|
Name |
Accession |
Description |
Interval |
E-value |
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
1-1068 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 2133.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 1 MPKRTDLKSiliigagpiiigQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADVTYIEPITWQVVERIIAK 80
Cdd:PRK05294 1 MPKRTDIKKiliigsgpivigQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 81 EKPDAILPTMGGQTALNCALDLWRNGVLDKYKVELIGATPEAIDKAEDRLKFKNAMTKIGLGSARSGVAHSMDEAWAVQK 160
Cdd:PRK05294 81 ERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 161 DVGFPVIIRPSFTMGGTGGGIAYNPEEFETICKRGLEASPTNELLIEESLIGWKEYEMEVVRDKADNCIIVCSIENLDPM 240
Cdd:PRK05294 161 EIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 241 GVHTGDSITVAPAQTLTDKEYQIMRNASLAVLREIGVDTGGSNVQFSVNPADGRMIVIEMNPRVSRSSALASKATGFPIA 320
Cdd:PRK05294 241 GVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVETGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 321 KIAAKLAVGFTLDELRNEITgGATPASFEPSIDYVVTKIPRFAFEKFPQADNRLTTQMKSVGEVMAIGRTFQESFQKALR 400
Cdd:PRK05294 321 KVAAKLAVGYTLDEIKNDIT-GKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 401 GLEVGVDGMNEK---TQDREILEKELGEPGPDRIWYVGDAFAQGFTMEEVHQLTHIDPWFLVQIKDIVDIELWLDEQSLD 477
Cdd:PRK05294 400 SLEIGVTGLDEDlfeEESLEELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 478 sIDKDMMLTLKKKGFSDRRLAKLLKTTDTAIREKRRALNVRPVYKRVDTCAGEFATNTAYMYSTYEEECESNPTDKKKIM 557
Cdd:PRK05294 480 -LDAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVL 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 558 VLGGGPNRIGQGIEFDYCCVHAAFAMREDGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIVDKEKPVGVIVQYG 637
Cdd:PRK05294 559 VLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFG 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 638 GQTPLKLALDLEANGVPIVGTSPDMIDAAEDRERFQKMLQELGLRQPPNRTARTEAEALALAQEIGYPLVVRPSYVLGGR 717
Cdd:PRK05294 639 GQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGR 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 718 AMEIVHEQRDLERYMREAVKVSHDSPVLLDRFLNDAIEVDVDCLSDGNRTFIGGVMEHIEQAGVHSGDSACSLPPYSLSQ 797
Cdd:PRK05294 719 AMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICDGEDVLIGGIMEHIEEAGVHSGDSACSLPPQTLSE 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 798 ETIAELKRQTALMAKGLNVVGLMNVQFAIQhkegQDVVFVLEVNPRASRTVPYVSKATGLQLAKIAARCMVGQSLDSQGI 877
Cdd:PRK05294 799 EIIEEIREYTKKLALELNVVGLMNVQFAVK----DDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGY 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 878 GAEVVPPYFSVKEAVFPFVKFPGVDTILGPEMKSTGEVMGVGKTFGEAFVKSQLGAGVKLPTSGKVFLSIKNSDKPRGVK 957
Cdd:PRK05294 875 TKGLIPPYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSGTVFLSVRDRDKEEVVE 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 958 VAKDLVELGFSVVATRGTAAAIAAEGIPVSVVNKVVEGRPHVVDMIKNNEIALVINTVeEKRNAITDSRAIRTSALIARA 1037
Cdd:PRK05294 955 LAKRLLELGFKILATSGTAKFLREAGIPVELVNKVHEGRPHIVDLIKNGEIDLVINTP-TGRQAIRDGFSIRRAALEYKV 1033
|
1050 1060 1070
....*....|....*....|....*....|...
gi 1864611846 1038 TTFTTIAGAEAAVEGMRYL--NELHVYDLQGLH 1068
Cdd:PRK05294 1034 PYITTLAGARAAVKAIEALkfGELEVRSLQEYH 1066
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
2-1053 |
0e+00 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 1628.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 2 PKRTDLKSILIIGAGPIIIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADVTYIEPITWQVVERIIAKE 81
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 82 KPDAILPTMGGQTALNCALDLWRNGVLDKYKVELIGATPEAIDKAEDRLKFKNAMTKIGLGSARSGVAHSMDEAWAVQKD 161
Cdd:TIGR01369 81 RPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 162 VGFPVIIRPSFTMGGTGGGIAYNPEEFETICKRGLEASPTNELLIEESLIGWKEYEMEVVRDKADNCIIVCSIENLDPMG 241
Cdd:TIGR01369 161 IGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 242 VHTGDSITVAPAQTLTDKEYQIMRNASLAVLREIGVDtGGSNVQFSVNPADGRMIVIEMNPRVSRSSALASKATGFPIAK 321
Cdd:TIGR01369 241 VHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIE-GGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 322 IAAKLAVGFTLDELRNEITGGaTPASFEPSIDYVVTKIPRFAFEKFPQADNRLTTQMKSVGEVMAIGRTFQESFQKALRG 401
Cdd:TIGR01369 320 VAAKLAVGYTLDELKNPVTGT-TPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 402 LE---VGVDGMNEKTQDREILEKELGEPGPDRIWYVGDAFAQGFTMEEVHQLTHIDPWFLVQIKDIVDIELWLDEQSLDS 478
Cdd:TIGR01369 399 LEigaTGFDLPDREVEPDEDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTD 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 479 IDKDMMLTLKKKGFSDRRLAKLLKTTDTAIREKRRALNVRPVYKRVDTCAGEFATNTAYMYSTYEEECESNP-TDKKKIM 557
Cdd:TIGR01369 479 LDPELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPfTDKKKVL 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 558 VLGGGPNRIGQGIEFDYCCVHAAFAMREDGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIVDKEKPVGVIVQYG 637
Cdd:TIGR01369 559 VLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFG 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 638 GQTPLKLALDLEANGVPIVGTSPDMIDAAEDRERFQKMLQELGLRQPPNRTARTEAEALALAQEIGYPLVVRPSYVLGGR 717
Cdd:TIGR01369 639 GQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGR 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 718 AMEIVHEQRDLERYMREAVKVSHDSPVLLDRFLNDAIEVDVDCLSDGNRTFIGGVMEHIEQAGVHSGDSACSLPPYSLSQ 797
Cdd:TIGR01369 719 AMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSA 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 798 ETIAELKRQTALMAKGLNVVGLMNVQFAIqhKEGQdvVFVLEVNPRASRTVPYVSKATGLQLAKIAARCMVGQSLDSQGI 877
Cdd:TIGR01369 799 EIVDRIKDIVRKIAKELNVKGLMNIQFAV--KDGE--VYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGV 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 878 GAEVVPPYFSVKEAVFPFVKFPGVDTILGPEMKSTGEVMGVGKTFGEAFVKSQLGAGVKLPTSGKVFLSIKNSDKPRGVK 957
Cdd:TIGR01369 875 GKEKEPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLD 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 958 VAKDLVELGFSVVATRGTAAAIAAEGIPVSVVNKVVEGRPHVVDMIKNNEIALVINTVEEKRNAITDSRAIRTSALIARA 1037
Cdd:TIGR01369 955 LARKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEGRPNILDLIKNGEIELVINTTSKGAGTATDGYKIRREALDYGV 1034
|
1050
....*....|....*.
gi 1864611846 1038 TTFTTIAGAEAAVEGM 1053
Cdd:TIGR01369 1035 PLITTLNTAEAFAEAL 1050
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
3-1058 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 1545.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 3 KRTDLKSILIIGAGPIIIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADVTYIEPITWQVVERIIAKEK 82
Cdd:PLN02735 19 KRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 83 PDAILPTMGGQTALNCALDLWRNGVLDKYKVELIGATPEAIDKAEDRLKFKNAMTKIGLGSARSGVAHSMDEAWAVQKDV 162
Cdd:PLN02735 99 PDALLPTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 163 G-FPVIIRPSFTMGGTGGGIAYNPEEFETICKRGLEASPTNELLIEESLIGWKEYEMEVVRDKADNCIIVCSIENLDPMG 241
Cdd:PLN02735 179 GeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 242 VHTGDSITVAPAQTLTDKEYQIMRNASLAVLREIGVDTGGSNVQFSVNPADGRMIVIEMNPRVSRSSALASKATGFPIAK 321
Cdd:PLN02735 259 VHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVECGGSNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 322 IAAKLAVGFTLDELRNEITGgATPASFEPSIDYVVTKIPRFAFEKFPQADNRLTTQMKSVGEVMAIGRTFQESFQKALRG 401
Cdd:PLN02735 339 MAAKLSVGYTLDQIPNDITL-KTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRS 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 402 LEVGVDG-----MNEKTQDREILEKELGEPGPDRIWYVGDAFAQGFTMEEVHQLTHIDPWFLVQIKDIVDIELWLDEQSL 476
Cdd:PLN02735 418 LETGFSGwgcakVKELDWDWEQLKYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSL 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 477 DSIDKDMMLTLKKKGFSDRRLAKLLKTTDTAIREKRRALNVRPVYKRVDTCAGEFATNTAYMYSTYEEECESNPTDKKKI 556
Cdd:PLN02735 498 SELSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPTNKKKV 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 557 MVLGGGPNRIGQGIEFDYCCVHAAFAMREDGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIVDKEKPVGVIVQY 636
Cdd:PLN02735 578 LILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQF 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 637 GGQTPLKLALDLE----------ANG---VPIVGTSPDMIDAAEDRERFQKMLQELGLRQPPNRTARTEAEALALAQEIG 703
Cdd:PLN02735 658 GGQTPLKLALPIQkyldknpppsASGngnVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKRIG 737
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 704 YPLVVRPSYVLGGRAMEIVHEQRDLERYMREAVKVSHDSPVLLDRFLNDAIEVDVDCLSDGN-RTFIGGVMEHIEQAGVH 782
Cdd:PLN02735 738 YPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALADSEgNVVIGGIMEHIEQAGVH 817
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 783 SGDSACSLPPYSLSQETIAELKRQTALMAKGLNVVGLMNVQFAIQHkegQDVVFVLEVNPRASRTVPYVSKATGLQLAKI 862
Cdd:PLN02735 818 SGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITP---SGEVYIIEANPRASRTVPFVSKAIGHPLAKY 894
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 863 AARCMVGQSLDSQGIGAEVVPPYFSVKEAVFPFVKFPGVDTILGPEMKSTGEVMGVGKTFGEAFVKSQLGAGVKLPTSGK 942
Cdd:PLN02735 895 ASLVMSGKSLKDLGFTEEVIPAHVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLPLSGT 974
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 943 VFLSIKNSDKPRGVKVAKDLVELGFSVVATRGTAAAIAAEGIPVSVVNKVVEGRPHVVDMIKNNEIALVINTVEEKRNAI 1022
Cdd:PLN02735 975 VFISLNDLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVLKLHEGRPHAGDMLANGQIQLMVITSSGDALDQ 1054
|
1050 1060 1070
....*....|....*....|....*....|....*.
gi 1864611846 1023 TDSRAIRTSALIARATTFTTIAGAEAAVEGMRYLNE 1058
Cdd:PLN02735 1055 KDGRQLRRMALAYKVPIITTVAGALATAQAVKSLKE 1090
|
|
| 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: 1487.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 1 MPKRTDLKSILIIGAGPIIIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADVTYIEPITWQVVERIIAK 80
Cdd:PRK12815 1 MPKDTDIQKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 81 EKPDAILPTMGGQTALNCALDLWRNGVLDKYKVELIGATPEAIDKAEDRLKFKNAMTKIGLGSARSGVAHSMDEAWAVQK 160
Cdd:PRK12815 81 EKPDALLATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 161 DVGFPVIIRPSFTMGGTGGGIAYNPEEFETICKRGLEASPTNELLIEESLIGWKEYEMEVVRDKADNCIIVCSIENLDPM 240
Cdd:PRK12815 161 KIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 241 GVHTGDSITVAPAQTLTDKEYQIMRNASLAVLREIGVdTGGSNVQFSVNPADGRMIVIEMNPRVSRSSALASKATGFPIA 320
Cdd:PRK12815 241 GIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGV-VGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 321 KIAAKLAVGFTLDELRNEITgGATPASFEPSIDYVVTKIPRFAFEKFPQADNRLTTQMKSVGEVMAIGRTFQESFQKALR 400
Cdd:PRK12815 320 KIAAKLAVGYTLNELKNPVT-GLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 401 GLEVGVDGMN----EKTQDREILEKELGEPGPDRIWYVGDAFAQGFTMEEVHQLTHIDPWFLVQIKDIVDIELWLDEQSL 476
Cdd:PRK12815 399 SLEIKRNGLSlpieLSGKSDEELLQDLRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEDGL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 477 DsIDKDMMLTLKKKGFSDRRLAKLLKTTDTAIREKRRALNVRPVYKRVDTCAGEFATNTAYMYSTYEEECESNPT-DKKK 555
Cdd:PRK12815 479 D-LSADLLRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGESEAEPSsEKKK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 556 IMVLGGGPNRIGQGIEFDYCCVHAAFAMREDGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIVDKEKPVGVIVQ 635
Cdd:PRK12815 558 VLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIVQ 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 636 YGGQTPLKLALDLEANGVPIVGTSPDMIDAAEDRERFQKMLQELGLRQPPNRTARTEAEALALAQEIGYPLVVRPSYVLG 715
Cdd:PRK12815 638 FGGQTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIG 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 716 GRAMEIVHEQRDLERYMREAVKVSHdsPVLLDRFLnDAIEVDVDCLSDGNRTFIGGVMEHIEQAGVHSGDSACSLPPYSL 795
Cdd:PRK12815 718 GQGMAVVYDEPALEAYLAENASQLY--PILIDQFI-DGKEYEVDAISDGEDVTIPGIIEHIEQAGVHSGDSIAVLPPQSL 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 796 SQETIAELKRQTALMAKGLNVVGLMNVQFAIQHkegqDVVFVLEVNPRASRTVPYVSKATGLQLAKIAARCMVGQSLDSQ 875
Cdd:PRK12815 795 SEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLAN----DEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLAEL 870
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 876 GIGAEVVP--PYFSVKEAVFPFVKFPGVDTILGPEMKSTGEVMGVGKTFGEAFVKSQLGAGVKLPTSGKVFLSIKNSDKP 953
Cdd:PRK12815 871 GYPNGLWPgsPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGTIFISVRDEDKP 950
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 954 RGVKVAKDLVELGFSVVATRGTAAAIAAEGIPVSVVNKVVEGRPHVVDMIKNNEIALVINTVEEKRnAITDSRAIRTSAL 1033
Cdd:PRK12815 951 EVTKLARRFAQLGFKLLATEGTANWLAEEGITTGVVEKVQEGSPSLLERIKQHRIVLVVNTSLSDS-ASEDAIKIRDEAL 1029
|
1050 1060 1070
....*....|....*....|....*....|....*.
gi 1864611846 1034 IARATTFTTIAGAEAAVEGMRYLnELHVYDLQGLHK 1069
Cdd:PRK12815 1030 STHIPVFTELETAQAFLQVLESL-ALTTQPIQELQE 1064
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
559-1054 |
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: 770.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 559 LGGGPNRIGQGIEFDYCCVHAAFAMREDGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIVDKEKPVGVIVQYGG 638
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 639 QTPLKLALDLEAN----GVPIVGTSPDMIDAAEDRERFQKMLQELGLRQPPNRTARTEAEALALAQEIGYPLVVRPSYVL 714
Cdd:COG0458 81 QTALNLAVELEEAgileGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 715 GGRAMEIVHEQRDLERYMREAVKVSHDSPVLLDRFLNDAIEVDVDCLSDGNRT-FIGGVMEHIEQAGVHSGDSACSLPPY 793
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNvIIVGIMEHIEPAGVHSGDSICVAPPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 794 SLSQETIAELKRQTALMAKGLNVVGLMNVQFAIQhkegQDVVFVLEVNPRASRTVPYVSKATGLQLAKIAARCMVGQSLD 873
Cdd:COG0458 241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD----DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 874 SQGIGAEVVP--PYFSVKEAVFPFVKFPGVDTILGPEMKSTGEVMGVGKTFGEAFVKSQLGAGVKLPtsGKVFLS-IKNS 950
Cdd:COG0458 317 ELGNDTGFEPtlDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLP--GTVLLSlVADD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 951 DKPRGVKVAKDLVELGFSVVATRGTAAAIAAEGIPVSVVNKVVEGRPHVVDMIKNNEIALVINTVEEKRnAITDSRAIRT 1030
Cdd:COG0458 395 DKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVINTLLGAK-SLGDSDGIIR 473
|
490 500
....*....|....*....|....
gi 1864611846 1031 SALIARATTFTTIAGAEAAVEGMR 1054
Cdd:COG0458 474 RALAAKVPYVTTLAAAAAAALAIK 497
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
22-561 |
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: 761.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 22 QACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADVTYIEPITWQVVERIIAKEKPDAILPTMGGQTALNCALD 101
Cdd:COG0458 10 QGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGGQTALNLAVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 102 LWRNGVLDKykVELIGATPEAIDKAEDRLKFKNAMTKIGLGSARSGVAHSMDEAWAVQKDVGFPVIIRPSFTMGGTGGGI 181
Cdd:COG0458 90 LEEAGILEG--VKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVLGGRGMGI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 182 AYNPEEFETICKRGLEASPTNELLIEESLIGWKEYEMEVVRDKADNCIIVCSIENLDPMGVHTGDSITVAPAQTLTDKEY 261
Cdd:COG0458 168 VYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAPPQTLSDKEY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 262 QIMRNASLAVLREIGVDtGGSNVQFSVNpaDGRMIVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGFTLDELRNEiTG 341
Cdd:COG0458 248 QRLRDATLKIARALGVV-GLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELGND-TG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 342 gatpasFEPSIDYVVTKIPRFAFEKFPQADNRLTTQMKSVGEVMAIGRTFQESFQKALRGLEVGVDGMN--EKTQDREIL 419
Cdd:COG0458 324 ------FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGTVllSLVADDDKE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 420 EKELGEPGPDRIWYVGDAFAQGFTMEEVHQLTHIDPWFLVQIKDIVDIELWLDEQSLDSIDkdmMLTLKKKGFSDRRLAK 499
Cdd:COG0458 398 EALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVINT---LLGAKSLGDSDGIIRR 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1864611846 500 LLKTTDTAIREKRRALNVRPVYKRVDTCAGEFATNTAYMYSTYEEECESNPTDKKKIMVLGG 561
Cdd:COG0458 475 ALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
128-333 |
2.42e-86 |
|
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: 277.26 E-value: 2.42e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 128 DRLKFKNAMTKIGLGSARS--GVAHSMDEAWAVQKDVGFPVIIRPSFTMGGTGGGIAYNPEEFETICKRGLEASPT---- 201
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGtaGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 202 NELLIEESLIGWKEYEMEVVRDKADNCIIVCSIENLDPMgvHTGDSITVAPAQTLTDKEYQIMRNASLAVLREIGVdTGG 281
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGY-VGA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1864611846 282 SNVQFSVNPADGRMIVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGFTLD 333
Cdd:pfam02786 158 GTVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
419-542 |
1.90e-64 |
|
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: 213.47 E-value: 1.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 419 LEKELGEPGPDRIWYVGDAFAQGFTMEEVHQLTHIDPWFLVQIKDIVDIELWLDEQSLDSIDKDMMLTLKKKGFSDRRLA 498
Cdd:smart01096 1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1864611846 499 KLLKTTDTAIREKRRALNVRPVYKRVDTCAGEFATNTAYMYSTY 542
Cdd:smart01096 81 KLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
941-1051 |
7.29e-47 |
|
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: 163.03 E-value: 7.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 941 GKVFLSIKNSDKPRGVKVAKDLVELGFSVVATRGTAAAIAAEGIPVSVVNKVVEGRPHVVDMIKNNEIALVINTVEEKRn 1020
Cdd:cd01424 1 GTVFISVADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEGRPNIVDLIKNGEIQLVINTPSGKR- 79
|
90 100 110
....*....|....*....|....*....|.
gi 1864611846 1021 AITDSRAIRTSALIARATTFTTIAGAEAAVE 1051
Cdd:cd01424 80 AIRDGFSIRRAALEYKVPYFTTLDTARAAVE 110
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
421-500 |
1.75e-34 |
|
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: 126.34 E-value: 1.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 421 KELGEPGPDRIWYVGDAFAQGFTMEEVHQLTHIDPWFLVQIKDIVDIELWLDEQSLDsIDKDMMLTLKKKGFSDRRLAKL 500
Cdd:pfam02787 1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAGLD-LDAELLREAKRLGFSDRQIAKL 79
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
668-873 |
5.46e-33 |
|
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: 127.04 E-value: 5.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 668 DRERFQKMLQELGLRQPPN--RTARTEAEALALAQEIGYPLVVRPSYVLGGRAMEIVHEQRDL----ERYMREAVKVSHD 741
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGtaGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELaelfALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 742 SPVLLDRFLNDAIEVDVDCLSDGNRTFIG-GVMEHIEQagVHSGDSACSLPPYSLSQETIAELKRQTALMAKGLNVVGLM 820
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITvCNRECSDQ--RRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1864611846 821 NVQFAIQHKEGQdvVFVLEVNPRASRTVPYVSKATGLQLAKIAARCMVGQSLD 873
Cdd:pfam02786 159 TVEFALDPFSGE--YYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
115-329 |
2.91e-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: 112.27 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 115 LIGATPEAIDKAEDRLKFKNAMTKIGLGSARSGVAHSMDEAWAVQKDVGFPVIIRPSFTMGGTGGGIAYNPEE----FET 190
Cdd:COG0439 41 LPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEEleaaLAE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 191 ICKRGLEASPTNELLIEESLIGwKEYEME-VVRDKAdncIIVCSI---ENLDPMGVHTGDsitVAPAQtLTDKEYQIMRN 266
Cdd:COG0439 121 ARAEAKAGSPNGEVLVEEFLEG-REYSVEgLVRDGE---VVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1864611846 267 ASLAVLREIGVDTGGSNVQFSVNPaDGRMIVIEMNPRVS--RSSALASKATGFPIAKIAAKLAVG 329
Cdd:COG0439 193 LVARALRALGYRRGAFHTEFLLTP-DGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALG 256
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
652-870 |
1.38e-22 |
|
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: 98.41 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 652 GVPivGTSPDMIDAAEDRERFQKMLQELGLRQPPNRTARTEAEALALAQEIGYPLVVRPSYVLGGRAMEIVHEQRDLERY 731
Cdd:COG0439 40 GLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 732 MREAVK----VSHDSPVLLDRFLnDAIEVDVDCLSDGNRTFIGGVMEHIEQA--GVHSGDSAcslpPYSLSQETIAELKR 805
Cdd:COG0439 118 LAEARAeakaGSPNGEVLVEEFL-EGREYSVEGLVRDGEVVVCSITRKHQKPpyFVELGHEA----PSPLPEELRAEIGE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1864611846 806 QTALMAKGLNVV-GLMNVQFAIqhkEGQDVVFVLEVNPRAS--RTVPYVSKATGLQLAKIAARCMVGQ 870
Cdd:COG0439 193 LVARALRALGYRrGAFHTEFLL---TPDGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGE 257
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
956-1033 |
6.27e-22 |
|
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: 91.01 E-value: 6.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 956 VKVAKDLVELGFSVVATRGTAAAIAAEGIPV-SVVNKVVEGRPH----VVDMIKNNEIALVINTVEEKRNAITDSRAIRT 1030
Cdd:pfam02142 3 VELAKALVELGFELLATGGTAKFLREAGIPVtEVVEKTGEGRPGgrvqIGDLIKNGEIDLVINTLYPFKATVHDGYAIRR 82
|
...
gi 1864611846 1031 SAL 1033
Cdd:pfam02142 83 AAE 85
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
956-1033 |
1.49e-21 |
|
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: 89.84 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 956 VKVAKDLVELGFSVVATRGTAAAIAAEGIPVS--VVNKVVEGRPHVVDMIKNNEIALVINTVEE-KRNAITDSRAIRTSA 1032
Cdd:smart00851 3 VEFAKRLAELGFELLATGGTAKFLREAGLPVVktLHPKVHGGIPQILDLIKNGEIDLVINTLYPfEAQAHEDGYSIRRAA 82
|
.
gi 1864611846 1033 L 1033
Cdd:smart00851 83 E 83
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
27-329 |
3.68e-15 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 78.82 E-value: 3.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 27 DYSGAQACKALREEGYRVILVNSNPATIMT------------DPEMADVTYIEpitwqVVERIIAKEKPDAILPTMGGQT 94
Cdd:COG3919 14 DINALAVARSLGEAGVRVIVVDRDPLGPAArsryvdevvvvpDPGDDPEAFVD-----ALLELAERHGPDVLIPTGDEYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 95 ALncaldlwrngvLDKYKVEL------IGATPEAIDKAEDRLKFKNAMTKIGLGSARSGVAHSMDEAWAVQKDVGFPVII 168
Cdd:COG3919 89 EL-----------LSRHRDELeehyrlPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGFPVVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 169 RPS--------FTMGGTGGGIAYNPEEFETICKRGLEASptNELLIEESLIGWKEYE--MEVVRDKADNCIIVCSIENL- 237
Cdd:COG3919 158 KPAdsvgydelSFPGKKKVFYVDDREELLALLRRIAAAG--YELIVQEYIPGDDGEMrgLTAYVDRDGEVVATFTGRKLr 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 238 -DPMGVHTGDSITVAPAQTLTDkeyqimrnASLAVLREIGVdTGGSNVQFSVNPADGRMIVIEMNPRVSRSSALASKAtG 316
Cdd:COG3919 236 hYPPAGGNSAARESVDDPELEE--------AARRLLEALGY-HGFANVEFKRDPRDGEYKLIEINPRFWRSLYLATAA-G 305
|
330
....*....|...
gi 1864611846 317 FPIAKIAAKLAVG 329
Cdd:COG3919 306 VNFPYLLYDDAVG 318
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
943-1048 |
2.91e-14 |
|
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: 69.85 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 943 VFLSIKNSDKPRGVKVAKDLVELGFSVVATRGTAAAIAAEGIPVSVVNKVVE-GRPHVVDMIKNN-EIALVINTVE--EK 1018
Cdd:cd00532 2 VFLSVSDHVKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRHEdGEPTVDAAIAEKgKFDVVINLRDprRD 81
|
90 100 110
....*....|....*....|....*....|
gi 1864611846 1019 RNAITDSRAIRTSALIARATTFTTIAGAEA 1048
Cdd:cd00532 82 RCTDEDGTALLRLARLYKIPVTTPNATAMF 111
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
659-874 |
9.99e-14 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 74.19 E-value: 9.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 659 SPDMIDAAEDRERFQKMLQELGLRQPPNRTARTEAEALALAQEIGYPLVVRPSY--------VLGGRAMEIVHEQRDLER 730
Cdd:COG3919 108 DADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGFPVVVKPADsvgydelsFPGKKKVFYVDDREELLA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 731 YMREAVKVSHDspVLLDRFL--NDAIEVDVDCLSDGN----RTFIGGVMEHIEQAGvhsGDSACslppysLSQETIAELK 804
Cdd:COG3919 188 LLRRIAAAGYE--LIVQEYIpgDDGEMRGLTAYVDRDgevvATFTGRKLRHYPPAG---GNSAA------RESVDDPELE 256
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 805 RQTALMAKGLNVVGLMNVQFAIQHKEGQDVVFvlEVNPRASRTVPYVSKAtGLQLAKIAARCMVGQSLDS 874
Cdd:COG3919 257 EAARRLLEALGYHGFANVEFKRDPRDGEYKLI--EINPRFWRSLYLATAA-GVNFPYLLYDDAVGRPLEP 323
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
617-892 |
5.99e-13 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 71.07 E-value: 5.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 617 LEDVLEIVDKEKPVGVIVqyGGQTPLKL----ALDLEANGVPIVGTSPDMIDAAEDRERFQKMLQELGLRQPPNRTARTE 692
Cdd:PRK12767 58 IDRLLDICKKEKIDLLIP--LIDPELPLlaqnRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 693 AEALA--LAQEIGYPLVVRPSYVLGGRAMEIVHEQRDLERYMreavkvSHDSPVLLDRFLNDaIEVDVDCLSDGNRTFIG 770
Cdd:PRK12767 136 EDFKAalAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLL------EYVPNLIIQEFIEG-QEYTVDVLCDLNGEVIS 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 771 GV-MEHIEqagVHSGDSacslppyslSQ-ETI--AELKRQTALMAKGLNVVGLMNVQFaiqhKEGQDVVFVLEVNPRASR 846
Cdd:PRK12767 209 IVpRKRIE---VRAGET---------SKgVTVkdPELFKLAERLAEALGARGPLNIQC----FVTDGEPYLFEINPRFGG 272
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1864611846 847 TVPyVSKATGLQLAKIAARCMvgqsldsqgIGAEVVPPYFSVKEAV 892
Cdd:PRK12767 273 GYP-LSYMAGANEPDWIIRNL---------LGGENEPIIGEYKEGL 308
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
649-872 |
6.80e-13 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 71.98 E-value: 6.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 649 EANGVPIVGTSPDMIDAAEDRERFQKMLQELGLrqP----PNRTARTEAEALALAQEIGYPLVVRPSYVLGGRAMEIVHE 724
Cdd:PRK06111 96 KEEGIVFIGPSADIIAKMGSKIEARRAMQAAGV--PvvpgITTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVET 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 725 QRDLERYM----REAVKVSHDSPVLLDRFLNDA--IEVDVDCLSDGNrtfiggvmehieqaGVHSGDSACSL-------- 790
Cdd:PRK06111 174 EQELTKAFesnkKRAANFFGNGEMYIEKYIEDPrhIEIQLLADTHGN--------------TVYLWERECSVqrrhqkvi 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 791 ---PPYSLSQETIAELKRQTALMAKGLNVVGLMNVQFAIqhkEGQDVVFVLEVNPRASRTVPYVSKATGLQLAKIAARCM 867
Cdd:PRK06111 240 eeaPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLV---DEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIA 316
|
....*
gi 1864611846 868 VGQSL 872
Cdd:PRK06111 317 AGEKL 321
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
74-340 |
1.23e-12 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 71.55 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 74 VERIIA---KEKPDAILPTMG-----GQTALNCaldlwrngvlDKYKVELIGATPEAIDKAEDRLKFKNAMTKIGL---- 141
Cdd:PRK08654 63 IERIIDvakKAGADAIHPGYGflaenPEFAKAC----------EKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVpvlp 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 142 GSARSgvAHSMDEAWAVQKDVGFPVIIRPSFTMGGTGGGIAYNPEEFEtickRGLEAS----------PTneLLIEESLI 211
Cdd:PRK08654 133 GTEEG--IEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELE----DAIESTqsiaqsafgdST--VFIEKYLE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 212 GWKEYEMEVVRDKADNCIIV----CSI----ENLdpmgvhtgdsITVAPAQTLTDKEYQIMRNASLAVLREIGVDTGGSn 283
Cdd:PRK08654 205 KPRHIEIQILADKHGNVIHLgdreCSIqrrhQKL----------IEEAPSPIMTPELRERMGEAAVKAAKAINYENAGT- 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1864611846 284 VQFSVNpaDGRMIVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGFTLDELRNEIT 340
Cdd:PRK08654 274 VEFLYS--NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELSFKQEDIT 328
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
649-873 |
3.04e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 67.09 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 649 EANGVPIVGTSPDMIDAAEDRERFQKMLQELGLRQPPNRTARTE--AEALALAQEIGYPLVVRPSYVLGGRAMEIVHEQR 726
Cdd:PRK12833 99 EAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVAslDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 727 DLERYM----REAVKVSHDSPVLLDRFLNDAIEVDVDCLSDGNRTfiggvmehieqagVHSGDSACSL-----------P 791
Cdd:PRK12833 179 QLAAELplaqREAQAAFGDGGVYLERFIARARHIEVQILGDGERV-------------VHLFERECSLqrrrqkileeaP 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 792 PYSLSQETIAELKRQTALMAKGLNVVGLMNVQFAIQHKEGQdvVFVLEVNPRASRTVPYVSKATGLQLAKIAARCMVGQS 871
Cdd:PRK12833 246 SPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARGE--FYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEP 323
|
..
gi 1864611846 872 LD 873
Cdd:PRK12833 324 LR 325
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
648-868 |
4.59e-11 |
|
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: 64.96 E-value: 4.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 648 LEANGVPIVGtSPDMIDAAEDRERFQKMLQELGLRQPPNRTARTEAEALALAQEIGYPLVVRPSYVLGGRAMEIVHEQRD 727
Cdd:COG0189 77 LEAAGVPVVN-DPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 728 LERYMrEAVKVSHDSPVLLDRFLNDAIEVDVDCLsdgnrtFIGG----VMEHIEQAG-----VHSGDSACslpPYSLSQE 798
Cdd:COG0189 156 LESIL-EALTELGSEPVLVQEFIPEEDGRDIRVL------VVGGepvaAIRRIPAEGefrtnLARGGRAE---PVELTDE 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 799 TIAELKRQTALMakGLNVVGlmnVQFAiqhkEGQDVVFVLEVNPRASrtVPYVSKATGLQLAKIAARCMV 868
Cdd:COG0189 226 ERELALRAAPAL--GLDFAG---VDLI----EDDDGPLVLEVNVTPG--FRGLERATGVDIAEAIADYLE 284
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
943-1039 |
1.36e-10 |
|
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: 59.62 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 943 VFLSIKNSDKPRGVKVAKDLVELGFSVVATRGTAAAIAAEGIPVSVVNKVVE----GRPHVVDMIKNNEIALVINtveek 1018
Cdd:cd01423 3 ILISIGSYSKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEepqnDKPSLRELLAEGKIDLVIN----- 77
|
90 100
....*....|....*....|...
gi 1864611846 1019 rnaITDSRA--IRTSALIARATT 1039
Cdd:cd01423 78 ---LPSNRGkrVLDNDYVMRRAA 97
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
30-317 |
2.44e-10 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 63.36 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 30 GAQACKALREE--GYRVILV---NSNPATIMTD-----PEMADVTYIEpitwqVVERIIAKEKPDAILPTMGGQTALnca 99
Cdd:PRK12767 12 RVQLVKALKKSllKGRVIGAdisELAPALYFADkfyvvPKVTDPNYID-----RLLDICKKEKIDLLIPLIDPELPL--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 100 ldLWRNgvLDKYK---VELIGATPEAIDKAEDRLKFKNAMTKIGLGSARSGVAHSMDEAWAVQ--KDVGFPVIIRPSFTM 174
Cdd:PRK12767 84 --LAQN--RDRFEeigVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALakGELQFPLFVKPRDGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 175 GGTGGGIAYNPEEFETICKRGLeasptnELLIEESLIGwKEYEMEVVRDKADNCIIVCSIENLDPMGVHTGDSITVapaq 254
Cdd:PRK12767 160 ASIGVFKVNDKEELEFLLEYVP------NLIIQEFIEG-QEYTVDVLCDLNGEVISIVPRKRIEVRAGETSKGVTV---- 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1864611846 255 tltdkEYQIMRNASLAVLREIGVDtGGSNVQFSVNpaDGRMIVIEMNPRVSRSSALASKAtGF 317
Cdd:PRK12767 229 -----KDPELFKLAERLAEALGAR-GPLNIQCFVT--DGEPYLFEINPRFGGGYPLSYMA-GA 282
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
109-339 |
3.17e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 63.97 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 109 DKYKVELIGATPEAIDKAEDRLKFKNAMTKIGL----GSarSGVAHSMDEAWAVQKDVGFPVIIRPsfTMGGTGGGI--A 182
Cdd:PRK07178 95 AERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVpvtpGS--EGNLADLDEALAEAERIGYPVMLKA--TSGGGGRGIrrC 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 183 YNPEEFETICKRGL-EASP---TNELLIEESLIGWKEYEMEVVRDKADNCIIV----CSIENldpmgvHTGDSITVAPAQ 254
Cdd:PRK07178 171 NSREELEQNFPRVIsEATKafgSAEVFLEKCIVNPKHIEVQILADSHGNVVHLferdCSIQR------RNQKLIEIAPSP 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 255 TLTDKEYQIMRNASLAVLREIGVDTGGSnVQFSVNpADGRMIVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGFTLDE 334
Cdd:PRK07178 245 QLTPEQRAYIGDLAVRAAKAVGYENAGT-VEFLLD-ADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLSY 322
|
....*
gi 1864611846 335 LRNEI 339
Cdd:PRK07178 323 KQEDI 327
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
643-790 |
5.67e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 63.08 E-value: 5.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 643 KLALDLEANGVPIVGTSPDMIDAAEDRERFQKMLQELGLRQPPNRTARTE--AEALALAQEIGYPLVVRPSYVLGGRAME 720
Cdd:PRK08654 90 EFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEdiEEAKEIAEEIGYPVIIKASAGGGGIGMR 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1864611846 721 IVHEQRDLERYMREAVKVSH----DSPVLLDRFLNDA--IEVDVDCLSDGNRtfiggvmehieqagVHSGDSACSL 790
Cdd:PRK08654 170 VVYSEEELEDAIESTQSIAQsafgDSTVFIEKYLEKPrhIEIQILADKHGNV--------------IHLGDRECSI 231
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
74-304 |
5.85e-10 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 63.62 E-value: 5.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 74 VERII--AKEK-PDAILPTMG-----GQTALNCAldlwRNGVldkykvELIGATPEAIDKAEDRLKFKNAMTKIGL---- 141
Cdd:PRK12999 67 IDEIIrvAKQAgVDAIHPGYGflsenPEFARACA----EAGI------TFIGPTAEVLRLLGDKVAARNAAIKAGVpvip 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 142 GSArsGVAHSMDEAWAVQKDVGFPVIIRPSFTMGGTGGGIAYNPEEFE---TICKRGLEASPTN-ELLIEESLIGWKEYE 217
Cdd:PRK12999 137 GSE--GPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEeafERAKREAKAAFGNdEVYLEKYVENPRHIE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 218 MEVVRDKADNciIV------CS--------IEnldpmgvhtgdsitVAPAQTLTDKEYQIMRNASLAVLREIGVDTGGSn 283
Cdd:PRK12999 215 VQILGDKHGN--VVhlyerdCSvqrrhqkvVE--------------IAPAPGLSEELRERICEAAVKLARAVGYVNAGT- 277
|
250 260
....*....|....*....|.
gi 1864611846 284 VQFSVNpADGRMIVIEMNPRV 304
Cdd:PRK12999 278 VEFLVD-ADGNFYFIEVNPRI 297
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
649-843 |
5.90e-10 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 63.62 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 649 EANGVPIVGTSPDMIDAAEDRERFQKMLQELGLRQPP--NRTARTEAEALALAQEIGYPLVVRPSYVLGGRAMEIVHEQR 726
Cdd:PRK12999 100 AEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPgsEGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 727 DL----ERYMREAVKVSHDSPVLLDRFLNDA--IEVDVdcLSDGNrtfiGGVmehieqagVHSGDSACSL---------- 790
Cdd:PRK12999 180 ELeeafERAKREAKAAFGNDEVYLEKYVENPrhIEVQI--LGDKH----GNV--------VHLYERDCSVqrrhqkvvei 245
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1864611846 791 -PPYSLSQETIAELKRQTALMAKGLNVVGLMNVQFAIQhKEGQdvvFVL-EVNPR 843
Cdd:PRK12999 246 aPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVD-ADGN---FYFiEVNPR 296
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
648-842 |
4.07e-09 |
|
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: 59.35 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 648 LEANGVPIVGTSPDMIDAAEDRERFQKMLQELGLRQPPNRTARTE--AEALALAQEIGYPLVVRPsyVLGG--RAMEIVH 723
Cdd:COG1181 75 LELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRGelADLEAIEEELGLPLFVKP--AREGssVGVSKVK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 724 EQRDLERYMREAVKvsHDSPVLLDRFLnDAIEVDVDCLsDGNRTFIGGVMEHIEQAGV-------HSGDSACSLPPySLS 796
Cdd:COG1181 153 NAEELAAALEEAFK--YDDKVLVEEFI-DGREVTVGVL-GNGGPRALPPIEIVPENGFydyeakyTDGGTEYICPA-RLP 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1864611846 797 QETIAELkRQTALMA-KGLNVVGLMNVQFaIQHKEGQdvVFVLEVNP 842
Cdd:COG1181 228 EELEERI-QELALKAfRALGCRGYARVDF-RLDEDGE--PYLLEVNT 270
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
116-408 |
5.65e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 59.66 E-value: 5.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 116 IGATPEAIDKAEDRLKFKNAMTKIGLgSARSGVAHSM---DEAWAVQKDVGFPVIIRPSFTMGGTGGGIAYNPEE----F 188
Cdd:PRK06111 103 IGPSADIIAKMGSKIEARRAMQAAGV-PVVPGITTNLedaEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQEltkaF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 189 ETICKRGLEASPTNELLIEESLIGWKEYEMEVVRDKADNCIIV----CSIENldpmgvHTGDSITVAPAQTLTDKEYQIM 264
Cdd:PRK06111 182 ESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLwereCSVQR------RHQKVIEEAPSPFLDEETRKAM 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 265 RNASLAVLREIGVdTGGSNVQFSVNPaDGRMIVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGFTLDELRNEI--TGG 342
Cdd:PRK06111 256 GERAVQAAKAIGY-TNAGTIEFLVDE-QKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLSFTQDDIkrSGH 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 343 AT--------PASFEPS----IDYVVTKIPRFAFEKFPQADNRLTTQMKS-VGEVMAIGRTFQESFQKALRGL-EVGVDG 408
Cdd:PRK06111 334 AIevriyaedPKTFFPSpgkiTDLTLPGGEGVRHDHAVENGVTVTPFYDPmIAKLIAHGETREEAISRLHDALeELKVEG 413
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
649-843 |
1.49e-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: 58.94 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 649 EANGVPIVGTSPDMIDAAEDRERFQKMLQELGLRQPP--NRTARTEAEALALAQEIGYPLVVRPSYVLGGRAMEIVHEQR 726
Cdd:COG1038 99 EEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPgtEGPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 727 DL----ERYMREAVKVSHDSPVLLDRFLNDA--IEVDVdcLSD--GNRtfiggvmehieqagVHSGDSACSL-------- 790
Cdd:COG1038 179 ELeeafESARREAKAAFGDDEVFLEKYIERPkhIEVQI--LGDkhGNI--------------VHLFERDCSVqrrhqkvv 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1864611846 791 ---PPYSLSQETIAELKrQTAL-MAKGLNVVGLMNVQFAIQhkEGQDVVFvLEVNPR 843
Cdd:COG1038 243 eiaPAPNLDEELREAIC-EAAVkLAKAVGYVNAGTVEFLVD--DDGNFYF-IEVNPR 295
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
116-304 |
6.33e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 56.35 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 116 IGATPEAIDKAEDRLKFKNAMTKIGL----GSArsGVAHSMDEAWAVQKDVGFPVIIRPsfTMGGTGGGI--AYNPEEFE 189
Cdd:PRK08591 103 IGPSAETIRLMGDKVTAKATMKKAGVpvvpGSD--GPVDDEEEALAIAKEIGYPVIIKA--TAGGGGRGMrvVRTEAELE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 190 ---TICKRGLEASPTN-ELLIEESLIGWKEYEMEVVRDKADNCIIV----CSI---------EnldpmgvhtgdsitvAP 252
Cdd:PRK08591 179 kafSMARAEAKAAFGNpGVYMEKYLENPRHIEIQVLADGHGNAIHLgerdCSLqrrhqkvleE---------------AP 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1864611846 253 AQTLTDKEYQIMRNASLAVLREIGVdTGGSNVQFSVNpADGRMIVIEMNPRV 304
Cdd:PRK08591 244 SPAITEELRRKIGEAAVKAAKAIGY-RGAGTIEFLYE-KNGEFYFIEMNTRI 293
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
649-875 |
6.73e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 56.29 E-value: 6.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 649 EANGVPIVGTSPDMIDAAEDRERFQKMLQELGLRQPPNRTA--RTEAEALALAQEIGYPLVVRPSYVLGGRAMEIVHEQR 726
Cdd:PRK08462 98 SHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGalKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDES 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 727 DLER-YM---REAVKVSHDSPVLLDRFLNDAIEVDVDCLSDGNrtfiGGVmehieqagVHSGDSACSL-----------P 791
Cdd:PRK08462 178 DLENlYLaaeSEALSAFGDGTMYMEKFINNPRHIEVQILGDKH----GNV--------IHVGERDCSLqrrhqklieesP 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 792 PYSLSQETIAELKRQTALMAKGLNVVGLMNVQFAIQHKegQDVVFvLEVNPRASRTVPYVSKATGLQLAKIAARCMVGQS 871
Cdd:PRK08462 246 AVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSN--LDFYF-MEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEE 322
|
....
gi 1864611846 872 LDSQ 875
Cdd:PRK08462 323 LPSQ 326
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
677-843 |
8.13e-08 |
|
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: 53.03 E-value: 8.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 677 QELGLRQPPNRTARTEAEALALAQEIGYPLVVRpSYVLG--GRAMEIVHEQRDLErymrEAVKVSHDSPVLLDRFLNDAI 754
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVK-ARRGGydGKGQYVVRSEADLP----QAWEELGDGPVIVEEFVPFDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 755 EVDVDCLSDGN-RTFIGGVMEHIEQAGVhsgdsaC--SLPPYSLSQETIAELKRQTALMAKGLNVVGLMNVQFAIqhKEG 831
Cdd:pfam02222 76 ELSVLVVRSVDgETAFYPVVETIQEDGI------CrlSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELFV--TED 147
|
170
....*....|..
gi 1864611846 832 QDVVFVlEVNPR 843
Cdd:pfam02222 148 GDLLIN-ELAPR 158
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
113-339 |
8.16e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 55.87 E-value: 8.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 113 VELIGATPEAIDKAEDRLKFKNAMTKIGL----GSarSGVAHSMDEAWAVQKDVGFPVIIRPSFTMGGTGGGIAYNPEE- 187
Cdd:PRK05586 100 IVFIGPDSETIELMGNKSNAREIMIKAGVpvvpGS--EGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEEl 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 188 ---FETICKRGLEASPTNELLIEESLIGWKEYEMEVVRDKADNCIIV----CSIENldpmgvHTGDSITVAPAQTLTDKE 260
Cdd:PRK05586 178 ikaFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLgerdCSLQR------RNQKVLEEAPSPVMTEEL 251
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1864611846 261 YQIMRNASLAVLREIGVDTGGSnVQFSVNpADGRMIVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGFTLDELRNEI 339
Cdd:PRK05586 252 RKKMGEIAVKAAKAVNYKNAGT-IEFLLD-KDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLSIKQEDI 328
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
74-304 |
5.33e-07 |
|
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: 53.93 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 74 VERII--AKEK-PDAILPTMG-----GQTALNCAldlwRNGVldkykvELIGATPEAIDKAEDRLKFKNAMTKIGL---- 141
Cdd:COG1038 66 IEEIIrvAKEKgVDAIHPGYGflsenPEFARACE----EAGI------TFIGPSPEVLEMLGDKVAARAAAIEAGVpvip 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 142 GSArsGVAHSMDEAWAVQKDVGFPVIIRPSftMGGTGGG--IAYNPEEFE---TICKRglEA-----SPtnELLIEESLI 211
Cdd:COG1038 136 GTE--GPVDDLEEALAFAEEIGYPVMLKAA--AGGGGRGmrVVRSEEELEeafESARR--EAkaafgDD--EVFLEKYIE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 212 GWKEYEMEVVRDKADNciIV------CS--------IEnldpmgvhtgdsitVAPAQTLTDKEYQIMRNASLAVLREIGV 277
Cdd:COG1038 208 RPKHIEVQILGDKHGN--IVhlferdCSvqrrhqkvVE--------------IAPAPNLDEELREAICEAAVKLAKAVGY 271
|
250 260
....*....|....*....|....*..
gi 1864611846 278 DTGGSnVQFSVNPaDGRMIVIEMNPRV 304
Cdd:COG1038 272 VNAGT-VEFLVDD-DGNFYFIEVNPRI 296
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
648-790 |
1.02e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 52.50 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 648 LEANGVPIVGTSPDMIDAAEDRERFQKMLQELGLRQPPNRTAR--TEAEALALAQEIGYPLVVRPSYVLGGRAMEIVHEQ 725
Cdd:PRK08591 95 CEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPvdDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTE 174
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1864611846 726 RDLERYMR----EAVKVSHDSPVLLDRFLNDA--IEVDVdcLSDGNrtfiGGVmehieqagVHSGDSACSL 790
Cdd:PRK08591 175 AELEKAFSmaraEAKAAFGNPGVYMEKYLENPrhIEIQV--LADGH----GNA--------IHLGERDCSL 231
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
656-873 |
1.27e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 52.02 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 656 VGTSPDMIDAAEDRERFQKMLQELGLRQPP--NRTARTEAEALALAQEIGYPLVVRPSYVLGGRAMEIVHEQRDL----E 729
Cdd:PRK05586 103 IGPDSETIELMGNKSNAREIMIKAGVPVVPgsEGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELikafN 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 730 RYMREAVKVSHDSPVLLDRFLNDAIEVDVDCLSD--GNRtfiggvmehieqagVHSGDSACSL-----------PPYSLS 796
Cdd:PRK05586 183 TAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDnyGNV--------------VHLGERDCSLqrrnqkvleeaPSPVMT 248
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1864611846 797 QETIAELKRQTALMAKGLNVVGLMNVQFAIQhKEGQdvVFVLEVNPRASRTVPYVSKATGLQLAKIAARCMVGQSLD 873
Cdd:PRK05586 249 EELRKKMGEIAVKAAKAVNYKNAGTIEFLLD-KDGN--FYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLS 322
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
116-339 |
1.88e-06 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 51.74 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 116 IGATPEAIDKAEDRLKFKNAMTKIGL----GSARSGvAHSMDEAWAVQKDVGFPVIIRPSFTMGGTGGGIAYNPEEFET- 190
Cdd:PRK08463 102 IGPKSEVIRKMGNKNIARYLMKKNGIpivpGTEKLN-SESMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDLENa 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 191 --ICKRGLEASPTN-ELLIEESLIGWKEYEMEVVRDKADNCIIV----CSIENldpmgvHTGDSITVAPAQTLTDKEYQI 263
Cdd:PRK08463 181 feSCKREALAYFNNdEVFMEKYVVNPRHIEFQILGDNYGNIIHLcerdCSIQR------RHQKVIEIAPCPSISDNLRKT 254
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1864611846 264 MRNASLAVLREIGVDTGGSnVQFSVNPADgRMIVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGFTLDELRNEI 339
Cdd:PRK08463 255 MGVTAVAAAKAVGYTNAGT-IEFLLDDYN-RFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEILDLEQSDI 328
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
613-865 |
4.26e-06 |
|
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: 49.65 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 613 EPLTLEDVLEIVDkEKPVGVIVQYGGQTPLKLALDLEANGVPIVgTSPDMIDAAEDRERFQKMLQELGLRQPPNRTARTE 692
Cdd:TIGR00768 35 INLTFNEGPRALA-ELDVVIVRIVSMFRGLAVLRYLESLGVPVI-NSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 693 AEALALAQEIGYPLVVRPSYVLGGRAMEIVHEQRDLE------RYMREAVKVshdspVLLDRFLNDAIEVDVDCLSDGNR 766
Cdd:TIGR00768 113 EEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQAAEsllehfEQLNGPQNL-----FLVQEYIKKPGGRDIRVFVVGDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 767 TFigGVMEHIE----QAGVHSGDSAcslPPYSLSQEtIAELKRQtALMAKGLNVVGlmnvqfaIQHKEGQDVVFVLEVNP 842
Cdd:TIGR00768 188 VV--AAIYRITsghwRSNLARGGKA---EPCSLTEE-IEELAIK-AAKALGLDVAG-------VDLLESEDGLLVNEVNA 253
|
250 260
....*....|....*....|...
gi 1864611846 843 RASRTVpyVSKATGLQLAKIAAR 865
Cdd:TIGR00768 254 NPEFKN--SVKTTGVNIAGKLLD 274
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
110-332 |
5.72e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 50.13 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 110 KYKVELIGATPEAIDKAEDRLKFKNAMTKIGL----GSarSGVAHSMDEAWAVQKDVGFPVIIRPSFTMGGTGGGIAYNP 185
Cdd:PRK08462 99 HHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVpvipGS--DGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 186 EEFETIC----KRGLEASPTNELLIEESLIGWKEYEMEVVRDKADNCIIV----CSIENldpmgvHTGDSITVAPAQTLT 257
Cdd:PRK08462 177 SDLENLYlaaeSEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAVVLD 250
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1864611846 258 DKEYQIMRNASLAVLREIGVDTGGSnVQFSVNpADGRMIVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGFTL 332
Cdd:PRK08462 251 EKTRERLHETAIKAAKAIGYEGAGT-FEFLLD-SNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL 323
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
644-872 |
1.09e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 49.33 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 644 LALDLEANGVPIVGTSPDMIDAAEDRERFQKMLQELGLRQPP--NRTARTEAEALALAQEIGYPLVVRPSYVLGGRAMEI 721
Cdd:PRK07178 90 LAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPgsEGNLADLDEALAEAERIGYPVMLKATSGGGGRGIRR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 722 VHEQRDLE----RYMREAVKVSHDSPVLLDRFLNDAIEVDVDCLSDGNrtfiGGVmehieqagVHSGDSACSL------- 790
Cdd:PRK07178 170 CNSREELEqnfpRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSH----GNV--------VHLFERDCSIqrrnqkl 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 791 ----PPYSLSQETIAELKRQTALMAKGLNVVGLMNVQFAIQHkegQDVVFVLEVNPRASRTVPYVSKATGLQLAKIAARC 866
Cdd:PRK07178 238 ieiaPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDA---DGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRI 314
|
....*.
gi 1864611846 867 MVGQSL 872
Cdd:PRK07178 315 ASGLPL 320
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
664-750 |
1.11e-05 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 49.38 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 664 DAAEDRERFQKMLQELGLRQPPNRTARTEAEALALAQEIGYPLVVRPSYVLGGR--AMEIVHEQrDLERYMREAVKVSHD 741
Cdd:PRK14016 210 DIACDKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPLDGNHGRgvTVNITTRE-EIEAAYAVASKESSD 288
|
....*....
gi 1864611846 742 spVLLDRFL 750
Cdd:PRK14016 289 --VIVERYI 295
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
28-302 |
1.30e-05 |
|
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: 48.18 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 28 YSGAQACKALREEGYRVILVNSNPATIMTDpemadvtyiepitwqvveriIAKEKPDAILPTMGGQTALNCALdlwrNGV 107
Cdd:COG1181 19 KSGRAVAAALDKAGYDVVPIGIDVEDLPAA--------------------LKELKPDVVFPALHGRGGEDGTI----QGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 108 LDKYKVELIGATPEA----IDKAedrlKFKNAMTKIGLGSARSGV--AHSMDEAWAVQKDVGFPVIIRPSftMGGTGGGI 181
Cdd:COG1181 75 LELLGIPYTGSGVLAsalaMDKA----LTKRVLAAAGLPTPPYVVlrRGELADLEAIEEELGLPLFVKPA--REGSSVGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 182 --AYNPEEFETICKRGLEASPtnELLIEESLIGwKEYEMEVVRDkaDNCIIVCSIEnLDPMGV--------HTGDSITVA 251
Cdd:COG1181 149 skVKNAEELAAALEEAFKYDD--KVLVEEFIDG-REVTVGVLGN--GGPRALPPIE-IVPENGfydyeakyTDGGTEYIC 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1864611846 252 PAQtLTDKEYQIMRNASLAVLREIGVdTGGSNVQFSVNpADGRMIVIEMNP 302
Cdd:COG1181 223 PAR-LPEELEERIQELALKAFRALGC-RGYARVDFRLD-EDGEPYLLEVNT 270
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
668-750 |
1.86e-05 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 47.80 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 668 DRERFQKMLQELGLRQPPNRTARTEAEALALAQEIGYPLVVRPsyVLGGR--AMEIVHEQRDLERYMREAVKvsHDSPVL 745
Cdd:PRK01372 98 DKLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKP--AREGSsvGVSKVKEEDELQAALELAFK--YDDEVL 173
|
....*
gi 1864611846 746 LDRFL 750
Cdd:PRK01372 174 VEKYI 178
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
35-208 |
2.35e-05 |
|
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: 47.63 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 35 KALREEGYRVILVnsnpatimtdpEMADVTYIEPITWQVVERIIAKEkPDAILPTmggQTALNCALDLWRngvldkyKVE 114
Cdd:COG0189 21 EAAQRRGHEVEVI-----------DPDDLTLDLGRAPELYRGEDLSE-FDAVLPR---IDPPFYGLALLR-------QLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 115 LIGAT----PEAIDKAEDRLKFKNAMTKIGLGSARSGVAHSMDEAWAVQKDVGFPVIIRPSFTMGGTGGGIAYNPEEFET 190
Cdd:COG0189 79 AAGVPvvndPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALES 158
|
170
....*....|....*...
gi 1864611846 191 ICKRgLEASPTNELLIEE 208
Cdd:COG0189 159 ILEA-LTELGSEPVLVQE 175
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
115-430 |
6.20e-05 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 47.15 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 115 LIGATPEAIDKAEDRLKFKNAMTKIGLGSARSGVAHSMDEAWAVQKDVGFPVIIRPSFTMGGTGGGIAYNPEEFETICKR 194
Cdd:PRK02186 94 LPAANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 195 GLEASpTNELLIEESLIGwKEYEMEVVRDKADNCIIVCSIENLDPMGvHTGDSITVAPAQTLTDKEYQIMRNASLAvLRE 274
Cdd:PRK02186 174 LRRAG-TRAALVQAYVEG-DEYSVETLTVARGHQVLGITRKHLGPPP-HFVEIGHDFPAPLSAPQRERIVRTVLRA-LDA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 275 IGVDTGGSNVQFSVNpaDGRMIVIEMNPRVSRS--SALASKATGFPIAKIAAKL----------------AVGFTLDELR 336
Cdd:PRK02186 250 VGYAFGPAHTELRVR--GDTVVIIEINPRLAGGmiPVLLEEAFGVDLLDHVIDLhlgvaafadptakrygAIRFVLPARS 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 337 NEITGgatpASFEPSIDYVVTKIpRFAFEKFPQADNRLTTQMKS-VGEVMAIGRTFQESFQKALR---GLEVGVDGMNEK 412
Cdd:PRK02186 328 GVLRG----LLFLPDDIAARPEL-RFHPLKQPGDALRLEGDFRDrIAAVVCAGDHRDSVAAAAERavaGLSIDIGDAARA 402
|
330
....*....|....*...
gi 1864611846 413 TQDReilekelgEPGPDR 430
Cdd:PRK02186 403 AALN--------DAGAGA 412
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
798-865 |
6.45e-05 |
|
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: 43.75 E-value: 6.45e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1864611846 798 ETIAELKRQTALMAKGLNVVGLMNVQFaiqhKEGQDVVFVLEVNPRASRTVPYvSKATGLQLAKIAAR 865
Cdd:pfam15632 44 EDDPELIEAARRLAEAFGLDGLFNVQF----RYDGDGPKLLEINPRMSGGIGY-SCLAGVNLPYLALK 106
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
587-873 |
1.07e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 46.38 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 587 GYETIMVNCNPE---------TVSTDYDTSDrlyfePLTLEDVLEIVDKEKPVGVIVQYGGQTPLKLALDLeanGVPivG 657
Cdd:PRK02186 27 GFTPYFLTANRGkypfldairVVTISADTSD-----PDRIHRFVSSLDGVAGIMSSSEYFIEVASEVARRL---GLP--A 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 658 TSPDMIDAAEDRERFQKMLQELGLRQPPNRTARTEAEALALAQEIGYPLVVRP---SYVLGGRAMEIVHEQRDLERYMRE 734
Cdd:PRK02186 97 ANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPrmgSGSVGVRLCASVAEAAAHCAALRR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 735 AVKvshdSPVLLDRFLnDAIEVDVDCLSDGNRTFIGGVMehieqaGVHSGDSACSLP-----PYSLSQETIAELKRqTAL 809
Cdd:PRK02186 177 AGT----RAALVQAYV-EGDEYSVETLTVARGHQVLGIT------RKHLGPPPHFVEighdfPAPLSAPQRERIVR-TVL 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1864611846 810 MAkgLNVVGLmnvQFAIQHKE---GQDVVFVLEVNPR-ASRTVP-YVSKATGLQLAKIAARCMVGQSLD 873
Cdd:PRK02186 245 RA--LDAVGY---AFGPAHTElrvRGDTVVIIEINPRlAGGMIPvLLEEAFGVDLLDHVIDLHLGVAAF 308
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
162-303 |
1.48e-04 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 316093 [Multi-domain] Cd Length: 160 Bit Score: 43.43 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 162 VGFPVIIRPSFTMGGTGGGIAYNPEE----FETICKrglEASPTNEL-----------LIEESLIGwKEYEMEVVRDKAD 226
Cdd:pfam13535 1 IPYPCVIKPSVGFFSVGVYKINNREEwkaaFAAIRE---EIEQWKEMypeavvdggsfLVEEYIEG-EEFAVDAYFDENG 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1864611846 227 NCIIVCSIENLDPMGVHTGDSITVAPAQTLTDKEYQIMrNASLAVLREIGVDTGGSNVQFSVNpADGRMIVIEMNPR 303
Cdd:pfam13535 77 EPVILNILKHDFASSEDVSDRIYVTSASIIRETQAAFT-EFLKRINALLGLKNFPVHIELRVD-EDGQIIPIEVNPL 151
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
618-843 |
4.51e-04 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 43.97 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 618 EDVLEIVDKEKPvGVIVqyggqtPLKLAL------DLEANGVPIVGTSpdmiDAAE---DRERFQKML-QELGLRQPPNR 687
Cdd:PRK09288 65 DALRAVIEREKP-DYIV------PEIEAIatdalvELEKEGFNVVPTA----RATRltmNREGIRRLAaEELGLPTSPYR 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 688 TARTEAEALALAQEIGYPLVVRPsyVLG--GRAMEIVHEQRDLERYMREAVKVS--HDSPVLLDRFlndaIEVDVD---- 759
Cdd:PRK09288 134 FADSLEELRAAVEEIGYPCVVKP--VMSssGKGQSVVRSPEDIEKAWEYAQEGGrgGAGRVIVEEF----IDFDYEitll 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 760 --CLSDGNRTF---IGgvmeHIEQagvhSGDSACSLPPYSLSQETIAELKRQTALMAKGLNVVGLMNVQFAIQhkeGQDV 834
Cdd:PRK09288 208 tvRAVDGGTHFcapIG----HRQE----DGDYRESWQPQPMSPAALEEAQEIAKKVTDALGGRGLFGVELFVK---GDEV 276
|
....*....
gi 1864611846 835 VFVlEVNPR 843
Cdd:PRK09288 277 YFS-EVSPR 284
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
675-865 |
4.54e-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: 42.69 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 675 MLQELGLRQPP-------NRTARTEAEALALAQEIGYPLVVRPSyVLGGR-AMEIVHEQRDLERYMREAVKvsHDSPVLL 746
Cdd:pfam07478 1 LLKAAGLPVVPfvtftraDWKLNPKEWCAQVEEALGYPVFVKPA-RLGSSvGVSKVESREELQAAIEEAFQ--YDEKVLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 747 DRFLnDAIEVDVDCLSDGNRTfIGGVMEHIEQAGV------HSGDSACSLPPYSLSQEtIAELKRQTALMA-KGLNVVGL 819
Cdd:pfam07478 78 EEGI-EGREIECAVLGNEDPE-VSPVGEIVPSGGFydyeakYIDDSAQIVVPADLEEE-QEEQIQELALKAyKALGCRGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1864611846 820 MNVQFAIQhKEGQdvVFVLEVNPRASRT----VPYVSKATGLQLAKIAAR 865
Cdd:pfam07478 155 ARVDFFLT-EDGE--IVLNEVNTIPGFTsismFPKLAAAAGVSFPDLVDQ 201
|
|
| PLN02891 |
PLN02891 |
IMP cyclohydrolase |
936-1001 |
7.78e-04 |
|
IMP cyclohydrolase
Pssm-ID: 178479 [Multi-domain] Cd Length: 547 Bit Score: 43.24 E-value: 7.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1864611846 936 KLPTSGKVFLSIKNSDKPRGVKVAKDLVELGFSVVATRGTAAAIAAEGIPVSVVNKVVeGRPHVVD 1001
Cdd:PLN02891 16 SSPSSGKKQALISLSDKTDLALLANGLQELGYTIVSTGGTASALEAAGVSVTKVEELT-NFPEMLD 80
|
|
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
950-986 |
9.53e-04 |
|
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: 43.09 E-value: 9.53e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1864611846 950 SDKpRG-VKVAKDLVELGFSVVATRGTAAAIAAEGIPV 986
Cdd:COG0138 11 SDK-TGlVEFARALVELGVEIISTGGTAKALREAGIPV 47
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
116-189 |
1.47e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 42.43 E-value: 1.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1864611846 116 IGATPEAI----DKAEDRLKFKNAMTKIGLGSArsGVAHSMDEAWAVQKDVGFPVIIRPSFTMGGTGGGIAYNPEEFE 189
Cdd:PRK12833 106 VGPDAQTIrtmgDKARARRTARRAGVPTVPGSD--GVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLA 181
|
|
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
950-986 |
1.57e-03 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 42.38 E-value: 1.57e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1864611846 950 SDKpRG-VKVAKDLVELGFSVVATRGTAAAIAAEGIPV 986
Cdd:PRK00881 12 SDK-TGiVEFAKALVELGVEILSTGGTAKLLAEAGIPV 48
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
666-843 |
2.69e-03 |
|
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: 39.68 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 666 AEDRERFQKMLQELGLRQPpnrTARTEAEALalaqEIGYPLVVRPSYVLGGRAMEIVHEQRDLERYMreavkvshdSPVL 745
Cdd:pfam02655 1 ASDKLKTYKALKNAGVPTP---ETLQAEELL----REEKKYVVKPRDGCGGEGVRKVENGREDEAFI---------ENVL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 746 LDRFLnDAIEVDVDCLSDG--------NRTFIggvmEHIEQAGVHSGDSACSlpPYSLSQETIAELKRQTALMaKGLNvv 817
Cdd:pfam02655 65 VQEFI-EGEPLSVSLLSDGekalplsvNRQYI----DNGGSGFVYAGNVTPS--RTELKEEIIELAEEVVECL-PGLR-- 134
|
170 180
....*....|....*....|....*.
gi 1864611846 818 GLMNVQFAIqhKEGQDVvfVLEVNPR 843
Cdd:pfam02655 135 GYVGVDLVL--KDNEPY--VIEVNPR 156
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
120-304 |
3.05e-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: 41.21 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 120 PEAIDKAEDRLKFKNAMTKIGLGSARSGVAHSMDEAWAVQKDVGFPVIIRPSfTMG--GTGGGIAYNPEEFETIckrgLE 197
Cdd:COG0026 81 PEALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTR-RGGydGKGQVVIKSAADLEAA----WA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 198 ASPTNELLIEEsligWKEYEME----VVRDKADNciIVC--SIENldpmgVHTgDSI---TVAPAQtLTDKEYQIMRNAS 268
Cdd:COG0026 156 ALGGGPCILEE----FVPFERElsviVARSPDGE--VATypVVEN-----VHR-NGIldeSIAPAR-ISEALAAEAEEIA 222
|
170 180 190
....*....|....*....|....*....|....*...
gi 1864611846 269 LAVLREIGVdTG--GsnVQFSVNPaDGRMIVIEMNPRV 304
Cdd:COG0026 223 KRIAEALDY-VGvlA--VEFFVTK-DGELLVNEIAPRP 256
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
133-235 |
5.39e-03 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 39.55 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864611846 133 KNAMTKIGLGSARSGVAHSMDEAWAVQKDVGFPVI-IRPSFTMGGTG--GGI--AYNPEEFETICK-----------RGL 196
Cdd:pfam08442 8 KEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYvVKAQVLAGGRGkaGGVklAKSPEEAKEVAKemlgknlvtkqTGP 87
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1864611846 197 EASPTNELLIEESLIGWKEYEMEVVRDKADNCI-IVCSIE 235
Cdd:pfam08442 88 DGQPVNKVLVEEALDIKKEYYLSIVLDRASKGPvIIASTE 127
|
|
| |
