|
Name |
Accession |
Description |
Interval |
E-value |
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
1-1068 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 2162.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 1 MPKRTDIQSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPVDWQTVAQIIEK 80
Cdd:PRK05294 1 MPKRTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 81 ERPDAVLPTMGGQTALNCALDLSREGVLEKFGVEMIGANEAAIDMAEDRDHFKAAMADIGLDTPTAMLAHSWEEAQEIQP 160
Cdd:PRK05294 81 ERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 161 KIGFPVIIRPSFTLGGSGGGIAYNREEFEYIVKNGIDLSPVNQVLLEESALGWKEFEMEVVRDKADNCIIICSIENLDPM 240
Cdd:PRK05294 161 EIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 241 GIHTGDSITVAPAQTLTDKEYQIMRDASLAVLRKIGVETGGSNVQFAINPENGRMIVIEMNPRVSRSSALASKATGFPIA 320
Cdd:PRK05294 241 GVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVETGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 321 KVAAKLAVGYTLDELKNDITGGlTPASFEPSIDYVVTKIPRFTFEKFPQADARLTTQMKAVGEAMAIGRTFQESFQKALR 400
Cdd:PRK05294 321 KVAAKLAVGYTLDEIKNDITGK-TPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 401 SMETGMDGLDERIDLTADDvtDQLRTKLANPSPEQVLYVADAFRAGFSIQDIFDLTAIDPWFLAQIQELVDVEKGVKDRI 480
Cdd:PRK05294 400 SLEIGVTGLDEDLFEEESL--EELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 481 LgEISAEEMYRLKQRGFSDLRLAKLVNDTEKAVRKHRHGLGVRPVYKRVDTCAAEFATTTAYMYSSYEEENEADPTDKQK 560
Cdd:PRK05294 478 L-PLDAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKK 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 561 IMVLGGGPNRIGQGIEFDYCCVHAALAMREDGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEVVATEKPAGVIVQ 640
Cdd:PRK05294 557 VLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQ 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 641 YGGQTPLKLARDLEAAGVPIIGTSPDSIDLAEDRERFQALLNKLGLKQPPNRTARSEEEAEKLAEEIGYPLVVRPSYVLG 720
Cdd:PRK05294 637 FGGQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLG 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 721 GRAMEIVRDREDLRSYMKNAVSVSNDAPVLLDRFLDDAIEVDVDAISDGENVIIGGIMEHIEQAGVHSGDSACSLPPFSL 800
Cdd:PRK05294 717 GRAMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICDGEDVLIGGIMEHIEEAGVHSGDSACSLPPQTL 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 801 SMELQDEMVEQVRKMALGLKVVGLMNTQFAIKGDDIYVLEVNPRASRTVPYVSKSVGRPLAKIAARCMVGQTLPEQGVGD 880
Cdd:PRK05294 797 SEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTK 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 881 AVYPDYYSVKESVFPFAKFQGVDPILGPEMKSTGEVMGVGRSFAEAFAKSQLGAGVLLPSTGKAFVSVREIDKPHVAEVA 960
Cdd:PRK05294 877 GLIPPYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSGTVFLSVRDRDKEEVVELA 956
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 961 RRLVELGFEVLATRGTANVLEEAGIQVTRVNKVTEGRPHIVDMIKNDEISFIINTVEGKQSTSDSYTIRREALMHKVGYT 1040
Cdd:PRK05294 957 KRLLELGFKILATSGTAKFLREAGIPVELVNKVHEGRPHIVDLIKNGEIDLVINTPTGRQAIRDGFSIRRAALEYKVPYI 1036
|
1050 1060 1070
....*....|....*....|....*....|
gi 516883186 1041 TTIAGAKATVQALDHL--GANDVFRLQDLH 1068
Cdd:PRK05294 1037 TTLAGARAAVKAIEALkfGELEVRSLQEYH 1066
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
2-1053 |
0e+00 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 1684.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 2 PKRTDIQSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPVDWQTVAQIIEKE 81
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 82 RPDAVLPTMGGQTALNCALDLSREGVLEKFGVEMIGANEAAIDMAEDRDHFKAAMADIGLDTPTAMLAHSWEEAQEIQPK 161
Cdd:TIGR01369 81 RPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 162 IGFPVIIRPSFTLGGSGGGIAYNREEFEYIVKNGIDLSPVNQVLLEESALGWKEFEMEVVRDKADNCIIICSIENLDPMG 241
Cdd:TIGR01369 161 IGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 242 IHTGDSITVAPAQTLTDKEYQIMRDASLAVLRKIGVEtGGSNVQFAINPENGRMIVIEMNPRVSRSSALASKATGFPIAK 321
Cdd:TIGR01369 241 VHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIE-GGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 322 VAAKLAVGYTLDELKNDITGGlTPASFEPSIDYVVTKIPRFTFEKFPQADARLTTQMKAVGEAMAIGRTFQESFQKALRS 401
Cdd:TIGR01369 320 VAAKLAVGYTLDELKNPVTGT-TPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 402 METGMDGLDERIDLTADDvtDQLRTKLANPSPEQVLYVADAFRAGFSIQDIFDLTAIDPWFLAQIQELVDVEKGVKDRIL 481
Cdd:TIGR01369 399 LEIGATGFDLPDREVEPD--EDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 482 GEISAEEMYRLKQRGFSDLRLAKLVNDTEKAVRKHRHGLGVRPVYKRVDTCAAEFATTTAYMYSSYEEE-NEADPTDKQK 560
Cdd:TIGR01369 477 TDLDPELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGErDDVPFTDKKK 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 561 IMVLGGGPNRIGQGIEFDYCCVHAALAMREDGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEVVATEKPAGVIVQ 640
Cdd:TIGR01369 557 VLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQ 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 641 YGGQTPLKLARDLEAAGVPIIGTSPDSIDLAEDRERFQALLNKLGLKQPPNRTARSEEEAEKLAEEIGYPLVVRPSYVLG 720
Cdd:TIGR01369 637 FGGQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLG 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 721 GRAMEIVRDREDLRSYMKNAVSVSNDAPVLLDRFLDDAIEVDVDAISDGENVIIGGIMEHIEQAGVHSGDSACSLPPFSL 800
Cdd:TIGR01369 717 GRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTL 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 801 SMELQDEMVEQVRKMALGLKVVGLMNTQFAIKGDDIYVLEVNPRASRTVPYVSKSVGRPLAKIAARCMVGQTLPEQGVGD 880
Cdd:TIGR01369 797 SAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGVGK 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 881 AVYPDYYSVKESVFPFAKFQGVDPILGPEMKSTGEVMGVGRSFAEAFAKSQLGAGVLLPSTGKAFVSVREIDKPHVAEVA 960
Cdd:TIGR01369 877 EKEPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLA 956
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 961 RRLVELGFEVLATRGTANVLEEAGIQVTRVNKVTEGRPHIVDMIKNDEISFIINTVE-GKQSTSDSYTIRREALMHKVGY 1039
Cdd:TIGR01369 957 RKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEGRPNILDLIKNGEIELVINTTSkGAGTATDGYKIRREALDYGVPL 1036
|
1050
....*....|....
gi 516883186 1040 TTTIAGAKATVQAL 1053
Cdd:TIGR01369 1037 ITTLNTAEAFAEAL 1050
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
3-1066 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 1562.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 3 KRTDIQSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPVDWQTVAQIIEKER 82
Cdd:PLN02735 19 KRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 83 PDAVLPTMGGQTALNCALDLSREGVLEKFGVEMIGANEAAIDMAEDRDHFKAAMADIGLDTPTAMLAHSWEEAQEIQPKI 162
Cdd:PLN02735 99 PDALLPTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 163 G-FPVIIRPSFTLGGSGGGIAYNREEFEYIVKNGIDLSPVNQVLLEESALGWKEFEMEVVRDKADNCIIICSIENLDPMG 241
Cdd:PLN02735 179 GeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 242 IHTGDSITVAPAQTLTDKEYQIMRDASLAVLRKIGVETGGSNVQFAINPENGRMIVIEMNPRVSRSSALASKATGFPIAK 321
Cdd:PLN02735 259 VHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVECGGSNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 322 VAAKLAVGYTLDELKNDITGGlTPASFEPSIDYVVTKIPRFTFEKFPQADARLTTQMKAVGEAMAIGRTFQESFQKALRS 401
Cdd:PLN02735 339 MAAKLSVGYTLDQIPNDITLK-TPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRS 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 402 METGMDGLDERIDLTADDVTDQLRTKLANPSPEQVLYVADAFRAGFSIQDIFDLTAIDPWFLAQIQELVDVEKGVKDRIL 481
Cdd:PLN02735 418 LETGFSGWGCAKVKELDWDWEQLKYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSL 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 482 GEISAEEMYRLKQRGFSDLRLAKLVNDTEKAVRKHRHGLGVRPVYKRVDTCAAEFATTTAYMYSSYEEENEADPTDKQKI 561
Cdd:PLN02735 498 SELSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPTNKKKV 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 562 MVLGGGPNRIGQGIEFDYCCVHAALAMREDGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEVVATEKPAGVIVQY 641
Cdd:PLN02735 578 LILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQF 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 642 GGQTPLKLARDLE----------AAG---VPIIGTSPDSIDLAEDRERFQALLNKLGLKQPPNRTARSEEEAEKLAEEIG 708
Cdd:PLN02735 658 GGQTPLKLALPIQkyldknpppsASGngnVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKRIG 737
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 709 YPLVVRPSYVLGGRAMEIVRDREDLRSYMKNAVSVSNDAPVLLDRFLDDAIEVDVDAISDGE-NVIIGGIMEHIEQAGVH 787
Cdd:PLN02735 738 YPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALADSEgNVVIGGIMEHIEQAGVH 817
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 788 SGDSACSLPPFSLSMELQDEMVEQVRKMALGLKVVGLMNTQFAI-KGDDIYVLEVNPRASRTVPYVSKSVGRPLAKIAAR 866
Cdd:PLN02735 818 SGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAItPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASL 897
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 867 CMVGQTLPEQGVGDAVYPDYYSVKESVFPFAKFQGVDPILGPEMKSTGEVMGVGRSFAEAFAKSQLGAGVLLPSTGKAFV 946
Cdd:PLN02735 898 VMSGKSLKDLGFTEEVIPAHVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLPLSGTVFI 977
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 947 SVREIDKPHVAEVARRLVELGFEVLATRGTANVLEEAGIQVTRVNKVTEGRPHIVDMIKNDEISFIINTVEG-KQSTSDS 1025
Cdd:PLN02735 978 SLNDLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVLKLHEGRPHAGDMLANGQIQLMVITSSGdALDQKDG 1057
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|...
gi 516883186 1026 YTIRREALMHKVGYTTTIAGAKATVQALDHLGANDV--FRLQD 1066
Cdd:PLN02735 1058 RQLRRMALAYKVPIITTVAGALATAQAVKSLKECPIemIALQD 1100
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
1-1069 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1534.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 1 MPKRTDIQSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPVDWQTVAQIIEK 80
Cdd:PRK12815 1 MPKDTDIQKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 81 ERPDAVLPTMGGQTALNCALDLSREGVLEKFGVEMIGANEAAIDMAEDRDHFKAAMADIGLDTPTAMLAHSWEEAQEIQP 160
Cdd:PRK12815 81 EKPDALLATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 161 KIGFPVIIRPSFTLGGSGGGIAYNREEFEYIVKNGIDLSPVNQVLLEESALGWKEFEMEVVRDKADNCIIICSIENLDPM 240
Cdd:PRK12815 161 KIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 241 GIHTGDSITVAPAQTLTDKEYQIMRDASLAVLRKIGVeTGGSNVQFAINPENGRMIVIEMNPRVSRSSALASKATGFPIA 320
Cdd:PRK12815 241 GIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGV-VGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 321 KVAAKLAVGYTLDELKNDITgGLTPASFEPSIDYVVTKIPRFTFEKFPQADARLTTQMKAVGEAMAIGRTFQESFQKALR 400
Cdd:PRK12815 320 KIAAKLAVGYTLNELKNPVT-GLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 401 SMETGMDGLDERIDLTADDvTDQLRTKLANPSPEQVLYVADAFRAGFSIQDIFDLTAIDPWFLAQIQELVDVEKGVKDRI 480
Cdd:PRK12815 399 SLEIKRNGLSLPIELSGKS-DEELLQDLRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEDG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 481 LgEISAEEMYRLKQRGFSDLRLAKLVNDTEKAVRKHRHGLGVRPVYKRVDTCAAEFATTTAYMYSSYEEENEADPT-DKQ 559
Cdd:PRK12815 478 L-DLSADLLRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGESEAEPSsEKK 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 560 KIMVLGGGPNRIGQGIEFDYCCVHAALAMREDGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEVVATEKPAGVIV 639
Cdd:PRK12815 557 KVLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIV 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 640 QYGGQTPLKLARDLEAAGVPIIGTSPDSIDLAEDRERFQALLNKLGLKQPPNRTARSEEEAEKLAEEIGYPLVVRPSYVL 719
Cdd:PRK12815 637 QFGGQTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVI 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 720 GGRAMEIVRDREDLRSYMKNAvsVSNDAPVLLDRFLdDAIEVDVDAISDGENVIIGGIMEHIEQAGVHSGDSACSLPPFS 799
Cdd:PRK12815 717 GGQGMAVVYDEPALEAYLAEN--ASQLYPILIDQFI-DGKEYEVDAISDGEDVTIPGIIEHIEQAGVHSGDSIAVLPPQS 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 800 LSMELQDEMVEQVRKMALGLKVVGLMNTQFAIKGDDIYVLEVNPRASRTVPYVSKSVGRPLAKIAARCMVGQTLPEQGVG 879
Cdd:PRK12815 794 LSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLAELGYP 873
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 880 DAVYP--DYYSVKESVFPFAKFQGVDPILGPEMKSTGEVMGVGRSFAEAFAKSQLGAGVLLPSTGKAFVSVREIDKPHVA 957
Cdd:PRK12815 874 NGLWPgsPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGTIFISVRDEDKPEVT 953
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 958 EVARRLVELGFEVLATRGTANVLEEAGIQVTRVNKVTEGRPHIVDMIKNDEISFIINTVEGKQSTSDSYTIRREALMHKV 1037
Cdd:PRK12815 954 KLARRFAQLGFKLLATEGTANWLAEEGITTGVVEKVQEGSPSLLERIKQHRIVLVVNTSLSDSASEDAIKIRDEALSTHI 1033
|
1050 1060 1070
....*....|....*....|....*....|..
gi 516883186 1038 GYTTTIAGAKATVQALDHLgANDVFRLQDLHQ 1069
Cdd:PRK12815 1034 PVFTELETAQAFLQVLESL-ALTTQPIQELQE 1064
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
564-1052 |
0e+00 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 772.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 564 LGGGPNRIGQGIEFDYCCVHAALAMREDGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEVVATEKPAGVIVQYGG 643
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 644 QTPLKLARDLEAA----GVPIIGTSPDSIDLAEDRERFQALLNKLGLKQPPNRTARSEEEAEKLAEEIGYPLVVRPSYVL 719
Cdd:COG0458 81 QTALNLAVELEEAgileGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 720 GGRAMEIVRDREDLRSYMKNAVSVSNDAPVLLDRFLDDAIEVDVDAISDGE-NVIIGGIMEHIEQAGVHSGDSACSLPPF 798
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEdNVIIVGIMEHIEPAGVHSGDSICVAPPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 799 SLSMELQDEMVEQVRKMALGLKVVGLMNTQFAIKGDDIYVLEVNPRASRTVPYVSKSVGRPLAKIAARCMVGQTLPEQGV 878
Cdd:COG0458 241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 879 GDAVYP--DYYSVKESVFPFAKFQGVDPILGPEMKSTGEVMGVGRSFAEAFAKSQLGAGVLLPstGKAFVS-VREIDKPH 955
Cdd:COG0458 321 DTGFEPtlDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLP--GTVLLSlVADDDKEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 956 VAEVARRLVELGFEVLATRGTANVLEEAGIQVTRVNKVTEGRPHIVDMIKNDEISFIINTVEGKQSTSDSYTIRREALMH 1035
Cdd:COG0458 399 ALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVINTLLGAKSLGDSDGIIRRALAA 478
|
490
....*....|....*..
gi 516883186 1036 KVGYTTTIAGAKATVQA 1052
Cdd:COG0458 479 KVPYVTTLAAAAAAALA 495
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
13-566 |
0e+00 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 754.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 13 LGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPVDWQTVAQIIEKERPDAVLPTMGG 92
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 93 QTALNCALDLSREGVLEkfGVEMIGANEAAIDMAEDRDHFKAAMADIGLDTPTAMLAHSWEEAQEIQPKIGFPVIIRPSF 172
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 173 TLGGSGGGIAYNREEFEYIVKNGIDLSPVNQVLLEESALGWKEFEMEVVRDKADNCIIICSIENLDPMGIHTGDSITVAP 252
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 253 AQTLTDKEYQIMRDASLAVLRKIGVEtGGSNVQFAINpeNGRMIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTL 332
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVV-GLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 333 DELKNDiTGgltpasFEPSIDYVVTKIPRFTFEKFPQADARLTTQMKAVGEAMAIGRTFQESFQKALRSMETGMDGldeR 412
Cdd:COG0458 316 DELGND-TG------FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPG---T 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 413 IDLTADDVTDQLRTKLANPSPEQVLYVADAFRAGFSIQDIFDLTAIDPWFLAQIQELVDVEKGVKDRILGEISAEEmyrL 492
Cdd:COG0458 386 VLLSLVADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVINTLLG---A 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516883186 493 KQRGFSDLRLAKLVNDTEKAVRKHRHGLGVRPVYKRVDTCAAEFATTTAYMYSSYEEENEADPTDKQKIMVLGG 566
Cdd:COG0458 463 KSLGDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
128-333 |
1.43e-81 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 264.17 E-value: 1.43e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 128 DRDHFKAAMADIGLDTP--TAMLAHSWEEAQEIQPKIGFPVIIRPSFTLGGSGGGIAYNREEFEYIVKNGIDLSPV---- 201
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVpgTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 202 NQVLLEESALGWKEFEMEVVRDKADNCIIICSIENLDPMgiHTGDSITVAPAQTLTDKEYQIMRDASLAVLRKIGVETGG 281
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 516883186 282 sNVQFAINPENGRMIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLD 333
Cdd:pfam02786 159 -TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
424-547 |
6.81e-61 |
|
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 198164 [Multi-domain] Cd Length: 124 Bit Score: 203.45 E-value: 6.81e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 424 LRTKLANPSPEQVLYVADAFRAGFSIQDIFDLTAIDPWFLAQIQELVDVEKGVKDRILGEISAEEMYRLKQRGFSDLRLA 503
Cdd:smart01096 1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 516883186 504 KLVNDTEKAVRKHRHGLGVRPVYKRVDTCAAEFATTTAYMYSSY 547
Cdd:smart01096 81 KLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
942-1051 |
6.24e-54 |
|
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate synthetase (CSP). CSP, a CarA and CarB heterodimer, catalyzes the production of carbamoyl phosphate which is subsequently employed in the metabolic pathways responsible for the synthesis of pyrimidine nucleotides or arginine. The MGS-like domain is the C-terminal domain of CarB and appears to play a regulatory role in CPS function by binding allosteric effector molecules, including UMP and ornithine.
Pssm-ID: 238712 [Multi-domain] Cd Length: 110 Bit Score: 183.06 E-value: 6.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 942 GKAFVSVREIDKPHVAEVARRLVELGFEVLATRGTANVLEEAGIQVTRVNKVTEGRPHIVDMIKNDEISFIINTVEGKQS 1021
Cdd:cd01424 1 GTVFISVADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEGRPNIVDLIKNGEIQLVINTPSGKRA 80
|
90 100 110
....*....|....*....|....*....|
gi 516883186 1022 TSDSYTIRREALMHKVGYTTTIAGAKATVQ 1051
Cdd:cd01424 81 IRDGFSIRRAALEYKVPYFTTLDTARAAVE 110
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
673-874 |
5.17e-31 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 121.26 E-value: 5.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 673 DRERFQALLNKLGLKQPPN--RTARSEEEAEKLAEEIGYPLVVRPSYVLGGRAMEIVRDREDLRSYMKNAVSVSNDAP-- 748
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGtaGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 749 --VLLDRFLDDAIEVDVDAISDGE-NVIIGGIMEHIEQagVHSGDSACSLPPFSLSMELQDEMVEQVRKMALGLKVVGLM 825
Cdd:pfam02786 81 pqVLVEKSLKGPKHIEYQVLRDAHgNCITVCNRECSDQ--RRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 516883186 826 NTQFAI--KGDDIYVLEVNPRASRTVPYVSKSVGRPLAKIAARCMVGQTLP 874
Cdd:pfam02786 159 TVEFALdpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
955-1041 |
7.01e-30 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 214855 [Multi-domain] Cd Length: 91 Bit Score: 113.72 E-value: 7.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 955 HVAEVARRLVELGFEVLATRGTANVLEEAGIQV--TRVNKVTEGRPHIVDMIKNDEISFIINTVEG--KQSTSDSYTIRR 1030
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPVvkTLHPKVHGGIPQILDLIKNGEIDLVINTLYPfeAQAHEDGYSIRR 80
|
90
....*....|.
gi 516883186 1031 EALMHKVGYTT 1041
Cdd:smart00851 81 AAENIDIPGPT 91
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
427-505 |
8.72e-30 |
|
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 460695 Cd Length: 79 Bit Score: 112.85 E-value: 8.72e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516883186 427 KLANPSPEQVLYVADAFRAGFSIQDIFDLTAIDPWFLAQIQELVDVEKGVKDRILgEISAEEMYRLKQRGFSDLRLAKL 505
Cdd:pfam02787 2 ELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAGL-DLDAELLREAKRLGFSDRQIAKL 79
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
956-1041 |
7.59e-27 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 460462 [Multi-domain] Cd Length: 93 Bit Score: 105.26 E-value: 7.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 956 VAEVARRLVELGFEVLATRGTANVLEEAGIQVTRV-NKVTEGRPH----IVDMIKNDEISFIINTVEGKQST-SDSYTIR 1029
Cdd:pfam02142 2 LVELAKALVELGFELLATGGTAKFLREAGIPVTEVvEKTGEGRPGgrvqIGDLIKNGEIDLVINTLYPFKATvHDGYAIR 81
|
90
....*....|..
gi 516883186 1030 REALMHKVGYTT 1041
Cdd:pfam02142 82 RAAENIDIPGPT 93
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
74-329 |
1.44e-26 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 109.96 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 74 VAQIIEKERPDAVLptmggqtALNCALDLSREGVLEKFGVEmiGANEAAIDMAEDRDHFKAAMADIGLDTPTAMLAHSWE 153
Cdd:COG0439 9 AAELARETGIDAVL-------SESEFAVETAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 154 EAQEIQPKIGFPVIIRPSFTLGGSGGGIAYNREE----FEYIVKNGIDLSPVNQVLLEESALGwKEFEME-VVRDKAdnc 228
Cdd:COG0439 80 EALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEEleaaLAEARAEAKAGSPNGEVLVEEFLEG-REYSVEgLVRDGE--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 229 IIICSI---ENLDPMGIHTGDsitVAPAQtLTDKEYQIMRDASLAVLRKIGVETGGSNVQFAINPeNGRMIVIEMNPRVS 305
Cdd:COG0439 156 VVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELVARALRALGYRRGAFHTEFLLTP-DGEPYLIEINARLG 230
|
250 260
....*....|....*....|....*.
gi 516883186 306 --RSSALASKATGFPIAKVAAKLAVG 329
Cdd:COG0439 231 geHIPPLTELATGVDLVREQIRLALG 256
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
654-871 |
2.14e-20 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 92.24 E-value: 2.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 654 EAAGVPiiGTSPDSIDLAEDRERFQALLNKLGLKQPPNRTARSEEEAEKLAEEIGYPLVVRPSYVLGGRAMEIVRDREDL 733
Cdd:COG0439 37 EELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 734 RSYMKNAVS----VSNDAPVLLDRFLdDAIEVDVDAISDGENVIIGGIMEHIEQA--GVHSGDSAcslpPFSLSMELQDE 807
Cdd:COG0439 115 EAALAEARAeakaGSPNGEVLVEEFL-EGREYSVEGLVRDGEVVVCSITRKHQKPpyFVELGHEA----PSPLPEELRAE 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516883186 808 MVEQVRKM--ALGLKvVGLMNTQFAI-KGDDIYVLEVNPRAS--RTVPYVSKSVGRPLAKIAARCMVGQ 871
Cdd:COG0439 190 IGELVARAlrALGYR-RGAFHTEFLLtPDGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGE 257
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
944-1049 |
5.71e-18 |
|
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to produce methylglyoxal. The family also includes the C-terminal domain in carbamoyl phosphate synthetase (CPS) where it catalyzes the last phosphorylation of a coaboxyphosphate intermediate to form the product carbamoyl phosphate and may also play a regulatory role. This family also includes inosine monophosphate cyclohydrolase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 238297 [Multi-domain] Cd Length: 112 Bit Score: 80.63 E-value: 5.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 944 AFVSVREIDKPHVAEVARRLVELGFEVLATRGTANVLEEAGIQVTRVNKVTE-GRPHIVDMIKN-DEISFIINTVEGKQS 1021
Cdd:cd00532 2 VFLSVSDHVKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRHEdGEPTVDAAIAEkGKFDVVINLRDPRRD 81
|
90 100 110
....*....|....*....|....*....|.
gi 516883186 1022 ---TSDSYTIRREALMHKVGYTTTIAGAKAT 1049
Cdd:cd00532 82 rctDEDGTALLRLARLYKIPVTTPNATAMFV 112
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
622-850 |
9.64e-16 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 79.54 E-value: 9.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 622 LEDVLEVVATEKPAGVIVqyGGQTPLKL---ARD-LEAAGVPIIGTSPDSIDLAEDRERFQALLNKLGLKQPPNRTARSE 697
Cdd:PRK12767 58 IDRLLDICKKEKIDLLIP--LIDPELPLlaqNRDrFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 698 E--EAEKLAEEIGYPLVVRPSYVLGGRAMEIVRDREDLRSYMknavsvSNDAPVLLDRFLDDaIEVDVDAISDGENVIIG 775
Cdd:PRK12767 136 EdfKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLL------EYVPNLIIQEFIEG-QEYTVDVLCDLNGEVIS 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516883186 776 GI-MEHIEqagVHSG--DSACSLPpfslsmelQDEMVEQVRKMALGLKVVGLMNTQFAIKGDDIYVLEVNPRASRTVP 850
Cdd:PRK12767 209 IVpRKRIE---VRAGetSKGVTVK--------DPELFKLAERLAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYP 275
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
9-329 |
7.48e-15 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 77.66 E-value: 7.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 9 SILILGAGPIVIGqacefdysgaqACKALREEGYRVILVNSNPATIMT------------DPEMADATYIEpvdwqTVAQ 76
Cdd:COG3919 7 RVVVLGGDINALA-----------VARSLGEAGVRVIVVDRDPLGPAArsryvdevvvvpDPGDDPEAFVD-----ALLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 77 IIEKERPDAVLPTMGGQTALncaldLSR-EGVLEKfGVEMIGANEAAIDMAEDRDHFKAAMADIGLDTPTAMLAHSWEEA 155
Cdd:COG3919 71 LAERHGPDVLIPTGDEYVEL-----LSRhRDELEE-HYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 156 QEIQPKIGFPVIIRPS--------FTLGGSGGGIAYNREEFEYIVKngiDLSPVNQVLLEEsalgwkEF------EMEVV 221
Cdd:COG3919 145 DALAEDLGFPVVVKPAdsvgydelSFPGKKKVFYVDDREELLALLR---RIAAAGYELIVQ------EYipgddgEMRGL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 222 ---RDKADNCIIICSIENL--DPMGIHTGDSITVAPAQTLtdkeyqimRDASLAVLRKIGVeTGGSNVQFAINPENGRMI 296
Cdd:COG3919 216 tayVDRDGEVVATFTGRKLrhYPPAGGNSAARESVDDPEL--------EEAARRLLEALGY-HGFANVEFKRDPRDGEYK 286
|
330 340 350
....*....|....*....|....*....|...
gi 516883186 297 VIEMNPRVSRSSALASKAtGFPIAKVAAKLAVG 329
Cdd:COG3919 287 LIEINPRFWRSLYLATAA-GVNFPYLLYDDAVG 318
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
613-843 |
1.47e-12 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 69.58 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 613 DRLYFEPLTLEDVLEVVATEKPAGVIVQYGG-QTPLKLARDLEAAGVPIIGtSPDSIDLAEDRERFQALLNKLGLKQPPN 691
Cdd:COG0189 36 DDLTLDLGRAPELYRGEDLSEFDAVLPRIDPpFYGLALLRQLEAAGVPVVN-DPEAIRRARDKLFTLQLLARAGIPVPPT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 692 RTARSEEEAEKLAEEIGYPLVVRPSYVLGGRAMEIVRDREDLRSYMKNAVSVSNDaPVLLDRFLDDAIEVDVDAI-SDGE 770
Cdd:COG0189 115 LVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEALTELGSE-PVLVQEFIPEEDGRDIRVLvVGGE 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516883186 771 nvIIGGIM----EHIEQAGVHSGDSACslppfslSMELQDEMVEQVRKMA--LGLKVVGLmntQFAIKGDDIYVLEVNP 843
Cdd:COG0189 194 --PVAAIRripaEGEFRTNLARGGRAE-------PVELTDEERELALRAApaLGLDFAGV---DLIEDDDGPLVLEVNV 260
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
109-340 |
6.17e-12 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 69.24 E-value: 6.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 109 EKFGVEMIGANEAAIDMAEDRDHFKAAMADIGL----DTPTAMlaHSWEEAQEIQPKIGFPVIIRPSFTLGGSGGGIAYN 184
Cdd:PRK08654 96 EKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVpvlpGTEEGI--EDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYS 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 185 REEFEYIVKNGIDLSPVN----QVLLEESALGWKEFEMEVVRDKADNCIII----CSI----ENLdpmgihtgdsITVAP 252
Cdd:PRK08654 174 EEELEDAIESTQSIAQSAfgdsTVFIEKYLEKPRHIEIQILADKHGNVIHLgdreCSIqrrhQKL----------IEEAP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 253 AQTLTDKEYQIMRDASLAVLRKIGVETGGSnVQFAInpENGRMIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTL 332
Cdd:PRK08654 244 SPIMTPELRERMGEAAVKAAKAINYENAGT-VEFLY--SNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEEL 320
|
....*...
gi 516883186 333 DELKNDIT 340
Cdd:PRK08654 321 SFKQEDIT 328
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
10-314 |
6.18e-12 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 67.99 E-value: 6.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 10 ILILGAGpivigqacefdySGAQACKALREE--GYRVILV---NSNPATIMTD-----PEMADATYIEpvdwqTVAQIIE 79
Cdd:PRK12767 4 ILVTSAG------------RRVQLVKALKKSllKGRVIGAdisELAPALYFADkfyvvPKVTDPNYID-----RLLDICK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 80 KERPDAVLPTMGGQTALncaldLSREGV-LEKFGVEMIGANEAAIDMAedRDHFKAA--MADIGLDTPTAMLAHSWEEAQ 156
Cdd:PRK12767 67 KEKIDLLIPLIDPELPL-----LAQNRDrFEEIGVKVLVSSKEVIEIC--NDKWLTYefLKENGIPTPKSYLPESLEDFK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 157 EIQ--PKIGFPVIIRPSFTLGGSGGGIAYNREEFEYIvkngidLSPVNQVLLEESALGwKEFEMEVVRDKADNCIIICSI 234
Cdd:PRK12767 140 AALakGELQFPLFVKPRDGSASIGVFKVNDKEELEFL------LEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVISIVPR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 235 ENLDPMGIHTGDSITVapaqtltdkEYQIMRDASLAVLRKIGvETGGSNVQFAINpeNGRMIVIEMNPRVSRSSALASKA 314
Cdd:PRK12767 213 KRIEVRAGETSKGVTV---------KDPELFKLAERLAEALG-ARGPLNIQCFVT--DGEPYLFEINPRFGGGYPLSYMA 280
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
583-876 |
8.10e-12 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 68.02 E-value: 8.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 583 HAALAMREDGYETIMVNCnpetvSTDYDTS-----------DRLYFEPLTLEDVLEVVATEKPAGVIVQYGGQTPLKLAR 651
Cdd:COG2232 16 ALAQSARRAGYRVYAVDL-----FADLDTRalaerwvrldaESCGFDLEDLPAALLELAAADDPDGLVYGSGFENFPELL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 652 DLEAAGVPIIGTSPDSIDLAEDRERFQALLNKLGLKQPPNRTARSEEEaeklaeeigYPLVVRPSYVLGGRAMEIVRDRE 731
Cdd:COG2232 91 ERLARRLPLLGNPPEVVRRVKDPLRFFALLDELGIPHPETRFEPPPDP---------GPWLVKPIGGAGGWHIRPADSEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 732 DLrsymknavsvsnDAPVLLDRFLDdAIEVDVDAISDGENVIIGGIME-HIEQAGVH----SGdsacSLPPFSLSMELQD 806
Cdd:COG2232 162 PP------------APGRYFQRYVE-GTPASVLFLADGSDARVLGFNRqLIGPAGERpfryGG----NIGPLALPPALAE 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516883186 807 EMVEQVRKMALGLKVVGLMNTQFAIKGDDIYVLEVNPRASRTVPYVSKSVGRPLAK--IAArCMvgQTLPEQ 876
Cdd:COG2232 225 EMRAIAEALVAALGLVGLNGVDFILDGDGPYVLEVNPRPQASLDLYEDATGGNLFDahLRA-CR--GELPEV 293
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
555-874 |
5.67e-11 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 65.72 E-value: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 555 PTDKQKIMVLGGGPNrigqgiefDYCCVHAaLAMRedGYETIMVNCNPETVS------TDYDTSDRLYFEPLTLEDVLEV 628
Cdd:COG3919 2 MTMRFRVVVLGGDIN--------ALAVARS-LGEA--GVRVIVVDRDPLGPAarsryvDEVVVVPDPGDDPEAFVDALLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 629 VATEKPAGVIVQYGGQTPLKLARDLE--AAGVPIIGTSPDSIDLAEDRERFQALLNKLGLKQPPNRTARSEEEAEKLAEE 706
Cdd:COG3919 71 LAERHGPDVLIPTGDEYVELLSRHRDelEEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAED 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 707 IGYPLVVRPSY--------VLGGRAMEIVRDREDLRSYMKNAVSvsNDAPVLLDRFL--DDAIEVDVDAISDGE-NVIIG 775
Cdd:COG3919 151 LGFPVVVKPADsvgydelsFPGKKKVFYVDDREELLALLRRIAA--AGYELIVQEYIpgDDGEMRGLTAYVDRDgEVVAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 776 GIMEHIEQAGVHSGDSACSLppfSLSMElqdEMVEQVRKMALGLKVVGLMNTQFAIKGDD--IYVLEVNPRASRTVPYVS 853
Cdd:COG3919 229 FTGRKLRHYPPAGGNSAARE---SVDDP---ELEEAARRLLEALGYHGFANVEFKRDPRDgeYKLIEINPRFWRSLYLAT 302
|
330 340
....*....|....*....|.
gi 516883186 854 KSvGRPLAKIAARCMVGQTLP 874
Cdd:COG3919 303 AA-GVNFPYLLYDDAVGRPLE 322
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
21-302 |
1.84e-10 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 63.20 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 21 GQACEFD---YSGAQACKALREEGYRVILVnsnpatimtdpemadatyiePVDWQTVAQIIEKERPDAVLPTMGGQTALN 97
Cdd:COG1181 9 GRSAEREvslKSGRAVAAALDKAGYDVVPI--------------------GIDVEDLPAALKELKPDVVFPALHGRGGED 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 98 CALdlsrEGVLEKFGVEMIGANEAAIDMAEDRDHFKAAMADIGLDTPTAML--AHSWEEAQEIQPKIGFPVIIRPSFtlG 175
Cdd:COG1181 69 GTI----QGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVlrRGELADLEAIEEELGLPLFVKPAR--E 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 176 GSGGGI--AYNREEFEYIVKNGIDLSPvnQVLLEESALGwKEFEMEVVRDKADNCiiicsienLDPMGI----------- 242
Cdd:COG1181 143 GSSVGVskVKNAEELAAALEEAFKYDD--KVLVEEFIDG-REVTVGVLGNGGPRA--------LPPIEIvpengfydyea 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516883186 243 --HTGDSITVAPAQtLTDKEYQIMRDASLAVLRKIGVEtGGSNVQFAINPEnGRMIVIEMNP 302
Cdd:COG1181 212 kyTDGGTEYICPAR-LPEELEERIQELALKAFRALGCR-GYARVDFRLDED-GEPYLLEVNT 270
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
647-843 |
3.19e-09 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 59.28 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 647 LKLARDLEAAGVPIIgTSPDSIDLAEDRERFQALLNKLGLKQPPNRTARSEEEAEKLAEEIGYPLVVRPSYVLGGRAMEI 726
Cdd:TIGR00768 63 LAVLRYLESLGVPVI-NSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 727 VRDREDLRSYMKNAVSVSNDAPV-LLDRFLDDAIEVDVDAISDGENVIigGIMEHIE----QAGVHSGDSAcslPPFSLS 801
Cdd:TIGR00768 142 ARDRQAAESLLEHFEQLNGPQNLfLVQEYIKKPGGRDIRVFVVGDEVV--AAIYRITsghwRSNLARGGKA---EPCSLT 216
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 516883186 802 MELQDEMVEQVRkmALGLKVVGLmntQFAIKGDDIYVLEVNP 843
Cdd:TIGR00768 217 EEIEELAIKAAK--ALGLDVAGV---DLLESEDGLLVNEVNA 253
|
|
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
944-1002 |
1.10e-08 |
|
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR transformylase/IMP cyclohydrolase PurH is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439908 Cd Length: 512 Bit Score: 58.88 E-value: 1.10e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 516883186 944 AFVSVReiDKPHVAEVARRLVELGFEVLATRGTANVLEEAGIQVTRVNKVTeGRPHIVD 1002
Cdd:COG0138 6 ALISVS--DKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVT-GFPEILD 61
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
653-843 |
1.82e-08 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 57.04 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 653 LEAAGVPIIGTSPDSIDLAEDRERFQALLNKLGLKQPPNRTARS--EEEAEKLAEEIGYPLVVRPsyVLGG--RAMEIVR 728
Cdd:COG1181 75 LELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRgeLADLEAIEEELGLPLFVKP--AREGssVGVSKVK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 729 DREDLRSYMKNAvsVSNDAPVLLDRFLdDAIEVDVdAISDGENVIIGGIMEHIEQAGV-------HSGDSACSLPPfsls 801
Cdd:COG1181 153 NAEELAAALEEA--FKYDDKVLVEEFI-DGREVTV-GVLGNGGPRALPPIEIVPENGFydyeakyTDGGTEYICPA---- 224
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 516883186 802 mELQDEMVEQVRKMA------LGLKVVGLMNTqFAIKGDDIYVLEVNP 843
Cdd:COG1181 225 -RLPEELEERIQELAlkafraLGCRGYARVDF-RLDEDGEPYLLEVNT 270
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
648-844 |
3.22e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 57.30 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 648 KLARDLEAAGVPIIGTSPDSIDLAEDRERFQALLNKLGLKQPPNRTA--RSEEEAEKLAEEIGYPLVVRPSYVLGGRAME 725
Cdd:PRK08654 90 EFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEgiEDIEEAKEIAEEIGYPVIIKASAGGGGIGMR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 726 IVRDREDL----RSYMKNAVSVSNDAPVLLDRFLDDA--IEVDVDAISDGeNVIiggimehieqagvHSGDSACSL---- 795
Cdd:PRK08654 170 VVYSEEELedaiESTQSIAQSAFGDSTVFIEKYLEKPrhIEIQILADKHG-NVI-------------HLGDRECSIqrrh 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 516883186 796 -------PPFSLSMELQDEMVEQVRKMAlglKVVGLMNT---QFAIKGDDIYVLEVNPR 844
Cdd:PRK08654 236 qklieeaPSPIMTPELRERMGEAAVKAA---KAINYENAgtvEFLYSNGNFYFLEMNTR 291
|
|
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
944-1002 |
3.40e-08 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 57.41 E-value: 3.40e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 516883186 944 AFVSVReiDKPHVAEVARRLVELGFEVLATRGTANVLEEAGIQVTRVNKVTeGRPHIVD 1002
Cdd:PRK00881 7 ALISVS--DKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVT-GFPEILD 62
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
650-844 |
5.07e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 56.69 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 650 ARDLEAAGVPIIGTSPDSIDLAEDRERFQALLNKLGLKQPPNRTAR--SEEEAEKLAEEIGYPLVVRPSYVLGGRAMEIV 727
Cdd:PRK12833 95 AEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVvaSLDAALEVAARIGYPLMIKAAAGGGGRGIRVA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 728 RDREDLRSYM----KNAVSVSNDAPVLLDRFLDDAIEVDVDAISDGENViiggimehieqagVHSGDSACSL-------- 795
Cdd:PRK12833 175 HDAAQLAAELplaqREAQAAFGDGGVYLERFIARARHIEVQILGDGERV-------------VHLFERECSLqrrrqkil 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 516883186 796 ---PPFSLSMELQDEMVEQVRKMA--LGLKVVGLMNTQFAIKGDDIYVLEVNPR 844
Cdd:PRK12833 242 eeaPSPSLTPAQRDALCASAVRLArqVGYRGAGTLEYLFDDARGEFYFIEMNTR 295
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
953-1030 |
8.11e-08 |
|
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases (CPS), including ammonia-dependent CPS Type I, and glutamine-dependent CPS Type III. These are multidomain proteins, in which MGS is the C-terminal domain.
Pssm-ID: 238711 [Multi-domain] Cd Length: 116 Bit Score: 51.53 E-value: 8.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 953 KPHVAEVARRLVELGFEVLATRGTANVLEEAGIQVTRVNKVTE----GRPHIVDMIKNDEISFIIN-TVEGKQSTSDSYT 1027
Cdd:cd01423 12 KPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEepqnDKPSLRELLAEGKIDLVINlPSNRGKRVLDNDY 91
|
...
gi 516883186 1028 IRR 1030
Cdd:cd01423 92 VMR 94
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
109-339 |
2.56e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 54.34 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 109 EKFGVEMIGANEAAIDMAEDRDHFKAAMADIGLD-TP-TAMLAHSWEEAQEIQPKIGFPVIIRPsfTLGGSGGGI----- 181
Cdd:PRK07178 95 AERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPvTPgSEGNLADLDEALAEAERIGYPVMLKA--TSGGGGRGIrrcns 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 182 -AYNREEFEYIVKNGIDLSPVNQVLLEESALGWKEFEMEVVRDKADNCIII----CSIENldpmgiHTGDSITVAPAQTL 256
Cdd:PRK07178 173 rEELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLferdCSIQR------RNQKLIEIAPSPQL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 257 TDKEYQIMRDASLAVLRKIGVETGGSnVQFAINpENGRMIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLDELK 336
Cdd:PRK07178 247 TPEQRAYIGDLAVRAAKAVGYENAGT-VEFLLD-ADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLSYKQ 324
|
...
gi 516883186 337 NDI 339
Cdd:PRK07178 325 EDI 327
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
29-301 |
3.90e-07 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 53.19 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 29 SGAQACKALREEGYRVIlvnsnpatimtdpemadatyiePVDWQ-TVAQIIEKERPDAVLptmggqtalNcAL------D 101
Cdd:PRK01372 24 SGAAVLAALREAGYDAH----------------------PIDPGeDIAAQLKELGFDRVF---------N-ALhgrggeD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 102 LSREGVLEKFGVEMIGANEAAIDMAEDRDHFKAAMADIGLDTPTAMLAHSWEEAQEIQPKIGFPVIIRPSftLGGSGGGI 181
Cdd:PRK01372 72 GTIQGLLELLGIPYTGSGVLASALAMDKLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKPA--REGSSVGV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 182 aynreefeYIVKNGIDLSPV--------NQVLLEESALGwKEFEMEVVRDKAdnciiICSIEnLDPMGI--------HTG 245
Cdd:PRK01372 150 --------SKVKEEDELQAAlelafkydDEVLVEKYIKG-RELTVAVLGGKA-----LPVIE-IVPAGEfydyeakyLAG 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 516883186 246 DSITVAPAQtLTDKEYQIMRDASLAVLRKIGVEtGGSNVQFAINpENGRMIVIEMN 301
Cdd:PRK01372 215 GTQYICPAG-LPAEIEAELQELALKAYRALGCR-GWGRVDFMLD-EDGKPYLLEVN 267
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
657-876 |
7.03e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 53.21 E-value: 7.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 657 GVPIIGTSPDSIDLAEDRERFQALLNKLGLKQPPNRTA--RSEEEAEKLAEEIGYPLVVRPSYVLGGRAMEIVRDREDL- 733
Cdd:PRK08462 101 NIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGalKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLe 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 734 RSYM---KNAVSVSNDAPVLLDRFLDDA--IEVDVDAISDGeNVIiggimehieqagvHSGDSACSL-----------PP 797
Cdd:PRK08462 181 NLYLaaeSEALSAFGDGTMYMEKFINNPrhIEVQILGDKHG-NVI-------------HVGERDCSLqrrhqklieesPA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 798 FSLSMELQDEMVEQVRKMALGLKVVGLMNTQFAI-KGDDIYVLEVNPRASRTVPyVSKSV-GRPLAKIAARCMVGQTLPE 875
Cdd:PRK08462 247 VVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLdSNLDFYFMEMNTRLQVEHT-VSEMVsGLDLIEWMIKIAEGEELPS 325
|
.
gi 516883186 876 Q 876
Cdd:PRK08462 326 Q 326
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
707-844 |
8.59e-07 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 50.08 E-value: 8.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 707 IGYPLVVRPSYVLGGRAMEIVRDREDLRSYMKNavsvsndapVLLDRFLDdAIEVDVDAISDGENVIIGGI-MEHIEQAG 785
Cdd:pfam02655 30 EEKKYVVKPRDGCGGEGVRKVENGREDEAFIEN---------VLVQEFIE-GEPLSVSLLSDGEKALPLSVnRQYIDNGG 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 786 VHSGDSACSLP-PFSLSMELQDEMVEQVRKMAlGLkvVGLMNTQFAIKGDDIYVLEVNPR 844
Cdd:pfam02655 100 SGFVYAGNVTPsRTELKEEIIELAEEVVECLP-GL--RGYVGVDLVLKDNEPYVIEVNPR 156
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
7-339 |
9.71e-07 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 52.51 E-value: 9.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 7 IQSILILGAGPIVIgqacefdysgaQACKALREEGYRVILVNSNPATIMTDPEMADATY---IEPV----DWQTVAQIIE 79
Cdd:PRK08463 2 IHKILIANRGEIAV-----------RVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYrigTDPIkgylDVKRIVEIAK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 80 KERPDAVLPTMGgqtALNCALDLSREgvLEKFGVEMIGANEAAIDMAEDRDHFKAAMADIGLD-TP-TAML-AHSWEEAQ 156
Cdd:PRK08463 71 ACGADAIHPGYG---FLSENYEFAKA--VEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPiVPgTEKLnSESMEEIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 157 EIQPKIGFPVIIRPSFTLGGSGGGIAYNREE----FEYIVKNGIDLSPVNQVLLEESALGWKEFEMEVVRDKADNCIII- 231
Cdd:PRK08463 146 IFARKIGYPVILKASGGGGGRGIRVVHKEEDlenaFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLc 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 232 ---CSIENldpmgiHTGDSITVAPAQTLTDKEYQIMRDASLAVLRKIGVETGGSnVQFAINpENGRMIVIEMNPRVSRSS 308
Cdd:PRK08463 226 erdCSIQR------RHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGT-IEFLLD-DYNRFYFMEMNTRIQVEH 297
|
330 340 350
....*....|....*....|....*....|.
gi 516883186 309 ALASKATGFPIAKVAAKLAVGYTLDELKNDI 339
Cdd:PRK08463 298 GVTEEITGIDLIVRQIRIAAGEILDLEQSDI 328
|
|
| PLN02891 |
PLN02891 |
IMP cyclohydrolase |
939-1002 |
1.08e-06 |
|
IMP cyclohydrolase
Pssm-ID: 178479 [Multi-domain] Cd Length: 547 Bit Score: 52.48 E-value: 1.08e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516883186 939 PSTGK--AFVSVReiDKPHVAEVARRLVELGFEVLATRGTANVLEEAGIQVTRVNKVTeGRPHIVD 1002
Cdd:PLN02891 18 PSSGKkqALISLS--DKTDLALLANGLQELGYTIVSTGGTASALEAAGVSVTKVEELT-NFPEMLD 80
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
592-844 |
1.76e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 52.16 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 592 GYETIMVNCNPETvstdYDTSDRLYFEPLTLE----DVLEVVATEKP--AGVIV--QYGGQTPLKLARDLeaaGVPiiGT 663
Cdd:PRK02186 27 GFTPYFLTANRGK----YPFLDAIRVVTISADtsdpDRIHRFVSSLDgvAGIMSssEYFIEVASEVARRL---GLP--AA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 664 SPDSIDLAEDRERFQALLNKLGLKQPPNRTARSEEEAEKLAEEIGYPLVVRPSYVLGGRAMEIVRDREDLRSYMKNAVSV 743
Cdd:PRK02186 98 NTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALRRA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 744 SNDApVLLDRFLDDAiEVDVDAISDGENVIIGGIMehieqaGVHSGDSACSLP-----PFSLSMELQDEMVEQVRKM--A 816
Cdd:PRK02186 178 GTRA-ALVQAYVEGD-EYSVETLTVARGHQVLGIT------RKHLGPPPHFVEighdfPAPLSAPQRERIVRTVLRAldA 249
|
250 260
....*....|....*....|....*...
gi 516883186 817 LGLKvVGLMNTQFAIKGDDIYVLEVNPR 844
Cdd:PRK02186 250 VGYA-FGPAHTELRVRGDTVVIIEINPR 276
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
649-844 |
2.27e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 51.57 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 649 LARDLEAAGVPIIGTSPDSIDLAEDRERFQALLNKLGLKQPPNRTA--RSEEEAEKLAEEIGYPLVVRPSYVLGGRAMEI 726
Cdd:PRK06111 91 FAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTnlEDAEEAIAIARQIGYPVMLKASAGGGGIGMQL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 727 VRDREDLRSYM----KNAVSVSNDAPVLLDRFLDDA--IEVDVDAISDGeNViiggimehieqagVHSGDSACSL----- 795
Cdd:PRK06111 171 VETEQELTKAFesnkKRAANFFGNGEMYIEKYIEDPrhIEIQLLADTHG-NT-------------VYLWERECSVqrrhq 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 516883186 796 -------PPFsLSMELQDEMVEQVRKMALGLKVVGLMNTQFAI-KGDDIYVLEVNPR 844
Cdd:PRK06111 237 kvieeapSPF-LDEETRKAMGERAVQAAKAIGYTNAGTIEFLVdEQKNFYFLEMNTR 292
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
150-339 |
2.78e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 51.25 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 150 HSWEEAQEIQPKIGFPVIIRPSFTLGGSGGGIAYNREEFEYIVKNGIDLSPVN----QVLLEESALGWKEFEMEVVRDKA 225
Cdd:PRK05586 139 ENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAfgddSMYIEKFIENPKHIEFQILGDNY 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 226 DNCIII----CSIENLDPMGIHTgdsitvAPAQTLTDKEYQIMRDASLAVLRKIGVETGGSnVQFAINpENGRMIVIEMN 301
Cdd:PRK05586 219 GNVVHLgerdCSLQRRNQKVLEE------APSPVMTEELRKKMGEIAVKAAKAVNYKNAGT-IEFLLD-KDGNFYFMEMN 290
|
170 180 190
....*....|....*....|....*....|....*...
gi 516883186 302 PRVSRSSALASKATGFPIAKVAAKLAVGYTLDELKNDI 339
Cdd:PRK05586 291 TRIQVEHPITEMITGVDLVKEQIKIAYGEKLSIKQEDI 328
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
649-844 |
4.11e-06 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 51.29 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 649 LARDLEAAGVPIIGTSPDSIDLAEDRERFQALLNKLGLKQPP--NRTARSEEEAEKLAEEIGYPLVVRPSYVLGGRAMEI 726
Cdd:PRK12999 95 FARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPgsEGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRI 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 727 VRDREDLRSYMKNAVSVS-----NDApVLLDRFLDDA--IEVDVdaISDGE-NViiggimehieqagVHSGDSACSL--- 795
Cdd:PRK12999 175 VRSEEELEEAFERAKREAkaafgNDE-VYLEKYVENPrhIEVQI--LGDKHgNV-------------VHLYERDCSVqrr 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516883186 796 --------PPFSLSMELQDEMVEQVRKMAlglKVVGLMN---TQFAIKGD-DIYVLEVNPR 844
Cdd:PRK12999 239 hqkvveiaPAPGLSEELRERICEAAVKLA---RAVGYVNagtVEFLVDADgNFYFIEVNPR 296
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
6-332 |
8.56e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 49.36 E-value: 8.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 6 DIQSILILGAGPIVIgqacefdysgaQACKALREEGYRVILVNSNP-----------ATIMTDPEMADATYIEPVDWQTV 74
Cdd:PRK08462 3 EIKRILIANRGEIAL-----------RAIRTIQEMGKEAIAIYSTAdkdalylkyadAKICIGGAKSSESYLNIPAIISA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 75 AQIIEKerpDAVLPTMG----GQTALNcaldlsregVLEKFGVEMIGANEAAIDMAEDRDHFKAAMADIGLdtPTAM--- 147
Cdd:PRK08462 72 AEIFEA---DAIFPGYGflseNQNFVE---------ICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGV--PVIPgsd 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 148 -LAHSWEEAQEIQPKIGFPVIIRPSFTLGGSGGGIAYNREEFE--YIVKNGIDLSPVNQ--VLLEESALGWKEFEMEVVR 222
Cdd:PRK08462 138 gALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLEnlYLAAESEALSAFGDgtMYMEKFINNPRHIEVQILG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 223 DKADNCIII----CSIENldpmgiHTGDSITVAPAQTLTDKEYQIMRDASLAVLRKIGVETGGSnVQFAINpENGRMIVI 298
Cdd:PRK08462 218 DKHGNVIHVgerdCSLQR------RHQKLIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGT-FEFLLD-SNLDFYFM 289
|
330 340 350
....*....|....*....|....*....|....
gi 516883186 299 EMNPRVSRSSALASKATGFPIAKVAAKLAVGYTL 332
Cdd:PRK08462 290 EMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL 323
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
648-844 |
1.27e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 48.94 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 648 KLARDLEAAGVPIIGTSPDSIDLAEDRERFQALLNKLGLKQPP--NRTARSEEEAEKLAEEIGYPLVVRPSYVLGGRAME 725
Cdd:PRK05586 90 KFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPgsEGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 726 IVRDREDLRSYMKNAVSVS----NDAPVLLDRFLDDAIEVDVDAISDG-ENViiggimehieqagVHSGDSACSL----- 795
Cdd:PRK05586 170 IVRSEEELIKAFNTAKSEAkaafGDDSMYIEKFIENPKHIEFQILGDNyGNV-------------VHLGERDCSLqrrnq 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 516883186 796 ------PPFSLSMELQDEMVEQVRKMAlglKVVGLMNT---QFAI-KGDDIYVLEVNPR 844
Cdd:PRK05586 237 kvleeaPSPVMTEELRKKMGEIAVKAA---KAVNYKNAgtiEFLLdKDGNFYFMEMNTR 292
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
650-844 |
2.02e-05 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 48.92 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 650 ARDL-EAAGVPIIGTSPDSIDLAEDRERFQAllnklglkqppnrtarseeeaeklaeEIGYPLVVRPSYVLGGRAMEIVR 728
Cdd:COG1038 122 ARAAaIEAGVPVIPGTEGPVDDLEEALAFAE--------------------------EIGYPVMLKAAAGGGGRGMRVVR 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 729 DREDLRSYMKNAVSVS-----NDApVLLDRFLDDA--IEVDVDAISDGeNViiggimehieqagVHSGDSACSL------ 795
Cdd:COG1038 176 SEEELEEAFESARREAkaafgDDE-VFLEKYIERPkhIEVQILGDKHG-NI-------------VHLFERDCSVqrrhqk 240
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 516883186 796 -----PPFSLSMELQDEMVEQVRKMAlglKVVGLMN--T-QFAI-KGDDIYVLEVNPR 844
Cdd:COG1038 241 vveiaPAPNLDEELREAICEAAVKLA---KAVGYVNagTvEFLVdDDGNFYFIEVNPR 295
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
109-339 |
4.30e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 47.33 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 109 EKFGVEMIGANEAAIDMAEDRDHFKAAM--ADI----GLDTPTAmlahSWEEAQEIQPKIGFPVIIRPSFTLGGSGGGIA 182
Cdd:PRK06111 96 KEEGIVFIGPSADIIAKMGSKIEARRAMqaAGVpvvpGITTNLE----DAEEAIAIARQIGYPVMLKASAGGGGIGMQLV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 183 YNREE----FEYIVKNGIDLSPVNQVLLEESALGWKEFEMEVVRDKADNCIII----CSIENldpmgiHTGDSITVAPAQ 254
Cdd:PRK06111 172 ETEQEltkaFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLwereCSVQR------RHQKVIEEAPSP 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 255 TLTDKEYQIMRDASLAVLRKIGVETGGSnVQFAINpENGRMIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLDE 334
Cdd:PRK06111 246 FLDEETRKAMGERAVQAAKAIGYTNAGT-IEFLVD-EQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLSF 323
|
....*
gi 516883186 335 LKNDI 339
Cdd:PRK06111 324 TQDDI 328
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
683-844 |
4.36e-05 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 44.94 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 683 KLGLKQPPNRTARSEEEAEKLAEEIGYPLVVRpSYVLG--GRAMEIVRDREDLRSymknAVSVSNDAPVLLDRFLDDAIE 760
Cdd:pfam02222 2 KLGLPTPRFMAAESLEELIEAGQELGYPCVVK-ARRGGydGKGQYVVRSEADLPQ----AWEELGDGPVIVEEFVPFDRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 761 VDVDAIS--DGEnVIIGGIMEHIEQAGVhsgdsaC--SLPPFSLSMELQDEMVEQVRKMALGLKVVGLMNTQFAIKGD-D 835
Cdd:pfam02222 77 LSVLVVRsvDGE-TAFYPVVETIQEDGI------CrlSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELFVTEDgD 149
|
....*....
gi 516883186 836 IYVLEVNPR 844
Cdd:pfam02222 150 LLINELAPR 158
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
108-304 |
4.55e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 47.10 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 108 LEKFGVEMIGANEAAIDMAEDRDHFKAAMADIGLdtPT----AMLAHSWEEAQEIQPKIGFPVIIRPsfTLGGSGGGI-- 181
Cdd:PRK08591 95 CEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGV--PVvpgsDGPVDDEEEALAIAKEIGYPVIIKA--TAGGGGRGMrv 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 182 AYNREEFEYIVK-----------NGidlspvnQVLLEESALGWKEFEMEVVRDKADNCIII----CSI---------Enl 237
Cdd:PRK08591 171 VRTEAELEKAFSmaraeakaafgNP-------GVYMEKYLENPRHIEIQVLADGHGNAIHLgerdCSLqrrhqkvleE-- 241
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516883186 238 dpmgihtgdsitvAPAQTLTDKEYQIMRDASLAVLRKIGVETGGSnVQFaINPENGRMIVIEMNPRV 304
Cdd:PRK08591 242 -------------APSPAITEELRRKIGEAAVKAAKAIGYRGAGT-IEF-LYEKNGEFYFIEMNTRI 293
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
35-193 |
1.48e-04 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 44.93 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 35 KALREEGYRVILVNsnpatimtdpemADATYIEPVDWQTVAQIIEKERPDAVLPTmggQTALNCALDLSRegVLEKFGVE 114
Cdd:COG0189 21 EAAQRRGHEVEVID------------PDDLTLDLGRAPELYRGEDLSEFDAVLPR---IDPPFYGLALLR--QLEAAGVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 115 MIGaNEAAIDMAEDRDHFKAAMADIGLDTPTAMLAHSWEEAQEIQPKIGFPVIIRPsftLGGSGG-GI--AYNREEFEYI 191
Cdd:COG0189 84 VVN-DPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKP---LDGSGGrGVflVEDEDALESI 159
|
..
gi 516883186 192 VK 193
Cdd:COG0189 160 LE 161
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
35-179 |
2.19e-04 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 44.26 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 35 KALREEG--YRVILVNSNPATIMTDPEmadatyiepvdwqtvaqiiEKERPDAVLPTMggqTALNCALDLSRegVLEKFG 112
Cdd:TIGR00768 18 EAAEELGidYKVVTPPAINLTFNEGPR-------------------ALAELDVVIVRI---VSMFRGLAVLR--YLESLG 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516883186 113 VEMIGANEAaIDMAEDRDHFKAAMADIGLDTPTAMLAHSWEEAQEIQPKIGFPVIIRPSFtlgGSGG 179
Cdd:TIGR00768 74 VPVINSSDA-ILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVF---GSWG 136
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
680-843 |
4.20e-04 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 42.69 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 680 LLNKLGLKQPP-------NRTARSEEEAEKLAEEIGYPLVVRPSyVLGGR-AMEIVRDREDLRSYMKNAvsVSNDAPVLL 751
Cdd:pfam07478 1 LLKAAGLPVVPfvtftraDWKLNPKEWCAQVEEALGYPVFVKPA-RLGSSvGVSKVESREELQAAIEEA--FQYDEKVLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 752 DRFLD-DAIEVdvdAISDGENVIIGGIMEHIEQAGV------HSGDSACSLPPFSLSMELQDEMVEQVRKM--ALGLKvv 822
Cdd:pfam07478 78 EEGIEgREIEC---AVLGNEDPEVSPVGEIVPSGGFydyeakYIDDSAQIVVPADLEEEQEEQIQELALKAykALGCR-- 152
|
170 180
....*....|....*....|..
gi 516883186 823 GLMNTQFAIKGDD-IYVLEVNP 843
Cdd:pfam07478 153 GLARVDFFLTEDGeIVLNEVNT 174
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
162-303 |
9.43e-04 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 316093 [Multi-domain] Cd Length: 160 Bit Score: 41.11 E-value: 9.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 162 IGFPVIIRPSFTLGGSGGGIAYNREEFEYIV----------KNGIDLSPVN--QVLLEESALGwKEFEMEVVRDKADNCI 229
Cdd:pfam13535 1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAFaaireeieqwKEMYPEAVVDggSFLVEEYIEG-EEFAVDAYFDENGEPV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516883186 230 IICSIENLDPMGIHTGDSITVAPAQTLTDKEYQIMrDASLAVLRKIGVETGGSNVQFAINpENGRMIVIEMNPR 303
Cdd:pfam13535 80 ILNILKHDFASSEDVSDRIYVTSASIIRETQAAFT-EFLKRINALLGLKNFPVHIELRVD-EDGQIIPIEVNPL 151
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
648-795 |
2.12e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 41.71 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 648 KLARDLEAAGVPIIGTSPDSIDLAEDRERFQALLNKLGLKQPPNRTAR--SEEEAEKLAEEIGYPLVVRPSYVLGGRAME 725
Cdd:PRK08591 90 DFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPvdDEEEALAIAKEIGYPVIIKATAGGGGRGMR 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516883186 726 IVRDREDLRSYMKNA-----VSVSNDApVLLDRFLDDAIEVDVDAISDGE-NVIiggimehieqagvHSGDSACSL 795
Cdd:PRK08591 170 VVRTEAELEKAFSMAraeakAAFGNPG-VYMEKYLENPRHIEIQVLADGHgNAI-------------HLGERDCSL 231
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
806-851 |
3.02e-03 |
|
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to carbamoyl phosphate synthetase. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.
Pssm-ID: 434824 [Multi-domain] Cd Length: 131 Bit Score: 39.13 E-value: 3.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 516883186 806 DEMVEQVRKMALGLKVVGLMNTQFAIKGDDIYVLEVNPRASRTVPY 851
Cdd:pfam15632 47 PELIEAARRLAEAFGLDGLFNVQFRYDGDGPKLLEINPRMSGGIGY 92
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
620-844 |
5.31e-03 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 40.49 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 620 LTLEDVLEVVATEKPAGV-IVQYGGQTPL--KLARDLEAAGVPIIGTSPDSIDLAEDRERFQALLNKLGLKQPPNRTARS 696
Cdd:PLN02257 46 LDISDSAAVISFCRKWGVgLVVVGPEAPLvaGLADDLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 697 EEEAEKLAEEIGYPLVVRPSYVLGGR----AMEIVRDREDLRSYMKNAVSVSNDAPVLLDRFLDDAiEVDVDAISDGENV 772
Cdd:PLN02257 126 PAAAKKYIKEQGAPIVVKADGLAAGKgvvvAMTLEEAYEAVDSMLVKGAFGSAGSEVVVEEFLDGE-EASFFALVDGENA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 773 I-IGGIMEHIE----QAGVHSGDSACSLPPFSLSMELQDEMVEQ-----VRKMAL-GLKVVGLMNTQFAI--KGDDIYVL 839
Cdd:PLN02257 205 IpLESAQDHKRvgdgDTGPNTGGMGAYSPAPVLTPELESKVMETiiyptVKGMAAeGCKFVGVLYAGLMIekKSGLPKLL 284
|
....*
gi 516883186 840 EVNPR 844
Cdd:PLN02257 285 EYNVR 289
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
121-304 |
7.18e-03 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 40.06 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 121 AAIDMAEDRDHFKAAMADIGLDTPTAMLAHSWEEAQEIQPKIGFPVIIRPSFtlGGSGG-GiaynreefEYIVKNGIDLS 199
Cdd:COG0026 82 EALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRR--GGYDGkG--------QVVIKSAADLE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 200 PVNQVLLEESAL--GWKEFEME----VVRDKADNCIIICSIENldpmgIHTgDSI---TVAPAQtLTDKEYQIMRDASLA 270
Cdd:COG0026 152 AAWAALGGGPCIleEFVPFERElsviVARSPDGEVATYPVVEN-----VHR-NGIldeSIAPAR-ISEALAAEAEEIAKR 224
|
170 180 190
....*....|....*....|....*....|....*....
gi 516883186 271 VLRKIGVeTGgsnVqFAInpE-----NGRMIVIEMNPRV 304
Cdd:COG0026 225 IAEALDY-VG---V-LAV--EffvtkDGELLVNEIAPRP 256
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
664-844 |
8.04e-03 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 39.75 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 664 SPDSIDLAEDRERFQALLNKLGLKQPPNRTARSEEEAEKLAEEIGYPLVVRpSYVLG--GRAMEIVRDREDLRSymknAV 741
Cdd:PRK06019 91 GPDALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLK-TRRGGydGKGQWVIRSAEDLEA----AW 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516883186 742 SVSNDAPVLLDRFLDDAIEVDV----DAisDG--------ENVIIGGIMehieqagvhsgdsACSLPPFSLSMELQDEMV 809
Cdd:PRK06019 166 ALLGSVPCILEEFVPFEREVSVivarGR--DGevvfyplvENVHRNGIL-------------RTSIAPARISAELQAQAE 230
|
170 180 190
....*....|....*....|....*....|....*.
gi 516883186 810 EQVRKMALGLKVVGLMNTQFAIKGDD-IYVLEVNPR 844
Cdd:PRK06019 231 EIASRIAEELDYVGVLAVEFFVTGDGeLLVNEIAPR 266
|
|
| |
