|
Name |
Accession |
Description |
Interval |
E-value |
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
1-1064 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 2155.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 1 MPKRTDLKSILIIGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADVTYIEPILWQTVEKIIAK 80
Cdd:PRK05294 1 MPKRTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 81 ERPDAILPTMGGQTALNCALDLSRNGVLAKYNVELIGASEDAIDKAEDRGRFKEAMEKIGLKCPESYVCHSMNEALSAQA 160
Cdd:PRK05294 81 ERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 161 KVGFPTLIRPSFTMGGSGGGIAYNKEEFMAICERGFDASPTHELLIEQSVLGWKEYEMEVVRDKADNAIIICSIENFDPM 240
Cdd:PRK05294 161 EIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 241 GVHTGDSITVAPAQTLTDKEYQIMRNASLAVLREIGVDTGGSNVQFSVNPANGELIVIEMNPRVSRSSALASKATGFPIA 320
Cdd:PRK05294 241 GVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVETGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 321 KVAAKLAVGYTLNELSNDITGgRTPASFEPSIDYVVTKIPRFAFEKFPAADDRLTTQMKSVGEVMAMGRTLQESMQKALR 400
Cdd:PRK05294 321 KVAAKLAVGYTLDEIKNDITG-KTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 401 GLETGLCGFNPR---TTDKSVILRELVNPGPERILYVADAFRIGMSKEEIFDVCAIDPWFLMQIEDLMQEEAKVAAGTLa 477
Cdd:PRK05294 400 SLEIGVTGLDEDlfeEESLEELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGL- 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 478 DLDFATMRRLKRKGFSDKRLSQLLNVSEKAVRDARFALKLHPVYKRVDTCAAEFDTDTAYLYSTYEEECEARPTDKKKIM 557
Cdd:PRK05294 479 PLDAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVL 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 558 ILGGGPNRIGQGIEFDYCCVHASLALRESGFETIMVNCNPETVSTDFDTSDRLYFEPLTLEDVLEIVRVEQPYGVIVHYG 637
Cdd:PRK05294 559 VLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFG 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 638 GQTPLKLANALVENGVNIIGTSADSIDAAEDRERFQKVLHDLGLRQPENRTARNEEEAIVLANEVGYPLVVRPSYVLGGR 717
Cdd:PRK05294 639 GQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGR 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 718 AMQVVHSDDELRTYMNEAVQVSEDSPVLLDFFLNHAIEVDVDCVSDGQEVVIGGIMQHVEQAGVHSGDSGCSLPPYSLSA 797
Cdd:PRK05294 719 AMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICDGEDVLIGGIMEHIEEAGVHSGDSACSLPPQTLSE 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 798 EIQDEIRRQTKAMAKALNVVGLMNVQFAVQDDVVYVLEVNPRASRTVPFVSKATSVPLAKIAARAMAGISLAEQNFTTEV 877
Cdd:PRK05294 799 EIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGL 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 878 IPDYYSVKEAVFPFMKFPGVDVILGPEMRSTGEVMGVGKTFSEAYLKAQLGAGERVPKVGKVFISVRDADKPYLETMARN 957
Cdd:PRK05294 879 IPPYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSGTVFLSVRDRDKEEVVELAKR 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 958 FQEQGYGLCATRGTAQYLTDKGFFVQTIHKVAEGRPHIIDYIKNGEIAVVVNTvVSDAQAVKDSHSIRRSALNQRIPLYT 1037
Cdd:PRK05294 959 LLELGFKILATSGTAKFLREAGIPVELVNKVHEGRPHIVDLIKNGEIDLVINT-PTGRQAIRDGFSIRRAALEYKVPYIT 1037
|
1050 1060
....*....|....*....|....*....
gi 495591993 1038 TLAGGEAVSEGVKSM--FMMDVYSVQELH 1064
Cdd:PRK05294 1038 TLAGARAAVKAIEALkfGELEVRSLQEYH 1066
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
2-1047 |
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: 1675.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 2 PKRTDLKSILIIGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADVTYIEPILWQTVEKIIAKE 81
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 82 RPDAILPTMGGQTALNCALDLSRNGVLAKYNVELIGASEDAIDKAEDRGRFKEAMEKIGLKCPESYVCHSMNEALSAQAK 161
Cdd:TIGR01369 81 RPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 162 VGFPTLIRPSFTMGGSGGGIAYNKEEFMAICERGFDASPTHELLIEQSVLGWKEYEMEVVRDKADNAIIICSIENFDPMG 241
Cdd:TIGR01369 161 IGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 242 VHTGDSITVAPAQTLTDKEYQIMRNASLAVLREIGVDtGGSNVQFSVNPANGELIVIEMNPRVSRSSALASKATGFPIAK 321
Cdd:TIGR01369 241 VHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIE-GGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 322 VAAKLAVGYTLNELSNDITGgRTPASFEPSIDYVVTKIPRFAFEKFPAADDRLTTQMKSVGEVMAMGRTLQESMQKALRG 401
Cdd:TIGR01369 320 VAAKLAVGYTLDELKNPVTG-TTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 402 LETGLCGFN-PRTTDKSV--ILRELVNPGPERILYVADAFRIGMSKEEIFDVCAIDPWFLMQIEDLMQEEAKVAAGTLAD 478
Cdd:TIGR01369 399 LEIGATGFDlPDREVEPDedLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTD 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 479 LDFATMRRLKRKGFSDKRLSQLLNVSEKAVRDARFALKLHPVYKRVDTCAAEFDTDTAYLYSTYEEECEARP-TDKKKIM 557
Cdd:TIGR01369 479 LDPELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPfTDKKKVL 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 558 ILGGGPNRIGQGIEFDYCCVHASLALRESGFETIMVNCNPETVSTDFDTSDRLYFEPLTLEDVLEIVRVEQPYGVIVHYG 637
Cdd:TIGR01369 559 VLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFG 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 638 GQTPLKLANALVENGVNIIGTSADSIDAAEDRERFQKVLHDLGLRQPENRTARNEEEAIVLANEVGYPLVVRPSYVLGGR 717
Cdd:TIGR01369 639 GQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGR 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 718 AMQVVHSDDELRTYMNEAVQVSEDSPVLLDFFLNHAIEVDVDCVSDGQEVVIGGIMQHVEQAGVHSGDSGCSLPPYSLSA 797
Cdd:TIGR01369 719 AMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSA 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 798 EIQDEIRRQTKAMAKALNVVGLMNVQFAVQDDVVYVLEVNPRASRTVPFVSKATSVPLAKIAARAMAGISLAEQNFTTEV 877
Cdd:TIGR01369 799 EIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGVGKEK 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 878 IPDYYSVKEAVFPFMKFPGVDVILGPEMRSTGEVMGVGKTFSEAYLKAQLGAGERVPKVGKVFISVRDADKPYLETMARN 957
Cdd:TIGR01369 879 EPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARK 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 958 FQEQGYGLCATRGTAQYLTDKGFFVQTIHKVAEGRPHIIDYIKNGEIAVVVNTVVSDAQAVKDSHSIRRSALNQRIPLYT 1037
Cdd:TIGR01369 959 LAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEGRPNILDLIKNGEIELVINTTSKGAGTATDGYKIRREALDYGVPLIT 1038
|
1050
....*....|
gi 495591993 1038 TLAGGEAVSE 1047
Cdd:TIGR01369 1039 TLNTAEAFAE 1048
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
3-1052 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 1569.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 3 KRTDLKSILIIGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADVTYIEPILWQTVEKIIAKER 82
Cdd:PLN02735 19 KRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 83 PDAILPTMGGQTALNCALDLSRNGVLAKYNVELIGASEDAIDKAEDRGRFKEAMEKIGLKCPESYVCHSMNEALSAQAKV 162
Cdd:PLN02735 99 PDALLPTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 163 G-FPTLIRPSFTMGGSGGGIAYNKEEFMAICERGFDASPTHELLIEQSVLGWKEYEMEVVRDKADNAIIICSIENFDPMG 241
Cdd:PLN02735 179 GeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 242 VHTGDSITVAPAQTLTDKEYQIMRNASLAVLREIGVDTGGSNVQFSVNPANGELIVIEMNPRVSRSSALASKATGFPIAK 321
Cdd:PLN02735 259 VHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVECGGSNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 322 VAAKLAVGYTLNELSNDITgGRTPASFEPSIDYVVTKIPRFAFEKFPAADDRLTTQMKSVGEVMAMGRTLQESMQKALRG 401
Cdd:PLN02735 339 MAAKLSVGYTLDQIPNDIT-LKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRS 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 402 LETGLCGFNPRTT-----DKSVILRELVNPGPERILYVADAFRIGMSKEEIFDVCAIDPWFLMQIEDLMQEEAKVAAGTL 476
Cdd:PLN02735 418 LETGFSGWGCAKVkeldwDWEQLKYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSL 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 477 ADLDFATMRRLKRKGFSDKRLSQLLNVSEKAVRDARFALKLHPVYKRVDTCAAEFDTDTAYLYSTYEEECEARPTDKKKI 556
Cdd:PLN02735 498 SELSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPTNKKKV 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 557 MILGGGPNRIGQGIEFDYCCVHASLALRESGFETIMVNCNPETVSTDFDTSDRLYFEPLTLEDVLEIVRVEQPYGVIVHY 636
Cdd:PLN02735 578 LILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQF 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 637 GGQTPLKLA----NALVEN---------GVNIIGTSADSIDAAEDRERFQKVLHDLGLRQPENRTARNEEEAIVLANEVG 703
Cdd:PLN02735 658 GGQTPLKLAlpiqKYLDKNpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKRIG 737
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 704 YPLVVRPSYVLGGRAMQVVHSDDELRTYMNEAVQVSEDSPVLLDFFLNHAIEVDVDCVSDGQ-EVVIGGIMQHVEQAGVH 782
Cdd:PLN02735 738 YPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALADSEgNVVIGGIMEHIEQAGVH 817
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 783 SGDSGCSLPPYSLSAEIQDEIRRQTKAMAKALNVVGLMNVQFAV-QDDVVYVLEVNPRASRTVPFVSKATSVPLAKIAAR 861
Cdd:PLN02735 818 SGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAItPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASL 897
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 862 AMAGISLAEQNFTTEVIPDYYSVKEAVFPFMKFPGVDVILGPEMRSTGEVMGVGKTFSEAYLKAQLGAGERVPKVGKVFI 941
Cdd:PLN02735 898 VMSGKSLKDLGFTEEVIPAHVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLPLSGTVFI 977
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 942 SVRDADKPYLETMARNFQEQGYGLCATRGTAQYLTDKGFFVQTIHKVAEGRPHIIDYIKNGEIAVVVNTVVSDAQAVKDS 1021
Cdd:PLN02735 978 SLNDLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVLKLHEGRPHAGDMLANGQIQLMVITSSGDALDQKDG 1057
|
1050 1060 1070
....*....|....*....|....*....|.
gi 495591993 1022 HSIRRSALNQRIPLYTTLAGGEAVSEGVKSM 1052
Cdd:PLN02735 1058 RQLRRMALAYKVPIITTVAGALATAQAVKSL 1088
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
1-1064 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1506.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 1 MPKRTDLKSILIIGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADVTYIEPILWQTVEKIIAK 80
Cdd:PRK12815 1 MPKDTDIQKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 81 ERPDAILPTMGGQTALNCALDLSRNGVLAKYNVELIGASEDAIDKAEDRGRFKEAMEKIGLKCPESYVCHSMNEALSAQA 160
Cdd:PRK12815 81 EKPDALLATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 161 KVGFPTLIRPSFTMGGSGGGIAYNKEEFMAICERGFDASPTHELLIEQSVLGWKEYEMEVVRDKADNAIIICSIENFDPM 240
Cdd:PRK12815 161 KIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 241 GVHTGDSITVAPAQTLTDKEYQIMRNASLAVLREIGVdTGGSNVQFSVNPANGELIVIEMNPRVSRSSALASKATGFPIA 320
Cdd:PRK12815 241 GIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGV-VGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 321 KVAAKLAVGYTLNELSNDITgGRTPASFEPSIDYVVTKIPRFAFEKFPAADDRLTTQMKSVGEVMAMGRTLQESMQKALR 400
Cdd:PRK12815 320 KIAAKLAVGYTLNELKNPVT-GLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 401 GLETGLCGFN--PRTTDKS--VILRELVNPGPERILYVADAFRIGMSKEEIFDVCAIDPWFLMQIEDLMQEEAKVAAGTL 476
Cdd:PRK12815 399 SLEIKRNGLSlpIELSGKSdeELLQDLRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEDGL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 477 aDLDFATMRRLKRKGFSDKRLSQLLNVSEKAVRDARFALKLHPVYKRVDTCAAEFDTDTAYLYSTYEEECEARPT-DKKK 555
Cdd:PRK12815 479 -DLSADLLRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGESEAEPSsEKKK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 556 IMILGGGPNRIGQGIEFDYCCVHASLALRESGFETIMVNCNPETVSTDFDTSDRLYFEPLTLEDVLEIVRVEQPYGVIVH 635
Cdd:PRK12815 558 VLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIVQ 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 636 YGGQTPLKLANALVENGVNIIGTSADSIDAAEDRERFQKVLHDLGLRQPENRTARNEEEAIVLANEVGYPLVVRPSYVLG 715
Cdd:PRK12815 638 FGGQTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIG 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 716 GRAMQVVHSDDELRTYMNEAVQVSEdsPVLLDFFLNhAIEVDVDCVSDGQEVVIGGIMQHVEQAGVHSGDSGCSLPPYSL 795
Cdd:PRK12815 718 GQGMAVVYDEPALEAYLAENASQLY--PILIDQFID-GKEYEVDAISDGEDVTIPGIIEHIEQAGVHSGDSIAVLPPQSL 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 796 SAEIQDEIRRQTKAMAKALNVVGLMNVQFAVQDDVVYVLEVNPRASRTVPFVSKATSVPLAKIAARAMAGISLAEQNFTT 875
Cdd:PRK12815 795 SEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLAELGYPN 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 876 EVIP--DYYSVKEAVFPFMKFPGVDVILGPEMRSTGEVMGVGKTFSEAYLKAQLGAGERVPKVGKVFISVRDADKPYLET 953
Cdd:PRK12815 875 GLWPgsPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGTIFISVRDEDKPEVTK 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 954 MARNFQEQGYGLCATRGTAQYLTDKGFFVQTIHKVAEGRPHIIDYIKNGEIAVVVNTVVSDAqAVKDSHSIRRSALNQRI 1033
Cdd:PRK12815 955 LARRFAQLGFKLLATEGTANWLAEEGITTGVVEKVQEGSPSLLERIKQHRIVLVVNTSLSDS-ASEDAIKIRDEALSTHI 1033
|
1050 1060 1070
....*....|....*....|....*....|.
gi 495591993 1034 PLYTTLAGGEAVSEGVKSMfMMDVYSVQELH 1064
Cdd:PRK12815 1034 PVFTELETAQAFLQVLESL-ALTTQPIQELQ 1063
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
559-1066 |
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: 762.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 559 LGGGPNRIGQGIEFDYCCVHASLALRESGFETIMVNCNPETVSTDFDTSDRLYFEPLTLEDVLEIVRVEQPYGVIVHYGG 638
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 639 QTPLKLANALVEN----GVNIIGTSADSIDAAEDRERFQKVLHDLGLRQPENRTARNEEEAIVLANEVGYPLVVRPSYVL 714
Cdd:COG0458 81 QTALNLAVELEEAgileGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 715 GGRAMQVVHSDDELRTYMNEAVQVSEDSPVLLDFFLNHAIEVDVDCVSDGQ-EVVIGGIMQHVEQAGVHSGDSGCSLPPY 793
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEdNVIIVGIMEHIEPAGVHSGDSICVAPPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 794 SLSAEIQDEIRRQTKAMAKALNVVGLMNVQFAVQDDVVYVLEVNPRASRTVPFVSKATSVPLAKIAARAMAGISLAEQNF 873
Cdd:COG0458 241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 874 TTEVIP--DYYSVKEAVFPFMKFPGVDVILGPEMRSTGEVMGVGKTFSEAYLKAQLGAGERVPkvGKVFIS-VRDADKPY 950
Cdd:COG0458 321 DTGFEPtlDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLP--GTVLLSlVADDDKEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 951 LETMARNFQEQGYGLCATRGTAQYLTDKGFFVQTIHKVAEGRPHIIDYIKNGEIAVVVNTVVsDAQAVKDSHSIRRSALN 1030
Cdd:COG0458 399 ALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVINTLL-GAKSLGDSDGIIRRALA 477
|
490 500 510
....*....|....*....|....*....|....*.
gi 495591993 1031 QRIPLYTTLAGGEAVSEGVKSMFMMDVYSVQELHDH 1066
Cdd:COG0458 478 AKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYY 513
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
13-561 |
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: 759.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 13 IGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADVTYIEPILWQTVEKIIAKERPDAILPTMGG 92
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 93 QTALNCALDLSRNGVLAkyNVELIGASEDAIDKAEDRGRFKEAMEKIGLKCPESYVCHSMNEALSAQAKVGFPTLIRPSF 172
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 173 TMGGSGGGIAYNKEEFMAICERGFDASPTHELLIEQSVLGWKEYEMEVVRDKADNAIIICSIENFDPMGVHTGDSITVAP 252
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 253 AQTLTDKEYQIMRNASLAVLREIGVDtGGSNVQFSVNpaNGELIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTL 332
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVV-GLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 333 NELSNDiTGgrtpasFEPSIDYVVTKIPRFAFEKFPAADDRLTTQMKSVGEVMAMGRTLQESMQKALRGLETGLCG--FN 410
Cdd:COG0458 316 DELGND-TG------FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 411 PRTTDKSVILRELVNPGPERILYVADAFRIGMSKEEIFDVCAIDPWFLMQIEDLMQEEAKVAagtLADLDFATMRRLKRK 490
Cdd:COG0458 389 SLVADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELE---EIILVINTLLGAKSL 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495591993 491 GFSDKRLSQLLNVSEKAVRDARFALKLHPVYKRVDTCAAEFDTDTAYLYSTYEEECEARPTDKKKIMILGG 561
Cdd:COG0458 466 GDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
128-333 |
1.54e-85 |
|
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: 274.95 E-value: 1.54e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 128 DRGRFKEAMEKIGLKCPESYVC--HSMNEALSAQAKVGFPTLIRPSFTMGGSGGGIAYNKEEFMAICERGFDASPT---- 201
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGpvETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 202 HELLIEQSVLGWKEYEMEVVRDKADNAIIICSIENFDPMgvHTGDSITVAPAQTLTDKEYQIMRNASLAVLREIGVdTGG 281
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGY-VGA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495591993 282 SNVQFSVNPANGELIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLN 333
Cdd:pfam02786 158 GTVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
419-542 |
4.18e-61 |
|
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 198164 [Multi-domain] Cd Length: 124 Bit Score: 203.84 E-value: 4.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 419 ILRELVNPGPERILYVADAFRIGMSKEEIFDVCAIDPWFLMQIEDLMQEEAKVAAGTLADLDFATMRRLKRKGFSDKRLS 498
Cdd:smart01096 1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 495591993 499 QLLNVSEKAVRDARFALKLHPVYKRVDTCAAEFDTDTAYLYSTY 542
Cdd:smart01096 81 KLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
937-1047 |
1.41e-45 |
|
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: 159.18 E-value: 1.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 937 GKVFISVRDADKPYLETMARNFQEQGYGLCATRGTAQYLTDKGFFVQTIHKVAEGRPHIIDYIKNGEIAVVVNTvVSDAQ 1016
Cdd:cd01424 1 GTVFISVADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEGRPNIVDLIKNGEIQLVINT-PSGKR 79
|
90 100 110
....*....|....*....|....*....|.
gi 495591993 1017 AVKDSHSIRRSALNQRIPLYTTLAGGEAVSE 1047
Cdd:cd01424 80 AIRDGFSIRRAALEYKVPYFTTLDTARAAVE 110
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
668-868 |
2.21e-32 |
|
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: 125.11 E-value: 2.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 668 DRERFQKVLHDLGLRQPEN--RTARNEEEAIVLANEVGYPLVVRPSYVLGGRAMQVVHSDDELR----TYMNEAVQVSED 741
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGtaGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAelfaLALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 742 SPVLLDFFLNHAIEVDVDCVSDGQE-VVIGGIMQHVEQagVHSGDSGCSLPPYSLSAEIQDEIRRQTKAMAKALNVVGLM 820
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGnCITVCNRECSDQ--RRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495591993 821 NVQFAVQ--DDVVYVLEVNPRASRTVPFVSKATSVPLAKIAARAMAGISL 868
Cdd:pfam02786 159 TVEFALDpfSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
421-500 |
1.16e-30 |
|
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 460695 Cd Length: 79 Bit Score: 115.55 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 421 RELVNPGPERILYVADAFRIGMSKEEIFDVCAIDPWFLMQIEDLMQEEAKVAAGTLaDLDFATMRRLKRKGFSDKRLSQL 500
Cdd:pfam02787 1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAGL-DLDAELLREAKRLGFSDRQIAKL 79
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
115-329 |
5.16e-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: 111.50 E-value: 5.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 115 LIGASEDAIDKAEDRGRFKEAMEKIGLKCPESYVCHSMNEALSAQAKVGFPTLIRPSFTMGGSGGGIAYNKEE----FMA 190
Cdd:COG0439 41 LPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEEleaaLAE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 191 ICERGFDASPTHELLIEQSVLGwKEYEMEVVRDkaDNAIIICSI---ENFDPMGVHTGDsitVAPAQtLTDKEYQIMRNA 267
Cdd:COG0439 121 ARAEAKAGSPNGEVLVEEFLEG-REYSVEGLVR--DGEVVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGEL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495591993 268 SLAVLREIGVDTGGSNVQFSVNPaNGELIVIEMNPRVS--RSSALASKATGFPIAKVAAKLAVG 329
Cdd:COG0439 194 VARALRALGYRRGAFHTEFLLTP-DGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALG 256
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
654-865 |
7.51e-26 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 108.04 E-value: 7.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 654 NIIGTSADSIDAAEDRERFQKVLHDLGLRQPENRTARNEEEAIVLANEVGYPLVVRPSYVLGGRAMQVVHSDDELRTYMN 733
Cdd:COG0439 40 GLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 734 EAVQ----VSEDSPVLLDFFLNHA-IEVDVdCVSDGQEVVIGgiMQHVEQAGVHSGDSGCSLPPySLSAEIQDEIRRQTK 808
Cdd:COG0439 120 EARAeakaGSPNGEVLVEEFLEGReYSVEG-LVRDGEVVVCS--ITRKHQKPPYFVELGHEAPS-PLPEELRAEIGELVA 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495591993 809 AMAKALNVV-GLMNVQFAV-QDDVVYVLEVNPRAS--RTVPFVSKATSVPLAKIAARAMAG 865
Cdd:COG0439 196 RALRALGYRrGAFHTEFLLtPDGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALG 256
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
955-1037 |
2.06e-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: 214855 [Multi-domain] Cd Length: 91 Bit Score: 95.23 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 955 ARNFQEQGYGLCATRGTAQYLTDKGF-FVQTIH-KVAEGRPHIIDYIKNGEIAVVVNTVVS-DAQAVKDSHSIRRSALNQ 1031
Cdd:smart00851 6 AKRLAELGFELLATGGTAKFLREAGLpVVKTLHpKVHGGIPQILDLIKNGEIDLVINTLYPfEAQAHEDGYSIRRAAENI 85
|
....*.
gi 495591993 1032 RIPLYT 1037
Cdd:smart00851 86 DIPGPT 91
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
955-1037 |
6.07e-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: 94.09 E-value: 6.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 955 ARNFQEQGYGLCATRGTAQYLTDKGFFVQ-TIHKVAEGRPH----IIDYIKNGEIAVVVNTVVSDAQAVKDSHSIRRSAL 1029
Cdd:pfam02142 6 AKALVELGFELLATGGTAKFLREAGIPVTeVVEKTGEGRPGgrvqIGDLIKNGEIDLVINTLYPFKATVHDGYAIRRAAE 85
|
....*...
gi 495591993 1030 NQRIPLYT 1037
Cdd:pfam02142 86 NIDIPGPT 93
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
9-329 |
3.39e-19 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 91.14 E-value: 3.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 9 SILIIGAGPIVIGqacefdysgaqACKALREEGYRVILVNSNPATIMT------------DPEMADVTYIEpilwqTVEK 76
Cdd:COG3919 7 RVVVLGGDINALA-----------VARSLGEAGVRVIVVDRDPLGPAArsryvdevvvvpDPGDDPEAFVD-----ALLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 77 IIAKERPDAILPTMGGQTALncaldLSRN-GVLAKYnVELIGASEDAIDKAEDRGRFKEAMEKIGLKCPESYVCHSMNEA 155
Cdd:COG3919 71 LAERHGPDVLIPTGDEYVEL-----LSRHrDELEEH-YRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 156 LSAQAKVGFPTLIRPS--------FTMGGSGGGIAYNKEEFMAICERGFDASptHELLIEQSVLGWKEYE--MEVVRDKA 225
Cdd:COG3919 145 DALAEDLGFPVVVKPAdsvgydelSFPGKKKVFYVDDREELLALLRRIAAAG--YELIVQEYIPGDDGEMrgLTAYVDRD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 226 DNAIIICSIENF--DPMGVHTGDSITVAPAQTLTDkeyqimrnASLAVLREIGVdTGGSNVQFSVNPANGELIVIEMNPR 303
Cdd:COG3919 223 GEVVATFTGRKLrhYPPAGGNSAARESVDDPELEE--------AARRLLEALGY-HGFANVEFKRDPRDGEYKLIEINPR 293
|
330 340
....*....|....*....|....*.
gi 495591993 304 VSRSSALASKAtGFPIAKVAAKLAVG 329
Cdd:COG3919 294 FWRSLYLATAA-GVNFPYLLYDDAVG 318
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
617-921 |
3.96e-16 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 80.70 E-value: 3.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 617 LEDVLEIVRVEQPYGVIVhyGGQTPLKL----ANALVENGVNIIGTSADSIDAAEDRERFQKVLHDLGLRQPENRTARNE 692
Cdd:PRK12767 58 IDRLLDICKKEKIDLLIP--LIDPELPLlaqnRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 693 E--EAIVLANEVGYPLVVRPSYVLGGRAMQVVHSDDELRTYMneavqvSEDSPVLLDFFLNHaIEVDVDCVSDGQEVVIG 770
Cdd:PRK12767 136 EdfKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLL------EYVPNLIIQEFIEG-QEYTVDVLCDLNGEVIS 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 771 GIMqhVEQAGVHSGDSgcslppYSLSAEIQDEIRRQTKAMAKALNVVGLMNVQFAVQDDVVYVLEVNPRASRTVPFvska 850
Cdd:PRK12767 209 IVP--RKRIEVRAGET------SKGVTVKDPELFKLAERLAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPL---- 276
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495591993 851 tsvplakiaaRAMAGIslaeqNFtTEVIPDYYSVKEAVFPFMKF-PGVdvilgpEMRSTGEVMGVGKTFSEA 921
Cdd:PRK12767 277 ----------SYMAGA-----NE-PDWIIRNLLGGENEPIIGEYkEGL------YMRRYDEVVIVEEELLEA 326
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
939-1045 |
3.60e-15 |
|
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: 72.54 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 939 VFISVRDADKPYLETMARNFQEQGYGLCATRGTAQYLTDKGFFVQTIHKVAE-GRPHIIDYIKN-GEIAVVVNTV--VSD 1014
Cdd:cd00532 2 VFLSVSDHVKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRHEdGEPTVDAAIAEkGKFDVVINLRdpRRD 81
|
90 100 110
....*....|....*....|....*....|.
gi 495591993 1015 AQAVKDSHSIRRSALNQRIPLYTTLAGGEAV 1045
Cdd:cd00532 82 RCTDEDGTALLRLARLYKIPVTTPNATAMFV 112
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
10-314 |
8.93e-15 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 76.85 E-value: 8.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 10 ILIIGAGpivigqacefdySGAQACKALREE--GYRVILV---NSNPATIMTD-----PEMADVTYIEPILwqtveKIIA 79
Cdd:PRK12767 4 ILVTSAG------------RRVQLVKALKKSllKGRVIGAdisELAPALYFADkfyvvPKVTDPNYIDRLL-----DICK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 80 KERPDAILPTMGGQTALncaldLSRNGV-LAKYNVELIGASEDAIDKAEDRGRFKEAMEKIGLKCPESYVCHSMNEALSA 158
Cdd:PRK12767 67 KEKIDLLIPLIDPELPL-----LAQNRDrFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 159 QA--KVGFPTLIRPSFTMGGSGGGIAYNKEEfmaiCERGFDASPthELLIEQSVLGwKEYEMEVVRDKadNAIIICSIen 236
Cdd:PRK12767 142 LAkgELQFPLFVKPRDGSASIGVFKVNDKEE----LEFLLEYVP--NLIIQEFIEG-QEYTVDVLCDL--NGEVISIV-- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 237 fdPM---GVHTGDSItvapaQTLTDKeYQIMRNASLAVLREIGVDtGGSNVQFSVNpaNGELIVIEMNPRVSRSSALASK 313
Cdd:PRK12767 211 --PRkriEVRAGETS-----KGVTVK-DPELFKLAERLAEALGAR-GPLNIQCFVT--DGEPYLFEINPRFGGGYPLSYM 279
|
.
gi 495591993 314 A 314
Cdd:PRK12767 280 A 280
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
549-868 |
4.46e-13 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 72.27 E-value: 4.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 549 RPTDKKKIMILGGGPNrigqgiefDYCCVHAslaLRESGFETIMVNCNPETVSTDFDTSDRLYFEPLT-------LEDVL 621
Cdd:COG3919 1 AMTMRFRVVVLGGDIN--------ALAVARS---LGEAGVRVIVVDRDPLGPAARSRYVDEVVVVPDPgddpeafVDALL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 622 EIVRvEQPYGVIV----HYggqtplklANALVEN------GVNIIGTSADSIDAAEDRERFQKVLHDLGLRQPENRTARN 691
Cdd:COG3919 70 ELAE-RHGPDVLIptgdEY--------VELLSRHrdeleeHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 692 EEEAIVLANEVGYPLVVRPSY--------VLGGRAMQVVHSDDELRTYMNEAVQVSEDsPVLLDFflnhaIEVDVD---- 759
Cdd:COG3919 141 ADDLDALAEDLGFPVVVKPADsvgydelsFPGKKKVFYVDDREELLALLRRIAAAGYE-LIVQEY-----IPGDDGemrg 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 760 ----CVSDGQEVVIGG---IMQHVEQAGVHSgdsgcslppYSLSAEIqDEIRRQTKAMAKALNVVGLMNVQFAV--QDDV 830
Cdd:COG3919 215 ltayVDRDGEVVATFTgrkLRHYPPAGGNSA---------ARESVDD-PELEEAARRLLEALGYHGFANVEFKRdpRDGE 284
|
330 340 350
....*....|....*....|....*....|....*...
gi 495591993 831 VYVLEVNPRASRTVPFVSKAtSVPLAKIAARAMAGISL 868
Cdd:COG3919 285 YKLIEINPRFWRSLYLATAA-GVNFPYLLYDDAVGRPL 321
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
643-839 |
3.28e-12 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 70.40 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 643 KLANALVENGVNIIGTSADSIDAAEDRERFQKVLHDLGLrqP----ENRTARNEEEAIVLANEVGYPLVVRPSYVLGGRA 718
Cdd:PRK08654 90 EFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGV--PvlpgTEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 719 MQVVHSDDELRTYMNEAVQVSE----DSPVLLDFFL---NHaIEVDVdcVSDGQEVVIggimqhveqagvHSGDSGCS-- 789
Cdd:PRK08654 168 MRVVYSEEELEDAIESTQSIAQsafgDSTVFIEKYLekpRH-IEIQI--LADKHGNVI------------HLGDRECSiq 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495591993 790 -----LPPYSLSAEIQDEIR-RQTKAMAKALNVVGLMN---VQFAVQDDVVYVLEVNPR 839
Cdd:PRK08654 233 rrhqkLIEEAPSPIMTPELReRMGEAAVKAAKAINYENagtVEFLYSNGNFYFLEMNTR 291
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
581-838 |
4.89e-12 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 68.04 E-value: 4.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 581 LALRESGFETIMVNcnPETVSTDFDTSDRLY-FEPLTLEDVLeIVRVEQPygvivHYGgqtpLKLANALVENGVNIIGtS 659
Cdd:COG0189 21 EAAQRRGHEVEVID--PDDLTLDLGRAPELYrGEDLSEFDAV-LPRIDPP-----FYG----LALLRQLEAAGVPVVN-D 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 660 ADSIDAAEDRERFQKVLHDLGLRQPENRTARNEEEAIVLANEVGYPLVVRPSYVLGGRAMQVVHSDDELRTYMnEAVQVS 739
Cdd:COG0189 88 PEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESIL-EALTEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 740 EDSPVLLDFFLNHAIEVDVDCvsdgqeVVIGG--------IMQHVE-QAGVHSGDSGCslpPYSLSAEIQDEIRRQTKAM 810
Cdd:COG0189 167 GSEPVLVQEFIPEEDGRDIRV------LVVGGepvaairrIPAEGEfRTNLARGGRAE---PVELTDEERELALRAAPAL 237
|
250 260
....*....|....*....|....*...
gi 495591993 811 akALNVVGlmnVQFAVQDDVVYVLEVNP 838
Cdd:COG0189 238 --GLDFAG---VDLIEDDDGPLVLEVNV 260
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
74-340 |
6.24e-12 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 69.24 E-value: 6.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 74 VEKIIA---KERPDAILPTMGGqtalncaldLSRNGVLA----KYNVELIGASEDAIDKAEDRGRFKEAMEKIGL----- 141
Cdd:PRK08654 63 IERIIDvakKAGADAIHPGYGF---------LAENPEFAkaceKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVpvlpg 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 142 --KCPESyvchsMNEALSAQAKVGFPTLIRPSFTMGGSGGGIAYNKEEF-------MAICERGFDASpthELLIEQSVLG 212
Cdd:PRK08654 134 teEGIED-----IEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELedaiestQSIAQSAFGDS---TVFIEKYLEK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 213 WKEYEMEVVRDKADNAIII----CSIENfdpmgVHTgDSITVAPAQTLTDKEYQIMRNASLAVLREIGVDTGGSnVQFSV 288
Cdd:PRK08654 206 PRHIEIQILADKHGNVIHLgdreCSIQR-----RHQ-KLIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGT-VEFLY 278
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 495591993 289 NpaNGELIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLNELSNDIT 340
Cdd:PRK08654 279 S--NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELSFKQEDIT 328
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
678-839 |
1.36e-11 |
|
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: 64.20 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 678 DLGLRQPENRTARNEEEAIVLANEVGYPLVVRpSYVLG--GRAMQVVHSDDELRtymnEAVQVSEDSPVLLDFFLNHAIE 755
Cdd:pfam02222 2 KLGLPTPRFMAAESLEELIEAGQELGYPCVVK-ARRGGydGKGQYVVRSEADLP----QAWEELGDGPVIVEEFVPFDRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 756 VDVDCVSDGQ-EVVIGGIMQHVEQAGVhsgdsgC--SLPPYSLSAEIQDEIRRQTKAMAKALNVVGLMNVQ-FAVQDDVV 831
Cdd:pfam02222 77 LSVLVVRSVDgETAFYPVVETIQEDGI------CrlSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVElFVTEDGDL 150
|
....*...
gi 495591993 832 YVLEVNPR 839
Cdd:pfam02222 151 LINELAPR 158
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
655-866 |
4.43e-11 |
|
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: 66.10 E-value: 4.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 655 IIGTSADSIDAAEDRERFQKVLHDLGLRQPENRTARNEEEaivlanevgYPLVVRPSYVLGGRAMQVVHSDDELRTymne 734
Cdd:COG2232 99 LLGNPPEVVRRVKDPLRFFALLDELGIPHPETRFEPPPDP---------GPWLVKPIGGAGGWHIRPADSEAPPAP---- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 735 avqvsedspvllDFFLNHAIE---VDVDCVSDGQEVVIGGI-MQHVEQAGVH----SGDSGcslpPYSLSAEIQDEIRRQ 806
Cdd:COG2232 166 ------------GRYFQRYVEgtpASVLFLADGSDARVLGFnRQLIGPAGERpfryGGNIG----PLALPPALAEEMRAI 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 807 TKAMAKALNVVGLMNVQFAVQDDVVYVLEVNPRASRTVPFVSKATSVPLAKIAARAMAGI 866
Cdd:COG2232 230 AEALVAALGLVGLNGVDFILDGDGPYVLEVNPRPQASLDLYEDATGGNLFDAHLRACRGE 289
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
102-339 |
1.85e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 64.35 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 102 LSRNGVLA----KYNVELIGASEDAIDKAEDRGRFKEAMEKIGLKC-PESYV-CHSMNEALSAQAKVGFPTLIRPsfTMG 175
Cdd:PRK07178 84 LSENAELAeicaERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVtPGSEGnLADLDEALAEAERIGYPVMLKA--TSG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 176 GSGGGI---------AYNKEEFMAICERGFDASpthELLIEQSVLGWKEYEMEVVRDKADNAIII----CSIENfdpmgv 242
Cdd:PRK07178 162 GGGRGIrrcnsreelEQNFPRVISEATKAFGSA---EVFLEKCIVNPKHIEVQILADSHGNVVHLferdCSIQR------ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 243 HTGDSITVAPAQTLTDKEYQIMRNASLAVLREIGVDTGGSnVQFSVNpANGELIVIEMNPRVSRSSALASKATGFPIAKV 322
Cdd:PRK07178 233 RNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGT-VEFLLD-ADGEVYFMEMNTRVQVEHTITEEITGIDIVRE 310
|
250
....*....|....*..
gi 495591993 323 AAKLAVGYTLNELSNDI 339
Cdd:PRK07178 311 QIRIASGLPLSYKQEDI 327
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
645-869 |
9.03e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 62.46 E-value: 9.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 645 ANALVENGVNIIGTSADSI----DAAEDRERFQK-----------VLHDLglrqpenrtarneEEAIVLANEVGYPLVVR 709
Cdd:PRK12833 95 AEAVEAAGLIFVGPDAQTIrtmgDKARARRTARRagvptvpgsdgVVASL-------------DAALEVAARIGYPLMIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 710 PSYVLGGRAMQVVHSDDELRTYM----NEAVQVSEDSPVLLDFFLNHAIEVDVDCVSDGQEVviggimqhveqagVHSGD 785
Cdd:PRK12833 162 AAAGGGGRGIRVAHDAAQLAAELplaqREAQAAFGDGGVYLERFIARARHIEVQILGDGERV-------------VHLFE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 786 SGCSL-----------PPYSLSAEIQDEIRRQTKAMAKALNVVGLMNVQFAVQD--DVVYVLEVNPRASRTVPFVSKATS 852
Cdd:PRK12833 229 RECSLqrrrqkileeaPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDarGEFYFIEMNTRIQVEHPVTEAITG 308
|
250
....*....|....*..
gi 495591993 853 VPLAKIAARAMAGISLA 869
Cdd:PRK12833 309 IDLVQEMLRIADGEPLR 325
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
644-839 |
1.04e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 61.97 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 644 LANALVENGVNIIGTSADSIDAAEDRERFQKVLHDLGLR-QPENRTA-RNEEEAIVLANEVGYPLVVRPSYVLGGRAMQV 721
Cdd:PRK06111 91 FAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPvVPGITTNlEDAEEAIAIARQIGYPVMLKASAGGGGIGMQL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 722 VHSDDELRTYM----NEAVQVSEDSPVLLDFFLNHA--IEVDVDCVSDGqevviggimqHVeqagVHSGDSGCSL----- 790
Cdd:PRK06111 171 VETEQELTKAFesnkKRAANFFGNGEMYIEKYIEDPrhIEIQLLADTHG----------NT----VYLWERECSVqrrhq 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495591993 791 ------PPYSLSAEIQDEIRRQTKAMAKALNVVGLMNVQFAVQDD-VVYVLEVNPR 839
Cdd:PRK06111 237 kvieeaPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQkNFYFLEMNTR 292
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
102-339 |
1.72e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 61.27 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 102 LSRNGVLAKY----NVELIGASEDAIDKAEDRGRFKEAMEKIGLKCPESY--VCHSMNEALSAQAKVGFPTLIRPSFTMG 175
Cdd:PRK05586 85 LSENSKFAKMckecNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSegEIENEEEALEIAKEIGYPVMVKASAGGG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 176 GSGGGIAYNKEEFMaiceRGFDASPTH--------ELLIEQSVLGWKEYEMEVVRDKADNAIII----CSIENfdpmgvH 243
Cdd:PRK05586 165 GRGIRIVRSEEELI----KAFNTAKSEakaafgddSMYIEKFIENPKHIEFQILGDNYGNVVHLgerdCSLQR------R 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 244 TGDSITVAPAQTLTDKEYQIMRNASLAVLREIGVDTGGSnVQFSVNpANGELIVIEMNPRVSRSSALASKATGFPIAKVA 323
Cdd:PRK05586 235 NQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGT-IEFLLD-KDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQ 312
|
250
....*....|....*.
gi 495591993 324 AKLAVGYTLNELSNDI 339
Cdd:PRK05586 313 IKIAYGEKLSIKQEDI 328
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
619-839 |
3.16e-09 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 61.31 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 619 DVLEIVRVEQPYGVI-VH--YG--GQTPlKLANALVENGVNIIGTSADSIDAAEDRERFQKVLHDLGLrqP----ENRTA 689
Cdd:PRK12999 66 DIDEIIRVAKQAGVDaIHpgYGflSENP-EFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGV--PvipgSEGPI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 690 RNEEEAIVLANEVGYPLVVRPSYVLGGRAMQVVHSDDELRTYMNEAVQVSE----DSPVLLDFFLNHA--IEVDVdcVSD 763
Cdd:PRK12999 143 DDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKaafgNDEVYLEKYVENPrhIEVQI--LGD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 764 GQevviGGImqhveqagVHSGDSGCSL-----------PPYSLSAEIQDEIRRQTKAMAKALNVVGLMNVQFAVQDDVVY 832
Cdd:PRK12999 221 KH----GNV--------VHLYERDCSVqrrhqkvveiaPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNF 288
|
....*...
gi 495591993 833 VL-EVNPR 839
Cdd:PRK12999 289 YFiEVNPR 296
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
74-403 |
9.43e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 58.89 E-value: 9.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 74 VEKIIA---KERPDAILPTMGGqtalncaldLSRNGVLA----KYNVELIGASEDAIDKAEDRGRFKEAMEKIGLKC--- 143
Cdd:PRK06111 63 LEKIIEiakKTGAEAIHPGYGL---------LSENASFAerckEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVvpg 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 144 PESYVcHSMNEALSAQAKVGFPTLIRPSFTMGGSGGGIAYNKEE----FMAICERGFDASPTHELLIEQSVLGWKEYEME 219
Cdd:PRK06111 134 ITTNL-EDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQEltkaFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 220 VVRDKADNAIII----CSIENfdpmgvHTGDSITVAPAQTLTDKEYQIMRNASLAVLREIGVdTGGSNVQFSVNPaNGEL 295
Cdd:PRK06111 213 LLADTHGNTVYLwereCSVQR------RHQKVIEEAPSPFLDEETRKAMGERAVQAAKAIGY-TNAGTIEFLVDE-QKNF 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 296 IVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLNELSNDITG----------GRTPASFEPS----IDYVVTKIPR 361
Cdd:PRK06111 285 YFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLSFTQDDIKRsghaievriyAEDPKTFFPSpgkiTDLTLPGGEG 364
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 495591993 362 FAFEKFPAADDRLTTQMKS-VGEVMAMGRTLQESMQKALRGLE 403
Cdd:PRK06111 365 VRHDHAVENGVTVTPFYDPmIAKLIAHGETREEAISRLHDALE 407
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
21-302 |
1.81e-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: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 21 GQACEFD---YSGAQACKALREEGYRVILVNSNPATIMTDpemadvtyiepilwqtvekiIAKERPDAILPTMGG----Q 93
Cdd:COG1181 9 GRSAEREvslKSGRAVAAALDKAGYDVVPIGIDVEDLPAA--------------------LKELKPDVVFPALHGrggeD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 94 TALNCALDLSR-----NGVLakynveligASEDAIDKAedrgRFKEAMEKIGLKCPESYVCHS--MNEALSAQAKVGFPT 166
Cdd:COG1181 69 GTIQGLLELLGipytgSGVL---------ASALAMDKA----LTKRVLAAAGLPTPPYVVLRRgeLADLEAIEEELGLPL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 167 LIRPSftMGGSGGGI--AYNKEEFMAICERGFDASptHELLIEQ---------SVLGWKEYE----MEVVRDKAdnaiiI 231
Cdd:COG1181 136 FVKPA--REGSSVGVskVKNAEELAAALEEAFKYD--DKVLVEEfidgrevtvGVLGNGGPRalppIEIVPENG-----F 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495591993 232 CSIEN-FDPmgvhtGDSITVAPAQtLTDKEYQIMRNASLAVLREIGVdTGGSNVQFSVNpANGELIVIEMNP 302
Cdd:COG1181 207 YDYEAkYTD-----GGTEYICPAR-LPEELEERIQELALKAFRALGC-RGYARVDFRLD-EDGEPYLLEVNT 270
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
690-839 |
2.18e-08 |
|
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: 58.55 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 690 RNEEEAIVLANEVGYPLVVRPSYVLGGRAMQVVHSDDELRTYMNEAvqVSE------DSPVLLDFFLNHA--IEVDVdcV 761
Cdd:COG1038 142 DDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESA--RREakaafgDDEVFLEKYIERPkhIEVQI--L 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 762 SDGQevviGGImqhveqagVHSGDSGCSL-----------PPYSLSAEIQDEIRRQTKAMAKALNVVGLMNVQFAV-QDD 829
Cdd:COG1038 218 GDKH----GNI--------VHLFERDCSVqrrhqkvveiaPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVdDDG 285
|
170
....*....|
gi 495591993 830 VVYVLEVNPR 839
Cdd:COG1038 286 NFYFIEVNPR 295
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
674-870 |
3.71e-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: 56.27 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 674 KVLHDLGLRQPENRTARNEEEAIV--LANEVGYPLVVRPsyVLGG--RAMQVVHSDDELRTYMNEAVQvsEDSPVLLDFF 749
Cdd:COG1181 101 RVLAAAGLPTPPYVVLRRGELADLeaIEEELGLPLFVKP--AREGssVGVSKVKNAEELAAALEEAFK--YDDKVLVEEF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 750 LNhAIEVDVdCVSDGQEVVIGGIMQHVEQAGV-------HSGDSGCSLPPySLSAEIQDEIRRQTKAMAKALNVVGLMNV 822
Cdd:COG1181 177 ID-GREVTV-GVLGNGGPRALPPIEIVPENGFydyeakyTDGGTEYICPA-RLPEELEERIQELALKAFRALGCRGYARV 253
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495591993 823 QFAVQDD-VVYVLEVNprasrTVPFVSKATSVPLakiAARAmAGISLAE 870
Cdd:COG1181 254 DFRLDEDgEPYLLEVN-----TLPGMTPTSLLPK---AAAA-AGISYEE 293
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
115-493 |
5.10e-08 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 57.16 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 115 LIGASEDAIDKAEDRGRFKEAMEKIGLKCPESYVCHSMNEALSAQAKVGFPTLIRPSFTMGGSGGGIAYNKEEFMAICER 194
Cdd:PRK02186 94 LPAANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 195 GFDASpTHELLIEQSVLGwKEYEMEVVRDkADNAIIICSIENF---DPMGVHTGDsitVAPAQTLTDKEYQIMRNASLAv 271
Cdd:PRK02186 174 LRRAG-TRAALVQAYVEG-DEYSVETLTV-ARGHQVLGITRKHlgpPPHFVEIGH---DFPAPLSAPQRERIVRTVLRA- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 272 LREIGVDTGGSNVQFSVNpaNGELIVIEMNPRVSRS--SALASKATGFPIAKVAAKL----------------AVGYTLN 333
Cdd:PRK02186 247 LDAVGYAFGPAHTELRVR--GDTVVIIEINPRLAGGmiPVLLEEAFGVDLLDHVIDLhlgvaafadptakrygAIRFVLP 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 334 ELSNDITGgrtpASFEPSIDYVVTKIpRFAFEKFPAADDRLTTQMKS-VGEVMAMGRTLQESMQKALRgLETGLC---GF 409
Cdd:PRK02186 325 ARSGVLRG----LLFLPDDIAARPEL-RFHPLKQPGDALRLEGDFRDrIAAVVCAGDHRDSVAAAAER-AVAGLSidiGD 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 410 NPRTTDKSVILRELVNPG--PERILYVADAFRIGMSKEEIFDVCAIDPWFLMqiedLMQEEAKVAAGTLADLdFATMRRL 487
Cdd:PRK02186 399 AARAAALNDAGAGAARPGlpPEAQAIVYGPGASEAPLAELDHLAAIDEAHLV----MLGDTGIVAPERARPL-LDAHRRL 473
|
....*.
gi 495591993 488 KRKGFS 493
Cdd:PRK02186 474 RDAGFA 479
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
666-839 |
6.49e-08 |
|
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: 53.16 E-value: 6.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 666 AEDRERFQKVLHDLGLRQPEnrTARNEEeaivlANEVGYPLVVRPSYVLGGRAMQVVHSDDELRTYMNEAVqVSEdspvl 745
Cdd:pfam02655 1 ASDKLKTYKALKNAGVPTPE--TLQAEE-----LLREEKKYVVKPRDGCGGEGVRKVENGREDEAFIENVL-VQE----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 746 ldfFLNhAIEVDVDCVSDGQEVVIGGI-MQHVEQAGVHSGDSGCSLP-PYSLSAEIQDEIRRqtkAMAKALNVVGLMNVQ 823
Cdd:pfam02655 68 ---FIE-GEPLSVSLLSDGEKALPLSVnRQYIDNGGSGFVYAGNVTPsRTELKEEIIELAEE---VVECLPGLRGYVGVD 140
|
170
....*....|....*.
gi 495591993 824 FAVQDDVVYVLEVNPR 839
Cdd:pfam02655 141 LVLKDNEPYVIEVNPR 156
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
643-878 |
2.23e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 54.72 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 643 KLANALVENGVNIIGTSADSIDAAEDRERFQKVLHDLGLrqP----ENRTARNEEEAIVLANEVGYPLVVRPSYVLGGRA 718
Cdd:PRK05586 90 KFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGV--PvvpgSEGEIENEEEALEIAKEIGYPVMVKASAGGGGRG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 719 MQVVHSDDEL----RTYMNEAVQVSEDSPVLLDFFLNHAIEVDVDCVSDGQEVViggimqhveqagVHSGDSGCSL---- 790
Cdd:PRK05586 168 IRIVRSEEELikafNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNV------------VHLGERDCSLqrrn 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 791 -------PPYSLSAEIQDEIRRQTKAMAKALNVVGLMNVQFAV-QDDVVYVLEVNPRASRTVPFVSKATSVPLAKIAARA 862
Cdd:PRK05586 236 qkvleeaPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKI 315
|
250
....*....|....*.
gi 495591993 863 MAGISLaeqNFTTEVI 878
Cdd:PRK05586 316 AYGEKL---SIKQEDI 328
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
658-741 |
1.36e-06 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 52.47 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 658 TSADSIDAAEDRERFQKVLHDLGLRQPENRTARNEEEAIVLANEVGYPLVVRPSYVLGGRAMQV-VHSDDELRTYMNEAV 736
Cdd:PRK14016 204 TSAIAVDIACDKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTVnITTREEIEAAYAVAS 283
|
....*
gi 495591993 737 QVSED 741
Cdd:PRK14016 284 KESSD 288
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
587-867 |
2.04e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 52.16 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 587 GFETIMVNCNPETvstdFDTSDRLYFEPLTLE--DVLEIVRVEQPY-GVIVHYGGQTPLKLANALVENGVNIIGTSADSI 663
Cdd:PRK02186 27 GFTPYFLTANRGK----YPFLDAIRVVTISADtsDPDRIHRFVSSLdGVAGIMSSSEYFIEVASEVARRLGLPAANTEAI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 664 DAAEDRERFQKVLHDLGLRQPENRTARNEEEAIVLANEVGYPLVVRPSYVLGGRAMQVVHSDDELRTYMNEAVQVSEDSp 743
Cdd:PRK02186 103 RTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALRRAGTRA- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 744 VLLDFFLNHAiEVDVDCVSDGQEVVIGGIMQHVEQAGVHSGDSGCSLPPySLSAEIQDEIRRQTKamaKALNVVGL---- 819
Cdd:PRK02186 182 ALVQAYVEGD-EYSVETLTVARGHQVLGITRKHLGPPPHFVEIGHDFPA-PLSAPQRERIVRTVL---RALDAVGYafgp 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 495591993 820 MNVQFAVQDDVVYVLEVNPR-ASRTVP-FVSKATSVPLAKIAARAMAGIS 867
Cdd:PRK02186 257 AHTELRVRGDTVVIIEINPRlAGGMIPvLLEEAFGVDLLDHVIDLHLGVA 306
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
691-839 |
3.33e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 50.96 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 691 NEEEAIVLANEVGYPLVVRPSYVLGGRAMQVVHSDDELRTYMNEAVQVSE----DSPVLLDFFLNHA--IEVDVdcVSDG 764
Cdd:PRK08591 140 DEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafgNPGVYMEKYLENPrhIEIQV--LADG 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 765 QevviGGImqhveqagVHSGDSGCSL-----------PPYSLSAEIQDEI-RRQTKAmAKALNVVGLMNVQFAVQDD-VV 831
Cdd:PRK08591 218 H----GNA--------IHLGERDCSLqrrhqkvleeaPSPAITEELRRKIgEAAVKA-AKAIGYRGAGTIEFLYEKNgEF 284
|
....*...
gi 495591993 832 YVLEVNPR 839
Cdd:PRK08591 285 YFIEMNTR 292
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
652-839 |
3.37e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 50.90 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 652 GVNIIGTSADSIDAAEDRERFQKVLHDLGLRQPENRTA--RNEEEAIVLANEVGYPLVVRPSYVLGGRAMQVVHSDDEL- 728
Cdd:PRK08462 101 NIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGalKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLe 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 729 RTYM---NEAVQVSEDSPVLLDFFLNHAIEVDVDCVSDGQEVVIggimqhveqagvHSGDSGCSL-----------PPYS 794
Cdd:PRK08462 181 NLYLaaeSEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVI------------HVGERDCSLqrrhqklieesPAVV 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495591993 795 LSAEIQDEIRRQTKAMAKALNVVGLMNVQFAVQDDV-VYVLEVNPR 839
Cdd:PRK08462 249 LDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLdFYFMEMNTR 294
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
755-866 |
5.13e-06 |
|
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: 46.84 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 755 EVDVDCVSDGQEVVI--------GGImQHVEQagvhsgdsgcslppyslsaeiQDEIRRQTKAMAKALNVVGLMNVQFAV 826
Cdd:pfam15632 15 EYSVDCLAGHGELIAavprrkgdGGI-QTLED---------------------DPELIEAARRLAEAFGLDGLFNVQFRY 72
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 495591993 827 QDDVVYVLEVNPRASRTVPfVSKATSVPLAKIAARAMAGI 866
Cdd:pfam15632 73 DGDGPKLLEINPRMSGGIG-YSCLAGVNLPYLALKLLLGL 111
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
78-339 |
6.49e-06 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 49.81 E-value: 6.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 78 IAKE-RPDAILPTMGGqtalncaldLSRNGVLAKyNVE-----LIGASEDAIDKAEDRGRFKEAMEKIGLKC---PESYV 148
Cdd:PRK08463 68 IAKAcGADAIHPGYGF---------LSENYEFAK-AVEdagiiFIGPKSEVIRKMGNKNIARYLMKKNGIPIvpgTEKLN 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 149 CHSMNEALSAQAKVGFPTLIRPSftMGGSGGGI-AYNKEEFMaicERGFDASP--------THELLIEQSVLGWKEYEME 219
Cdd:PRK08463 138 SESMEEIKIFARKIGYPVILKAS--GGGGGRGIrVVHKEEDL---ENAFESCKrealayfnNDEVFMEKYVVNPRHIEFQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 220 VVRDKADNAIII----CSIENfdpmgvHTGDSITVAPAQTLTDKEYQIMRNASLAVLREIGVDTGGSnVQFSVNPANgEL 295
Cdd:PRK08463 213 ILGDNYGNIIHLcerdCSIQR------RHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGT-IEFLLDDYN-RF 284
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 495591993 296 IVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLNELSNDI 339
Cdd:PRK08463 285 YFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEILDLEQSDI 328
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
84-332 |
7.60e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 49.74 E-value: 7.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 84 DAILPTMGGqtalncaldLSRNG----VLAKYNVELIGASEDAIDKAEDRGRFKEAMEKIGLKC-PESY-VCHSMNEALS 157
Cdd:PRK08462 78 DAIFPGYGF---------LSENQnfveICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPViPGSDgALKSYEEAKK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 158 AQAKVGFPTLIRPSFTMGGSGGGIAYNKEE----FMAICERGFDASPTHELLIEQSVLGWKEYEMEVVRDKADNAIII-- 231
Cdd:PRK08462 149 IAKEIGYPVILKAAAGGGGRGMRVVEDESDlenlYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVge 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 232 --CSIENfdpmgvHTGDSITVAPAQTLTDKEYQIMRNASLAVLREIGVDTGGSnVQFSVNpANGELIVIEMNPRVSRSSA 309
Cdd:PRK08462 229 rdCSLQR------RHQKLIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGT-FEFLLD-SNLDFYFMEMNTRLQVEHT 300
|
250 260
....*....|....*....|...
gi 495591993 310 LASKATGFPIAKVAAKLAVGYTL 332
Cdd:PRK08462 301 VSEMVSGLDLIEWMIKIAEGEEL 323
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
102-304 |
7.91e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 49.80 E-value: 7.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 102 LSRNG----VLAKYNVELIGASEDAIDKAEDRGRFKEAMEKIGLKC-PESY-VCHSMNEALSAQAKVGFPTLIRPsfTMG 175
Cdd:PRK08591 85 LSENAdfaeICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVvPGSDgPVDDEEEALAIAKEIGYPVIIKA--TAG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 176 GSGGGI--AYNKEEFmaicERGFDASPTH--------ELLIEQSVLGWKEYEMEVVRDKADNAIII----CSI------- 234
Cdd:PRK08591 163 GGGRGMrvVRTEAEL----EKAFSMARAEakaafgnpGVYMEKYLENPRHIEIQVLADGHGNAIHLgerdCSLqrrhqkv 238
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495591993 235 --EnfdpmgvhtgdsitvAPAQTLTDKEYQIMRNASLAVLREIGVdTGGSNVQFSVNpANGELIVIEMNPRV 304
Cdd:PRK08591 239 leE---------------APSPAITEELRRKIGEAAVKAAKAIGY-RGAGTIEFLYE-KNGEFYFIEMNTRI 293
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
74-304 |
1.41e-05 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 49.37 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 74 VEKII--AKER-PDAILPTMGGqtalncaldLSRNGVLAKY----NVELIGASEDAIDKAEDRGRFKEAMEKIGLKC-PE 145
Cdd:PRK12999 67 IDEIIrvAKQAgVDAIHPGYGF---------LSENPEFARAcaeaGITFIGPTAEVLRLLGDKVAARNAAIKAGVPViPG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 146 SYV-CHSMNEALSAQAKVGFPTLIRPSftMGGSGGG--IAYNKEEFmaicERGFDASPTH--------ELLIEQSVLGWK 214
Cdd:PRK12999 138 SEGpIDDIEEALEFAEEIGYPIMLKAS--AGGGGRGmrIVRSEEEL----EEAFERAKREakaafgndEVYLEKYVENPR 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 215 EYEMEVVRDKADNAIII----CS--------IEnfdpmgvhtgdsitVAPAQTLTDKEYQIMRNASLAVLREIGVDTGGS 282
Cdd:PRK12999 212 HIEVQILGDKHGNVVHLyerdCSvqrrhqkvVE--------------IAPAPGLSEELRERICEAAVKLARAVGYVNAGT 277
|
250 260
....*....|....*....|..
gi 495591993 283 nVQFSVNpANGELIVIEMNPRV 304
Cdd:PRK12999 278 -VEFLVD-ADGNFYFIEVNPRI 297
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
35-206 |
1.09e-04 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 45.32 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 35 KALREEGYRVILVnsnpatimtdpEMADVTYIEPILWQtVEKIIAKERPDAILPTmggQTALNCALDLSRNgvLAKYNVE 114
Cdd:COG0189 21 EAAQRRGHEVEVI-----------DPDDLTLDLGRAPE-LYRGEDLSEFDAVLPR---IDPPFYGLALLRQ--LEAAGVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 115 LIGASEdAIDKAEDRGRFKEAMEKIGLKCPESYVCHSMNEALSAQAKVGFPTLIRPSFTMGGSGGGIAYNKEEFMAICER 194
Cdd:COG0189 84 VVNDPE-AIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEA 162
|
170
....*....|..
gi 495591993 195 gFDASPTHELLI 206
Cdd:COG0189 163 -LTELGSEPVLV 173
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
679-838 |
1.54e-04 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 44.23 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 679 LGLRQPENRTARNEEEAIVLAnEVGYPLVVRPSyVLGGR-AMQVVHSDDELRTYMNEAVQVSEDspVLLDFFLN-HAIEV 756
Cdd:pfam07478 13 VTFTRADWKLNPKEWCAQVEE-ALGYPVFVKPA-RLGSSvGVSKVESREELQAAIEEAFQYDEK--VLVEEGIEgREIEC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 757 ------DVDCVSDGQEVVIGGIMQHVEQAGVHSGDSGCslpPYSLSAEIQDEIRRQTKAMAKALNVVGLMNVQFAVQ-DD 829
Cdd:pfam07478 89 avlgneDPEVSPVGEIVPSGGFYDYEAKYIDDSAQIVV---PADLEEEQEEQIQELALKAYKALGCRGLARVDFFLTeDG 165
|
....*....
gi 495591993 830 VVYVLEVNP 838
Cdd:pfam07478 166 EIVLNEVNT 174
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
644-869 |
5.69e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 43.55 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 644 LANALVENGVNIIGTSADSIDAAEDRERFQKVLHDLGLrqP----ENRTARNEEEAIVLANEVGYPLVVRPSYVLGGRAM 719
Cdd:PRK07178 90 LAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGV--PvtpgSEGNLADLDEALAEAERIGYPVMLKATSGGGGRGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 720 QVVHSDDELRT----YMNEAVQVSEDSPVLLDFFLNHAIEVDVDCVSDGQEVVIggimqhveqagvHSGDSGCS------ 789
Cdd:PRK07178 168 RRCNSREELEQnfprVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVV------------HLFERDCSiqrrnq 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 790 -LPPYSLSAEIQDEIRRQTKAMA-KALNVVGLMN---VQFAV-QDDVVYVLEVNPRASRTVPFVSKATSVPLAKIAARAM 863
Cdd:PRK07178 236 kLIEIAPSPQLTPEQRAYIGDLAvRAAKAVGYENagtVEFLLdADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIA 315
|
....*.
gi 495591993 864 AGISLA 869
Cdd:PRK07178 316 SGLPLS 321
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
939-1038 |
1.83e-03 |
|
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: 39.21 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 939 VFISVRDADKPYLETMARNFQEQGYGLCATRGTAQYLTDKGFFVQTIHKVAE----GRPHIIDYIKNGEIAVVVNTVVSD 1014
Cdd:cd01423 3 ILISIGSYSKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEepqnDKPSLRELLAEGKIDLVINLPSNR 82
|
90 100
....*....|....*....|....
gi 495591993 1015 AQAVKDSHSIRRSALNQRIPLYTT 1038
Cdd:cd01423 83 GKRVLDNDYVMRRAADDFAVPLIT 106
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
119-304 |
8.28e-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: 39.67 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 119 SEDAIDKAEDRGRFKEAMEKIGLKCPESYVCHSMNEALSAQAKVGFPTLIRPSfTMG--GSGGGIAYNKEEFmaicERGF 196
Cdd:COG0026 80 GPEALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTR-RGGydGKGQVVIKSAADL----EAAW 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495591993 197 DASPTHELLIEQSVlgwkEYEME----VVRDKADNAIIICSIENfdpmgVHTgDSI---TVAPAQtLTDKEYQIMRNASL 269
Cdd:COG0026 155 AALGGGPCILEEFV----PFERElsviVARSPDGEVATYPVVEN-----VHR-NGIldeSIAPAR-ISEALAAEAEEIAK 223
|
170 180 190
....*....|....*....|....*....|....*..
gi 495591993 270 AVLREIGVdTG--GsnVQFSVNPaNGELIVIEMNPRV 304
Cdd:COG0026 224 RIAEALDY-VGvlA--VEFFVTK-DGELLVNEIAPRP 256
|
|
| |
