLCTLPLGVLKQQppAVQFVPPLPEWKTS 669
Cdd:PLN03000 379 GNGRLVQALAENVPILYEKTVQTIRYGSNGVKVIAGNQ-------VYEGDMVLCTVPLGVLKNG--SIKFVPELPQRKLD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 670 AVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWN---LYKAPILLALVAGEAAGIMENISDDVIVGR 746
Cdd:PLN03000 450 CIKRLGFGLLNKVAMLFPYVFWSTDLDTFGHLTEDPNYRGEFFLFYSyapVAGGPLLIALVAGEAAHKFETMPPTDAVTR 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 747 CLAILKGIFGSSA--VPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGpsipgapqpipRLFFAGEHTI 824
Cdd:PLN03000 530 VLHILRGIYEPQGinVPDPLQTVCTRWGGDPFSLGSYSNVAVGASGDDYDILAESVGDG-----------RLFFAGEATT 598
|
650 660
....*....|....*....|..
gi 530360925 825 RNYPATVHGALLSGLREAGRIA 846
Cdd:PLN03000 599 RRYPATMHGAFVTGLREAANMA 620
|
|
| PLN02529 |
PLN02529 |
lysine-specific histone demethylase 1 |
227-845 |
8.74e-117 |
|
lysine-specific histone demethylase 1
Pssm-ID: 178144 [Multi-domain] Cd Length: 738 Bit Score: 372.30 E-value: 8.74e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 227 QKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSdtvLVHRVHSYLERHGLINFGIYKRI-KPLPTKKT-GKVIII 304
Cdd:PLN02529 90 QNDYIVVRNHILARWRSNVGIWLSKGQIKETVSSEYEH---LISAAYDFLLYNGYINFGVSPSFaSPIPEEGTeGSVIIV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 305 GSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVAT---FRKGNYVA-DLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKC 380
Cdd:PLN02529 167 GAGLAGLAAARQLLSFGFKVVVLEGRNRPGGRVYTqkmGRKGQFAAvDLGGSVITGIHANPLGVLARQLSIPLHKVRDNC 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 381 PLYEANGQAVPKEKDEMVEQEFNRLLEATSylshqldfnvlnnkpvslgqalevviqlqekhvkdeqiehwkkivktqeE 460
Cdd:PLN02529 247 PLYKPDGALVDKEIDSNIEFIFNKLLDKVT-------------------------------------------------E 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 461 LKELLNKMVNlkekikelhqqykeasevkpprDITAeflvkskhrdltalckeydelaetqGKLEEKLQELEAnppsdVY 540
Cdd:PLN02529 278 LRQIMGGFAN----------------------DISL-------------------------GSVLERLRQLYG-----VA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 541 LSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGC 620
Cdd:PLN02529 306 RSTEERQLLDWHLANLEYANAGCLSDLSAAYWDQDDPYEMGGDHCFLAGGNWRLINALCEGVPIFYGKTVDTIKYGNDGV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 621 EVIAvntrsTSQtfIYKCDAVLCTLPLGVLKQQppAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGH 700
Cdd:PLN02529 386 EVIA-----GSQ--VFQADMVLCTVPLGVLKKR--TIRFEPELPRRKLAAIDRLGFGLLNKVAMVFPSVFWGEELDTFGC 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 701 VGSTTASRGELFLFWNLYK---APILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSA--VPQPKETVVSRWRADP 775
Cdd:PLN02529 457 LNESSNKRGEFFLFYGYHTvsgGPALVALVAGEAAQRFENTDPSTLLHRVLSVLRGIYNPKGinVPDPIQTICTRWGSDP 536
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 776 WARGSYSYVAAGSSGNDYDLMAQpitpgpSIPGapqpipRLFFAGEHTIRNYPATVHGALLSGLREAGRI 845
Cdd:PLN02529 537 LSYGSYSHVRVQSSGSDYDILAE------SVSG------RLFFAGEATTRQYPATMHGAFLSGLREASRI 594
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
300-847 |
7.19e-113 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 379.60 E-value: 7.19e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYV-ADLGAMVVTGLGGN--------PMAVVSKQVN 370
Cdd:PLN02976 695 KIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGRVYTDRSSLSVpVDLGASIITGVEADvaterrpdPSSLICAQLG 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 371 MELAKIKQKCPLYE-ANGQAVPKEKDEMVEQEFNRLLEatsylshQLDFNVLNNKPVSLGQALEvviqlqekhvkdEQIE 449
Cdd:PLN02976 775 LELTVLNSDCPLYDvVTGEKVPADLDEALEAEYNSLLD-------DMVLLVAQKGEHAMKMSLE------------DGLE 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 450 HwkkivktqeELKEllNKMVNLKEKIKElhqqykeasevkpprditaeflvkskhrdlTALCKEYDELAETQgKLEEKLQ 529
Cdd:PLN02976 836 Y---------ALKR--RRMPRPGVDIDE------------------------------TELGNAADDLYDSA-STGVDGG 873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 530 ELEANPPSDVyLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFE-FTGSHLTVRNGYSCVPVALAEGLDIKLNT 608
Cdd:PLN02976 874 HCEKESKEDV-LSPLERRVMNWHFAHLEYGCAALLKEVSLPYWNQDDVYGgFGGAHCMIKGGYSNVVESLAEGLDIHLNH 952
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 609 AVRQVRY-------TASGCEVIAVNTRSTSQtfiYKCDAVLCTLPLGVLKQQppAVQFVPPLPEWKTSAVQRMGFGNLNK 681
Cdd:PLN02976 953 VVTDVSYgskdagaSGSSRKKVKVSTSNGSE---FLGDAVLITVPLGCLKAE--TIKFSPPLPDWKYSSIQRLGFGVLNK 1027
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 682 VVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYK---APILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSS 758
Cdd:PLN02976 1028 VVLEFPEVFWDDSVDYFGATAEETDLRGQCFMFWNVKKtvgAPVLIALVVGKAAIDGQSMSSSDHVNHALMVLRKLFGEA 1107
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 759 AVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGpsipgapqpiprLFFAGEHTIRNYPATVHGALLSG 838
Cdd:PLN02976 1108 LVPDPVASVVTDWGRDPFSYGAYSYVAIGASGEDYDILGRPVENC------------LFFAGEATCKEHPDTVGGAMMSG 1175
|
....*....
gi 530360925 839 LREAGRIAD 847
Cdd:PLN02976 1176 LREAVRIID 1184
|
|
| Amino_oxidase |
pfam01593 |
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ... |
308-845 |
1.80e-98 |
|
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.
Pssm-ID: 396255 [Multi-domain] Cd Length: 446 Bit Score: 314.81 E-value: 1.80e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 308 VSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGgNPMAVVSKQVNMELakiKQKCPLYEA-- 385
Cdd:pfam01593 1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVRDDGFLIELGAMWFHGAQ-PPLLALLKELGLED---RLVLPDPAPfy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 386 -----NGQAVPKEKdEMVEQEFNRLLEAtsylshqldfnvlnnkpvslgqalevviqlqekhvkdeqiehwkkivktqee 460
Cdd:pfam01593 77 tvlfaGGRRYPGDF-RRVPAGWEGLLEF---------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 461 lkellNKMVNLKEKIKELHqqykeasevkpprditaeFLVKSKHRDLTALCKeydelaetqGKLEEKLQELEANPPSDVY 540
Cdd:pfam01593 104 -----GRLLSIPEKLRLGL------------------AALASDALDEFDLDD---------FSLAESLLFLGRRGPGDVE 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 541 LSsrDRQILDWHFANLEFANAT-----PLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAE---GLDIKLNTAVRQ 612
Cdd:pfam01593 152 VW--DRLIDPELFAALPFASGAfagdpSELSAGLALPLLWALLGEGGSLLLPRGGLGALPDALAAqllGGDVRLNTRVRS 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 613 VRYTASGCEVIAVNTRStsqtfiYKCDAVLCTLPLGVLKqqppAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWD 692
Cdd:pfam01593 230 IDREGDGVTVTLTDGEV------IEADAVIVTVPLGVLK----RILFTPPLPPEKARAIRNLGYGPVNKVHLEFDRKFWP 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 693 PSvNLFGHVGSTTASRGELFLF--WNLY----KAPILLALV-AGEAAGIMENISDDVIVGRCLAILKGIFGSsAVPQPKE 765
Cdd:pfam01593 300 DL-GLLGLLSELLTGLGTAFSWltFPNRappgKGLLLLVYVgPGDRARELEGLSDEELLQAVLRDLRKLFGE-EAPEPLR 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 766 TVVSRWRADPWARGSYSYVAAGSSGNDYDlmaqpitpgpsiPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRI 845
Cdd:pfam01593 378 VLVSDWHTDPWPRGSYSLPQYGPGHDDYR------------PLARTPDPGLFFAGEHTSTGYPGTVEGAIESGRRAARAV 445
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
300-851 |
3.17e-72 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 244.45 E-value: 3.17e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKG--NYVADLGAMVVTGLGGNPMAVVsKQVNMELakik 377
Cdd:COG1231 9 DVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGddGLYAELGAMRIPPSHTNLLALA-RELGLPL---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 378 qkCPLYEANGQAVpkekdemveqefnrlleatsYlshqldfnVLNNKPVSLGQalevviqlqekhvkdeqiehwkkIVKT 457
Cdd:COG1231 84 --EPFPNENGNAL--------------------L--------YLGGKRVRAGE-----------------------IAAD 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 458 QEELKELLNKMVnlkekikelhqqykeasevkppRDITAEFlvkskhRDLTALCKEYDElaetqgkleEKLQE-LEANPp 536
Cdd:COG1231 111 LRGVAELLAKLL----------------------RALAAAL------DPWAHPAAELDR---------ESLAEwLRRNG- 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 537 sdvyLSSRDRQILDwhfANLEFANATPLSTLSLKHWDQD-DDFEFTGSHLTVRNGYSCVPVALAEGL--DIKLNTAVRQV 613
Cdd:COG1231 153 ----ASPSARRLLG---LLGAGEYGADPDELSLLDLLRYaASAGGGAQQFRIVGGMDQLPRALAAELgdRIRLGAPVTRI 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 614 RYTASGCEVIavntrsTSQTFIYKCDAVLCTLPLGVLKQqppaVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDP 693
Cdd:COG1231 226 RQDGDGVTVT------TDDGGTVRADAVIVTVPPSVLRR----IEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEE 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 694 SvnlfGHVGSTTASRGELFL-FWNLY----KAPILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAvPQPKETVV 768
Cdd:COG1231 296 D----GLYGGISLTDLPIRQtWYPSNgpdgGAGVLLGYVGGDDARALAALSPEERVAAALEQLARIFGVYA-AEPVDYVS 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 769 SRWRADPWARGSYSYVAAGSSGNDYDLMAQPItpgpsipgapqpiPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQ 848
Cdd:COG1231 371 TDWGRDPWSRGAYAAAPPGQLTAAGPALAEPD-------------GRIHFAGEHTSDEWPGWVEGALESGERAAAEILAR 437
|
...
gi 530360925 849 FLG 851
Cdd:COG1231 438 LGG 440
|
|
| PLN02268 |
PLN02268 |
probable polyamine oxidase |
301-842 |
1.50e-71 |
|
probable polyamine oxidase
Pssm-ID: 177909 [Multi-domain] Cd Length: 435 Bit Score: 242.29 E-value: 1.50e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 301 VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGG-NPMAVVSKQVNMELAKIK-- 377
Cdd:PLN02268 3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIGGRVHTDYSFGFPVDMGASWLHGVCNeNPLAPLIGRLGLPLYRTSgd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 378 ---------QKCPLYEANGQAVPKEKDEMVEQEFNRLLEATsylshqldfnvlnnkpvslgqalevviqlqeKHVKDEQI 448
Cdd:PLN02268 83 nsvlydhdlESYALFDMDGNQVPQELVTKVGETFERILEET-------------------------------EKVRDEHE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 449 EHwkkivktqeelkellnkmVNLKEKIKelhqqykeasevkpprditaefLVKSKHRDLtalckeydelaetqgkleeKL 528
Cdd:PLN02268 132 ED------------------MSLLQAIS----------------------IVLERHPEL-------------------RL 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 529 QELeanppsdvylssrDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEftGSHLTVRNGYSCVPVALAEGLDIKLNT 608
Cdd:PLN02268 153 EGL-------------AHEVLQWYLCRMEGWFAADADTISLKSWDQEELLE--GGHGLMVRGYDPVINTLAKGLDIRLNH 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 609 AVRQVRYTASGCEViavnTRSTSQTFIykCDAVLCTLPLGVLKQQppAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDR 688
Cdd:PLN02268 218 RVTKIVRRYNGVKV----TVEDGTTFV--ADAAIIAVPLGVLKAN--IIKFEPELPEWKEEAISDLGVGIENKIALHFDS 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 689 VFWdPSVNLFGHVGSTTASRGelfLFWNLYKA---PILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSavPQPKE 765
Cdd:PLN02268 290 VFW-PNVEFLGVVAPTSYGCS---YFLNLHKAtghPVLVYMPAGRLARDIEKLSDEAAANFAMSQLKKMLPDA--TEPVQ 363
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530360925 766 TVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITpgpsipgapqpipRLFFAGEHTIRNYPATVHGALLSGLREA 842
Cdd:PLN02268 364 YLVSRWGSDPNSLGCYSYDLVGKPHDLYERLRAPVD-------------NLFFAGEATSSDFPGSVHGAYSTGVMAA 427
|
|
| PLN02568 |
PLN02568 |
polyamine oxidase |
297-845 |
2.97e-41 |
|
polyamine oxidase
Pssm-ID: 215308 [Multi-domain] Cd Length: 539 Bit Score: 159.61 E-value: 2.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 297 KTGKVIIIGSGVSGLAAARQLQSFG-----MDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNm 371
Cdd:PLN02568 4 KKPRIVIIGAGMAGLTAANKLYTSSaandmFELTVVEGGDRIGGRINTSEFGGERIEMGATWIHGIGGSPVYKIAQEAG- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 372 elakikqkcplyeANGQAVPKEKdemveqefnrlleatsylshqldFNVLNNKPVSLGQALEVViqlqekhvkDEQIEHw 451
Cdd:PLN02568 83 -------------SLESDEPWEC-----------------------MDGFPDRPKTVAEGGFEV---------DPSIVE- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 452 kkivktqeELKELLNKMVNLKEKiKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALCKeydelaetQGkLEEKLQEL 531
Cdd:PLN02568 117 --------SISTLFRGLMDDAQG-KLIEPSEVDEVDFVKLAAKAARVCESGGGGSVGSFLR--------RG-LDAYWDSV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 532 EANPPSDVYLSSRDRQILDWHFA---NLE--FANATPLSTLSLkhwDQDDDF-EFTGSHLTVRNGYSCVPVALAEGLD-- 603
Cdd:PLN02568 179 SADEQIKGYGGWSRKLLEEAIFTmheNTQrtYTSADDLSTLDL---AAESEYrMFPGEEITIAKGYLSVIEALASVLPpg 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 604 -IKLNTAVRQVRYTAsgcEVIAVNTRSTSqtfIYKCDAVLCTLPLGVLKQQ--PPAVQFVPPLPEWKTSAVQRMGFGNLN 680
Cdd:PLN02568 256 tIQLGRKVTRIEWQD---EPVKLHFADGS---TMTADHVIVTVSLGVLKAGigEDSGLFSPPLPDFKTDAISRLGFGVVN 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 681 KVVLCF----DRVFWD----PSVNLFGHvGSTTASRGELFLFW-----NLY----KAPILLALVAGEAAGIMENISDDVI 743
Cdd:PLN02568 330 KLFVELsprpDGSPEDvakfPFLQMAFH-RSDSEARHDKIPWWmrrtaSICpihkNSSVLLSWFAGKEALELEKLSDEEI 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 744 V-------------------GRCLAILKGIFGSSAVPQPKETVV--SRWRADPWARGSYSYVAAGSSGNDYDLMAQPITP 802
Cdd:PLN02568 409 IrgvqttlssflkrrvaglgSQSHPLCNGGASSNDGSRWKFVKVlkSKWGTDPLFLGSYSYVAVGSSGDDLDRMAEPLPR 488
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 530360925 803 GPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRI 845
Cdd:PLN02568 489 ISDHDQAGGPPLQLLFAGEATHRTHYSTTHGAYFSGLREANRL 531
|
|
| PLN02676 |
PLN02676 |
polyamine oxidase |
296-842 |
1.00e-36 |
|
polyamine oxidase
Pssm-ID: 215362 [Multi-domain] Cd Length: 487 Bit Score: 145.24 E-value: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 296 KKTGKVIIIGSGVSGLAAARQLQSFGM-DVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGnpmavvsKQVNmela 374
Cdd:PLN02676 24 KPSPSVIIVGAGMSGISAAKTLSEAGIeDILILEATDRIGGRMRKANFAGVSVELGANWVEGVGG-------PESN---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 375 kikqkcPLYEangqavpkekdeMVEQefnrlLEATSYLShqlDF-NVLNNkpvslgqalevvIQLQEKHVKDEqiehwkk 453
Cdd:PLN02676 93 ------PIWE------------LANK-----LKLRTFYS---DFdNLSSN------------IYKQDGGLYPK------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 454 ivktqeelkellnkmvnlkekiKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALckeydelaetqgkleeKLQELEA 533
Cdd:PLN02676 128 ----------------------KVVQKSMKVADASDEFGENLSISLSAKKAVDISIL----------------TAQRLFG 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 534 NPPSdvylsSRDRQILDWHFANLEFA---------NATPLSTLSlkhwDQDDDFEFTGShltvRNGYSCVPVALAEG--- 601
Cdd:PLN02676 170 QVPK-----TPLEMVIDYYNYDYEFAepprvtslkNTEPNPTFV----DFGEDEYFVAD----PRGYESLVYYLAEQfls 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 602 ------LD--IKLNTAVRQVRYTASGcevIAVNTRSTSqtfIYKCDAVLCTLPLGVLkqQPPAVQFVPPLPEWKTSAVQR 673
Cdd:PLN02676 237 tksgkiTDprLKLNKVVREISYSKNG---VTVKTEDGS---VYRAKYVIVSVSLGVL--QSDLIKFKPPLPDWKIEAIYQ 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 674 MGFGNLNKVVLCFDRVFWdPSVN-----LFGHVgsttaSRGeLFLFW----NLYK-APILLALVAGEAAGIMENISDDVI 743
Cdd:PLN02676 309 FDMAVYTKIFLKFPYKFW-PSGPgteffLYAHE-----RRG-YYPFWqhleNEYPgSNVLFVTVTDEESRRIEQQPDSET 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 744 VGRCLAILKGIFGSSaVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITpgpsipgapqpipRLFFAGEHT 823
Cdd:PLN02676 382 KAEIMEVLRKMFGPN-IPEATDILVPRWWSNRFFKGSYSNWPIGVSRYEFDQIRAPVG-------------RVYFTGEHT 447
|
570
....*....|....*....
gi 530360925 824 IRNYPATVHGALLSGLREA 842
Cdd:PLN02676 448 SEKYNGYVHGAYLAGIDTA 466
|
|
| SWIRM |
pfam04433 |
SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid ... |
206-284 |
3.63e-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: 3.63e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530360925 206 DRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEapynSDTVLVHRVHSYLERHGLINF 284
Cdd:pfam04433 4 DKLHPIEKRLLPEFFNGKSKTPEVYLEIRNFILNLWRENPKEYLTKTDARRALK----GDVNLISRIHEFLERWGLINF 78
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
300-351 |
1.69e-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: 1.69e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 530360925 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGA 351
Cdd:COG1232 3 RVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRTVEVDGFRIDRGP 54
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
303-362 |
2.45e-14 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 68.33 E-value: 2.45e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 303 IIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPM 362
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYSYRVPGYVFDYGAHIFHGSDEPNV 60
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
300-355 |
6.61e-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: 6.61e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 530360925 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVT 355
Cdd:COG1233 5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTFERPGFRFDVGPSVLT 60
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
300-351 |
4.93e-13 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 71.06 E-value: 4.93e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 530360925 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 |
1.06e-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: 1.06e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 530360925 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 530360925 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 |
2.68e-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: 2.68e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 530360925 298 TGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRkgnyVADLG 350
Cdd:COG3349 3 PPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGGRARSFP----DPDTG 51
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
300-345 |
4.33e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 59.52 E-value: 4.33e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 530360925 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNY 345
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAASFEFGGL 46
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
288-335 |
4.36e-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: 4.36e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 530360925 288 KRIKPLPTKKTGK-VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 335
Cdd:COG0493 110 WVKPPPPAPRTGKkVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG 158
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
290-335 |
6.88e-09 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 59.02 E-value: 6.88e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 530360925 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 |
2.64e-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: 2.64e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 530360925 301 VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGrvaTFRKGNY 345
Cdd:COG2072 9 VVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGG---TWRDNRY 50
|
|
| PLN02576 |
PLN02576 |
protoporphyrinogen oxidase |
301-351 |
3.00e-08 |
|
protoporphyrinogen oxidase
Pssm-ID: 215314 [Multi-domain] Cd Length: 496 Bit Score: 57.33 E-value: 3.00e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 530360925 301 VIIIGSGVSGLAAARQLQS-FGMDVTLLEARDRVGGRVATFRKGNYVADLGA 351
Cdd:PLN02576 15 VAVVGAGVSGLAAAYALASkHGVNVLVTEARDRVGGNITSVSEDGFIWEEGP 66
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
274-335 |
7.84e-08 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 55.57 E-value: 7.84e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530360925 274 SYLERHG---LINFGIYKRIKPLPTKKtgKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 335
Cdd:PRK11749 115 GRLERYItdwAMETGWVLFKRAPKTGK--KVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG 177
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
300-339 |
2.35e-07 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 53.97 E-value: 2.35e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 530360925 300 KVIIIGSGVSGLAAARQLQSfGMDVTLLEARDRVGGRVAT 339
Cdd:COG2907 5 RIAVIGSGISGLTAAWLLSR-RHDVTLFEANDRLGGHTHT 43
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
367-533 |
4.27e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.61 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 367 KQVNMELAKIKQKcpLYEANGQAvpKEKDEMVEQ------EFNRLLEATSYLSHQLD--FNVLNNKPVSLGQALEVVIQL 438
Cdd:COG1340 67 DELNEKVKELKEE--RDELNEKL--NELREELDElrkelaELNKAGGSIDKLRKEIErlEWRQQTEVLSPEEEKELVEKI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 439 QEKhvkDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQ------------------YKEASEVKPPRD-ITAEFL 499
Cdd:COG1340 143 KEL---EKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKikelaeeaqelheemielYKEADELRKEADeLHKEIV 219
|
170 180 190
....*....|....*....|....*....|....
gi 530360925 500 VKSKHRDltALCKEYDELAETQGKLEEKLQELEA 533
Cdd:COG1340 220 EAQEKAD--ELHEEIIELQKELRELRKELKKLRK 251
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
300-341 |
5.65e-07 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 52.40 E-value: 5.65e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 530360925 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRvATFR 341
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSG-ASGR 41
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
292-335 |
1.45e-06 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 51.80 E-value: 1.45e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 530360925 292 PLPTKKTGK-VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 335
Cdd:PRK12771 130 PAPAPDTGKrVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGG 174
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
281-342 |
2.24e-06 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 51.40 E-value: 2.24e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530360925 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 |
3.82e-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: 3.82e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 530360925 298 TGKVIIIGSGVSGLAAARQLQ----SFGMDVTLLEARDRVGGRVATFRKGNYVADLGA 351
Cdd:TIGR00562 2 KKHVVIIGGGISGLCAAYYLEkeipELPVELTLVEASDRVGGKIQTVKEDGYLIERGP 59
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
300-341 |
4.32e-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: 4.32e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 530360925 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEaRDRVGGRvATFR 341
Cdd:COG0665 4 DVVVIGGGIAGLSTAYHLARRGLDVTVLE-RGRPGSG-ASGR 43
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
288-335 |
1.58e-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: 1.58e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 530360925 288 KRIKPLP-TKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 335
Cdd:PRK12775 419 KPVKPPRfSKKLGKVAICGSGPAGLAAAADLVKYGVDVTVYEALHVVGG 467
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
430-533 |
1.80e-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: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 430 QALEVVIQLQEKHVKDEQIEHWKK-----IVKTQEELKELLNKMVNLKEKIKELHQQYKEA-SEVKpprdiTAEFLVK-- 501
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKelpaeLAELEDELAALEARLEAAKTELEDLEKEIKRLeLEIE-----EVEARIKky 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 530360925 502 -------SKHRDLTALCKEYDELAETQGKLEEKLQELEA 533
Cdd:COG1579 79 eeqlgnvRNNKEYEALQKEIESLKRRISDLEDEILELME 117
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
289-335 |
1.84e-05 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 48.57 E-value: 1.84e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 530360925 289 RIKPLPTKKTGK-VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 335
Cdd:PRK12814 183 RYIPERAPKSGKkVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGG 230
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
371-545 |
1.99e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 371 MELAKIKQKCPL----------------YEANGQAVPKEKDEMVEQE---FNRLLEATSYLSHQldfnvlnNKPVSLGQA 431
Cdd:PRK03918 429 EELKKAKGKCPVcgrelteehrkelleeYTAELKRIEKELKEIEEKErklRKELRELEKVLKKE-------SELIKLKEL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 432 LEVVIQLQEK---HVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVkpprditaEFLVKSKHRDLT 508
Cdd:PRK03918 502 AEQLKELEEKlkkYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL--------EKKLDELEEELA 573
|
170 180 190
....*....|....*....|....*....|....*...
gi 530360925 509 ALCKEYDELA-ETQGKLEEKLQELEanPPSDVYLSSRD 545
Cdd:PRK03918 574 ELLKELEELGfESVEELEERLKELE--PFYNEYLELKD 609
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
440-533 |
2.83e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 440 EKHVKDEQIEHWKKIVKTQEELKELLNKMVN--------LKEKIKELHQQYKEASEVKP-PRDItaEFLVKSKHRDLTAL 510
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEELAELLKELEElgfesveeLEERLKELEPFYNEYLELKDaEKEL--EREEKELKKLEEEL 628
|
90 100
....*....|....*....|...
gi 530360925 511 CKEYDELAETQGKLEEKLQELEA 533
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEE 651
|
|
| PLN02487 |
PLN02487 |
zeta-carotene desaturase |
292-346 |
2.90e-05 |
|
zeta-carotene desaturase
Pssm-ID: 215268 [Multi-domain] Cd Length: 569 Bit Score: 47.87 E-value: 2.90e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 292 PLPTKKTG---KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATF--RKGNYV 346
Cdd:PLN02487 66 PEPEAYKGpklKVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGGKVGSFvdKNGNHI 125
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
300-350 |
3.16e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 47.58 E-value: 3.16e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 530360925 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG--RVATFrKGNYVaDLG 350
Cdd:PRK07208 6 SVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGisRTVTY-KGNRF-DIG 56
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
287-335 |
4.01e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 47.45 E-value: 4.01e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 530360925 287 YKRIKPLPT-KKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 335
Cdd:PRK13984 271 YSEILDDEPeKKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGG 320
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
300-336 |
5.47e-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: 5.47e-05
10 20 30
....*....|....*....|....*....|....*..
gi 530360925 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGR 336
Cdd:COG0654 5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPD 41
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
300-339 |
8.40e-05 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 45.50 E-value: 8.40e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 530360925 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 |
8.44e-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: 8.44e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530360925 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 530360925 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 |
1.12e-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: 1.12e-04
10 20 30
....*....|....*....|....*....|....*
gi 530360925 299 GKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRV 333
Cdd:pfam07992 153 KRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRL 187
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
290-335 |
1.70e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 45.01 E-value: 1.70e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 530360925 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 |
1.77e-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: 1.77e-04
10 20 30
....*....|....*....|....*....|....
gi 530360925 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRV 333
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRL 34
|
|
| LhgO |
COG0579 |
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism]; |
301-334 |
2.62e-04 |
|
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
Pssm-ID: 440344 [Multi-domain] Cd Length: 418 Bit Score: 44.37 E-value: 2.62e-04
10 20 30
....*....|....*....|....*....|....*
gi 530360925 301 VIIIGSGVSGLAAARQL-QSFGMDVTLLEARDRVG 334
Cdd:COG0579 7 VVIIGAGIVGLALARELsRYEDLKVLVLEKEDDVA 41
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
436-548 |
3.61e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 436 IQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKppRDITAEFLVKSK-----HRDLTAL 510
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL--AQAQEELESLQEeaeelQEELEEL 120
|
90 100 110
....*....|....*....|....*....|....*...
gi 530360925 511 CKEYDELAETQGKLEEKLQELEANppsdvyLSSRDRQI 548
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSE------IAEREEEL 152
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
301-335 |
3.84e-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: 3.84e-04
10 20 30
....*....|....*....|....*....|....*
gi 530360925 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 ... |
392-548 |
4.25e-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: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 392 KEKDEMVEQEFNRLLEATSYLSHQL-----DFNVLNNKPVSLGQALEVVIQLQEKhVKDEQIEHWKKIVKTQEELKELLN 466
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIekkqqEINEKTTEISNTQTQLNQLKDEQNK-IKKQLSEKQKELEQNNKKIKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 467 KMVNLKEKIKELHQQyKEA---SEVKpprditaEFLvKSKHRDLTALCKEYD-------ELAETQGKLEEKLQELEANPp 536
Cdd:TIGR04523 289 QLNQLKSEISDLNNQ-KEQdwnKELK-------SEL-KNQEKKLEEIQNQISqnnkiisQLNEQISQLKKELTNSESEN- 358
|
170
....*....|..
gi 530360925 537 sdvylSSRDRQI 548
Cdd:TIGR04523 359 -----SEKQREL 365
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
300-336 |
9.68e-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: 400379 [Multi-domain] Cd Length: 301 Bit Score: 42.31 E-value: 9.68e-04
10 20 30
....*....|....*....|....*....|....*...
gi 530360925 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEA-RDRVGGR 336
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDeGTCPYGG 39
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
23-98 |
1.35e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 42.36 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 23 AGPGTAGGSENGSEVAAQPAGLSGPAEVGPGAVGERTPRKKEPPRASPP----GGLAEPPGSAGPQAGPTVVPGSATPME 98
Cdd:PHA03378 699 RAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPaaapGRARPPAAAPGRARPPAAAPGAPTPQP 778
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
296-337 |
1.36e-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: 1.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 530360925 296 KKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRV 337
Cdd:COG1251 140 APGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQ 181
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
300-356 |
1.47e-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: 1.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 530360925 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKgnyvadLGAMVVTG 356
Cdd:COG0771 6 KVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPAPELAAAELEA------PGVEVVLG 56
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
296-335 |
1.57e-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: 1.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 530360925 296 KKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 335
Cdd:PRK12778 429 KNGKKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGG 468
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
392-532 |
1.86e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 392 KEKDEMVEQEFNRLLEATSYLSHQLDFNVLNN-KPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLN---- 466
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDlSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAeagv 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 467 --------------KMVNLKEKIKELHQQYKE-ASEVKPPRDITAEFLVKSKHRDLT----ALCKEYDELAETQGKLEEK 527
Cdd:COG4717 382 edeeelraaleqaeEYQELKEELEELEEQLEElLGELEELLEALDEEELEEELEELEeeleELEEELEELREELAELEAE 461
|
....*
gi 530360925 528 LQELE 532
Cdd:COG4717 462 LEQLE 466
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
438-533 |
2.01e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 438 LQEKHVKDEQIEhwKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPprditaeflVKSKHRDLTALCKEY--- 514
Cdd:PRK03918 240 IEELEKELESLE--GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKE---------KAEEYIKLSEFYEEYlde 308
|
90 100
....*....|....*....|
gi 530360925 515 -DELAETQGKLEEKLQELEA 533
Cdd:PRK03918 309 lREIEKRLSRLEEEINGIEE 328
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
392-534 |
2.04e-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: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 392 KEKDEMVEQEFNRLLEATSYLSHQLDF--NVLNNKPVSLGQALEVVIQLQ-EKHVKDEQIEHWKKIVKTQEELKELLNK- 467
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDElrAELTLLNEEAANLRERLESLErRIAATERRLEDLEEQIEELSEDIESLAAe 860
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530360925 468 MVNLKEKIKELHQQYKEASEVKpprditaeflvKSKHRDLTALCKEYDELAETQGKLEEKLQELEAN 534
Cdd:TIGR02168 861 IEELEELIEELESELEALLNER-----------ASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
|
| MRPL52 |
pfam18699 |
Mitoribosomal protein mL52; Members of this family include the mamalian mitoribosomal proteins ... |
417-490 |
2.14e-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: 2.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530360925 417 DFNVLNNKPVSLGQalevviqLQEKHvKDEQIEHWKKIVKTQEELKELLnKMVNLKEKIKELHQQYKEASEVKP 490
Cdd:pfam18699 25 DFSFADGRPAPVTS-------GQLKR-KLKQIELAKKIVKLSSEVDEAE-ERYKRKQEEEEEEIQKIIDNKLKP 89
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
367-532 |
2.20e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 367 KQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEfNRLLEATSYLSH-QLDFNVLNNKPVSLGQALEVVIQLQ--EKHV 443
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKE-ERLEELKKKLKElEKRLEELEERHELYEEAKAKKEELErlKKRL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 444 KDEQIEHWKKIVKT--------QEELKELLNKMVNLKEKIKELHQ---QYKEASEVKP--PRDITAEF---LVKSKHRDL 507
Cdd:PRK03918 382 TGLTPEKLEKELEElekakeeiEEEISKITARIGELKKEIKELKKaieELKKAKGKCPvcGRELTEEHrkeLLEEYTAEL 461
|
170 180
....*....|....*....|....*
gi 530360925 508 TALCKEYDELAETQGKLEEKLQELE 532
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELE 486
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
294-339 |
2.57e-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: 39.41 E-value: 2.57e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 530360925 294 PTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLL--------EARDRVGGRVAT 339
Cdd:smart01002 16 GGVPPAKVVVIGAGVVGLGAAATAKGLGAEVTVLdvrparlrQLESLLGARFTT 69
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
399-533 |
2.90e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 399 EQEFNRLLEATSYLSHQLDfnvlnnkpvSLGQALEVVIQLQEKHVKDEQI-EHWKKIVKTQEELKELLNKMVNLKEKIKE 477
Cdd:COG4717 87 EEEYAELQEELEELEEELE---------ELEAELEELREELEKLEKLLQLlPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530360925 478 LHQQY-------KEASEVKppRDITAEFLVKS--KHRDLTALCKEYDELAETQGKLEEKLQELEA 533
Cdd:COG4717 158 LRELEeeleeleAELAELQ--EELEELLEQLSlaTEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
301-359 |
3.51e-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: 3.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530360925 301 VIIIGSGVSG----LAAARQlqsfGMDVTLLEARDRVGGR-----VATFRkGNYVADlgAMVVTGLGG 359
Cdd:pfam12831 2 VVVVGGGPAGvaaaIAAARA----GAKVLLVERRGFLGGMltsglVGPDM-GFYLNK--EQVVGGIAR 62
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
436-532 |
3.67e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 436 IQLQEKHVKDEQIEhwkkIVKTQEELKELLNKMVNLKEKIKELHQQYKEasevKPPRDITAEFLVKSKH-----RDLTAL 510
Cdd:PRK03918 614 LEREEKELKKLEEE----LDKAFEELAETEKRLEELRKELEELEKKYSE----EEYEELREEYLELSRElaglrAELEEL 685
|
90 100
....*....|....*....|..
gi 530360925 511 CKEYDELAETQGKLEEKLQELE 532
Cdd:PRK03918 686 EKRREEIKKTLEKLKEELEERE 707
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
286-339 |
3.99e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 40.88 E-value: 3.99e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 530360925 286 IYKRIKPLPTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVAT 339
Cdd:PRK12843 4 VVSELSPERWDAEFDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGTTAT 57
|
|
| PRK06847 |
PRK06847 |
hypothetical protein; Provisional |
300-335 |
4.15e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235874 [Multi-domain] Cd Length: 375 Bit Score: 40.24 E-value: 4.15e-03
10 20 30
....*....|....*....|....*....|....*...
gi 530360925 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARD--RVGG 335
Cdd:PRK06847 6 KVLIVGGGIGGLSAAIALRRAGIAVDLVEIDPewRVYG 43
|
|
| Ald |
COG0686 |
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ... |
299-339 |
4.19e-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: 4.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 530360925 299 GKVIIIGSGVSGLAAARQLQSFGMDVTLL--------EARDRVGGRVAT 339
Cdd:COG0686 169 AKVVILGGGVVGTNAARMALGLGADVTVLdinldrlrRLDDIFGGRVTT 217
|
|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
300-460 |
4.21e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 168661 [Multi-domain] Cd Length: 373 Bit Score: 40.44 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEardrvggrvatfrKGNYVADLGAMVvtGLGGNpmaVVSKQVNMELAK-IKQ 378
Cdd:PRK06753 2 KIAIIGAGIGGLTAAALLQEQGHEVKVFE-------------KNESVKEVGAGI--GIGDN---VIKKLGNHDLAKgIKN 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 379 kcplyeaNGQAVPkekdemveqEFNRLLEATSYLSH-QLDFNVLNnkpVSLGQalEVVIQLQEKHVKDEQIEHWKKIVKT 457
Cdd:PRK06753 64 -------AGQILS---------TMNLLDDKGTLLNKvKLKSNTLN---VTLHR--QTLIDIIKSYVKEDAIFTGKEVTKI 122
|
...
gi 530360925 458 QEE 460
Cdd:PRK06753 123 ENE 125
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
299-339 |
4.23e-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: 4.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 530360925 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 |
5.35e-03 |
|
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.
Pssm-ID: 426165 [Multi-domain] Cd Length: 213 Bit Score: 39.40 E-value: 5.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 530360925 294 PTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRV 333
Cdd:pfam01262 24 PGVAPAKVLVIGGGVAGLNAAATAKGLGAIVTILDVRPAR 63
|
|
| mnmC |
PRK01747 |
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ... |
300-334 |
5.79e-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: 5.79e-03
10 20 30
....*....|....*....|....*....|....*
gi 530360925 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVG 334
Cdd:PRK01747 262 DAAIIGGGIAGAALALALARRGWQVTLYEADEAPA 296
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
22-110 |
6.37e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 40.35 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 22 EAGPGTAGGSENGSEVAAQPAGLSGPAEVGPGAVGERTPRKKEPPRASPPgglAEPPGSAGPQAGPTVVPGSATPMETGI 101
Cdd:PRK07764 382 ERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQP---APAPAPAPAPPSPAGNAPAGGAPSPPP 458
|
....*....
gi 530360925 102 AETPEGRRT 110
Cdd:PRK07764 459 AAAPSAQPA 467
|
|
| PTZ00306 |
PTZ00306 |
NADH-dependent fumarate reductase; Provisional |
288-338 |
6.58e-03 |
|
NADH-dependent fumarate reductase; Provisional
Pssm-ID: 140327 [Multi-domain] Cd Length: 1167 Bit Score: 40.15 E-value: 6.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 530360925 288 KRIK-PLPTKktgkVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVA 338
Cdd:PTZ00306 402 KRIAgSLPAR----VIVVGGGLAGCSAAIEAASCGAQVILLEKEAKLGGNSA 449
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
289-335 |
7.85e-03 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 39.78 E-value: 7.85e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 530360925 289 RIKPLPtkktGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 335
Cdd:PRK06292 164 ELDKLP----KSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILP 206
|
|
| murD |
PRK14106 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional |
300-378 |
8.73e-03 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
Pssm-ID: 184511 [Multi-domain] Cd Length: 450 Bit Score: 39.57 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 300 KVIIIGSGVSGLAAARQLQSFGMDVTLLE--ARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIK 377
Cdd:PRK14106 7 KVLVVGAGVSGLALAKFLKKLGAKVILTDekEEDQLKEALEELGELGIELVLGEYPEEFLEGVDLVVVSPGVPLDSPPVV 86
|
.
gi 530360925 378 Q 378
Cdd:PRK14106 87 Q 87
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
368-533 |
8.85e-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: 40.04 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 368 QVNMELAKIKQKCPLYEANGQAVPKE----KDEMVEQEfNRLLEATS-YLSHQLDFNVLNNKPVSLGQALEVVIQLQEKh 442
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKleelRLEVSELE-EEIEELQKeLYALANEISRLEQQKQILRERLANLERQLEE- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 443 vKDEQIEHWK-KIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPprdiTAEFLVKSKHRDLTALCKEYDELAETQ 521
Cdd:TIGR02168 321 -LEAQLEELEsKLDELAEELAELEEKLEELKEELESLEAELEELEAELE----ELESRLEELEEQLETLRSKVAQLELQI 395
|
170
....*....|..
gi 530360925 522 GKLEEKLQELEA 533
Cdd:TIGR02168 396 ASLNNEIERLEA 407
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
301-335 |
9.14e-03 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 39.43 E-value: 9.14e-03
10 20 30
....*....|....*....|....*....|....*
gi 530360925 301 VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 335
Cdd:COG1053 6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
20-105 |
9.61e-03 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 39.63 E-value: 9.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 20 GTEAGPGTAGG--SENGSEVAAQPAGLSGPAEVG---PGAVGERTPrkkEPPRASPPGGLAEPPGSAGpQAGPTVVPGSA 94
Cdd:COG5164 99 TTPAGDGGATGppDDGGATGPPDDGGSTTPPSGGsttPPGDGGSTP---PGPGSTGPGGSTTPPGDGG-STTPPGPGGST 174
|
90
....*....|.
gi 530360925 95 TPMETGIAETP 105
Cdd:COG5164 175 TPPDDGGSTTP 185
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
367-562 |
9.90e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 367 KQVNMELAKIKQKcpLYEANGQAV-PKEKDEMVEQEFNRLLEATSYLSHQLdfNVLNNKPVSLgqalevviQLQEKHVKD 445
Cdd:COG4372 69 EQARSELEQLEEE--LEELNEQLQaAQAELAQAQEELESLQEEAEELQEEL--EELQKERQDL--------EQQRKQLEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360925 446 EQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPPRDITAefLVKSKHRdlTALCKEYDELAETQGKLE 525
Cdd:COG4372 137 QIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE--LLKEANR--NAEKEEELAEAEKLIESL 212
|
170 180 190
....*....|....*....|....*....|....*..
gi 530360925 526 EKLQELEANPPSDVYLSSRDRQILDWHFANLEFANAT 562
Cdd:COG4372 213 PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
|
| |
