|
Name |
Accession |
Description |
Interval |
E-value |
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
1-1069 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 2213.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 1 MPKRTDIKSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPIHWEVVRKIIEK 80
Cdd:PRK05294 1 MPKRTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 81 ERPDAVLPTMGGQTALNCALELERQGVLEEFGVTMIGATADAIDKAEDRRRFDVAMKKIGLETARSGIAHTMEEALAVAA 160
Cdd:PRK05294 81 ERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 161 DVGFPCIIRPSFTMGGSGGGIAYNREEFEEICARGLDLSPTKELLIDESLIGWKEYEMEVVRDKNDNCIIVCSIENFDAM 240
Cdd:PRK05294 161 EIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 241 GIHTGDSITVAPAQTLTDKEYQIMRNASMAVLREIGVETGGSNVQFAVNPKNGRLIVIEMNPRVSRSSALASKATGFPIA 320
Cdd:PRK05294 241 GVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVETGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 321 KVAAKLAVGYTLDELMNDITGgRTPASFEPSIDYVVTKIPRFNFEKFAGANDRLTTQMKSVGEVMAIGRTQQESLQKALR 400
Cdd:PRK05294 321 KVAAKLAVGYTLDEIKNDITG-KTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 401 GLEVGATGFDPKvsLDDPEALTKIRRELKDAGADRIWYIADAFRAGLSVDGVFNLTNIDRWFLVQIEELVRLEEKVAEvG 480
Cdd:PRK05294 400 SLEIGVTGLDED--LFEEESLEELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKE-N 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 481 ITGLNADFLRQLKRKGFADARLAKLAGVREAEIRKLRDQYDLHPVYKRVDTCAAEFATDTAYMYSTYEEECEANPStDRE 560
Cdd:PRK05294 477 GLPLDAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPS-DRK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 561 KIMVLGGGPNRIGQGIEFDYCCVHASLALREDGYETIMVNCNPETVSTDYDTSDRLYFEPVTLEDVLEIVRIEKPKGVIV 640
Cdd:PRK05294 556 KVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIV 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 641 QYGGQTPLKLARALEAAGVPVIGTSPDAIDRAEDRERFQHAVERLKLKQPANATVTAIEMAVEKAKEIGYPLVVRPSYVL 720
Cdd:PRK05294 636 QFGGQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVL 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 721 GGRAMEIVYDEADLRRYFQTAVSVSNDAPVLLDHFLDDAVEVDVDAICDGEMVLIGGIMEHIEQAGVHSGDSACSLPAYT 800
Cdd:PRK05294 716 GGRAMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICDGEDVLIGGIMEHIEEAGVHSGDSACSLPPQT 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 801 LSQEIQDVMRQQVQKLAFELQVRGLMNVQFAVKNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAARVMAGKSLAEQGVT 880
Cdd:PRK05294 796 LSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYT 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 881 KEVIPPYYSVKEVVLPFNKFPGVDPLLGPEMRSTGEVMGVGRTFAEAFAKAQLGSNSTMKKHGRALLSVREGDKERVVDL 960
Cdd:PRK05294 876 KGLIPPYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSGTVFLSVRDRDKEEVVEL 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 961 AAKLLKQGFELDATHGTAIVLGEAGINPRLVNKVHEGRPHIQDRIKNGEYTYIINTTSGRRAIEDSRVIRRSALQYKVHY 1040
Cdd:PRK05294 956 AKRLLELGFKILATSGTAKFLREAGIPVELVNKVHEGRPHIVDLIKNGEIDLVINTPTGRQAIRDGFSIRRAALEYKVPY 1035
|
1050 1060 1070
....*....|....*....|....*....|.
1C3O_C 1041 DTTLNGGFATAMALNADATEK--VISVQEMH 1069
Cdd:PRK05294 1036 ITTLAGARAAVKAIEALKFGEleVRSLQEYH 1066
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
2-1054 |
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: 1827.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 2 PKRTDIKSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPIHWEVVRKIIEKE 81
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 82 RPDAVLPTMGGQTALNCALELERQGVLEEFGVTMIGATADAIDKAEDRRRFDVAMKKIGLETARSGIAHTMEEALAVAAD 161
Cdd:TIGR01369 81 RPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 162 VGFPCIIRPSFTMGGSGGGIAYNREEFEEICARGLDLSPTKELLIDESLIGWKEYEMEVVRDKNDNCIIVCSIENFDAMG 241
Cdd:TIGR01369 161 IGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 242 IHTGDSITVAPAQTLTDKEYQIMRNASMAVLREIGVEtGGSNVQFAVNPKNGRLIVIEMNPRVSRSSALASKATGFPIAK 321
Cdd:TIGR01369 241 VHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIE-GGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 322 VAAKLAVGYTLDELMNDITGgRTPASFEPSIDYVVTKIPRFNFEKFAGANDRLTTQMKSVGEVMAIGRTQQESLQKALRG 401
Cdd:TIGR01369 320 VAAKLAVGYTLDELKNPVTG-TTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 402 LEVGATGFDpkVSLDDPEALTKIRRELKDAGADRIWYIADAFRAGLSVDGVFNLTNIDRWFLVQIEELVRLEEKVAEVGI 481
Cdd:TIGR01369 399 LEIGATGFD--LPDREVEPDEDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 482 TGLNADFLRQLKRKGFADARLAKLAGVREAEIRKLRDQYDLHPVYKRVDTCAAEFATDTAYMYSTYEEECEANPSTDREK 561
Cdd:TIGR01369 477 TDLDPELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKKK 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 562 IMVLGGGPNRIGQGIEFDYCCVHASLALREDGYETIMVNCNPETVSTDYDTSDRLYFEPVTLEDVLEIVRIEKPKGVIVQ 641
Cdd:TIGR01369 557 VLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQ 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 642 YGGQTPLKLARALEAAGVPVIGTSPDAIDRAEDRERFQHAVERLKLKQPANATVTAIEMAVEKAKEIGYPLVVRPSYVLG 721
Cdd:TIGR01369 637 FGGQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLG 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 722 GRAMEIVYDEADLRRYFQTAVSVSNDAPVLLDHFLDDAVEVDVDAICDGEMVLIGGIMEHIEQAGVHSGDSACSLPAYTL 801
Cdd:TIGR01369 717 GRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTL 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 802 SQEIQDVMRQQVQKLAFELQVRGLMNVQFAVKNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAARVMAGKSLAEQGVTK 881
Cdd:TIGR01369 797 SAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGVGK 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 882 EVIPPYYSVKEVVLPFNKFPGVDPLLGPEMRSTGEVMGVGRTFAEAFAKAQLGSNSTMKKHGRALLSVREGDKERVVDLA 961
Cdd:TIGR01369 877 EKEPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLA 956
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 962 AKLLKQGFELDATHGTAIVLGEAGINPRLVNKVHEGRPHIQDRIKNGEYTYIINTTS-GRRAIEDSRVIRRSALQYKVHY 1040
Cdd:TIGR01369 957 RKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEGRPNILDLIKNGEIELVINTTSkGAGTATDGYKIRREALDYGVPL 1036
|
1050
....*....|....
1C3O_C 1041 DTTLNGGFATAMAL 1054
Cdd:TIGR01369 1037 ITTLNTAEAFAEAL 1050
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
3-1056 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 1508.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 3 KRTDIKSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPIHWEVVRKIIEKER 82
Cdd:PLN02735 19 KRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 83 PDAVLPTMGGQTALNCALELERQGVLEEFGVTMIGATADAIDKAEDRRRFDVAMKKIGLETARSGIAHTMEEALAVAADV 162
Cdd:PLN02735 99 PDALLPTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 163 G-FPCIIRPSFTMGGSGGGIAYNREEFEEICARGLDLSPTKELLIDESLIGWKEYEMEVVRDKNDNCIIVCSIENFDAMG 241
Cdd:PLN02735 179 GeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 242 IHTGDSITVAPAQTLTDKEYQIMRNASMAVLREIGVETGGSNVQFAVNPKNGRLIVIEMNPRVSRSSALASKATGFPIAK 321
Cdd:PLN02735 259 VHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVECGGSNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 322 VAAKLAVGYTLDELMNDITgGRTPASFEPSIDYVVTKIPRFNFEKFAGANDRLTTQMKSVGEVMAIGRTQQESLQKALRG 401
Cdd:PLN02735 339 MAAKLSVGYTLDQIPNDIT-LKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRS 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 402 LEVGATGFDPKVSLDDPEALTKIRRELKDAGADRIWYIADAFRAGLSVDGVFNLTNIDRWFLVQIEELVRLEEKVAEVGI 481
Cdd:PLN02735 418 LETGFSGWGCAKVKELDWDWEQLKYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSL 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 482 TGLNADFLRQLKRKGFADARLAKLAGVREAEIRKLRDQYDLHPVYKRVDTCAAEFATDTAYMYSTYEEECEANPsTDREK 561
Cdd:PLN02735 498 SELSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAP-TNKKK 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 562 IMVLGGGPNRIGQGIEFDYCCVHASLALREDGYETIMVNCNPETVSTDYDTSDRLYFEPVTLEDVLEIVRIEKPKGVIVQ 641
Cdd:PLN02735 577 VLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQ 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 642 YGGQTPLKLARALE----------AAG---VPVIGTSPDAIDRAEDRERFQHAVERLKLKQPANATVTAIEMAVEKAKEI 708
Cdd:PLN02735 657 FGGQTPLKLALPIQkyldknpppsASGngnVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKRI 736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 709 GYPLVVRPSYVLGGRAMEIVYDEADLRRYFQTAVSVSNDAPVLLDHFLDDAVEVDVDAICDGE-MVLIGGIMEHIEQAGV 787
Cdd:PLN02735 737 GYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALADSEgNVVIGGIMEHIEQAGV 816
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 788 HSGDSACSLPAYTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAV-KNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAA 866
Cdd:PLN02735 817 HSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAItPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYAS 896
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 867 RVMAGKSLAEQGVTKEVIPPYYSVKEVVLPFNKFPGVDPLLGPEMRSTGEVMGVGRTFAEAFAKAQLGSNSTMKKHGRAL 946
Cdd:PLN02735 897 LVMSGKSLKDLGFTEEVIPAHVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLPLSGTVF 976
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 947 LSVREGDKERVVDLAAKLLKQGFELDATHGTAIVLGEAGINPRLVNKVHEGRPHIQDRIKNGEYTYIINTTSGRRA-IED 1025
Cdd:PLN02735 977 ISLNDLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVLKLHEGRPHAGDMLANGQIQLMVITSSGDALdQKD 1056
|
1050 1060 1070
....*....|....*....|....*....|.
1C3O_C 1026 SRVIRRSALQYKVHYDTTLNGGFATAMALNA 1056
Cdd:PLN02735 1057 GRQLRRMALAYKVPIITTVAGALATAQAVKS 1087
|
|
| 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: 1503.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 1 MPKRTDIKSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPIHWEVVRKIIEK 80
Cdd:PRK12815 1 MPKDTDIQKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 81 ERPDAVLPTMGGQTALNCALELERQGVLEEFGVTMIGATADAIDKAEDRRRFDVAMKKIGLETARSGIAHTMEEALAVAA 160
Cdd:PRK12815 81 EKPDALLATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 161 DVGFPCIIRPSFTMGGSGGGIAYNREEFEEICARGLDLSPTKELLIDESLIGWKEYEMEVVRDKNDNCIIVCSIENFDAM 240
Cdd:PRK12815 161 KIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 241 GIHTGDSITVAPAQTLTDKEYQIMRNASMAVLREIGVeTGGSNVQFAVNPKNGRLIVIEMNPRVSRSSALASKATGFPIA 320
Cdd:PRK12815 241 GIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGV-VGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 321 KVAAKLAVGYTLDELMNDITgGRTPASFEPSIDYVVTKIPRFNFEKFAGANDRLTTQMKSVGEVMAIGRTQQESLQKALR 400
Cdd:PRK12815 320 KIAAKLAVGYTLNELKNPVT-GLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 401 GLEVGATGFDPKVSLdDPEALTKIRRELKDAGADRIWYIADAFRAGLSVDGVFNLTNIDRWFLVQIEELVRLEEKVAEVG 480
Cdd:PRK12815 399 SLEIKRNGLSLPIEL-SGKSDEELLQDLRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEDG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 481 ITgLNADFLRQLKRKGFADARLAKLAGVREAEIRKLRDQYDLHPVYKRVDTCAAEFATDTAYMYSTYEEECEANPSTDRE 560
Cdd:PRK12815 478 LD-LSADLLRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGESEAEPSSEKK 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 561 KIMVLGGGPNRIGQGIEFDYCCVHASLALREDGYETIMVNCNPETVSTDYDTSDRLYFEPVTLEDVLEIVRIEKPKGVIV 640
Cdd:PRK12815 557 KVLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIV 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 641 QYGGQTPLKLARALEAAGVPVIGTSPDAIDRAEDRERFQHAVERLKLKQPANATVTAIEMAVEKAKEIGYPLVVRPSYVL 720
Cdd:PRK12815 637 QFGGQTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVI 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 721 GGRAMEIVYDEADLRRYFQTAvsVSNDAPVLLDHFLdDAVEVDVDAICDGEMVLIGGIMEHIEQAGVHSGDSACSLPAYT 800
Cdd:PRK12815 717 GGQGMAVVYDEPALEAYLAEN--ASQLYPILIDQFI-DGKEYEVDAISDGEDVTIPGIIEHIEQAGVHSGDSIAVLPPQS 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 801 LSQEIQDVMRQQVQKLAFELQVRGLMNVQFAVKNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAARVMAGKSLAEQGVT 880
Cdd:PRK12815 794 LSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLAELGYP 873
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 881 KEVIP--PYYSVKEVVLPFNKFPGVDPLLGPEMRSTGEVMGVGRTFAEAFAKAQLGSNSTMKKHGRALLSVREGDKERVV 958
Cdd:PRK12815 874 NGLWPgsPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGTIFISVRDEDKPEVT 953
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 959 DLAAKLLKQGFELDATHGTAIVLGEAGINPRLVNKVHEGRPHIQDRIKNGEYTYIINTTSGRRAIEDSRVIRRSALQYKV 1038
Cdd:PRK12815 954 KLARRFAQLGFKLLATEGTANWLAEEGITTGVVEKVQEGSPSLLERIKQHRIVLVVNTSLSDSASEDAIKIRDEALSTHI 1033
|
1050 1060 1070
....*....|....*....|....*....|.
1C3O_C 1039 HYDTTLNGGFATAMALNADATEkVISVQEMH 1069
Cdd:PRK12815 1034 PVFTELETAQAFLQVLESLALT-TQPIQELQ 1063
|
|
| 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: 770.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 13 LGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPIHWEVVRKIIEKERPDAVLPTMGG 92
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 93 QTALNCALELERQGVLEefGVTMIGATADAIDKAEDRRRFDVAMKKIGLETARSGIAHTMEEALAVAADVGFPCIIRPSF 172
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 173 TMGGSGGGIAYNREEFEEICARGLDLSPTKELLIDESLIGWKEYEMEVVRDKNDNCIIVCSIENFDAMGIHTGDSITVAP 252
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 253 AQTLTDKEYQIMRNASMAVLREIGVEtGGSNVQFAVnpKNGRLIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTL 332
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVV-GLCNIQFAV--DDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 333 DELMNDiTGgrtpasFEPSIDYVVTKIPRFNFEKFAGANDRLTTQMKSVGEVMAIGRTQQESLQKALRGLEVGATG--FD 410
Cdd:COG0458 316 DELGND-TG------FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 411 PKVSLDDPEALTKIRRELkdagaDRIWYIADAFRAGLSVDGVFNLTNIDRWFLVQIEELVRLEEKVAEVgitGLNADFLR 490
Cdd:COG0458 389 SLVADDDKEEALLLARRL-----ARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEI---ILVINTLL 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1C3O_C 491 QLKRKGFADARLAKLAGVREAEIRKLRDQYDLHPVYKRVDTCAAEFATDTAYMYSTYEEECEANPSTDREKIMVLG 566
Cdd:COG0458 461 GAKSLGDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
565-1067 |
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: 765.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 565 LGGGPNRIGQGIEFDYCCVHASLALREDGYETIMVNCNPETVSTDYDTSDRLYFEPVTLEDVLEIVRIEKPKGVIVQYGG 644
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 645 QTPLKLARALEAA----GVPVIGTSPDAIDRAEDRERFQHAVERLKLKQPANATVTAIEMAVEKAKEIGYPLVVRPSYVL 720
Cdd:COG0458 81 QTALNLAVELEEAgileGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 721 GGRAMEIVYDEADLRRYFQTAVSVSNDAPVLLDHFLDDAVEVDVDAICDGEM-VLIGGIMEHIEQAGVHSGDSACSLPAY 799
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDnVIIVGIMEHIEPAGVHSGDSICVAPPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 800 TLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAVKNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAARVMAGKSLAEQGV 879
Cdd:COG0458 241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 880 TKEVIP--PYYSVKEVVLPFNKFPGVDPLLGPEMRSTGEVMGVGRTFAEAFAKAQLGSNstMKKHGRALLS-VREGDKER 956
Cdd:COG0458 321 DTGFEPtlDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLE--IGLPGTVLLSlVADDDKEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 957 VVDLAAKLLKQGFELDATHGTAIVLGEAGINPRLVNKVHEGRPHIQDRIKNGEYTYIINTTSGRRAIEDSRVIRRSALQY 1036
Cdd:COG0458 399 ALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVINTLLGAKSLGDSDGIIRRALAA 478
|
490 500 510
....*....|....*....|....*....|.
1C3O_C 1037 KVHYDTTLNGGFATAMALNADATEKVISVQE 1067
Cdd:COG0458 479 KVPYVTTLAAAAAAALAIKAVETEAGEFEEA 509
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
128-333 |
2.06e-92 |
|
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: 293.44 E-value: 2.06e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 128 DRRRFDVAMKKIGLETARSGIA--HTMEEALAVAADVGFPCIIRPSFTMGGSGGGIAYNREEFEEICARGLDLSPT---- 201
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGpvETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 202 KELLIDESLIGWKEYEMEVVRDKNDNCIIVCSIENFDAMgiHTGDSITVAPAQTLTDKEYQIMRNASMAVLREIGVETGG 281
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
1C3O_C 282 sNVQFAVNPKNGRLIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLD 333
Cdd:pfam02786 159 -TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
538-931 |
2.65e-78 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 278.97 E-value: 2.65e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 538 TDTAYMYSTYEEECEANPSTDREKIMVLGGGPNRIGQGIEFDYCCVHASLALREDGYETIMVNCNPETVSTDYDTSDRLY 617
Cdd:PLN02735 2 SLADTVTRAWSAATKAGKRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 618 FEPVTLEDVLEIVRIEKPKGVIVQYGGQTPLKLARA------LEAAGVPVIGTSPDAIDRAEDRERFQHAVERLKLKQPA 691
Cdd:PLN02735 82 IAPMTPELVEQVIAKERPDALLPTMGGQTALNLAVAlaesgiLEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 692 NATVTAIEMAVEKAKEIG-YPLVVRPSYVLGGRAMEIVYDEADLRRYFQTAVSVSNDAPVLLDHFLDDAVEVDVDAICD- 769
Cdd:PLN02735 162 SGIATTLDECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDl 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 770 GEMVLIGGIMEHIEQAGVHSGDSACSLPAYTLSQEIQDVMRQQVQKLAFELQVR-GLMNVQFAV--KNNEVYLIEVNPRA 846
Cdd:PLN02735 242 ADNVVIICSIENIDPMGVHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVEcGGSNVQFAVnpVDGEVMIIEMNPRV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 847 ARTVPFVSKATGVPLAKVAARVMAGKSLAE--QGVTKEViPPYY--SVKEVV-----LPFNKFPGVDPLLGPEMRSTGEV 917
Cdd:PLN02735 322 SRSSALASKATGFPIAKMAAKLSVGYTLDQipNDITLKT-PASFepSIDYVVtkiprFAFEKFPGSQPILTTQMKSVGEA 400
|
410
....*....|....
1C3O_C 918 MGVGRTFAEAFAKA 931
Cdd:PLN02735 401 MALGRTFQESFQKA 414
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
424-547 |
1.70e-62 |
|
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: 207.69 E-value: 1.70e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 424 IRRELKDAGADRIWYIADAFRAGLSVDGVFNLTNIDRWFLVQIEELVRLEEKVAEVGITGLNADFLRQLKRKGFADARLA 503
Cdd:smart01096 1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
1C3O_C 504 KLAGVREAEIRKLRDQYDLHPVYKRVDTCAAEFATDTAYMYSTY 547
Cdd:smart01096 81 KLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
943-1052 |
3.13e-46 |
|
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: 161.11 E-value: 3.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 943 GRALLSVREGDKERVVDLAAKLLKQGFELDATHGTAIVLGEAGINPRLVNKVHEGRPHIQDRIKNGEYTYIINTTSGRRA 1022
Cdd:cd01424 1 GTVFISVADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEGRPNIVDLIKNGEIQLVINTPSGKRA 80
|
90 100 110
....*....|....*....|....*....|
1C3O_C 1023 IEDSRVIRRSALQYKVHYDTTLNGGFATAM 1052
Cdd:cd01424 81 IRDGFSIRRAALEYKVPYFTTLDTARAAVE 110
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
944-1050 |
2.24e-36 |
|
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: 133.02 E-value: 2.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 944 RALLSVREGDKERVVDLAAKLLKQGFELDATHGTAIVLGEAGINPRLVNKVHE-GRPHIQDRIKN-GEYTYIINTTSGRR 1021
Cdd:cd00532 1 GVFLSVSDHVKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRHEdGEPTVDAAIAEkGKFDVVINLRDPRR 80
|
90 100 110
....*....|....*....|....*....|..
1C3O_C 1022 A---IEDSRVIRRSALQYKVHYDTTLNGGFAT 1050
Cdd:cd00532 81 DrctDEDGTALLRLARLYKIPVTTPNATAMFV 112
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
674-874 |
3.17e-36 |
|
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: 136.28 E-value: 3.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 674 DRERFQHAVERLKLKQP--ANATVTAIEMAVEKAKEIGYPLVVRPSYVLGGRAMEIVYDEADLRRYFQTAVSVSNDAP-- 749
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVpgTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 750 --VLLDHFLDDAVEVDVDAICDGE-MVLIGGIMEHIEQagVHSGDSACSLPAYTLSQEIQDVMRQQVQKLAFELQVRGLM 826
Cdd:pfam02786 81 pqVLVEKSLKGPKHIEYQVLRDAHgNCITVCNRECSDQ--RRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
1C3O_C 827 NVQFAV--KNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAARVMAGKSL 874
Cdd:pfam02786 159 TVEFALdpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
426-505 |
4.62e-31 |
|
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: 116.71 E-value: 4.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 426 RELKDAGADRIWYIADAFRAGLSVDGVFNLTNIDRWFLVQIEELVRLEEKVAEVGITgLNADFLRQLKRKGFADARLAKL 505
Cdd:pfam02787 1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAGLD-LDAELLREAKRLGFSDRQIAKL 79
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
72-329 |
9.41e-27 |
|
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: 110.73 E-value: 9.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 72 EVVRKIIEKERPDAVLPTmggqtalnCALELERQGVL-EEFGVTmiGATADAIDKAEDRRRFDVAMKKIGLETARSGIAH 150
Cdd:COG0439 7 AAAAELARETGIDAVLSE--------SEFAVETAAELaEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 151 TMEEALAVAADVGFPCIIRPSFTMGGSGGGIAYNREE----FEEICARGLDLSPTKELLIDESLIGwKEYEME-VVRDKN 225
Cdd:COG0439 77 SPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEEleaaLAEARAEAKAGSPNGEVLVEEFLEG-REYSVEgLVRDGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 226 dncIIVCSI---ENFDAMGIHTGDsitVAPAQtLTDKEYQIMRNASMAVLREIGVETGGSNVQFAVNPkNGRLIVIEMNP 302
Cdd:COG0439 156 ---VVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELVARALRALGYRRGAFHTEFLLTP-DGEPYLIEINA 227
|
250 260
....*....|....*....|....*....
1C3O_C 303 RVS--RSSALASKATGFPIAKVAAKLAVG 329
Cdd:COG0439 228 RLGgeHIPPLTELATGVDLVREQIRLALG 256
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
651-872 |
1.32e-24 |
|
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: 104.57 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 651 ARALEAAGVPviGTSPDAIDRAEDRERFQHAVERLKLKQPANATVTAIEMAVEKAKEIGYPLVVRPSYVLGGRAMEIVYD 730
Cdd:COG0439 33 AELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 731 EADLRRYFQTAVS----VSNDAPVLLDHFLdDAVEVDVDAICDGEMVLIGGIMEHIeQAGVHSGDSACSLPAyTLSQEIQ 806
Cdd:COG0439 111 EEELEAALAEARAeakaGSPNGEVLVEEFL-EGREYSVEGLVRDGEVVVCSITRKH-QKPPYFVELGHEAPS-PLPEELR 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 807 DVMRQQVQKLAFELQV-RGLMNVQFAV-KNNEVYLIEVNPRA--ARTVPFVSKATGVPLAKVAARVMAGK 872
Cdd:COG0439 188 AEIGELVARALRALGYrRGAFHTEFLLtPDGEPYLIEINARLggEHIPPLTELATGVDLVREQIRLALGE 257
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
956-1042 |
1.41e-24 |
|
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: 98.70 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 956 RVVDLAAKLLKQGFELDATHGTAIVLGEAGINP--RLVNKVHEGRPHIQDRIKNGEYTYIINTTSG--RRAIEDSRVIRR 1031
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPVvkTLHPKVHGGIPQILDLIKNGEIDLVINTLYPfeAQAHEDGYSIRR 80
|
90
....*....|.
1C3O_C 1032 SALQYKVHYDT 1042
Cdd:smart00851 81 AAENIDIPGPT 91
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
956-1042 |
8.88e-23 |
|
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: 93.71 E-value: 8.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 956 RVVDLAAKLLKQGFELDATHGTAIVLGEAGINPR-LVNKVHEGRPH----IQDRIKNGEYTYIINTTSGRRAIE-DSRVI 1029
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTeVVEKTGEGRPGgrvqIGDLIKNGEIDLVINTLYPFKATVhDGYAI 80
|
90
....*....|...
1C3O_C 1030 RRSALQYKVHYDT 1042
Cdd:pfam02142 81 RRAAENIDIPGPT 93
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
623-852 |
5.88e-18 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 86.48 E-value: 5.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 623 LEDVLEIVRIEKPKGVIVqyGGQTPLK-LAR---ALEAAGVPVIGTSPDAIDRAEDRERFQHAVERLKLKQPANATVTAI 698
Cdd:PRK12767 58 IDRLLDICKKEKIDLLIP--LIDPELPlLAQnrdRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 699 EMAVE--KAKEIGYPLVVRPSYVLGGRAMEIVYDEADLRRYFQTAvsvsndAPVLLDHFLDDAvEVDVDAICDGEMVLIG 776
Cdd:PRK12767 136 EDFKAalAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYV------PNLIIQEFIEGQ-EYTVDVLCDLNGEVIS 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1C3O_C 777 GI-MEHIEqagVHSGDSacsLPAYTlsqEIQDVMRQQVQKLAFELQVRGLMNVQFAVKNNEVYLIEVNPRAARTVPF 852
Cdd:PRK12767 209 IVpRKRIE---VRAGET---SKGVT---VKDPELFKLAERLAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPL 276
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
10-314 |
1.25e-16 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 82.24 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 10 ILILGAGpivigqacefdySGAQACKALREE--GYRVILV---NSNPATIMTD-----PEMADATYIEPIHwevvrKIIE 79
Cdd:PRK12767 4 ILVTSAG------------RRVQLVKALKKSllKGRVIGAdisELAPALYFADkfyvvPKVTDPNYIDRLL-----DICK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 80 KERPDAVLPTMGGQTALNCAlELERqgvLEEFGVTMIGATADAIDKAEDRRRFDVAMKKIGLETARSGIAHTMEEALAV- 158
Cdd:PRK12767 67 KEKIDLLIPLIDPELPLLAQ-NRDR---FEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAAl 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 159 -AADVGFPCIIRPSFTMGGSGGGIAYNREEFEEICARGldlsptKELLIDESLIGwKEYEMEVVRDKNDNCIIVCSIENF 237
Cdd:PRK12767 143 aKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYV------PNLIIQEFIEG-QEYTVDVLCDLNGEVISIVPRKRI 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1C3O_C 238 DAMGIHTGDSITVapaqtltdkEYQIMRNASMAVLREIGvETGGSNVQFAVNpkNGRLIVIEMNPRVSRSSALASKA 314
Cdd:PRK12767 216 EVRAGETSKGVTV---------KDPELFKLAERLAEALG-ARGPLNIQCFVT--DGEPYLFEINPRFGGGYPLSYMA 280
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
555-884 |
2.91e-16 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 81.90 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 555 PSTDREKIMVLGGGPNrigqgiefDYCCVHAslaLREDGYETIMVNCNPETVSTDYDTSDRLYFEP-------VTLEDVL 627
Cdd:COG3919 1 AMTMRFRVVVLGGDIN--------ALAVARS---LGEAGVRVIVVDRDPLGPAARSRYVDEVVVVPdpgddpeAFVDALL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 628 EIVRiEKPKGVIVQYGGQTPLKLARALE--AAGVPVIGTSPDAIDRAEDRERFQHAVERLKLKQPANATVTAIEMAVEKA 705
Cdd:COG3919 70 ELAE-RHGPDVLIPTGDEYVELLSRHRDelEEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 706 KEIGYPLVVRPSY--------VLGGRAMEIVYDEADLRRYFQTAVSvsNDAPVLLDHFL--DDAVEVDVDAICD--GEMV 773
Cdd:COG3919 149 EDLGFPVVVKPADsvgydelsFPGKKKVFYVDDREELLALLRRIAA--AGYELIVQEYIpgDDGEMRGLTAYVDrdGEVV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 774 LIGG---IMEHIEQAGVhsgdsacslPAYTLSQEIQDVMRQqVQKLAFELQVRGLMNVQFAV--KNNEVYLIEVNPRAAR 848
Cdd:COG3919 227 ATFTgrkLRHYPPAGGN---------SAARESVDDPELEEA-ARRLLEALGYHGFANVEFKRdpRDGEYKLIEINPRFWR 296
|
330 340 350
....*....|....*....|....*....|....*.
1C3O_C 849 TVPFVSKAtGVPLAKVAARVMAGKSLAEQGVTKEVI 884
Cdd:COG3919 297 SLYLATAA-GVNFPYLLYDDAVGRPLEPVPAYREGV 331
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
9-329 |
4.41e-15 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 78.43 E-value: 4.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 9 SILILGAGPIVIGqacefdysgaqACKALREEGYRVILVNSNPATIMT------------DPEMADATYIEpihweVVRK 76
Cdd:COG3919 7 RVVVLGGDINALA-----------VARSLGEAGVRVIVVDRDPLGPAArsryvdevvvvpDPGDDPEAFVD-----ALLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 77 IIEKERPDAVLPTMggqtalNCALEL--ERQGVLEEfGVTMIGATADAIDKAEDRRRFDVAMKKIGLETARSGIAHTMEE 154
Cdd:COG3919 71 LAERHGPDVLIPTG------DEYVELlsRHRDELEE-HYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 155 ALAVAADVGFPCIIRPS--------FTMGGSGGGIAYNREEFEEICARGLDLSPtkELLIDESLIGWKEYE--MEVVRDK 224
Cdd:COG3919 144 LDALAEDLGFPVVVKPAdsvgydelSFPGKKKVFYVDDREELLALLRRIAAAGY--ELIVQEYIPGDDGEMrgLTAYVDR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 225 NDNCIIVCSIENF----DAMGIHTGdsITVAPAQTLTDkeyqimrnASMAVLREIGVeTGGSNVQFAVNPKNGRLIVIEM 300
Cdd:COG3919 222 DGEVVATFTGRKLrhypPAGGNSAA--RESVDDPELEE--------AARRLLEALGY-HGFANVEFKRDPRDGEYKLIEI 290
|
330 340
....*....|....*....|....*....
1C3O_C 301 NPRVSRSSALASKAtGFPIAKVAAKLAVG 329
Cdd:COG3919 291 NPRFWRSLYLATAA-GVNFPYLLYDDAVG 318
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
651-875 |
6.83e-15 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 78.64 E-value: 6.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 651 ARALEAAGVPVIGTSPDAI----DRAEDRERFQHAveRLKLKQPANATVTAIEMAVEKAKEIGYPLVVRPSYVLGGRAME 726
Cdd:PRK12833 95 AEAVEAAGLIFVGPDAQTIrtmgDKARARRTARRA--GVPTVPGSDGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIR 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 727 IVYDEADLRRYFQTAVSVSN----DAPVLLDHFLDDAVEVDVDAICDGEMVliggimehieqagVHSGDSACSL------ 796
Cdd:PRK12833 173 VAHDAAQLAAELPLAQREAQaafgDGGVYLERFIARARHIEVQILGDGERV-------------VHLFERECSLqrrrqk 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 797 -----PAYTLSQEIQDVMRQQVQKLAFELQVRGLMNVQ--FAVKNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAARVM 869
Cdd:PRK12833 240 ileeaPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEylFDDARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIA 319
|
....*.
1C3O_C 870 AGKSLA 875
Cdd:PRK12833 320 DGEPLR 325
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
649-875 |
3.57e-13 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 73.48 E-value: 3.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 649 KLARALEAAGVPVIGTSPDAIDRAEDRERFQHAVER--LKLKQPANATVTAIEMAVEKAKEIGYPLVVRPSYVLGGRAME 726
Cdd:PRK08654 90 EFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKagVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 727 IVYDEADLRRYFQTAVSVSN----DAPVLLDHFLDDAVEVDVDAICDGEmvliGGImehieqagVHSGDSACSL------ 796
Cdd:PRK08654 170 VVYSEEELEDAIESTQSIAQsafgDSTVFIEKYLEKPRHIEIQILADKH----GNV--------IHLGDRECSIqrrhqk 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 797 -----PAYTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAVKNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAARVMAG 871
Cdd:PRK08654 238 lieeaPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAG 317
|
....
1C3O_C 872 KSLA 875
Cdd:PRK08654 318 EELS 321
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
109-340 |
4.24e-13 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 73.09 E-value: 4.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 109 EEFGVTMIGATADAIDKAEDRRRFDVAMKKIG---LETARSGIAhTMEEALAVAADVGFPCIIRPSFTMGGSGGGIAYNR 185
Cdd:PRK08654 96 EKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGvpvLPGTEEGIE-DIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 186 EEFEEICARGLDLS------PTkeLLIDESLIGWKEYEMEVVRDKNDNCIIV----CSIENFdamgiHTgDSITVAPAQT 255
Cdd:PRK08654 175 EELEDAIESTQSIAqsafgdST--VFIEKYLEKPRHIEIQILADKHGNVIHLgdreCSIQRR-----HQ-KLIEEAPSPI 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 256 LTDKEYQIMRNASMAVLREIGVETGGSnVQFAVNpkNGRLIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLDEL 335
Cdd:PRK08654 247 MTPELRERMGEAAVKAAKAINYENAGT-VEFLYS--NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELSFK 323
|
....*
1C3O_C 336 MNDIT 340
Cdd:PRK08654 324 QEDIT 328
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
649-874 |
4.36e-13 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 72.91 E-value: 4.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 649 KLARALEAAGVPVIGTSPDAIDRAEDRERFQHAVERLKLkqP----ANATVTAIEMAVEKAKEIGYPLVVRPSYVLGGRA 724
Cdd:PRK08591 90 DFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGV--PvvpgSDGPVDDEEEALAIAKEIGYPVIIKATAGGGGRG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 725 MEIVYDEADLRRYFQTA-----VSVSNDApVLLDHFLDDAVEVDVDAICDGEmvliGGImehieqagVHSGDSACSL--- 796
Cdd:PRK08591 168 MRVVRTEAELEKAFSMAraeakAAFGNPG-VYMEKYLENPRHIEIQVLADGH----GNA--------IHLGERDCSLqrr 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 797 --------PAYTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAV-KNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAAR 867
Cdd:PRK08591 235 hqkvleeaPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYeKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIR 314
|
....*..
1C3O_C 868 VMAGKSL 874
Cdd:PRK08591 315 IAAGEPL 321
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
650-875 |
1.06e-12 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 71.60 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 650 LARALEAAGVPVIGTSPDAIDRAEDRerfqhaVERLKLKQPANATV--------TAIEMAVEKAKEIGYPLVVRPSYVLG 721
Cdd:PRK06111 91 FAERCKEEGIVFIGPSADIIAKMGSK------IEARRAMQAAGVPVvpgittnlEDAEEAIAIARQIGYPVMLKASAGGG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 722 GRAMEIVYDEADLRRYFQT----AVSVSNDAPVLLDHFLDDAVEVDVDAICDGEmvliggimEHIeqagVHSGDSACSL- 796
Cdd:PRK06111 165 GIGMQLVETEQELTKAFESnkkrAANFFGNGEMYIEKYIEDPRHIEIQLLADTH--------GNT----VYLWERECSVq 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 797 ----------PAYTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAVKNNE-VYLIEVNPRAARTVPFVSKATGVPLAKVA 865
Cdd:PRK06111 233 rrhqkvieeaPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKnFYFLEMNTRLQVEHPVTEEITGIDLVEQQ 312
|
250
....*....|
1C3O_C 866 ARVMAGKSLA 875
Cdd:PRK06111 313 LRIAAGEKLS 322
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
625-879 |
1.65e-12 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 72.09 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 625 DVLEIVRIEKPKGVIVQYGGQTPL----KLARALEAAGVPVIGTSPDAIDRAEDRERFQHAVERLKLKQ-PANAT-VTAI 698
Cdd:PRK12999 66 DIDEIIRVAKQAGVDAIHPGYGFLsenpEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPViPGSEGpIDDI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 699 EMAVEKAKEIGYPLVVRPSYVLGGRAMEIVYDEADLRRYFQTAVSVS-----NDApVLLDHFLDDAVEVDVDAICDGEmv 773
Cdd:PRK12999 146 EEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAkaafgNDE-VYLEKYVENPRHIEVQILGDKH-- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 774 liGGImehieqagVHSGDSACSL-----------PAYTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAV-KNNEVYLIE 841
Cdd:PRK12999 223 --GNV--------VHLYERDCSVqrrhqkvveiaPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVdADGNFYFIE 292
|
250 260 270 280
....*....|....*....|....*....|....*....|
1C3O_C 842 VNPR--AARTVpfVSKATGVPLAKVAARVMAGKSLAEQGV 879
Cdd:PRK12999 293 VNPRiqVEHTV--TEEVTGIDIVQSQILIAEGATLHDLEI 330
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
654-875 |
2.03e-12 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 70.51 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 654 LEAAGVPVIGTSPDAIDRAEDrerfqhaverlklkqpanatvtaiemAVEKAKEIGYPLVVRPSYVLGGRAMEIVYDEAD 733
Cdd:PRK05586 123 MIKAGVPVVPGSEGEIENEEE--------------------------ALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 734 LRRYFQTAVSVS----NDAPVLLDHFLDDAVEVDVDAICDGemvlIGGImehieqagVHSGDSACSL-----------PA 798
Cdd:PRK05586 177 LIKAFNTAKSEAkaafGDDSMYIEKFIENPKHIEFQILGDN----YGNV--------VHLGERDCSLqrrnqkvleeaPS 244
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1C3O_C 799 YTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAV-KNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAARVMAGKSLA 875
Cdd:PRK05586 245 PVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLS 322
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
21-339 |
2.27e-12 |
|
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: 68.98 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 21 GQACEFD---YSGAQACKALREEGYRVILVNSNPATIMTDpemadatyiepihwevvrkiIEKERPDAVLPTMGGQTALN 97
Cdd:COG1181 9 GRSAEREvslKSGRAVAAALDKAGYDVVPIGIDVEDLPAA--------------------LKELKPDVVFPALHGRGGED 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 98 CALelerQGVLEEFGVTMIG----ATADAIDKAedrrrfdvAMKKI----GLETARSGI--AHTMEEALAVAADVGFPCI 167
Cdd:COG1181 69 GTI----QGLLELLGIPYTGsgvlASALAMDKA--------LTKRVlaaaGLPTPPYVVlrRGELADLEAIEEELGLPLF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 168 IRPSftMGGSGGGI--AYNREEFEEICARGLDLSPtkELLIDESLIGwKEYEMEVVrdKNDNCIIVCSIE--------NF 237
Cdd:COG1181 137 VKPA--REGSSVGVskVKNAEELAAALEEAFKYDD--KVLVEEFIDG-REVTVGVL--GNGGPRALPPIEivpengfyDY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 238 DAMGIhTGDSITVAPAQtLTDKEYQIMRNASMAVLREIGVEtGGSNVQFAVNPkNGRLIVIEMN--PRVSRSSalaskat 315
Cdd:COG1181 210 EAKYT-DGGTEYICPAR-LPEELEERIQELALKAFRALGCR-GYARVDFRLDE-DGEPYLLEVNtlPGMTPTS------- 278
|
330 340
....*....|....*....|....
1C3O_C 316 GFPIAkvAAklAVGYTLDELMNDI 339
Cdd:COG1181 279 LLPKA--AA--AAGISYEELIERI 298
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
109-404 |
4.85e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 66.20 E-value: 4.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 109 EEFGVTMIGATADAI----DKAEDRRrfdvAMKKIGLETArSGIAHTM---EEALAVAADVGFPCIIRPSFTMGGSGGGI 181
Cdd:PRK06111 96 KEEGIVFIGPSADIIakmgSKIEARR----AMQAAGVPVV-PGITTNLedaEEAIAIARQIGYPVMLKASAGGGGIGMQL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 182 AYNREE----FEEICARGLDLSPTKELLIDESLIGWKEYEMEVVRDKNDNCIIV----CSIENfdamgiHTGDSITVAPA 253
Cdd:PRK06111 171 VETEQEltkaFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLwereCSVQR------RHQKVIEEAPS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 254 QTLTDKEYQIMRNASMAVLREIGVETGGSnVQFAVNpKNGRLIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLD 333
Cdd:PRK06111 245 PFLDEETRKAMGERAVQAAKAIGYTNAGT-IEFLVD-EQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLS 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 334 ELMNDITG----------GRTPASFEPS----IDYVVTKIPRFNFEKFAGANDRLTTQMKS-VGEVMAIGRTQQESLQK- 397
Cdd:PRK06111 323 FTQDDIKRsghaievriyAEDPKTFFPSpgkiTDLTLPGGEGVRHDHAVENGVTVTPFYDPmIAKLIAHGETREEAISRl 402
|
....*....
1C3O_C 398 --ALRGLEV 404
Cdd:PRK06111 403 hdALEELKV 411
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
109-339 |
6.25e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 65.89 E-value: 6.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 109 EEFGVTMIGATADAI----DKAEDRRrfdvAMKKIGLET--ARSGIAHTMEEALAVAADVGFPCIIRPsfTMGGSGGGI- 181
Cdd:PRK07178 95 AERGIKFIGPSAEVIrrmgDKTEARR----AMIKAGVPVtpGSEGNLADLDEALAEAERIGYPVMLKA--TSGGGGRGIr 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 182 ----------AYNREEFEEICARGldlspTKELLIDESLIGWKEYEMEVVRDKNDNCIIV----CSIENfdamgiHTGDS 247
Cdd:PRK07178 169 rcnsreeleqNFPRVISEATKAFG-----SAEVFLEKCIVNPKHIEVQILADSHGNVVHLferdCSIQR------RNQKL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 248 ITVAPAQTLTDKEYQIMRNASMAVLREIGVETGGSnVQFAVNpKNGRLIVIEMNPRVSRSSALASKATGFPIAKVAAKLA 327
Cdd:PRK07178 238 IEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGT-VEFLLD-ADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIA 315
|
250
....*....|..
1C3O_C 328 VGYTLDELMNDI 339
Cdd:PRK07178 316 SGLPLSYKQEDI 327
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
614-872 |
1.44e-10 |
|
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: 63.42 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 614 DRLYFEPVTLEDVLEIVRIEKPKGVIVQYGG-QTPLKLARALEAAGVPVIGtSPDAIDRAEDRERFQHAVERLKLKQPAN 692
Cdd:COG0189 36 DDLTLDLGRAPELYRGEDLSEFDAVLPRIDPpFYGLALLRQLEAAGVPVVN-DPEAIRRARDKLFTLQLLARAGIPVPPT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 693 ATVTAIEMAVEKAKEIGYPLVVRPSYVLGGRAMEIVYDEADLRRYFQTAVSVSNDaPVLLDHFLDDAVEVDVDAIC-DGE 771
Cdd:COG0189 115 LVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEALTELGSE-PVLVQEFIPEEDGRDIRVLVvGGE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 772 MVligGIMEHIEQAG-----VHSGDSACslpAYTLSQEiqdvMRQQVQKLA--FELQVRGlmnVQFAVKNNEVYLIEVNP 844
Cdd:COG0189 194 PV---AAIRRIPAEGefrtnLARGGRAE---PVELTDE----ERELALRAApaLGLDFAG---VDLIEDDDGPLVLEVNV 260
|
250 260
....*....|....*....|....*...
1C3O_C 845 RAArtVPFVSKATGVPLAKVAARVMAGK 872
Cdd:COG0189 261 TPG--FRGLERATGVDIAEAIADYLEAR 286
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
60-190 |
1.61e-10 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 64.39 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 60 MADAtyiepihwEVVRKIIEKERPDAVLPTMggqTALNCA--LELERQGvleeFGVTmigATADAIDKAEDR---RRFdv 134
Cdd:PRK09288 61 MLDG--------DALRAVIEREKPDYIVPEI---EAIATDalVELEKEG----FNVV---PTARATRLTMNRegiRRL-- 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
1C3O_C 135 AMKKIGLETARSGIAHTMEEALAVAADVGFPCIIRPsfTMGGSGGG--IAYNREEFEE 190
Cdd:PRK09288 121 AAEELGLPTSPYRFADSLEELRAAVEEIGYPCVVKP--VMSSSGKGqsVVRSPEDIEK 176
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
625-845 |
2.92e-10 |
|
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: 64.72 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 625 DVLEIVRIEKPKGVIVQYGGQTPL----KLARALEAAGVPVIGTSPDAIDRAEDRERFQHAVERLKLKQ-PANAT-VTAI 698
Cdd:COG1038 65 DIEEIIRVAKEKGVDAIHPGYGFLsenpEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPViPGTEGpVDDL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 699 EMAVEKAKEIGYPLVVRPSYVLGGRAMEIVYDEADLRRYFQTAVSVS-----NDApVLLDHFLDDA--VEVDVDAICDGE 771
Cdd:COG1038 145 EEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAkaafgDDE-VFLEKYIERPkhIEVQILGDKHGN 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 772 MVliggimeHIeqagvHSGDsaCSL-----------PAYTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAV-KNNEVYL 839
Cdd:COG1038 224 IV-------HL-----FERD--CSVqrrhqkvveiaPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVdDDGNFYF 289
|
....*.
1C3O_C 840 IEVNPR 845
Cdd:COG1038 290 IEVNPR 295
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
618-863 |
8.47e-10 |
|
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: 61.86 E-value: 8.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 618 FEPVTLED-VLEIVRIEKPKGVIvqYGG---QTPLKLARAleAAGVPVIGTSPDAIDRAEDRERFQHAVERLKLKQPAna 693
Cdd:COG2232 56 FDLEDLPAaLLELAAADDPDGLV--YGSgfeNFPELLERL--ARRLPLLGNPPEVVRRVKDPLRFFALLDELGIPHPE-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 694 TVTAIEMAvekakeiGYPLVVRPSYVLGGRAMEIVYDEADLR--RYFQ-----TAVSVSndapvlldhFLddavevdvda 766
Cdd:COG2232 130 TRFEPPPD-------PGPWLVKPIGGAGGWHIRPADSEAPPApgRYFQryvegTPASVL---------FL---------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 767 iCDG-EMVLIGGIMEHIEQAGVH----SGdsaCSLPaYTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAVKNNEVYLIE 841
Cdd:COG2232 184 -ADGsDARVLGFNRQLIGPAGERpfryGG---NIGP-LALPPALAEEMRAIAEALVAALGLVGLNGVDFILDGDGPYVLE 258
|
250 260
....*....|....*....|..
1C3O_C 842 VNPRAARTVPFVSKATGVPLAK 863
Cdd:COG2232 259 VNPRPQASLDLYEDATGGNLFD 280
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
635-862 |
1.33e-08 |
|
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: 57.36 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 635 PKGVIVQYGgqtpLKLARALEAAGVPVIgTSPDAIDRAEDRERFQHAVERLKLKQPANATVTAIEMAVEKAKEIGYPLVV 714
Cdd:TIGR00768 54 VRIVSMFRG----LAVLRYLESLGVPVI-NSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 715 RPSYVLGGRAMEIVYDEADLRRYFQTAVSVSNDAPV-LLDHFLDDAVEVDVDAICDGEMVLigGIMEHIE----QAGVHS 789
Cdd:TIGR00768 129 KPVFGSWGRGVSLARDRQAAESLLEHFEQLNGPQNLfLVQEYIKKPGGRDIRVFVVGDEVV--AAIYRITsghwRSNLAR 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1C3O_C 790 GDSACSLPaytLSQEIQDVMRQQVQklAFELQVRGlmnVQFAVKNNEVYLIEVNPraarTVPF--VSKATGVPLA 862
Cdd:TIGR00768 207 GGKAEPCS---LTEEIEELAIKAAK--ALGLDVAG---VDLLESEDGLLVNEVNA----NPEFknSVKTTGVNIA 269
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
109-339 |
1.68e-08 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 58.29 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 109 EEFGVTMIGATADAIDKAEDRRRFDVAMKKIGL------ETARSgiaHTMEEALAVAADVGFPCIIRPSFTMGGSGGGIA 182
Cdd:PRK08463 95 EDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIpivpgtEKLNS---ESMEEIKIFARKIGYPVILKASGGGGGRGIRVV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 183 YNREEFE---EICAR-GLDLSPTKELLIDESLIGWKEYEMEVVRDKNDNCIIV----CSIENfdamgiHTGDSITVAPAQ 254
Cdd:PRK08463 172 HKEEDLEnafESCKReALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLcerdCSIQR------RHQKVIEIAPCP 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 255 TLTDKEYQIMRNASMAVLREIGVETGGSnVQFAVNPKNgRLIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLDE 334
Cdd:PRK08463 246 SISDNLRKTMGVTAVAAAKAVGYTNAGT-IEFLLDDYN-RFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEILDL 323
|
....*
1C3O_C 335 LMNDI 339
Cdd:PRK08463 324 EQSDI 328
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
654-844 |
1.89e-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: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 654 LEAAGVPVIGTSPDAIDRAEDRERFQHAVERLKLKQPANATVTAIEMAV--EKAKEIGYPLVVRPsyVLGG--RAMEIVY 729
Cdd:COG1181 75 LELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRGELADleAIEEELGLPLFVKP--AREGssVGVSKVK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 730 DEADLRRYFQTAVSvsNDAPVLLDHFLDdAVEVDVdAICDGEMVLIGGIMEHIEQAGV-------HSGDSACSLPAyTLS 802
Cdd:COG1181 153 NAEELAAALEEAFK--YDDKVLVEEFID-GREVTV-GVLGNGGPRALPPIEIVPENGFydyeakyTDGGTEYICPA-RLP 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....
1C3O_C 803 QEIQDVMRQQVQKlAFE-LQVRGLMNVQFAV-KNNEVYLIEVNP 844
Cdd:COG1181 228 EELEERIQELALK-AFRaLGCRGYARVDFRLdEDGEPYLLEVNT 270
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
108-190 |
2.10e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 57.89 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 108 LEEFGVTMIGATADAI----DKAEDRRrfdvAMKKIGLET--ARSGIAHTMEEALAVAADVGFPCIIRPsfTMGGSGGGI 181
Cdd:PRK08591 95 CEDSGFTFIGPSAETIrlmgDKVTAKA----TMKKAGVPVvpGSDGPVDDEEEALAIAKEIGYPVIIKA--TAGGGGRGM 168
|
90
....*....|.
1C3O_C 182 --AYNREEFEE 190
Cdd:PRK08591 169 rvVRTEAELEK 179
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
109-304 |
3.64e-08 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 57.84 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 109 EEFGVTMIGATADAI----DKAEDRRrfdvAMKKIGLETARS--GIAHTMEEALAVAADVGFPCIIRPSftMGGSGGG-- 180
Cdd:PRK12999 100 AEAGITFIGPTAEVLrllgDKVAARN----AAIKAGVPVIPGseGPIDDIEEALEFAEEIGYPIMLKAS--AGGGGRGmr 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 181 IAYNREEFEEICAR---------GLDlsptkELLIDESLIGWKEYEMEVVRDKNDNciIV------CS--------IEnf 237
Cdd:PRK12999 174 IVRSEEELEEAFERakreakaafGND-----EVYLEKYVENPRHIEVQILGDKHGN--VVhlyerdCSvqrrhqkvVE-- 244
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1C3O_C 238 damgihtgdsitVAPAQTLTDKEYQIMRNASMAVLREIGVETGGSnVQFAVNPkNGRLIVIEMNPRV 304
Cdd:PRK12999 245 ------------IAPAPGLSEELRERICEAAVKLARAVGYVNAGT-VEFLVDA-DGNFYFIEVNPRI 297
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
658-877 |
6.13e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 56.29 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 658 GVPVIGTSPDAIDRAEDRERFQHAVER--LKLKQPANATVTAIEMAVEKAKEIGYPLVVRPSYVLGGRAMEIVYDEADLR 735
Cdd:PRK08462 101 NIKFIGPSVEVMALMSDKSKAKEVMKRagVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 736 RYF----QTAVSVSNDAPVLLDHFLDDAVEVDVDAICDGEmvliGGImehieqagVHSGDSACSL-----------PAYT 800
Cdd:PRK08462 181 NLYlaaeSEALSAFGDGTMYMEKFINNPRHIEVQILGDKH----GNV--------IHVGERDCSLqrrhqklieesPAVV 248
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1C3O_C 801 LSQEIQDVMRQQVQKLAFELQVRGLMNVQFAV-KNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAARVMAGKSLAEQ 877
Cdd:PRK08462 249 LDEKTRERLHETAIKAAKAIGYEGAGTFEFLLdSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPSQ 326
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
109-339 |
9.22e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 55.87 E-value: 9.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 109 EEFGVTMIGATADAIDKAEDRRRFDVAMKKIGLET--ARSGIAHTMEEALAVAADVGFPCIIRPSFTMGGSGGGIAYNRE 186
Cdd:PRK05586 96 KECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVvpGSEGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 187 EF---------EEICARGLDlsptkELLIDESLIGWKEYEMEVVRDKNDNCIIV----CSIENFDAMGIHTgdsitvAPA 253
Cdd:PRK05586 176 ELikafntaksEAKAAFGDD-----SMYIEKFIENPKHIEFQILGDNYGNVVHLgerdCSLQRRNQKVLEE------APS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 254 QTLTDKEYQIMRNASMAVLREIGVETGGSnVQFAVNpKNGRLIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLD 333
Cdd:PRK05586 245 PVMTEELRKKMGEIAVKAAKAVNYKNAGT-IEFLLD-KDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLS 322
|
....*.
1C3O_C 334 ELMNDI 339
Cdd:PRK05586 323 IKQEDI 328
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
35-191 |
1.13e-06 |
|
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: 51.48 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 35 KALREEGYRVILVNsnpatimtdpemADATYIEPIHWEVVRKIIEKERPDAVLPTmggQTALNCALELERQgvLEEFGVT 114
Cdd:COG0189 21 EAAQRRGHEVEVID------------PDDLTLDLGRAPELYRGEDLSEFDAVLPR---IDPPFYGLALLRQ--LEAAGVP 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1C3O_C 115 MIGaTADAIDKAEDRRRFDVAMKKIGLETARSGIAHTMEEALAVAADVGFPCIIRPSFTMGGSGGGIAYNREEFEEI 191
Cdd:COG0189 84 VVN-DPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESI 159
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
650-875 |
1.38e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 52.03 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 650 LARALEAAGVPVIGTSPDAIDRAEDRERFQHAVER--LKLKQPANATVTAIEMAVEKAKEIGYPLVVRPSYVLGGRAMEI 727
Cdd:PRK07178 90 LAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKagVPVTPGSEGNLADLDEALAEAERIGYPVMLKATSGGGGRGIRR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 728 VYDEADLRRYFQTAVSVSNDAPVLLDHFLDDAV------EVDVDAICDGEMvliggimehieqagVHSGDSACSL----- 796
Cdd:PRK07178 170 CNSREELEQNFPRVISEATKAFGSAEVFLEKCIvnpkhiEVQILADSHGNV--------------VHLFERDCSIqrrnq 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 797 ------PAYTLSQEiqdvMRQQVQKLAfelqVR-----GLMN---VQFAV-KNNEVYLIEVNPRAARTVPFVSKATGVPL 861
Cdd:PRK07178 236 klieiaPSPQLTPE----QRAYIGDLA----VRaakavGYENagtVEFLLdADGEVYFMEMNTRVQVEHTITEEITGIDI 307
|
250
....*....|....
1C3O_C 862 AKVAARVMAGKSLA 875
Cdd:PRK07178 308 VREQIRIASGLPLS 321
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
162-303 |
1.54e-06 |
|
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: 49.20 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 162 VGFPCIIRPSFTMGGSGGGIAYNREEFEEICARGL-DLSPTKEL-----------LIdESLIGWKEYEMEVVRDKNDNCI 229
Cdd:pfam13535 1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIReEIEQWKEMypeavvdggsfLV-EEYIEGEEFAVDAYFDENGEPV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1C3O_C 230 IVCSIENFDAMGIHTGDSITVAPAQTLTDKEYQIMrNASMAVLREIGVETGGSNVQFAVNpKNGRLIVIEMNPR 303
Cdd:pfam13535 80 ILNILKHDFASSEDVSDRIYVTSASIIRETQAAFT-EFLKRINALLGLKNFPVHIELRVD-EDGQIIPIEVNPL 151
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
29-301 |
5.08e-06 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 49.72 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 29 SGAQACKALREEGYRVILVnsnpatimtDPEMADATyiepihwevvrkIIEKERPDAVLptmggqTALN-------CAle 101
Cdd:PRK01372 24 SGAAVLAALREAGYDAHPI---------DPGEDIAA------------QLKELGFDRVF------NALHgrggedgTI-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 102 lerQGVLEEFGVTMIG----ATADAIDKAedrrRFDVAMKKIGLETARSGIAHTMEEALAVAADVGFPCIIRPSftMGGS 177
Cdd:PRK01372 75 ---QGLLELLGIPYTGsgvlASALAMDKL----RTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKPA--REGS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 178 GGG--IAYNREEFEEICARGLDLSPtkELLIDESLIGwKEYEMEVVRDKndnciIVCSIE--------NFDAMGIhTGDS 247
Cdd:PRK01372 146 SVGvsKVKEEDELQAALELAFKYDD--EVLVEKYIKG-RELTVAVLGGK-----ALPVIEivpagefyDYEAKYL-AGGT 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
1C3O_C 248 ITVAPAQtLTDKEYQIMRNASMAVLREIGVEtGGSNVQFAVNpKNGRLIVIEMN 301
Cdd:PRK01372 217 QYICPAG-LPAEIEAELQELALKAYRALGCR-GWGRVDFMLD-EDGKPYLLEVN 267
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
703-845 |
6.03e-06 |
|
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: 47.38 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 703 EKAKEIGYPLVVRPSYVLGGRAMEIVYDEADLRRYFQtavsvsndaPVLLDHFLDdAVEVDVDAICDGEMVLIGGI-MEH 781
Cdd:pfam02655 25 EELLREEKKYVVKPRDGCGGEGVRKVENGREDEAFIE---------NVLVQEFIE-GEPLSVSLLSDGEKALPLSVnRQY 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
1C3O_C 782 IEQAGVHSGDSACSLPA-YTLSQEIQDVMRQQVQKLAfelQVRGLMNVQFAVKNNEVYLIEVNPR 845
Cdd:pfam02655 95 IDNGGSGFVYAGNVTPSrTELKEEIIELAEEVVECLP---GLRGYVGVDLVLKDNEPYVIEVNPR 156
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
651-873 |
8.09e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 50.23 E-value: 8.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 651 ARALEAAGVPviGTSPDAIDRAEDRERFQHAVERLKLKQPANATVTAIEMAVEKAKEIGYPLVVRPSYVLGGRAMEIVYD 730
Cdd:PRK02186 86 SEVARRLGLP--AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCAS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 731 EADLRRYFQTAVSVSNDApVLLDHFLDDAvEVDVDAICDGEMVLIGGIMEHIEQAGVHSGDSACSLPAYTLS---QEIQD 807
Cdd:PRK02186 164 VAEAAAHCAALRRAGTRA-ALVQAYVEGD-EYSVETLTVARGHQVLGITRKHLGPPPHFVEIGHDFPAPLSApqrERIVR 241
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1C3O_C 808 VMRQQVQKLAFELqvrGLMNVQFAVKNNEVYLIEVNPR-AARTVP-FVSKATGVPLAKVAARVMAGKS 873
Cdd:PRK02186 242 TVLRALDAVGYAF---GPAHTELRVRGDTVVIIEINPRlAGGMIPvLLEEAFGVDLLDHVIDLHLGVA 306
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
946-1033 |
9.08e-06 |
|
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: 45.75 E-value: 9.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 946 LLSVREGDKERVVDLAAKLLKQGFELDATHGTAIVLGEAGINPRLVNKVHE----GRPHIQDRIKNGEYTYIINTTSGRR 1021
Cdd:cd01423 4 LISIGSYSKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEepqnDKPSLRELLAEGKIDLVINLPSNRG 83
|
90
....*....|....
1C3O_C 1022 AIEDSR--VIRRSA 1033
Cdd:cd01423 84 KRVLDNdyVMRRAA 97
|
|
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
944-1006 |
1.78e-05 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 48.55 E-value: 1.78e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1C3O_C 944 RALLSVreGDKERVVDLAAKLLKQGFELDATHGTAIVLGEAGINprlVNKVHE--GRPHIQD-RIK 1006
Cdd:PRK00881 6 RALISV--SDKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIP---VTEVSDvtGFPEILDgRVK 66
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
651-912 |
2.15e-05 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 48.27 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 651 ARALEAAGVPVIGTSPDAIDRAEDRE--RF---QHAVERLKLKQPANATvtAIEMAVEKAKEIGYPLVVRPSYVLGGRAM 725
Cdd:PRK08463 91 AKAVEDAGIIFIGPKSEVIRKMGNKNiaRYlmkKNGIPIVPGTEKLNSE--SMEEIKIFARKIGYPVILKASGGGGGRGI 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 726 EIVYDEADLRRYFQT----AVSVSNDAPVLLDHFLDDAVEVDVDAICDGemvlIGGImehieqagVHSGDSACSL----- 796
Cdd:PRK08463 169 RVVHKEEDLENAFESckreALAYFNNDEVFMEKYVVNPRHIEFQILGDN----YGNI--------IHLCERDCSIqrrhq 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 797 ------PAYTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAV-KNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAARVM 869
Cdd:PRK08463 237 kvieiaPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLdDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIA 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
1C3O_C 870 AGKSL-------AEQGVTKEVIPPYYSVKEVVLPF-NKFPGVDPLLGPEMR 912
Cdd:PRK08463 317 AGEILdleqsdiKPRGFAIEARITAENVWKNFIPSpGKITEYYPALGPSVR 367
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
1-190 |
2.40e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 48.21 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 1 MPKRtdIKSILILGAGPIVIgqacefdysgaQACKALREEGYRVILVNSN------PA-----TIMTDPEMADATYIEPi 69
Cdd:PRK12833 1 MPSR--IRKVLVANRGEIAV-----------RIIRAARELGMRTVAACSDadrdslAArmadeAVHIGPSHAAKSYLNP- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 70 hwEVVRKIIEKERPDAVLPTMGGqTALNCALelerQGVLEEFGVTMIGATADAI----DKAEDRRRFDVAmkkiGLET-- 143
Cdd:PRK12833 67 --AAILAAARQCGADAIHPGYGF-LSENAAF----AEAVEAAGLIFVGPDAQTIrtmgDKARARRTARRA----GVPTvp 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
1C3O_C 144 ARSGIAHTMEEALAVAADVGFPCIIRPSFTMGGSGGGIAYNREEFEE 190
Cdd:PRK12833 136 GSDGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAA 182
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
109-304 |
2.61e-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: 48.54 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 109 EEFGVTMIGATADAIDKAEDRRRFDVAMKKIGLETARS--GIAHTMEEALAVAADVGFPCIIRPSftMGGSGGG--IAYN 184
Cdd:COG1038 99 EEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGteGPVDDLEEALAFAEEIGYPVMLKAA--AGGGGRGmrVVRS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 185 REEFEEICAR---------GLDlsptkELLIDESLIGWKEYEMEVVRDKNDNciIV------CS--------IEnfdamg 241
Cdd:COG1038 177 EEELEEAFESarreakaafGDD-----EVFLEKYIERPKHIEVQILGDKHGN--IVhlferdCSvqrrhqkvVE------ 243
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
1C3O_C 242 ihtgdsitVAPAQTLTDKEYQIMRNASMAVLREIGVETGGSnVQFAVNpKNGRLIVIEMNPRV 304
Cdd:COG1038 244 --------IAPAPNLDEELREAICEAAVKLAKAVGYVNAGT-VEFLVD-DDGNFYFIEVNPRI 296
|
|
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
944-1006 |
4.27e-05 |
|
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: 47.33 E-value: 4.27e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1C3O_C 944 RALLSVreGDKERVVDLAAKLLKQGFELDATHGTAIVLGEAGINprlVNKVHE--GRPHIQD-RIK 1006
Cdd:COG0138 5 RALISV--SDKTGLVEFARALVELGVEIISTGGTAKALREAGIP---VTEVSEvtGFPEILDgRVK 65
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
653-845 |
8.62e-05 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 46.28 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 653 ALEAAGVPVIgtsPDAidRAE----DRE---RFqhAVERLKLKQPANATVTAIEMAVEKAKEIGYPLVVRPsyVLG--GR 723
Cdd:PRK09288 93 ELEKEGFNVV---PTA--RATrltmNREgirRL--AAEELGLPTSPYRFADSLEELRAAVEEIGYPCVVKP--VMSssGK 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 724 AMEIVYDEADLRRYFQTAVSVS--NDAPVLLDHFLDDAVEVDVDAIC--DGEMVLIGGImEHIEQagvhSGDSACSL-PA 798
Cdd:PRK09288 164 GQSVVRSPEDIEKAWEYAQEGGrgGAGRVIVEEFIDFDYEITLLTVRavDGGTHFCAPI-GHRQE----DGDYRESWqPQ 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
1C3O_C 799 yTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAVKNNEVYLIEVNPR 845
Cdd:PRK09288 239 -PMSPAALEEAQEIAKKVTDALGGRGLFGVELFVKGDEVYFSEVSPR 284
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
137-304 |
1.54e-04 |
|
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: 43.40 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 137 KKIGLETARSGIAHTMEEALAVAADVGFPCIIRPSfTMGGSGGGIAYNREEfeeicargLDLSPTKELLIDESLI--GWK 214
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKAR-RGGYDGKGQYVVRSE--------ADLPQAWEELGDGPVIveEFV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 215 EYEME----VVRDKNDNCIIVCSIENFDAMGIHTgdsITVAPAQTLTDKE---YQIMRNAsMAVLREIGVetggsnvqFA 287
Cdd:pfam02222 72 PFDRElsvlVVRSVDGETAFYPVVETIQEDGICR---LSVAPARVPQAIQaeaQDIAKRL-VDELGGVGV--------FG 139
|
170 180
....*....|....*....|
1C3O_C 288 VN---PKNGRLIVIEMNPRV 304
Cdd:pfam02222 140 VElfvTEDGDLLINELAPRP 159
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
117-305 |
2.40e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 45.22 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 117 GATADAIDKAEDRRRFDVAMKKIGLETARSGIAHTMEEALAVAADVGFPCIIRPSFTMGGSGGGIAYNREEFEEICARGL 196
Cdd:PRK02186 96 AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALR 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 197 DlSPTKELLIdESLIGWKEYEMEVVRDkNDNCIIVCSIENFDAMGIHTGDSITVAPAQTLTDKEYQIMRNASMAvLREIG 276
Cdd:PRK02186 176 R-AGTRAALV-QAYVEGDEYSVETLTV-ARGHQVLGITRKHLGPPPHFVEIGHDFPAPLSAPQRERIVRTVLRA-LDAVG 251
|
170 180
....*....|....*....|....*....
1C3O_C 277 VETGGSNVQFAVnpKNGRLIVIEMNPRVS 305
Cdd:PRK02186 252 YAFGPAHTELRV--RGDTVVIIEINPRLA 278
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
112-332 |
2.69e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 44.74 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 112 GVTMIGATADAIDKAEDRRRFDVAMKKIGLET--ARSGIAHTMEEALAVAADVGFPCIIRPSftMGGSGGGI-------- 181
Cdd:PRK08462 101 NIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVipGSDGALKSYEEAKKIAKEIGYPVILKAA--AGGGGRGMrvvedesd 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 182 ---AYNREEFEEICARGlDLSPTKELLIDESligwKEYEMEVVRDKNDNCIIV----CSIENfdamgiHTGDSITVAPAQ 254
Cdd:PRK08462 179 lenLYLAAESEALSAFG-DGTMYMEKFINNP----RHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAV 247
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1C3O_C 255 TLTDKEYQIMRNASMAVLREIGVETGGSnVQFAVNpKNGRLIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTL 332
Cdd:PRK08462 248 VLDEKTRERLHETAIKAAKAIGYEGAGT-FEFLLD-SNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL 323
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
683-845 |
5.33e-04 |
|
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: 41.86 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 683 ERLKLKQPANATVTAIEMAVEKAKEIGYPLVVRpSYVLG--GRAMEIVYDEADLrryfQTAVSVSNDAPVLLDHFLDDAV 760
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVK-ARRGGydGKGQYVVRSEADL----PQAWEELGDGPVIVEEFVPFDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 761 EVDVDAI--CDGEMVlIGGIMEHIEQAGVhsgdsaCSL---PAyTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAVKNN 835
Cdd:pfam02222 76 ELSVLVVrsVDGETA-FYPVVETIQEDGI------CRLsvaPA-RVPQAIQAEAQDIAKRLVDELGGVGVFGVELFVTED 147
|
170
....*....|.
1C3O_C 836 -EVYLIEVNPR 845
Cdd:pfam02222 148 gDLLINELAPR 158
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
653-850 |
2.99e-03 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 40.86 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 653 ALEAAGVPVIG----TSpdAIdrAEDRERFQHAVERLKLKQPANATVTAIEMAVEKAKEIGYPLVVRPsyVLGGR--AME 726
Cdd:PRK01372 77 LLELLGIPYTGsgvlAS--AL--AMDKLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKP--AREGSsvGVS 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 727 IVYDEADLRRYFQTAVSVsnDAPVLLDHFLdDAVEVDVdAICDGEMVligGIMEhIEQAGV--------HSGDSACSLPA 798
Cdd:PRK01372 151 KVKEEDELQAALELAFKY--DDEVLVEKYI-KGRELTV-AVLGGKAL---PVIE-IVPAGEfydyeakyLAGGTQYICPA 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1C3O_C 799 YtLSQEIQdvmrQQVQKLAFE----LQVRGLMNVQFAVKN-NEVYLIEVN-----------PRAARTV 850
Cdd:PRK01372 223 G-LPAEIE----AELQELALKayraLGCRGWGRVDFMLDEdGKPYLLEVNtqpgmtshslvPMAARAA 285
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
120-304 |
3.96e-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: 40.83 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 120 ADAIDKAEDR---RRFdvaMKKIGLETARSGIAHTMEEALAVAADVGFPCIIRPSfTMG--GSGGGIAYNREEFEEIcAR 194
Cdd:COG0026 81 PEALEIAQDRlleKAF---LAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTR-RGGydGKGQVVIKSAADLEAA-WA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 195 GLDLSPtkelLIDESLIgwkEYEME----VVRDKNDNCIIVCSIENfdamgIHTgDSI---TVAPAQtLTDKEYQIMRNA 267
Cdd:COG0026 156 ALGGGP----CILEEFV---PFERElsviVARSPDGEVATYPVVEN-----VHR-NGIldeSIAPAR-ISEALAAEAEEI 221
|
170 180 190 200
....*....|....*....|....*....|....*....|
1C3O_C 268 SMAVLREIGVeTGgsnVqFAVN---PKNGRLIVIEMNPRV 304
Cdd:COG0026 222 AKRIAEALDY-VG---V-LAVEffvTKDGELLVNEIAPRP 256
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
814-884 |
6.42e-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: 37.98 E-value: 6.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1C3O_C 814 QKLAFELQVRGLMNVQFAVKNNEVYLIEVNPRAARTVPfVSKATGVPLAKVAARVMAGKSLAEQGVTKEVI 884
Cdd:pfam15632 54 RRLAEAFGLDGLFNVQFRYDGDGPKLLEINPRMSGGIG-YSCLAGVNLPYLALKLLLGLETPDPVEPRLGL 123
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
654-756 |
9.89e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 39.75 E-value: 9.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C3O_C 654 LEAAGVPVigtspdaidraedrerfqhaverlklkqPANATVTAIEMAVEKAKEIGYPLVVRPSYVLGGRAMEI-VYDEA 732
Cdd:PRK14016 222 LAAAGVPV----------------------------PEGRVVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTVnITTRE 273
|
90 100
....*....|....*....|....
1C3O_C 733 DLRRYFQTAVSVSNDapVLLDHFL 756
Cdd:PRK14016 274 EIEAAYAVASKESSD--VIVERYI 295
|
|
| |
