|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02328 |
PLN02328 |
lysine-specific histone demethylase 1 homolog |
204-846 |
4.68e-127 |
|
lysine-specific histone demethylase 1 homolog
Pssm-ID: 215187 [Multi-domain] Cd Length: 808 Bit Score: 401.68 E-value: 4.68e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 204 LPHDRMTSQE-AACFPDIISGPQQTQkvFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSdtvLVHRVHSYLERHGL 282
Cdd:PLN02328 142 FPVDSLTEEEiEANVVSTIGGTEQAN--YIVVRNHILARWRSNVSNWLTRDHALESIRAEHKN---LVDSAYNFLLEHGY 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 283 INFGIYKRIKPLPTK-----KTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFR-KGNYV---ADLGAM 353
Cdd:PLN02328 217 INFGVAPVIKEAQLRsfegvEPANVVVVGAGLAGLVAARQLLSMGFKVVVLEGRARPGGRVKTMKmKGDGVvaaADLGGS 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 354 VVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEFNRLLEAtsylshqldfnvlnnkpvslgqal 433
Cdd:PLN02328 297 VLTGINGNPLGVLARQLGLPLHKVRDICPLYLPDGKAVDAEIDSKIEASFNKLLDR------------------------ 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 434 evVIQLQEKHVkdeqiehwkkivktqEELKELlnkMVNLKEKIKELHQQYKeasevkpprditaeflvkskhrdltalck 513
Cdd:PLN02328 353 --VCKLRQAMI---------------EEVKSV---DVNLGTALEAFRHVYK----------------------------- 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 514 eydeLAETQgkleeklqeleanppsdvylssRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYS 593
Cdd:PLN02328 384 ----VAEDP----------------------QERMLLNWHLANLEYANASLMSNLSMAYWDQDDPYEMGGDHCFIPGGND 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 594 CVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRstsqtfiYKCDAVLCTLPLGVLKQQppAVQFVPPLPEWKTSAVQ 673
Cdd:PLN02328 438 TFVRELAKDLPIFYERTVESIRYGVDGVIVYAGGQE-------FHGDMVLCTVPLGVLKKG--SIEFYPELPQRKKDAIQ 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 674 RMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFW---NLYKAPILLALVAGEAAGIMENISDDVIVGRCLA 750
Cdd:PLN02328 509 RLGYGLLNKVALLFPYNFWGGEIDTFGHLTEDPSMRGEFFLFYsysSVSGGPLLIALVAGDAAVKFETLSPVESVKRVLQ 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 751 ILKGIFGSS--AVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGpsipgapqpipRLFFAGEHTIRNY 828
Cdd:PLN02328 589 ILRGIFHPKgiVVPDPVQAVCTRWGKDCFTYGSYSYVAVGSSGDDYDILAESVGDG-----------RVFFAGEATNKQY 657
|
650
....*....|....*...
gi 528941334 829 PATVHGALLSGLREAGRI 846
Cdd:PLN02328 658 PATMHGAFLSGMREAANI 675
|
|
| PLN03000 |
PLN03000 |
amine oxidase |
199-847 |
1.64e-125 |
|
amine oxidase
Pssm-ID: 178578 [Multi-domain] Cd Length: 881 Bit Score: 399.78 E-value: 1.64e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 199 AFQSRLPHDRMTSQE--AACFPdIISGPQQTQkvFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSdtvLVHRVHSY 276
Cdd:PLN03000 86 ALTAGFPADSLTEEEieFGVVP-IVGGIEQVN--YILIRNHIISKWRENISSWVTKEMFLGSIPKHCSS---LLDSAYNY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 277 LERHGLINFGIYKRIK-PLPTKKT-GKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFR-KGNYV---ADL 350
Cdd:PLN03000 160 LVTHGYINFGIAQAIKdKFPAQSSkSSVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGGRVYTKKmEANRVgaaADL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 351 GAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEFNRLLEATSYLsHQLDFNVlnNKPVSLG 430
Cdd:PLN03000 240 GGSVLTGTLGNPLGIIARQLGSSLYKVRDKCPLYRVDGKPVDPDVDLKVEVAFNQLLDKASKL-RQLMGDV--SMDVSLG 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 431 QALEVVIQLQEKHVKDEQIehwkkivktqeelkellnkmvnlkekikelhqqykeasevkpprditaeflvkskhrdlta 510
Cdd:PLN03000 317 AALETFRQVSGNDVATEEM------------------------------------------------------------- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 511 lckeydelaetqgkleeklqeleanppsdvylssrdrQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRN 590
Cdd:PLN03000 336 -------------------------------------GLFNWHLANLEYANAGLVSKLSLAFWDQDDPYDMGGDHCFLPG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 591 GYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTrstsqtfIYKCDAVLCTLPLGVLKQQppAVQFVPPLPEWKTS 670
Cdd:PLN03000 379 GNGRLVQALAENVPILYEKTVQTIRYGSNGVKVIAGNQ-------VYEGDMVLCTVPLGVLKNG--SIKFVPELPQRKLD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 671 AVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWN---LYKAPILLALVAGEAAGIMENISDDVIVGR 747
Cdd:PLN03000 450 CIKRLGFGLLNKVAMLFPYVFWSTDLDTFGHLTEDPNYRGEFFLFYSyapVAGGPLLIALVAGEAAHKFETMPPTDAVTR 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 748 CLAILKGIFGSSA--VPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGpsipgapqpipRLFFAGEHTI 825
Cdd:PLN03000 530 VLHILRGIYEPQGinVPDPLQTVCTRWGGDPFSLGSYSNVAVGASGDDYDILAESVGDG-----------RLFFAGEATT 598
|
650 660
....*....|....*....|..
gi 528941334 826 RNYPATVHGALLSGLREAGRIA 847
Cdd:PLN03000 599 RRYPATMHGAFVTGLREAANMA 620
|
|
| PLN02529 |
PLN02529 |
lysine-specific histone demethylase 1 |
228-846 |
8.50e-117 |
|
lysine-specific histone demethylase 1
Pssm-ID: 178144 [Multi-domain] Cd Length: 738 Bit Score: 372.69 E-value: 8.50e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 228 QKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSdtvLVHRVHSYLERHGLINFGIYKRI-KPLPTKKT-GKVIII 305
Cdd:PLN02529 90 QNDYIVVRNHILARWRSNVGIWLSKGQIKETVSSEYEH---LISAAYDFLLYNGYINFGVSPSFaSPIPEEGTeGSVIIV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 306 GSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVAT---FRKGNYVA-DLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKC 381
Cdd:PLN02529 167 GAGLAGLAAARQLLSFGFKVVVLEGRNRPGGRVYTqkmGRKGQFAAvDLGGSVITGIHANPLGVLARQLSIPLHKVRDNC 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 382 PLYEANGQAVPKEKDEMVEQEFNRLLEATSylshqldfnvlnnkpvslgqalevviqlqekhvkdeqiehwkkivktqeE 461
Cdd:PLN02529 247 PLYKPDGALVDKEIDSNIEFIFNKLLDKVT-------------------------------------------------E 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 462 LKELLNKMVNlkekikelhqqykeasevkpprDITAeflvkskhrdltalckeydelaetqGKLEEKLQELEAnppsdVY 541
Cdd:PLN02529 278 LRQIMGGFAN----------------------DISL-------------------------GSVLERLRQLYG-----VA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 542 LSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGC 621
Cdd:PLN02529 306 RSTEERQLLDWHLANLEYANAGCLSDLSAAYWDQDDPYEMGGDHCFLAGGNWRLINALCEGVPIFYGKTVDTIKYGNDGV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 622 EVIAvntrsTSQtfIYKCDAVLCTLPLGVLKQQppAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGH 701
Cdd:PLN02529 386 EVIA-----GSQ--VFQADMVLCTVPLGVLKKR--TIRFEPELPRRKLAAIDRLGFGLLNKVAMVFPSVFWGEELDTFGC 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 702 VGSTTASRGELFLFWNLYK---APILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSA--VPQPKETVVSRWRADP 776
Cdd:PLN02529 457 LNESSNKRGEFFLFYGYHTvsgGPALVALVAGEAAQRFENTDPSTLLHRVLSVLRGIYNPKGinVPDPIQTICTRWGSDP 536
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 777 WARGSYSYVAAGSSGNDYDLMAQpitpgpSIPGapqpipRLFFAGEHTIRNYPATVHGALLSGLREAGRI 846
Cdd:PLN02529 537 LSYGSYSHVRVQSSGSDYDILAE------SVSG------RLFFAGEATTRQYPATMHGAFLSGLREASRI 594
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
301-848 |
7.36e-113 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 379.60 E-value: 7.36e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYV-ADLGAMVVTGLGGN--------PMAVVSKQVN 371
Cdd:PLN02976 695 KIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGRVYTDRSSLSVpVDLGASIITGVEADvaterrpdPSSLICAQLG 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 372 MELAKIKQKCPLYE-ANGQAVPKEKDEMVEQEFNRLLEatsylshQLDFNVLNNKPVSLGQALEvviqlqekhvkdEQIE 450
Cdd:PLN02976 775 LELTVLNSDCPLYDvVTGEKVPADLDEALEAEYNSLLD-------DMVLLVAQKGEHAMKMSLE------------DGLE 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 451 HwkkivktqeELKEllNKMVNLKEKIKElhqqykeasevkpprditaeflvkskhrdlTALCKEYDELAETQgKLEEKLQ 530
Cdd:PLN02976 836 Y---------ALKR--RRMPRPGVDIDE------------------------------TELGNAADDLYDSA-STGVDGG 873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 531 ELEANPPSDVyLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFE-FTGSHLTVRNGYSCVPVALAEGLDIKLNT 609
Cdd:PLN02976 874 HCEKESKEDV-LSPLERRVMNWHFAHLEYGCAALLKEVSLPYWNQDDVYGgFGGAHCMIKGGYSNVVESLAEGLDIHLNH 952
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 610 AVRQVRY-------TASGCEVIAVNTRSTSQtfiYKCDAVLCTLPLGVLKQQppAVQFVPPLPEWKTSAVQRMGFGNLNK 682
Cdd:PLN02976 953 VVTDVSYgskdagaSGSSRKKVKVSTSNGSE---FLGDAVLITVPLGCLKAE--TIKFSPPLPDWKYSSIQRLGFGVLNK 1027
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 683 VVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYK---APILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSS 759
Cdd:PLN02976 1028 VVLEFPEVFWDDSVDYFGATAEETDLRGQCFMFWNVKKtvgAPVLIALVVGKAAIDGQSMSSSDHVNHALMVLRKLFGEA 1107
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 760 AVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGpsipgapqpiprLFFAGEHTIRNYPATVHGALLSG 839
Cdd:PLN02976 1108 LVPDPVASVVTDWGRDPFSYGAYSYVAIGASGEDYDILGRPVENC------------LFFAGEATCKEHPDTVGGAMMSG 1175
|
....*....
gi 528941334 840 LREAGRIAD 848
Cdd:PLN02976 1176 LREAVRIID 1184
|
|
| Amino_oxidase |
pfam01593 |
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ... |
309-846 |
1.84e-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: 1.84e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 309 VSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGgNPMAVVSKQVNMELakiKQKCPLYEA-- 386
Cdd:pfam01593 1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVRDDGFLIELGAMWFHGAQ-PPLLALLKELGLED---RLVLPDPAPfy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 387 -----NGQAVPKEKdEMVEQEFNRLLEAtsylshqldfnvlnnkpvslgqalevviqlqekhvkdeqiehwkkivktqee 461
Cdd:pfam01593 77 tvlfaGGRRYPGDF-RRVPAGWEGLLEF---------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 462 lkellNKMVNLKEKIKELHqqykeasevkpprditaeFLVKSKHRDLTALCKeydelaetqGKLEEKLQELEANPPSDVY 541
Cdd:pfam01593 104 -----GRLLSIPEKLRLGL------------------AALASDALDEFDLDD---------FSLAESLLFLGRRGPGDVE 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 542 LSsrDRQILDWHFANLEFANAT-----PLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAE---GLDIKLNTAVRQ 613
Cdd:pfam01593 152 VW--DRLIDPELFAALPFASGAfagdpSELSAGLALPLLWALLGEGGSLLLPRGGLGALPDALAAqllGGDVRLNTRVRS 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 614 VRYTASGCEVIAVNTRStsqtfiYKCDAVLCTLPLGVLKqqppAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWD 693
Cdd:pfam01593 230 IDREGDGVTVTLTDGEV------IEADAVIVTVPLGVLK----RILFTPPLPPEKARAIRNLGYGPVNKVHLEFDRKFWP 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 694 PSvNLFGHVGSTTASRGELFLF--WNLY----KAPILLALV-AGEAAGIMENISDDVIVGRCLAILKGIFGSsAVPQPKE 766
Cdd:pfam01593 300 DL-GLLGLLSELLTGLGTAFSWltFPNRappgKGLLLLVYVgPGDRARELEGLSDEELLQAVLRDLRKLFGE-EAPEPLR 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 767 TVVSRWRADPWARGSYSYVAAGSSGNDYDlmaqpitpgpsiPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRI 846
Cdd:pfam01593 378 VLVSDWHTDPWPRGSYSLPQYGPGHDDYR------------PLARTPDPGLFFAGEHTSTGYPGTVEGAIESGRRAARAV 445
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
301-852 |
2.32e-72 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 244.83 E-value: 2.32e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKG--NYVADLGAMVVTGLGGNPMAVVsKQVNMELakik 378
Cdd:COG1231 9 DVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGddGLYAELGAMRIPPSHTNLLALA-RELGLPL---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 379 qkCPLYEANGQAVpkekdemveqefnrlleatsYlshqldfnVLNNKPVSLGQalevviqlqekhvkdeqiehwkkIVKT 458
Cdd:COG1231 84 --EPFPNENGNAL--------------------L--------YLGGKRVRAGE-----------------------IAAD 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 459 QEELKELLNKMVnlkekikelhqqykeasevkppRDITAEFlvkskhRDLTALCKEYDElaetqgkleEKLQE-LEANPp 537
Cdd:COG1231 111 LRGVAELLAKLL----------------------RALAAAL------DPWAHPAAELDR---------ESLAEwLRRNG- 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 538 sdvyLSSRDRQILDwhfANLEFANATPLSTLSLKHWDQD-DDFEFTGSHLTVRNGYSCVPVALAEGL--DIKLNTAVRQV 614
Cdd:COG1231 153 ----ASPSARRLLG---LLGAGEYGADPDELSLLDLLRYaASAGGGAQQFRIVGGMDQLPRALAAELgdRIRLGAPVTRI 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 615 RYTASGCEVIavntrsTSQTFIYKCDAVLCTLPLGVLKQqppaVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDP 694
Cdd:COG1231 226 RQDGDGVTVT------TDDGGTVRADAVIVTVPPSVLRR----IEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEE 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 695 SvnlfGHVGSTTASRGELFL-FWNLY----KAPILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAvPQPKETVV 769
Cdd:COG1231 296 D----GLYGGISLTDLPIRQtWYPSNgpdgGAGVLLGYVGGDDARALAALSPEERVAAALEQLARIFGVYA-AEPVDYVS 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 770 SRWRADPWARGSYSYVAAGSSGNDYDLMAQPItpgpsipgapqpiPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQ 849
Cdd:COG1231 371 TDWGRDPWSRGAYAAAPPGQLTAAGPALAEPD-------------GRIHFAGEHTSDEWPGWVEGALESGERAAAEILAR 437
|
...
gi 528941334 850 FLG 852
Cdd:COG1231 438 LGG 440
|
|
| PLN02268 |
PLN02268 |
probable polyamine oxidase |
302-843 |
1.52e-71 |
|
probable polyamine oxidase
Pssm-ID: 177909 [Multi-domain] Cd Length: 435 Bit Score: 242.29 E-value: 1.52e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 302 VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGG-NPMAVVSKQVNMELAKIK-- 378
Cdd:PLN02268 3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIGGRVHTDYSFGFPVDMGASWLHGVCNeNPLAPLIGRLGLPLYRTSgd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 379 ---------QKCPLYEANGQAVPKEKDEMVEQEFNRLLEATsylshqldfnvlnnkpvslgqalevviqlqeKHVKDEQI 449
Cdd:PLN02268 83 nsvlydhdlESYALFDMDGNQVPQELVTKVGETFERILEET-------------------------------EKVRDEHE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 450 EHwkkivktqeelkellnkmVNLKEKIKelhqqykeasevkpprditaefLVKSKHRDLtalckeydelaetqgkleeKL 529
Cdd:PLN02268 132 ED------------------MSLLQAIS----------------------IVLERHPEL-------------------RL 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 530 QELeanppsdvylssrDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEftGSHLTVRNGYSCVPVALAEGLDIKLNT 609
Cdd:PLN02268 153 EGL-------------AHEVLQWYLCRMEGWFAADADTISLKSWDQEELLE--GGHGLMVRGYDPVINTLAKGLDIRLNH 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 610 AVRQVRYTASGCEViavnTRSTSQTFIykCDAVLCTLPLGVLKQQppAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDR 689
Cdd:PLN02268 218 RVTKIVRRYNGVKV----TVEDGTTFV--ADAAIIAVPLGVLKAN--IIKFEPELPEWKEEAISDLGVGIENKIALHFDS 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 690 VFWdPSVNLFGHVGSTTASRGelfLFWNLYKA---PILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSavPQPKE 766
Cdd:PLN02268 290 VFW-PNVEFLGVVAPTSYGCS---YFLNLHKAtghPVLVYMPAGRLARDIEKLSDEAAANFAMSQLKKMLPDA--TEPVQ 363
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528941334 767 TVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITpgpsipgapqpipRLFFAGEHTIRNYPATVHGALLSGLREA 843
Cdd:PLN02268 364 YLVSRWGSDPNSLGCYSYDLVGKPHDLYERLRAPVD-------------NLFFAGEATSSDFPGSVHGAYSTGVMAA 427
|
|
| PLN02568 |
PLN02568 |
polyamine oxidase |
298-846 |
2.11e-41 |
|
polyamine oxidase
Pssm-ID: 215308 [Multi-domain] Cd Length: 539 Bit Score: 159.99 E-value: 2.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 298 KTGKVIIIGSGVSGLAAARQLQSFG-----MDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNm 372
Cdd:PLN02568 4 KKPRIVIIGAGMAGLTAANKLYTSSaandmFELTVVEGGDRIGGRINTSEFGGERIEMGATWIHGIGGSPVYKIAQEAG- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 373 elakikqkcplyeANGQAVPKEKdemveqefnrlleatsylshqldFNVLNNKPVSLGQALEVViqlqekhvkDEQIEHw 452
Cdd:PLN02568 83 -------------SLESDEPWEC-----------------------MDGFPDRPKTVAEGGFEV---------DPSIVE- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 453 kkivktqeELKELLNKMVNLKEKiKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALCKeydelaetQGkLEEKLQEL 532
Cdd:PLN02568 117 --------SISTLFRGLMDDAQG-KLIEPSEVDEVDFVKLAAKAARVCESGGGGSVGSFLR--------RG-LDAYWDSV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 533 EANPPSDVYLSSRDRQILDWHFA---NLE--FANATPLSTLSLkhwDQDDDF-EFTGSHLTVRNGYSCVPVALAEGLD-- 604
Cdd:PLN02568 179 SADEQIKGYGGWSRKLLEEAIFTmheNTQrtYTSADDLSTLDL---AAESEYrMFPGEEITIAKGYLSVIEALASVLPpg 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 605 -IKLNTAVRQVRYTAsgcEVIAVNTRSTSqtfIYKCDAVLCTLPLGVLKQQ--PPAVQFVPPLPEWKTSAVQRMGFGNLN 681
Cdd:PLN02568 256 tIQLGRKVTRIEWQD---EPVKLHFADGS---TMTADHVIVTVSLGVLKAGigEDSGLFSPPLPDFKTDAISRLGFGVVN 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 682 KVVLCF----DRVFWD----PSVNLFGHvGSTTASRGELFLFW-----NLY----KAPILLALVAGEAAGIMENISDDVI 744
Cdd:PLN02568 330 KLFVELsprpDGSPEDvakfPFLQMAFH-RSDSEARHDKIPWWmrrtaSICpihkNSSVLLSWFAGKEALELEKLSDEEI 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 745 V-------------------GRCLAILKGIFGSSAVPQPKETVV--SRWRADPWARGSYSYVAAGSSGNDYDLMAQPITP 803
Cdd:PLN02568 409 IrgvqttlssflkrrvaglgSQSHPLCNGGASSNDGSRWKFVKVlkSKWGTDPLFLGSYSYVAVGSSGDDLDRMAEPLPR 488
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 528941334 804 GPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRI 846
Cdd:PLN02568 489 ISDHDQAGGPPLQLLFAGEATHRTHYSTTHGAYFSGLREANRL 531
|
|
| PLN02676 |
PLN02676 |
polyamine oxidase |
297-843 |
1.01e-36 |
|
polyamine oxidase
Pssm-ID: 215362 [Multi-domain] Cd Length: 487 Bit Score: 145.24 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 297 KKTGKVIIIGSGVSGLAAARQLQSFGM-DVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGnpmavvsKQVNmela 375
Cdd:PLN02676 24 KPSPSVIIVGAGMSGISAAKTLSEAGIeDILILEATDRIGGRMRKANFAGVSVELGANWVEGVGG-------PESN---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 376 kikqkcPLYEangqavpkekdeMVEQefnrlLEATSYLShqlDF-NVLNNkpvslgqalevvIQLQEKHVKDEqiehwkk 454
Cdd:PLN02676 93 ------PIWE------------LANK-----LKLRTFYS---DFdNLSSN------------IYKQDGGLYPK------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 455 ivktqeelkellnkmvnlkekiKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALckeydelaetqgkleeKLQELEA 534
Cdd:PLN02676 128 ----------------------KVVQKSMKVADASDEFGENLSISLSAKKAVDISIL----------------TAQRLFG 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 535 NPPSdvylsSRDRQILDWHFANLEFA---------NATPLSTLSlkhwDQDDDFEFTGShltvRNGYSCVPVALAEG--- 602
Cdd:PLN02676 170 QVPK-----TPLEMVIDYYNYDYEFAepprvtslkNTEPNPTFV----DFGEDEYFVAD----PRGYESLVYYLAEQfls 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 603 ------LD--IKLNTAVRQVRYTASGcevIAVNTRSTSqtfIYKCDAVLCTLPLGVLkqQPPAVQFVPPLPEWKTSAVQR 674
Cdd:PLN02676 237 tksgkiTDprLKLNKVVREISYSKNG---VTVKTEDGS---VYRAKYVIVSVSLGVL--QSDLIKFKPPLPDWKIEAIYQ 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 675 MGFGNLNKVVLCFDRVFWdPSVN-----LFGHVgsttaSRGeLFLFW----NLYK-APILLALVAGEAAGIMENISDDVI 744
Cdd:PLN02676 309 FDMAVYTKIFLKFPYKFW-PSGPgteffLYAHE-----RRG-YYPFWqhleNEYPgSNVLFVTVTDEESRRIEQQPDSET 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 745 VGRCLAILKGIFGSSaVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITpgpsipgapqpipRLFFAGEHT 824
Cdd:PLN02676 382 KAEIMEVLRKMFGPN-IPEATDILVPRWWSNRFFKGSYSNWPIGVSRYEFDQIRAPVG-------------RVYFTGEHT 447
|
570
....*....|....*....
gi 528941334 825 IRNYPATVHGALLSGLREA 843
Cdd:PLN02676 448 SEKYNGYVHGAYLAGIDTA 466
|
|
| SWIRM |
pfam04433 |
SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid ... |
207-285 |
3.64e-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: 3.64e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528941334 207 DRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEapynSDTVLVHRVHSYLERHGLINF 285
Cdd:pfam04433 4 DKLHPIEKRLLPEFFNGKSKTPEVYLEIRNFILNLWRENPKEYLTKTDARRALK----GDVNLISRIHEFLERWGLINF 78
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
301-352 |
1.65e-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: 1.65e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 528941334 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGA 352
Cdd:COG1232 3 RVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRTVEVDGFRIDRGP 54
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
304-363 |
2.38e-14 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 68.33 E-value: 2.38e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 304 IIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPM 363
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYSYRVPGYVFDYGAHIFHGSDEPNV 60
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
301-356 |
6.62e-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: 6.62e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 528941334 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVT 356
Cdd:COG1233 5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTFERPGFRFDVGPSVLT 60
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
301-352 |
4.94e-13 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 71.06 E-value: 4.94e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 528941334 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 |
1.05e-10 |
|
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two symmetrical pairs of) sites. This is achieved by two enzymes (crtP and crtQ) in cyanobacteria (Gloeobacter being an exception) and plants, but by a single enzyme in most other bacteria and in fungi. This single enzyme is called the bacterial-type phytoene desaturase, or CrtI. Most members of this family, part of the larger pfam01593, which also contains amino oxidases, are CrtI itself; it is likely that all members act on either phytoene or on related compounds such as dehydrosqualene, for carotenoid biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 274273 [Multi-domain] Cd Length: 495 Bit Score: 64.99 E-value: 1.05e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 528941334 302 VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVT 356
Cdd:TIGR02734 1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGRAGVLEDDGFRFDTGPTVIT 55
|
|
| PRK11883 |
PRK11883 |
protoporphyrinogen oxidase; Reviewed |
301-352 |
1.44e-09 |
|
protoporphyrinogen oxidase; Reviewed
Pssm-ID: 237009 [Multi-domain] Cd Length: 451 Bit Score: 61.40 E-value: 1.44e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 528941334 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 |
2.68e-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 528941334 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 |
4.11e-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: 4.11e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 528941334 289 KRIKPLPTKKTGK-VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 336
Cdd:COG0493 110 WVKPPPPAPRTGKkVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG 158
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
301-346 |
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 528941334 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNY 346
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAASFEFGGL 46
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
291-336 |
6.26e-09 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 59.41 E-value: 6.26e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 528941334 291 IKPL-PTKKTGK-VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 336
Cdd:PRK12810 133 VKPDpPVKRTGKkVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGG 180
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
302-346 |
2.43e-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: 2.43e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 528941334 302 VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGrvaTFRKGNY 346
Cdd:COG2072 9 VVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGG---TWRDNRY 50
|
|
| PLN02576 |
PLN02576 |
protoporphyrinogen oxidase |
302-352 |
2.68e-08 |
|
protoporphyrinogen oxidase
Pssm-ID: 215314 [Multi-domain] Cd Length: 496 Bit Score: 57.33 E-value: 2.68e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 528941334 302 VIIIGSGVSGLAAARQLQS-FGMDVTLLEARDRVGGRVATFRKGNYVADLGA 352
Cdd:PLN02576 15 VAVVGAGVSGLAAAYALASkHGVNVLVTEARDRVGGNITSVSEDGFIWEEGP 66
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
275-336 |
7.13e-08 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 55.96 E-value: 7.13e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528941334 275 SYLERHG---LINFGIYKRIKPLPTKKtgKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 336
Cdd:PRK11749 115 GRLERYItdwAMETGWVLFKRAPKTGK--KVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG 177
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
301-340 |
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 528941334 301 KVIIIGSGVSGLAAARQLQSfGMDVTLLEARDRVGGRVAT 340
Cdd:COG2907 5 RIAVIGSGISGLTAAWLLSR-RHDVTLFEANDRLGGHTHT 43
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
301-342 |
5.13e-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: 5.13e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 528941334 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRvATFR 342
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSG-ASGR 41
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
368-534 |
6.76e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.84 E-value: 6.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 368 KQVNMELAKIKQKcpLYEANGQAvpKEKDEMVEQ------EFNRLLEATSYLSHQLD--FNVLNNKPVSLGQALEVVIQL 439
Cdd:COG1340 67 DELNEKVKELKEE--RDELNEKL--NELREELDElrkelaELNKAGGSIDKLRKEIErlEWRQQTEVLSPEEEKELVEKI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 440 QEKhvkDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQ------------------YKEASEVKPPRD-ITAEFL 500
Cdd:COG1340 143 KEL---EKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKikelaeeaqelheemielYKEADELRKEADeLHKEIV 219
|
170 180 190
....*....|....*....|....*....|....
gi 528941334 501 VKSKHRDltALCKEYDELAETQGKLEEKLQELEA 534
Cdd:COG1340 220 EAQEKAD--ELHEEIIELQKELRELRKELKKLRK 251
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
293-336 |
1.41e-06 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 51.80 E-value: 1.41e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 528941334 293 PLPTKKTGK-VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 336
Cdd:PRK12771 130 PAPAPDTGKrVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGG 174
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
282-343 |
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 528941334 282 LINFGIYK--RIKPLPTKK---TGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRK 343
Cdd:COG1148 118 LVRMAVAKakLLEPLEPIKvpvNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQLHK 184
|
|
| proto_IX_ox |
TIGR00562 |
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ... |
299-352 |
3.73e-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: 3.73e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 528941334 299 TGKVIIIGSGVSGLAAARQLQ----SFGMDVTLLEARDRVGGRVATFRKGNYVADLGA 352
Cdd:TIGR00562 2 KKHVVIIGGGISGLCAAYYLEkeipELPVELTLVEASDRVGGKIQTVKEDGYLIERGP 59
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
301-342 |
4.07e-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: 4.07e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 528941334 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEaRDRVGGRvATFR 342
Cdd:COG0665 4 DVVVIGGGIAGLSTAYHLARRGLDVTVLE-RGRPGSG-ASGR 43
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
289-336 |
1.57e-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: 1.57e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 528941334 289 KRIKPLP-TKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 336
Cdd:PRK12775 419 KPVKPPRfSKKLGKVAICGSGPAGLAAAADLVKYGVDVTVYEALHVVGG 467
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
290-336 |
1.82e-05 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 48.57 E-value: 1.82e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 528941334 290 RIKPLPTKKTGK-VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 336
Cdd:PRK12814 183 RYIPERAPKSGKkVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGG 230
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
431-534 |
2.26e-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: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 431 QALEVVIQLQEKHVKDEQIEHWKK-----IVKTQEELKELLNKMVNLKEKIKELHQQYKEA-SEVKpprdiTAEFLVK-- 502
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKelpaeLAELEDELAALEARLEAAKTELEDLEKEIKRLeLEIE-----EVEARIKky 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 528941334 503 -------SKHRDLTALCKEYDELAETQGKLEEKLQELEA 534
Cdd:COG1579 79 eeqlgnvRNNKEYEALQKEIESLKRRISDLEDEILELME 117
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
372-546 |
2.35e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 372 MELAKIKQKCPL----------------YEANGQAVPKEKDEMVEQE---FNRLLEATSYLSHQldfnvlnNKPVSLGQA 432
Cdd:PRK03918 429 EELKKAKGKCPVcgrelteehrkelleeYTAELKRIEKELKEIEEKErklRKELRELEKVLKKE-------SELIKLKEL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 433 LEVVIQLQEK---HVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVkpprditaEFLVKSKHRDLT 509
Cdd:PRK03918 502 AEQLKELEEKlkkYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL--------EKKLDELEEELA 573
|
170 180 190
....*....|....*....|....*....|....*...
gi 528941334 510 ALCKEYDELA-ETQGKLEEKLQELEanPPSDVYLSSRD 546
Cdd:PRK03918 574 ELLKELEELGfESVEELEERLKELE--PFYNEYLELKD 609
|
|
| PLN02487 |
PLN02487 |
zeta-carotene desaturase |
293-347 |
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 528941334 293 PLPTKKTG---KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATF--RKGNYV 347
Cdd:PLN02487 66 PEPEAYKGpklKVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGGKVGSFvdKNGNHI 125
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
441-534 |
3.11e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 441 EKHVKDEQIEHWKKIVKTQEELKELLNKMVN--------LKEKIKELHQQYKEASEVKP-PRDItaEFLVKSKHRDLTAL 511
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEELAELLKELEElgfesveeLEERLKELEPFYNEYLELKDaEKEL--EREEKELKKLEEEL 628
|
90 100
....*....|....*....|...
gi 528941334 512 CKEYDELAETQGKLEEKLQELEA 534
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEE 651
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
301-351 |
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 528941334 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG--RVATFrKGNYVaDLG 351
Cdd:PRK07208 6 SVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGisRTVTY-KGNRF-DIG 56
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
288-336 |
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 528941334 288 YKRIKPLPT-KKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 336
Cdd:PRK13984 271 YSEILDDEPeKKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGG 320
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
301-337 |
5.43e-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: 5.43e-05
10 20 30
....*....|....*....|....*....|....*..
gi 528941334 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGR 337
Cdd:COG0654 5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPD 41
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
301-340 |
7.63e-05 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 45.50 E-value: 7.63e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 528941334 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEaRDRVGGRVAT 340
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIE-GGEPGGQLAT 40
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
288-357 |
8.46e-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: 8.46e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528941334 288 YKRIKPLPTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEA-RDRVggrvatfrkgNYVADLGAMVVTG 357
Cdd:COG0569 84 RRRMERGIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVIDKdPERV----------ERLAEEDVLVIVG 144
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
300-334 |
1.00e-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: 1.00e-04
10 20 30
....*....|....*....|....*....|....*
gi 528941334 300 GKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRV 334
Cdd:pfam07992 153 KRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRL 187
|
|
| PLN02612 |
PLN02612 |
phytoene desaturase |
290-342 |
1.18e-04 |
|
phytoene desaturase
Pssm-ID: 215330 [Multi-domain] Cd Length: 567 Bit Score: 45.60 E-value: 1.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 528941334 290 RIKPLPTKKTgKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFR 342
Cdd:PLN02612 85 RSAPRPAKPL-KVVIAGAGLAGLSTAKYLADAGHKPILLEARDVLGGKVAAWK 136
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
301-334 |
1.67e-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: 1.67e-04
10 20 30
....*....|....*....|....*....|....
gi 528941334 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRV 334
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRL 34
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
291-336 |
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 528941334 291 IKPLPT--KKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 336
Cdd:PRK12831 130 IDLSETeeKKGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGG 177
|
|
| LhgO |
COG0579 |
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism]; |
302-335 |
2.60e-04 |
|
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
Pssm-ID: 440344 [Multi-domain] Cd Length: 418 Bit Score: 44.37 E-value: 2.60e-04
10 20 30
....*....|....*....|....*....|....*
gi 528941334 302 VIIIGSGVSGLAAARQL-QSFGMDVTLLEARDRVG 335
Cdd:COG0579 7 VVIIGAGIVGLALARELsRYEDLKVLVLEKEDDVA 41
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
302-336 |
3.59e-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: 3.59e-04
10 20 30
....*....|....*....|....*....|....*
gi 528941334 302 VIIIGSGVSGLAAARQLQSFGMDVTLLEaRDRVGG 336
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVE-KGRLGG 39
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
39-99 |
4.18e-04 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 44.29 E-value: 4.18e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528941334 39 AAPPAGLSGPGEAGPGAAGERTPRKKEPPRASPP----GGLAEPPGSAGPQAGPTAVPGSATPME 99
Cdd:PHA03378 714 AQRPAAATGRARPPAAAPGRARPPAAAPGRARPPaaapGRARPPAAAPGRARPPAAAPGAPTPQP 778
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
393-549 |
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 528941334 393 KEKDEMVEQEFNRLLEATSYLSHQL-----DFNVLNNKPVSLGQALEVVIQLQEKhVKDEQIEHWKKIVKTQEELKELLN 467
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIekkqqEINEKTTEISNTQTQLNQLKDEQNK-IKKQLSEKQKELEQNNKKIKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 468 KMVNLKEKIKELHQQyKEA---SEVKpprditaEFLvKSKHRDLTALCKEYD-------ELAETQGKLEEKLQELEANPp 537
Cdd:TIGR04523 289 QLNQLKSEISDLNNQ-KEQdwnKELK-------SEL-KNQEKKLEEIQNQISqnnkiisQLNEQISQLKKELTNSESEN- 358
|
170
....*....|..
gi 528941334 538 sdvylSSRDRQI 549
Cdd:TIGR04523 359 -----SEKQREL 365
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
437-549 |
4.54e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 437 IQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKppRDITAEFLVKSK-----HRDLTAL 511
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL--AQAQEELESLQEeaeelQEELEEL 120
|
90 100 110
....*....|....*....|....*....|....*...
gi 528941334 512 CKEYDELAETQGKLEEKLQELEANppsdvyLSSRDRQI 549
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSE------IAEREEEL 152
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
301-337 |
8.49e-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: 8.49e-04
10 20 30
....*....|....*....|....*....|....*...
gi 528941334 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEA-RDRVGGR 337
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDeGTCPYGG 39
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
297-338 |
1.32e-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: 1.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 528941334 297 KKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRV 338
Cdd:COG1251 140 APGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQ 181
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
301-357 |
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 528941334 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKgnyvadLGAMVVTG 357
Cdd:COG0771 6 KVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPAPELAAAELEA------PGVEVVLG 56
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
297-336 |
1.59e-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: 1.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 528941334 297 KKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 336
Cdd:PRK12778 429 KNGKKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGG 468
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
295-340 |
2.15e-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: 2.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 528941334 295 PTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLL--------EARDRVGGRVAT 340
Cdd:smart01002 16 GGVPPAKVVVIGAGVVGLGAAATAKGLGAEVTVLdvrparlrQLESLLGARFTT 69
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
439-534 |
2.21e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 439 LQEKHVKDEQIEhwKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPprditaeflVKSKHRDLTALCKEY--- 515
Cdd:PRK03918 240 IEELEKELESLE--GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKE---------KAEEYIKLSEFYEEYlde 308
|
90 100
....*....|....*....|
gi 528941334 516 -DELAETQGKLEEKLQELEA 534
Cdd:PRK03918 309 lREIEKRLSRLEEEINGIEE 328
|
|
| MRPL52 |
pfam18699 |
Mitoribosomal protein mL52; Members of this family include the mamalian mitoribosomal proteins ... |
418-491 |
2.29e-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: 2.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528941334 418 DFNVLNNKPVSLGQalevviqLQEKHvKDEQIEHWKKIVKTQEELKELLnKMVNLKEKIKELHQQYKEASEVKP 491
Cdd:pfam18699 25 DFSFADGRPAPVTS-------GQLKR-KLKQIELAKKIVKLSSEVDEAE-ERYKRKQEEEEEEIQKIIDNKLKP 89
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
393-535 |
2.30e-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: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 393 KEKDEMVEQEFNRLLEATSYLSHQLDF--NVLNNKPVSLGQALEVVIQLQ-EKHVKDEQIEHWKKIVKTQEELKELLNK- 468
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDElrAELTLLNEEAANLRERLESLErRIAATERRLEDLEEQIEELSEDIESLAAe 860
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528941334 469 MVNLKEKIKELHQQYKEASEVKpprditaeflvKSKHRDLTALCKEYDELAETQGKLEEKLQELEAN 535
Cdd:TIGR02168 861 IEELEELIEELESELEALLNER-----------ASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
393-533 |
2.40e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 393 KEKDEMVEQEFNRLLEATSYLSHQLDFNVLNN-KPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLN---- 467
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDlSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAeagv 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 468 --------------KMVNLKEKIKELHQQYKE-ASEVKPPRDITAEFLVKSKHRDLT----ALCKEYDELAETQGKLEEK 528
Cdd:COG4717 382 edeeelraaleqaeEYQELKEELEELEEQLEElLGELEELLEALDEEELEEELEELEeeleELEEELEELREELAELEAE 461
|
....*
gi 528941334 529 LQELE 533
Cdd:COG4717 462 LEQLE 466
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
368-533 |
2.49e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 368 KQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEfNRLLEATSYLSH-QLDFNVLNNKPVSLGQALEVVIQLQ--EKHV 444
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKE-ERLEELKKKLKElEKRLEELEERHELYEEAKAKKEELErlKKRL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 445 KDEQIEHWKKIVKT--------QEELKELLNKMVNLKEKIKELHQ---QYKEASEVKP--PRDITAEF---LVKSKHRDL 508
Cdd:PRK03918 382 TGLTPEKLEKELEElekakeeiEEEISKITARIGELKKEIKELKKaieELKKAKGKCPvcGRELTEEHrkeLLEEYTAEL 461
|
170 180
....*....|....*....|....*
gi 528941334 509 TALCKEYDELAETQGKLEEKLQELE 533
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELE 486
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
302-360 |
3.19e-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: 3.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528941334 302 VIIIGSGVSG----LAAARQlqsfGMDVTLLEARDRVGGR-----VATFRkGNYVADlgAMVVTGLGG 360
Cdd:pfam12831 2 VVVVGGGPAGvaaaIAAARA----GAKVLLVERRGFLGGMltsglVGPDM-GFYLNK--EQVVGGIAR 62
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
400-534 |
3.75e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 400 EQEFNRLLEATSYLSHQLDfnvlnnkpvSLGQALEVVIQLQEKHVKDEQI-EHWKKIVKTQEELKELLNKMVNLKEKIKE 478
Cdd:COG4717 87 EEEYAELQEELEELEEELE---------ELEAELEELREELEKLEKLLQLlPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528941334 479 LHQQY-------KEASEVKppRDITAEFLVKS--KHRDLTALCKEYDELAETQGKLEEKLQELEA 534
Cdd:COG4717 158 LRELEeeleeleAELAELQ--EELEELLEQLSlaTEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
|
| Ald |
COG0686 |
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ... |
300-340 |
3.78e-03 |
|
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and metabolism]; Alanine dehydrogenase (includes sporulation protein SpoVN) is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440450 [Multi-domain] Cd Length: 372 Bit Score: 40.38 E-value: 3.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 528941334 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 |
3.79e-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: 3.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 528941334 300 GKVIIIGSGVSGLAAARQLQSFGMDVTLL--------EARDRVGGRVAT 340
Cdd:cd05305 169 AKVVILGAGVVGENAARVALGLGAEVTVLdinlerlrYLDDIFGGRVTT 217
|
|
| PRK06847 |
PRK06847 |
hypothetical protein; Provisional |
301-336 |
3.84e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235874 [Multi-domain] Cd Length: 375 Bit Score: 40.63 E-value: 3.84e-03
10 20 30
....*....|....*....|....*....|....*...
gi 528941334 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARD--RVGG 336
Cdd:PRK06847 6 KVLIVGGGIGGLSAAIALRRAGIAVDLVEIDPewRVYG 43
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
287-340 |
3.96e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 40.88 E-value: 3.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 528941334 287 IYKRIKPLPTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVAT 340
Cdd:PRK12843 4 VVSELSPERWDAEFDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGTTAT 57
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
437-533 |
4.00e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 437 IQLQEKHVKDEQIEhwkkIVKTQEELKELLNKMVNLKEKIKELHQQYKEasevKPPRDITAEFLVKSKH-----RDLTAL 511
Cdd:PRK03918 614 LEREEKELKKLEEE----LDKAFEELAETEKRLEELRKELEELEKKYSE----EEYEELREEYLELSRElaglrAELEEL 685
|
90 100
....*....|....*....|..
gi 528941334 512 CKEYDELAETQGKLEEKLQELE 533
Cdd:PRK03918 686 EKRREEIKKTLEKLKEELEERE 707
|
|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
301-461 |
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 528941334 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEardrvggrvatfrKGNYVADLGAMVvtGLGGNpmaVVSKQVNMELAK-IKQ 379
Cdd:PRK06753 2 KIAIIGAGIGGLTAAALLQEQGHEVKVFE-------------KNESVKEVGAGI--GIGDN---VIKKLGNHDLAKgIKN 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 380 kcplyeaNGQAVPkekdemveqEFNRLLEATSYLSH-QLDFNVLNnkpVSLGQalEVVIQLQEKHVKDEQIEHWKKIVKT 458
Cdd:PRK06753 64 -------AGQILS---------TMNLLDDKGTLLNKvKLKSNTLN---VTLHR--QTLIDIIKSYVKEDAIFTGKEVTKI 122
|
...
gi 528941334 459 QEE 461
Cdd:PRK06753 123 ENE 125
|
|
| AlaDh_PNT_C |
pfam01262 |
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
295-334 |
5.07e-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: 5.07e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 528941334 295 PTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRV 334
Cdd:pfam01262 24 PGVAPAKVLVIGGGVAGLNAAATAKGLGAIVTILDVRPAR 63
|
|
| mnmC |
PRK01747 |
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ... |
301-335 |
5.70e-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: 5.70e-03
10 20 30
....*....|....*....|....*....|....*
gi 528941334 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVG 335
Cdd:PRK01747 262 DAAIIGGGIAGAALALALARRGWQVTLYEADEAPA 296
|
|
| PTZ00306 |
PTZ00306 |
NADH-dependent fumarate reductase; Provisional |
289-339 |
6.59e-03 |
|
NADH-dependent fumarate reductase; Provisional
Pssm-ID: 140327 [Multi-domain] Cd Length: 1167 Bit Score: 40.15 E-value: 6.59e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 528941334 289 KRIK-PLPTKktgkVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVA 339
Cdd:PTZ00306 402 KRIAgSLPAR----VIVVGGGLAGCSAAIEAASCGAQVILLEKEAKLGGNSA 449
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
290-336 |
7.59e-03 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 39.78 E-value: 7.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 528941334 290 RIKPLPtkktGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 336
Cdd:PRK06292 164 ELDKLP----KSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILP 206
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
35-117 |
8.37e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 39.97 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 35 GSEVAAPPAGLSGPGEAGPGAAGERTPRKKEPPRASPPGGLAEPPGSAGPQAGPtAVPGSATPMETGIAETPEGRRTSRR 114
Cdd:PRK07764 617 APAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWP-AKAGGAAPAAPPPAPAPAAPAAPAG 695
|
...
gi 528941334 115 KRA 117
Cdd:PRK07764 696 AAP 698
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
302-336 |
8.39e-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: 8.39e-03
10 20 30
....*....|....*....|....*....|....*
gi 528941334 302 VIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGG 336
Cdd:COG1053 6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
|
|
| murD |
PRK14106 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional |
301-379 |
8.45e-03 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
Pssm-ID: 184511 [Multi-domain] Cd Length: 450 Bit Score: 39.57 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 301 KVIIIGSGVSGLAAARQLQSFGMDVTLLE--ARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIK 378
Cdd:PRK14106 7 KVLVVGAGVSGLALAKFLKKLGAKVILTDekEEDQLKEALEELGELGIELVLGEYPEEFLEGVDLVVVSPGVPLDSPPVV 86
|
.
gi 528941334 379 Q 379
Cdd:PRK14106 87 Q 87
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
369-534 |
9.56e-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: 39.65 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 369 QVNMELAKIKQKCPLYEANGQAVPKE----KDEMVEQEfNRLLEATS-YLSHQLDFNVLNNKPVSLGQALEVVIQLQEKh 443
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKleelRLEVSELE-EEIEELQKeLYALANEISRLEQQKQILRERLANLERQLEE- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528941334 444 vKDEQIEHWK-KIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPprdiTAEFLVKSKHRDLTALCKEYDELAETQ 522
Cdd:TIGR02168 321 -LEAQLEELEsKLDELAEELAELEEKLEELKEELESLEAELEELEAELE----ELESRLEELEEQLETLRSKVAQLELQI 395
|
170
....*....|..
gi 528941334 523 GKLEEKLQELEA 534
Cdd:TIGR02168 396 ASLNNEIERLEA 407
|
|
| |
