|
Name |
Accession |
Description |
Interval |
E-value |
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
1-1081 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 2186.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 1 MPKRTDIKKILIIGAGPIVIGQACEFDYSGTQACKALKEEGFQVVLLNSNPATIMTDPDFADRTYIEPVTPEILAMIIEK 80
Cdd:PRK05294 1 MPKRTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 81 ERPDAVLPTLGGQTALNTAVAVAESGVLEKYGVELIGAKLPAIKMAEDRTLFKEAMQRINLTVPRSGLAHNHAEAMEIIK 160
Cdd:PRK05294 81 ERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 161 EIGFPAIIRPSFTLGGTGGGIAYNMEEYEKMSVAGIEASPTSEILIEESVIGWKEYELEVMRDTADNVVIICSIENFDPM 240
Cdd:PRK05294 161 EIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 241 GVHTGDSITVAPAQTLTDKEYQILRDASLKIIREIGVDTGGSNIQFGINPRDGRLVVIEMNPRVSRSSALASKATGFPIA 320
Cdd:PRK05294 241 GVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVETGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 321 KIAAKLAVGYTLDEITNDITRETPACFEPTIDYVVTKVPRFTFEKFPAADATLTTQMKSVGEVMAIGRTFKESLQKAIRS 400
Cdd:PRK05294 321 KVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 401 LEIGSSGFESRLFDSKAetrraltgKEQqlLMEKLRTPNWERLWYLGDAFRSGMTVEEIFAVTAFDPWFLHNIKQIIDKE 480
Cdd:PRK05294 401 LEIGVTGLDEDLFEEES--------LEE--LREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 481 DELKqvnveEEANDNLKEVIREAKQYGFSDKHLGNLWGKTEDEVRQLRLSLGIKPVFKRVDTCAAEFVAYTPYLYSTYEE 560
Cdd:PRK05294 471 EELK-----ENGLPLDAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 561 ECEAEPTDRKKIMILGGGPNRIGQGIEFDYCCVHGVFALAEDGYETIMVNCNPETVSTDYDTSDRLYFEPLTYEDVLNIV 640
Cdd:PRK05294 546 ECESNPSDRKKVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEII 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 641 ELEKPEGVIVQFGGQTPLKLAVSLEKAGVPIIGTSPDAIDRAEDRERFQEMLHKLGLRQPENGTARSFEEAEKVADRIGY 720
Cdd:PRK05294 626 EKEKPKGVIVQFGGQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGY 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 721 PVVVRPSYVLGGRAMEIVYDVDNLRRYMHTAVQASPEHPILIDKFLDEAIEIDVDALCDGTEAVIGGIMEHIEEAGIHSG 800
Cdd:PRK05294 706 PVLVRPSYVLGGRAMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICDGEDVLIGGIMEHIEEAGVHSG 785
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 801 DSACSLPPYSISREIADEIRRQTKMMALELNVRGLMNVQYAIKDDVIYILEVNPRASRTAPFVSKATGRPLAKLAARIMS 880
Cdd:PRK05294 786 DSACSLPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVML 865
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 881 GKTLRELGITEEIEPTHISVKEAVFPFVKFPGVDTILGPEMKSTGEVMGIDDNFAKAFAKAQLGAGVKLPTSGKVFISVR 960
Cdd:PRK05294 866 GKKLAELGYTKGLIPPYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSGTVFLSVR 945
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 961 DADKKHIVSAAKKLYDNGFELVATRGTAAYLQEKGIPVLVVNKVLEGRPHIVDSIKNNEICMVINTTQGAQAVADSFSIR 1040
Cdd:PRK05294 946 DRDKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELVNKVHEGRPHIVDLIKNGEIDLVINTPTGRQAIRDGFSIR 1025
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 500471923 1041 RNALVSNIAYYTTASGARAVVDGIIAMRQEELSVKPIQDYL 1081
Cdd:PRK05294 1026 RAALEYKVPYITTLAGARAAVKAIEALKFGELEVRSLQEYH 1066
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
2-1061 |
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: 1686.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 2 PKRTDIKKILIIGAGPIVIGQACEFDYSGTQACKALKEEGFQVVLLNSNPATIMTDPDFADRTYIEPVTPEILAMIIEKE 81
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 82 RPDAVLPTLGGQTALNTAVAVAESGVLEKYGVELIGAKLPAIKMAEDRTLFKEAMQRINLTVPRSGLAHNHAEAMEIIKE 161
Cdd:TIGR01369 81 RPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 162 IGFPAIIRPSFTLGGTGGGIAYNMEEYEKMSVAGIEASPTSEILIEESVIGWKEYELEVMRDTADNVVIICSIENFDPMG 241
Cdd:TIGR01369 161 IGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 242 VHTGDSITVAPAQTLTDKEYQILRDASLKIIREIGVDtGGSNIQFGINPRDGRLVVIEMNPRVSRSSALASKATGFPIAK 321
Cdd:TIGR01369 241 VHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIE-GGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 322 IAAKLAVGYTLDEITNDITRETPACFEPTIDYVVTKVPRFTFEKFPAADATLTTQMKSVGEVMAIGRTFKESLQKAIRSL 401
Cdd:TIGR01369 320 VAAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 402 EIGSSGFESRLFDskaetrraltGKEQQLLMEKLRTPNWERLWYLGDAFRSGMTVEEIFAVTAFDPWFLHNIKQIIDKED 481
Cdd:TIGR01369 400 EIGATGFDLPDRE----------VEPDEDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 482 ELKQVNVEEEANDNLkeviREAKQYGFSDKHLGNLWGKTEDEVRQLRLSLGIKPVFKRVDTCAAEFVAYTPYLYSTYEEE 561
Cdd:TIGR01369 470 ELEEVKLTDLDPELL----RRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 562 C-EAEPTDRKKIMILGGGPNRIGQGIEFDYCCVHGVFALAEDGYETIMVNCNPETVSTDYDTSDRLYFEPLTYEDVLNIV 640
Cdd:TIGR01369 546 RdDVPFTDKKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNII 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 641 ELEKPEGVIVQFGGQTPLKLAVSLEKAGVPIIGTSPDAIDRAEDRERFQEMLHKLGLRQPENGTARSFEEAEKVADRIGY 720
Cdd:TIGR01369 626 ELEKPEGVIVQFGGQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGY 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 721 PVVVRPSYVLGGRAMEIVYDVDNLRRYMHTAVQASPEHPILIDKFLDEAIEIDVDALCDGTEAVIGGIMEHIEEAGIHSG 800
Cdd:TIGR01369 706 PVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSG 785
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 801 DSACSLPPYSISREIADEIRRQTKMMALELNVRGLMNVQYAIKDDVIYILEVNPRASRTAPFVSKATGRPLAKLAARIMS 880
Cdd:TIGR01369 786 DSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVML 865
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 881 GKTLRELGITEEIEPTHISVKEAVFPFVKFPGVDTILGPEMKSTGEVMGIDDNFAKAFAKAQLGAGVKLPTSGKVFISVR 960
Cdd:TIGR01369 866 GKKLEELGVGKEKEPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVR 945
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 961 DADKKHIVSAAKKLYDNGFELVATRGTAAYLQEKGIPVLVVNKVLEGRPHIVDSIKNNEICMVINTT-QGAQAVADSFSI 1039
Cdd:TIGR01369 946 DKDKEELLDLARKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEGRPNILDLIKNGEIELVINTTsKGAGTATDGYKI 1025
|
1050 1060
....*....|....*....|..
gi 500471923 1040 RRNALVSNIAYYTTASGARAVV 1061
Cdd:TIGR01369 1026 RREALDYGVPLITTLNTAEAFA 1047
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
3-1080 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 1635.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 3 KRTDIKKILIIGAGPIVIGQACEFDYSGTQACKALKEEGFQVVLLNSNPATIMTDPDFADRTYIEPVTPEILAMIIEKER 82
Cdd:PLN02735 19 KRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 83 PDAVLPTLGGQTALNTAVAVAESGVLEKYGVELIGAKLPAIKMAEDRTLFKEAMQRINLTVPRSGLAHNHAEAMEIIKEI 162
Cdd:PLN02735 99 PDALLPTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 163 G-FPAIIRPSFTLGGTGGGIAYNMEEYEKMSVAGIEASPTSEILIEESVIGWKEYELEVMRDTADNVVIICSIENFDPMG 241
Cdd:PLN02735 179 GeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 242 VHTGDSITVAPAQTLTDKEYQILRDASLKIIREIGVDTGGSNIQFGINPRDGRLVVIEMNPRVSRSSALASKATGFPIAK 321
Cdd:PLN02735 259 VHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVECGGSNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 322 IAAKLAVGYTLDEITNDITRETPACFEPTIDYVVTKVPRFTFEKFPAADATLTTQMKSVGEVMAIGRTFKESLQKAIRSL 401
Cdd:PLN02735 339 MAAKLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 402 EIGSSGFESrlfdskaETRRALTGKEQQlLMEKLRTPNWERLWYLGDAFRSGMTVEEIFAVTAFDPWFLHNIKQIIDKED 481
Cdd:PLN02735 419 ETGFSGWGC-------AKVKELDWDWEQ-LKYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQ 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 482 ELKQVNVEEEANDNLKEVireaKQYGFSDKHLGNLWGKTEDEVRQLRLSLGIKPVFKRVDTCAAEFVAYTPYLYSTYEEE 561
Cdd:PLN02735 491 FLKSRSLSELSKDDFYEV----KRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGE 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 562 CEAEPTDRKKIMILGGGPNRIGQGIEFDYCCVHGVFALAEDGYETIMVNCNPETVSTDYDTSDRLYFEPLTYEDVLNIVE 641
Cdd:PLN02735 567 CESAPTNKKKVLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVID 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 642 LEKPEGVIVQFGGQTPLKLAVSLEKA-------------GVPIIGTSPDAIDRAEDRERFQEMLHKLGLRQPENGTARSF 708
Cdd:PLN02735 647 LERPDGIIVQFGGQTPLKLALPIQKYldknpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSE 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 709 EEAEKVADRIGYPVVVRPSYVLGGRAMEIVYDVDNLRRYMHTAVQASPEHPILIDKFLDEAIEIDVDALCDGT-EAVIGG 787
Cdd:PLN02735 727 ADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALADSEgNVVIGG 806
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 788 IMEHIEEAGIHSGDSACSLPPYSISREIADEIRRQTKMMALELNVRGLMNVQYAI-KDDVIYILEVNPRASRTAPFVSKA 866
Cdd:PLN02735 807 IMEHIEQAGVHSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAItPSGEVYIIEANPRASRTVPFVSKA 886
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 867 TGRPLAKLAARIMSGKTLRELGITEEIEPTHISVKEAVFPFVKFPGVDTILGPEMKSTGEVMGIDDNFAKAFAKAQLGAG 946
Cdd:PLN02735 887 IGHPLAKYASLVMSGKSLKDLGFTEEVIPAHVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAG 966
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 947 VKLPTSGKVFISVRDADKKHIVSAAKKLYDNGFELVATRGTAAYLQEKGIPVLVVNKVLEGRPHIVDSIKNNEICMVINT 1026
Cdd:PLN02735 967 QRLPLSGTVFISLNDLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVLKLHEGRPHAGDMLANGQIQLMVIT 1046
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*
gi 500471923 1027 TQG-AQAVADSFSIRRNALVSNIAYYTTASGARAVVDGIIAMRQEELSVKPIQDY 1080
Cdd:PLN02735 1047 SSGdALDQKDGRQLRRMALAYKVPIITTVAGALATAQAVKSLKECPIEMIALQDF 1101
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
1-1082 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1605.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 1 MPKRTDIKKILIIGAGPIVIGQACEFDYSGTQACKALKEEGFQVVLLNSNPATIMTDPDFADRTYIEPVTPEILAMIIEK 80
Cdd:PRK12815 1 MPKDTDIQKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 81 ERPDAVLPTLGGQTALNTAVAVAESGVLEKYGVELIGAKLPAIKMAEDRTLFKEAMQRINLTVPRSGLAHNHAEAMEIIK 160
Cdd:PRK12815 81 EKPDALLATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 161 EIGFPAIIRPSFTLGGTGGGIAYNMEEYEKMSVAGIEASPTSEILIEESVIGWKEYELEVMRDTADNVVIICSIENFDPM 240
Cdd:PRK12815 161 KIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 241 GVHTGDSITVAPAQTLTDKEYQILRDASLKIIREIGVdTGGSNIQFGINPRDGRLVVIEMNPRVSRSSALASKATGFPIA 320
Cdd:PRK12815 241 GIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGV-VGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 321 KIAAKLAVGYTLDEITNDITRETPACFEPTIDYVVTKVPRFTFEKFPAADATLTTQMKSVGEVMAIGRTFKESLQKAIRS 400
Cdd:PRK12815 320 KIAAKLAVGYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 401 LEIGSSGFESRLfdskaetrrALTGKEQQLLMEKLRTPNWERLWYLGDAFRSGMTVEEIFAVTAFDPWFLHNIKQIIDKE 480
Cdd:PRK12815 400 LEIKRNGLSLPI---------ELSGKSDEELLQDLRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 481 DELKQvnveeeANDNL-KEVIREAKQYGFSDKHLGNLWGKTEDEVRQLRLSLGIKPVFKRVDTCAAEFVAYTPYLYSTYE 559
Cdd:PRK12815 471 KKLAE------DGLDLsADLLRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYF 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 560 EECEAEPT-DRKKIMILGGGPNRIGQGIEFDYCCVHGVFALAEDGYETIMVNCNPETVSTDYDTSDRLYFEPLTYEDVLN 638
Cdd:PRK12815 545 GESEAEPSsEKKKVLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLN 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 639 IVELEKPEGVIVQFGGQTPLKLAVSLEKAGVPIIGTSPDAIDRAEDRERFQEMLHKLGLRQPENGTARSFEEAEKVADRI 718
Cdd:PRK12815 625 VAEAENIKGVIVQFGGQTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRI 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 719 GYPVVVRPSYVLGGRAMEIVYDVDNLRRYMHTAvqASPEHPILIDKFLDeAIEIDVDALCDGTEAVIGGIMEHIEEAGIH 798
Cdd:PRK12815 705 GYPVLIRPSYVIGGQGMAVVYDEPALEAYLAEN--ASQLYPILIDQFID-GKEYEVDAISDGEDVTIPGIIEHIEQAGVH 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 799 SGDSACSLPPYSISREIADEIRRQTKMMALELNVRGLMNVQYAIKDDVIYILEVNPRASRTAPFVSKATGRPLAKLAARI 878
Cdd:PRK12815 782 SGDSIAVLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKV 861
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 879 MSGKTLRELGITEEIEPTH--ISVKEAVFPFVKFPGVDTILGPEMKSTGEVMGIDDNFAKAFAKAQLGAGVKLPTSGKVF 956
Cdd:PRK12815 862 LLGKSLAELGYPNGLWPGSpfIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGTIF 941
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 957 ISVRDADKKHIVSAAKKLYDNGFELVATRGTAAYLQEKGIPVLVVNKVLEGRPHIVDSIKNNEICMVINTTQGAQAVADS 1036
Cdd:PRK12815 942 ISVRDEDKPEVTKLARRFAQLGFKLLATEGTANWLAEEGITTGVVEKVQEGSPSLLERIKQHRIVLVVNTSLSDSASEDA 1021
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*.
gi 500471923 1037 FSIRRNALVSNIAYYTTASGARAVVDGIIAMRQEELSVKPIQDYLK 1082
Cdd:PRK12815 1022 IKIRDEALSTHIPVFTELETAQAFLQVLESLALTTQPIQELQEKHK 1067
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
575-1080 |
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: 806.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 575 LGGGPNRIGQGIEFDYCCVHGVFALAEDGYETIMVNCNPETVSTDYDTSDRLYFEPLTYEDVLNIVELEKPEGVIVQFGG 654
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 655 QTPLKLAVSLEKA----GVPIIGTSPDAIDRAEDRERFQEMLHKLGLRQPENGTARSFEEAEKVADRIGYPVVVRPSYVL 730
Cdd:COG0458 81 QTALNLAVELEEAgileGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 731 GGRAMEIVYDVDNLRRYMHTAVQASPEHPILIDKFLDEAIEIDVDALCDGT-EAVIGGIMEHIEEAGIHSGDSACSLPPY 809
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEdNVIIVGIMEHIEPAGVHSGDSICVAPPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 810 SISREIADEIRRQTKMMALELNVRGLMNVQYAIKDDVIYILEVNPRASRTAPFVSKATGRPLAKLAARIMSGKTLRELGI 889
Cdd:COG0458 241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 890 TEEIEPT--HISVKEAVFPFVKFPGVDTILGPEMKSTGEVMGIDDNFAKAFAKAQLGAGVKLPtsGKVFIS-VRDADKKH 966
Cdd:COG0458 321 DTGFEPTldYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLP--GTVLLSlVADDDKEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 967 IVSAAKKLYDNGFELVATRGTAAYLQEKGIPVLVVNKVLEGRPHIVDSIKNNEICMVINTTQGAQAVADSFSIRRNALVS 1046
Cdd:COG0458 399 ALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVINTLLGAKSLGDSDGIIRRALAA 478
|
490 500 510
....*....|....*....|....*....|....
gi 500471923 1047 NIAYYTTASGARAVVDGIIAMRQEELSVKPIQDY 1080
Cdd:COG0458 479 KVPYVTTLAAAAAAALAIKAVETEAGEFEEATAY 512
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
13-577 |
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: 749.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 13 IGAGPIVIGQACEFDYSGTQACKALKEEGFQVVLLNSNPATIMTDPDFADRTYIEPVTPEILAMIIEKERPDAVLPTLGG 92
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 93 QTALNTAVAVAESGVLEkyGVELIGAKLPAIKMAEDRTLFKEAMQRINLTVPRSGLAHNHAEAMEIIKEIGFPAIIRPSF 172
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 173 TLGGTGGGIAYNMEEYEKMSVAGIEASPTSEILIEESVIGWKEYELEVMRDTADNVVIICSIENFDPMGVHTGDSITVAP 252
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 253 AQTLTDKEYQILRDASLKIIREIGVDtGGSNIQFGINprDGRLVVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTL 332
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVV-GLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 333 DEITNDiTRetpacFEPTIDYVVTKVPRFTFEKFPAADATLTTQMKSVGEVMAIGRTFKESLQKAIRSLEIGSSGfesRL 412
Cdd:COG0458 316 DELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPG---TV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 413 FDSKAETRRAltgkeqqlLMEKLRTPNWERLWYLGDAFRSGMTVEEIFAVTAFDPWFLHNIKQIIDKEDELKQVNveeea 492
Cdd:COG0458 387 LLSLVADDDK--------EEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEII----- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 493 ndNLKEVIREAKQYGFSDKHLGNLWGKTEDEVRQLRLSLGIKPVFKRVDTCAAEFVAYTPYLYSTYEEECEAEPTDRKKI 572
Cdd:COG0458 454 --LVINTLLGAKSLGDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKV 531
|
....*
gi 500471923 573 MILGG 577
Cdd:COG0458 532 VVIGS 536
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
128-333 |
4.22e-80 |
|
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: 260.31 E-value: 4.22e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 128 DRTLFKEAMQRINLTVPRS--GLAHNHAEAMEIIKEIGFPAIIRPSFTLGGTGGGIAYNMEEYEKMSVAGIEASPTS--- 202
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGtaGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAfgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 203 -EILIEESVIGWKEYELEVMRDTADNVVIICSIENFDPMgvHTGDSITVAPAQTLTDKEYQILRDASLKIIREIGVdTGG 281
Cdd:pfam02786 81 pQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGY-VGA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 500471923 282 SNIQFGINPRDGRLVVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLD 333
Cdd:pfam02786 158 GTVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
431-558 |
2.42e-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: 204.61 E-value: 2.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 431 LMEKLRTPNWERLWYLGDAFRSGMTVEEIFAVTAFDPWFLHNIKQIIDKEDELKQVNVEEEANDNLkeviREAKQYGFSD 510
Cdd:smart01096 1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLL----RKAKRLGFSD 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 500471923 511 KHLGNLWGKTEDEVRQLRLSLGIKPVFKRVDTCAAEFVAYTPYLYSTY 558
Cdd:smart01096 77 RQIAKLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
953-1061 |
5.59e-50 |
|
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: 171.89 E-value: 5.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 953 GKVFISVRDADKKHIVSAAKKLYDNGFELVATRGTAAYLQEKGIPVLVVNKVLEGRPHIVDSIKNNEICMVINTTQGAQA 1032
Cdd:cd01424 1 GTVFISVADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEGRPNIVDLIKNGEIQLVINTPSGKRA 80
|
90 100
....*....|....*....|....*....
gi 500471923 1033 VADSFSIRRNALVSNIAYYTTASGARAVV 1061
Cdd:cd01424 81 IRDGFSIRRAALEYKVPYFTTLDTARAAV 109
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
684-885 |
7.15e-34 |
|
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: 129.35 E-value: 7.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 684 DRERFQEMLHKLGLRQPEN--GTARSFEEAEKVADRIGYPVVVRPSYVLGGRAMEIVYDVDNLRRYMHTAVQASPE---- 757
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGtaGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 758 HPILIDKFLDEAIEIDVDALCDGT-EAVIGGIMEHIEEagIHSGDSACSLPPYSISREIADEIRRQTKMMALELNVRGLM 836
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHgNCITVCNRECSDQ--RRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 500471923 837 NVQYAI--KDDVIYILEVNPRASRTAPFVSKATGRPLAKLAARIMSGKTLR 885
Cdd:pfam02786 159 TVEFALdpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
433-516 |
2.23e-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: 114.78 E-value: 2.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 433 EKLRTPNWERLWYLGDAFRSGMTVEEIFAVTAFDPWFLHNIKQIIDKEDELKqvnveEEANDNLKEVIREAKQYGFSDKH 512
Cdd:pfam02787 1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELK-----EAGLDLDAELLREAKRLGFSDRQ 75
|
....
gi 500471923 513 LGNL 516
Cdd:pfam02787 76 IAKL 79
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
72-329 |
3.44e-29 |
|
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: 117.67 E-value: 3.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 72 EILAMIIEKERPDAVLpTLGGQTALNTAVAVAESGvlekygveLIGAKLPAIKMAEDRTLFKEAMQRINLTVPRSGLAHN 151
Cdd:COG0439 7 AAAAELARETGIDAVL-SESEFAVETAAELAEELG--------LPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 152 HAEAMEIIKEIGFPAIIRPSFTLGGTGGGIAYNMEEYEKmSVAGIEA-----SPTSEILIEESVIGwKEYELEVMrdTAD 226
Cdd:COG0439 78 PEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEA-ALAEARAeakagSPNGEVLVEEFLEG-REYSVEGL--VRD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 227 NVVIICSI---ENFDPMGVHTGDsitVAPAQtLTDKEYQILRDASLKIIREIGVDTGGSNIQFGINPrDGRLVVIEMNPR 303
Cdd:COG0439 154 GEVVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELVARALRALGYRRGAFHTEFLLTP-DGEPYLIEINAR 228
|
250 260
....*....|....*....|....*...
gi 500471923 304 VS--RSSALASKATGFPIAKIAAKLAVG 329
Cdd:COG0439 229 LGgeHIPPLTELATGVDLVREQIRLALG 256
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
966-1052 |
8.40e-28 |
|
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: 107.95 E-value: 8.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 966 HIVSAAKKLYDNGFELVATRGTAAYLQEKGIPV--LVVNKVLEGRPHIVDSIKNNEICMVINTT--QGAQAVADSFSIRR 1041
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPVvkTLHPKVHGGIPQILDLIKNGEIDLVINTLypFEAQAHEDGYSIRR 80
|
90
....*....|.
gi 500471923 1042 NALVSNIAYYT 1052
Cdd:smart00851 81 AAENIDIPGPT 91
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
967-1052 |
1.94e-26 |
|
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: 104.11 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 967 IVSAAKKLYDNGFELVATRGTAAYLQEKGIPV-LVVNKVLEGRPH----IVDSIKNNEICMVINTTQG-AQAVADSFSIR 1040
Cdd:pfam02142 2 LVELAKALVELGFELLATGGTAKFLREAGIPVtEVVEKTGEGRPGgrvqIGDLIKNGEIDLVINTLYPfKATVHDGYAIR 81
|
90
....*....|..
gi 500471923 1041 RNALVSNIAYYT 1052
Cdd:pfam02142 82 RAAENIDIPGPT 93
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
665-882 |
1.61e-25 |
|
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: 107.27 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 665 EKAGVPiiGTSPDAIDRAEDRERFQEMLHKLGLRQPENGTARSFEEAEKVADRIGYPVVVRPSYVLGGRAMEIVYDVDNL 744
Cdd:COG0439 37 EELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 745 RRYMHTAVQ----ASPEHPILIDKFLdEAIEIDVDALCDGTEAVIGGIMEHIEEA--GIHSGDSAcslpPYSISREIADE 818
Cdd:COG0439 115 EAALAEARAeakaGSPNGEVLVEEFL-EGREYSVEGLVRDGEVVVCSITRKHQKPpyFVELGHEA----PSPLPEELRAE 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500471923 819 IRRQTKMMALELNV-RGLMNVQYAI-KDDVIYILEVNPRAS--RTAPFVSKATGRPLAKLAARIMSGK 882
Cdd:COG0439 190 IGELVARALRALGYrRGAFHTEFLLtPDGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGE 257
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
955-1060 |
1.61e-16 |
|
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: 76.40 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 955 VFISVRDADKKHIVSAAKKLYDNGFELVATRGTAAYLQEKGIPVLVVNKVLE-GRPHIVDSIKNN-EICMVINTTQGAQA 1032
Cdd:cd00532 2 VFLSVSDHVKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRHEdGEPTVDAAIAEKgKFDVVINLRDPRRD 81
|
90 100 110
....*....|....*....|....*....|.
gi 500471923 1033 VA---DSFSIRRNALVSNIAYYTTASGARAV 1060
Cdd:cd00532 82 RCtdeDGTALLRLARLYKIPVTTPNATAMFV 112
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
634-862 |
1.81e-15 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 78.77 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 634 EDVLNIVELEKPEGVIVqfGGQTPLKL----AVSLEKAGVPIIGTSPDAIDRAEDRERFQEMLHKLGLRQPENGTARSFE 709
Cdd:PRK12767 59 DRLLDICKKEKIDLLIP--LIDPELPLlaqnRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 710 EAEKV--ADRIGYPVVVRPSYVLGGRAMEIVYDVDNLRRYMHTAVqaspehPILIDKFLDEaIEIDVDALCDGTEAVIGG 787
Cdd:PRK12767 137 DFKAAlaKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYVP------NLIIQEFIEG-QEYTVDVLCDLNGEVISI 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500471923 788 I-MEHIEeagIHSGDSacslppysiSREIA---DEIRRQTKMMALELNVRGLMNVQYAIKDDVIYILEVNPRASRTAPF 862
Cdd:PRK12767 210 VpRKRIE---VRAGET---------SKGVTvkdPELFKLAERLAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPL 276
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
9-329 |
6.75e-15 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 77.66 E-value: 6.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 9 KILIIGAGPIVIGqacefdysgtqACKALKEEGFQVVLLNSNPATIMTDPDFADRTYIEP-------VTPEILAMIIEKE 81
Cdd:COG3919 7 RVVVLGGDINALA-----------VARSLGEAGVRVIVVDRDPLGPAARSRYVDEVVVVPdpgddpeAFVDALLELAERH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 82 RPDAVLPTlggqtALNTAVAVAES-GVLEKYgVELIGAKLPAIKMAEDRTLFKEAMQRINLTVPRSGLAHNHAEAMEIIK 160
Cdd:COG3919 76 GPDVLIPT-----GDEYVELLSRHrDELEEH-YRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 161 EIGFPAIIRPS--------FTLGGTGGGIAYNMEEYEKMsVAGIEASPTsEILIEESVIGWKEYE--LEVMRDTADNVVI 230
Cdd:COG3919 150 DLGFPVVVKPAdsvgydelSFPGKKKVFYVDDREELLAL-LRRIAAAGY-ELIVQEYIPGDDGEMrgLTAYVDRDGEVVA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 231 ICSIENF--DPMGVHTGDSITVAPaqtltDKEyqiLRDASLKIIREIGVdTGGSNIQFGINPRDGRLVVIEMNPRVSRSS 308
Cdd:COG3919 228 TFTGRKLrhYPPAGGNSAARESVD-----DPE---LEEAARRLLEALGY-HGFANVEFKRDPRDGEYKLIEINPRFWRSL 298
|
330 340
....*....|....*....|.
gi 500471923 309 ALASKAtGFPIAKIAAKLAVG 329
Cdd:COG3919 299 YLATAA-GVNFPYLLYDDAVG 318
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
566-884 |
3.61e-13 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 72.65 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 566 PTDRKKIMILGGGPNrigqgiefDYCCVHgvfALAEDGYETIMVNCNPETVSTDYDTSDRLYFEPLTYED-------VLN 638
Cdd:COG3919 2 MTMRFRVVVLGGDIN--------ALAVAR---SLGEAGVRVIVVDRDPLGPAARSRYVDEVVVVPDPGDDpeafvdaLLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 639 IVELEKPEgVIVQFGGQTPLKLAVSLEK--AGVPIIGTSPDAIDRAEDRERFQEMLHKLGLRQPENGTARSFEEAEKVAD 716
Cdd:COG3919 71 LAERHGPD-VLIPTGDEYVELLSRHRDEleEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 717 RIGYPVVVRPSY--------VLGGRAMEIVYDVDNLRRYMHTAVQAspEHPILIDKFL--DEAIEIDVDALCDGT-EAVI 785
Cdd:COG3919 150 DLGFPVVVKPADsvgydelsFPGKKKVFYVDDREELLALLRRIAAA--GYELIVQEYIpgDDGEMRGLTAYVDRDgEVVA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 786 GGIMEHIEEAGIHSGDSAcslppYSISREIaDEIRRQTKMMALELNVRGLMNVQ--YAIKDDVIYILEVNPRASRTAPFV 863
Cdd:COG3919 228 TFTGRKLRHYPPAGGNSA-----ARESVDD-PELEEAARRLLEALGYHGFANVEfkRDPRDGEYKLIEINPRFWRSLYLA 301
|
330 340
....*....|....*....|.
gi 500471923 864 SKAtGRPLAKLAARIMSGKTL 884
Cdd:COG3919 302 TAA-GVNFPYLLYDDAVGRPL 321
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
641-877 |
4.71e-13 |
|
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: 70.84 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 641 ELEKPEGVIVQF-GGQTPLKLAVSLEKAGVPIIgTSPDAIDRAEDRERFQEMLHKLGLRQPENGTARSFEEAEKVADRIG 719
Cdd:TIGR00768 45 ALAELDVVIVRIvSMFRGLAVLRYLESLGVPVI-NSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 720 YPVVVRPSYVLGGRAMEIVYDVDNLRR-YMHTAVQASPEHPILIDKFLDEAIEIDVDALCDGTEAVigGIMEHIEEAG-- 796
Cdd:TIGR00768 124 FPVVLKPVFGSWGRGVSLARDRQAAESlLEHFEQLNGPQNLFLVQEYIKKPGGRDIRVFVVGDEVV--AAIYRITSGHwr 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 797 --IHSGDSAcslPPYSISREIADEIRRQTKMMALElnVRGlmnVQYAIKDDVIYILEVNPRASRTApfVSKATGRPLAKL 874
Cdd:TIGR00768 202 snLARGGKA---EPCSLTEEIEELAIKAAKALGLD--VAG---VDLLESEDGLLVNEVNANPEFKN--SVKTTGVNIAGK 271
|
...
gi 500471923 875 AAR 877
Cdd:TIGR00768 272 LLD 274
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
955-1062 |
1.34e-12 |
|
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: 65.40 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 955 VFISVRDADKKHIVSAAKKLYDNGFELVATRGTAAYLQEKGIPVLVVNKVLE----GRPHIVDSIKNNEICMVINTTQ-G 1029
Cdd:cd01423 3 ILISIGSYSKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEepqnDKPSLRELLAEGKIDLVINLPSnR 82
|
90 100 110
....*....|....*....|....*....|....
gi 500471923 1030 AQAVADSFSIRRNALVS-NIAYYTTASGARAVVD 1062
Cdd:cd01423 83 GKRVLDNDYVMRRAADDfAVPLITNPKCAKLFIE 116
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
661-885 |
2.72e-12 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 70.55 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 661 AVSLEKAGVPIIGTSPDAIDRAEDRERFQEMLHKLGLrqP----ENGTARSFEEAEKVADRIGYPVVVRPSYVLGGRAME 736
Cdd:PRK12833 95 AEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGV--PtvpgSDGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIR 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 737 IVYDVDNLRRYMHTA---VQASPEHP-ILIDKFLDEAIEIDVDALCDGTEAViggimehieeagiHSGDSACSL------ 806
Cdd:PRK12833 173 VAHDAAQLAAELPLAqreAQAAFGDGgVYLERFIARARHIEVQILGDGERVV-------------HLFERECSLqrrrqk 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 807 -----PPYSISREIADEIRRQTKMMALELNVRGLMNVQYAIKD--DVIYILEVNPRASRTAPFVSKATGRPLAKLAARIM 879
Cdd:PRK12833 240 ileeaPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDarGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIA 319
|
....*.
gi 500471923 880 SGKTLR 885
Cdd:PRK12833 320 DGEPLR 325
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
624-877 |
1.07e-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: 66.89 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 624 DRLYFEPLTYEDVLNIVELEKPEGVIVQFGG-QTPLKLAVSLEKAGVPIIGtSPDAIDRAEDRERFQEMLHKLGLRQPEN 702
Cdd:COG0189 36 DDLTLDLGRAPELYRGEDLSEFDAVLPRIDPpFYGLALLRQLEAAGVPVVN-DPEAIRRARDKLFTLQLLARAGIPVPPT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 703 GTARSFEEAEKVADRIGYPVVVRPSYVLGGRAMEIVYDVDNLRRYMHTaVQASPEHPILIDKFLDEAIEIDVDALC-DGT 781
Cdd:COG0189 115 LVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEA-LTELGSEPVLVQEFIPEEDGRDIRVLVvGGE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 782 eaVIGGIMEHIEEAG----IHSGDSACslpPYSISREIADEIRRQTKMMALELNvrGlmnVQYAIKDDVIYILEVNPRAS 857
Cdd:COG0189 194 --PVAAIRRIPAEGEfrtnLARGGRAE---PVELTDEERELALRAAPALGLDFA--G---VDLIEDDDGPLVLEVNVTPG 263
|
250 260
....*....|....*....|
gi 500471923 858 RTApfVSKATGRPLAKLAAR 877
Cdd:COG0189 264 FRG--LERATGVDIAEAIAD 281
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
659-885 |
1.10e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 68.47 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 659 KLAVSLEKAGVPIIGTSPDAIDRAEDRERFQEMLHKLGLrqP----ENGTARSFEEAEKVADRIGYPVVVRPSYVLGGRA 734
Cdd:PRK08654 90 EFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGV--PvlpgTEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 735 MEIVYDVDNLRRY----MHTAVQASPEHPILIDKFLDEAIEIDVDALCDGTEAViggimehieeagIHSGDSACslppyS 810
Cdd:PRK08654 168 MRVVYSEEELEDAiestQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNV------------IHLGDREC-----S 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 811 ISRE------------IADEIRRQTKMMAL----ELNVRGLMNVQYAIKDDVIYILEVNPRASRTAPFVSKATGRPLAKL 874
Cdd:PRK08654 231 IQRRhqklieeapspiMTPELRERMGEAAVkaakAINYENAGTVEFLYSNGNFYFLEMNTRLQVEHPITEMVTGIDIVKE 310
|
250
....*....|.
gi 500471923 875 AARIMSGKTLR 885
Cdd:PRK08654 311 QIKIAAGEELS 321
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
109-340 |
1.66e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 68.09 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 109 EKYGVELIGAKLPAIKMAEDRTLFKEAMQRINL-TVP-RSGLAHNHAEAMEIIKEIGFPAIIRPSFTLGGTGGGIAYNME 186
Cdd:PRK08654 96 EKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVpVLPgTEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 187 EYEK-----MSVAGiEASPTSEILIEESVIGWKEYELEVMRDTADNVVII----CSIENfdpmgVHTgDSITVAPAQTLT 257
Cdd:PRK08654 176 ELEDaiestQSIAQ-SAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLgdreCSIQR-----RHQ-KLIEEAPSPIMT 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 258 DKEYQILRDASLKIIREIGVDTGGSnIQFGINprDGRLVVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLDEITN 337
Cdd:PRK08654 249 PELRERMGEAAVKAAKAINYENAGT-VEFLYS--NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELSFKQE 325
|
...
gi 500471923 338 DIT 340
Cdd:PRK08654 326 DIT 328
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
109-335 |
3.71e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 66.66 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 109 EKYGVELIGAKLPAIKMAEDRTLFKEAMQRINL-TVPRS-GLAHNHAEAMEIIKEIGFPAIIRPsfTLGGTGGGI----- 181
Cdd:PRK07178 95 AERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVpVTPGSeGNLADLDEALAEAERIGYPVMLKA--TSGGGGRGIrrcns 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 182 -AYNMEEYEKMSVAGIEASPTSEILIEESVIGWKEYELEVMRDTADNVVII----CSIENfdpmgvHTGDSITVAPAQTL 256
Cdd:PRK07178 173 rEELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLferdCSIQR------RNQKLIEIAPSPQL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 257 TDKEYQILRDASLKIIREIGVDTGGSnIQFgINPRDGRLVVIEMNPRVSRSSALASKATGFPIAK----IAAKLAVGYTL 332
Cdd:PRK07178 247 TPEQRAYIGDLAVRAAKAVGYENAGT-VEF-LLDADGEVYFMEMNTRVQVEHTITEEITGIDIVReqirIASGLPLSYKQ 324
|
...
gi 500471923 333 DEI 335
Cdd:PRK07178 325 EDI 327
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
659-884 |
4.35e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 66.27 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 659 KLAVSLEKAGVPIIGTSPDAIDRAEDRERFQEMLHKLGLrqP----ENGTARSFEEAEKVADRIGYPVVVRPSYVLGGRA 734
Cdd:PRK05586 90 KFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGV--PvvpgSEGEIENEEEALEIAKEIGYPVMVKASAGGGGRG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 735 MEIVYDVDNLRRYMHTAVQASP----EHPILIDKFLDEAIEIDVDALCDGTEAViggimehieeagIHSGDSACSL---- 806
Cdd:PRK05586 168 IRIVRSEEELIKAFNTAKSEAKaafgDDSMYIEKFIENPKHIEFQILGDNYGNV------------VHLGERDCSLqrrn 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 807 -------PPYSISREIADEIRRQTKMMALELNVRGLMNVQYAI-KDDVIYILEVNPRASRTAPFVSKATGRPLAKLAARI 878
Cdd:PRK05586 236 qkvleeaPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKI 315
|
....*.
gi 500471923 879 MSGKTL 884
Cdd:PRK05586 316 AYGEKL 321
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
6-349 |
1.83e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 64.38 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 6 DIKKILIIGAGPIVIgqacefdysgtQACKALKEEGFQVVLLNSNP-----------ATIMTDPDFADRTYIEpvtpeIL 74
Cdd:PRK08462 3 EIKRILIANRGEIAL-----------RAIRTIQEMGKEAIAIYSTAdkdalylkyadAKICIGGAKSSESYLN-----IP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 75 AMIIEKE--RPDAVLPTLGGQTALNTAVAVAEsgvleKYGVELIGAKLPAIKMAEDRTLFKEAMQRINLTV-PRS-GLAH 150
Cdd:PRK08462 67 AIISAAEifEADAIFPGYGFLSENQNFVEICS-----HHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPViPGSdGALK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 151 NHAEAMEIIKEIGFPAIIRPSFTLGGTGGGIAYNMEEYEKMSVA----GIEASPTSEILIEESVIGWKEYELEVMRDTAD 226
Cdd:PRK08462 142 SYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENLYLAaeseALSAFGDGTMYMEKFINNPRHIEVQILGDKHG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 227 NVVII----CSIENfdpmgvHTGDSITVAPAQTLTDKEYQILRDASLKIIREIGVDTGGSnIQFGINpRDGRLVVIEMNP 302
Cdd:PRK08462 222 NVIHVgerdCSLQR------RHQKLIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGT-FEFLLD-SNLDFYFMEMNT 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 500471923 303 RVSRSSALASKATGFPIAKIAAKLAVGYTLDE----------ITNDITRETPACFEP 349
Cdd:PRK08462 294 RLQVEHTVSEMVSGLDLIEWMIKIAEGEELPSqesiklkghaIECRITAEDPKKFYP 350
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
9-314 |
2.67e-10 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 62.98 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 9 KILIIGAGpivigqacefdySGTQACKALKEEGfqvvllnsNPATIM-TDPD-------FADRTYIEP-VTP----EILA 75
Cdd:PRK12767 3 NILVTSAG------------RRVQLVKALKKSL--------LKGRVIgADISelapalyFADKFYVVPkVTDpnyiDRLL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 76 MIIEKERPDAVLPTlggqTALNTAVAVAESGVLEKYGVELIGAKLPAIKMAEDRTLFKEAMQRINLTVPRSGLAHN--HA 153
Cdd:PRK12767 63 DICKKEKIDLLIPL----IDPELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESleDF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 154 EAMEIIKEIGFPAIIRPSFTLGGTGGGIAYNMEEYEkmsvagIEASPTSEILIEESVIGwKEYELEVMRDTADNVVIICS 233
Cdd:PRK12767 139 KAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELE------FLLEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVISIVP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 234 IENFDPMGVHTGDSITVapaqtltdkEYQILRDASLKIIREIGVDtGGSNIQFGInpRDGRLVVIEMNPRVSRSSALASK 313
Cdd:PRK12767 212 RKRIEVRAGETSKGVTV---------KDPELFKLAERLAEALGAR-GPLNIQCFV--TDGEPYLFEINPRFGGGYPLSYM 279
|
.
gi 500471923 314 A 314
Cdd:PRK12767 280 A 280
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
664-854 |
5.12e-10 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 62.05 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 664 LEKAGVPIIGTSPDAIDRAEDRERFQEMLHKLGLRQPENGTARSFE--EAEKVADRIGYPVVVRPsyVLGG--RAMEIVY 739
Cdd:COG1181 75 LELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRGElaDLEAIEEELGLPLFVKP--AREGssVGVSKVK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 740 DVDNLRRYMHTAVQASPEhpILIDKFLDeAIEIDVdALCDGTEAVIGGIMEHIEEAGI-------HSGDSACSLPPySIS 812
Cdd:COG1181 153 NAEELAAALEEAFKYDDK--VLVEEFID-GREVTV-GVLGNGGPRALPPIEIVPENGFydyeakyTDGGTEYICPA-RLP 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 500471923 813 REIADEIRRQTKMMALELNVRGL------MNvqyaiKDDVIYILEVNP 854
Cdd:COG1181 228 EELEERIQELALKAFRALGCRGYarvdfrLD-----EDGEPYLLEVNT 270
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
667-874 |
1.71e-09 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 61.09 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 667 AGVPIIGTSPDAIDRAEDRERFQEMLHKLGLRQPEngtaRSFEeaekvADRIGYPVVVRPSYVLGGRAMEIvydvdnlrr 746
Cdd:COG2232 95 RRLPLLGNPPEVVRRVKDPLRFFALLDELGIPHPE----TRFE-----PPPDPGPWLVKPIGGAGGWHIRP--------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 747 ymhtavqASPEHPILIDKFLDEAIE---IDVDALCDGTEAVIGGIME-HIEEAG----IHSGdsacSLPPYSISREIADE 818
Cdd:COG2232 157 -------ADSEAPPAPGRYFQRYVEgtpASVLFLADGSDARVLGFNRqLIGPAGerpfRYGG----NIGPLALPPALAEE 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500471923 819 IRRQTKMMALELNVRGLMNVQYAIKDDVIYILEVNPRASRTAPFVSKATGRPLAKL 874
Cdd:COG2232 226 MRAIAEALVAALGLVGLNGVDFILDGDGPYVLEVNPRPQASLDLYEDATGGNLFDA 281
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
109-339 |
6.77e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 59.34 E-value: 6.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 109 EKYGVELIGAKLPAIKMAEDRTLFKEAMQRINL-TVPRS-GLAHNHAEAMEIIKEIGFPAIIRPSFTLGGTGGGIAYNME 186
Cdd:PRK05586 96 KECNIVFIGPDSETIELMGNKSNAREIMIKAGVpVVPGSeGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 187 EYEKM-SVAGIEASPT---SEILIEESVIGWKEYELEVMRDTADNVVII----CSIENfdpmgvHTGDSITVAPAQTLTD 258
Cdd:PRK05586 176 ELIKAfNTAKSEAKAAfgdDSMYIEKFIENPKHIEFQILGDNYGNVVHLgerdCSLQR------RNQKVLEEAPSPVMTE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 259 KEYQILRDASLKIIREIGVDTGGSnIQFGINpRDGRLVVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLDEITND 338
Cdd:PRK05586 250 ELRKKMGEIAVKAAKAVNYKNAGT-IEFLLD-KDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLSIKQED 327
|
.
gi 500471923 339 I 339
Cdd:PRK05586 328 I 328
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
108-336 |
2.09e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 57.89 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 108 LEKYGVELIGAKLPAIKMAEDRTLFKEAMQRINL-TVPRS-GLAHNHAEAMEIIKEIGFPAIIRPsfTLGGTGGGI--AY 183
Cdd:PRK08591 95 CEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVpVVPGSdGPVDDEEEALAIAKEIGYPVIIKA--TAGGGGRGMrvVR 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 184 NMEEYEKM-SVAGIEASPT---SEILIEESVIGWKEYELEVMRDTADNVVII----CSI---------Enfdpmgvhtgd 246
Cdd:PRK08591 173 TEAELEKAfSMARAEAKAAfgnPGVYMEKYLENPRHIEIQVLADGHGNAIHLgerdCSLqrrhqkvleE----------- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 247 sitvAPAQTLTDKEYQILRDASLKIIREIGVdTGGSNIQFgINPRDGRLVVIEMNPRVSRSSALASKATGFPIAK----I 322
Cdd:PRK08591 242 ----APSPAITEELRRKIGEAAVKAAKAIGY-RGAGTIEF-LYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKeqirI 315
|
250
....*....|....
gi 500471923 323 AAKLAVGYTLDEIT 336
Cdd:PRK08591 316 AAGEPLSIKQEDIV 329
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
634-855 |
6.19e-08 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 56.30 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 634 EDVLNIVELEKPEgVIVqfggqtPLKLAVS------LEKAGVPIIgtsPDAidRAE----DRERFQEMLHK-LGLRqpen 702
Cdd:PRK09288 65 DALRAVIEREKPD-YIV------PEIEAIAtdalveLEKEGFNVV---PTA--RATrltmNREGIRRLAAEeLGLP---- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 703 gTAR-----SFEEAEKVADRIGYPVVVRPsyVLG--GRAMEIVYDVDNLRRYMHTAVQASPEHP--ILIDKFLDEAIEID 773
Cdd:PRK09288 129 -TSPyrfadSLEELRAAVEEIGYPCVVKP--VMSssGKGQSVVRSPEDIEKAWEYAQEGGRGGAgrVIVEEFIDFDYEIT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 774 ---VDALCDGTE--AVIGgimeHIEEagihSGDSACSLPPYSISREIADEIRRQTKMMALELNVRGLMNVQYAIKDDVIY 848
Cdd:PRK09288 206 lltVRAVDGGTHfcAPIG----HRQE----DGDYRESWQPQPMSPAALEEAQEIAKKVTDALGGRGLFGVELFVKGDEVY 277
|
....*..
gi 500471923 849 ILEVNPR 855
Cdd:PRK09288 278 FSEVSPR 284
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
665-884 |
9.39e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 55.91 E-value: 9.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 665 EKAGVPIIGTSPDAIDRAEDRERFQEMLHKLGLrqP----ENGTARSFEEAEKVADRIGYPVVVRPSYVLGGRAMEIVYD 740
Cdd:PRK08462 98 SHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGV--PvipgSDGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVED 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 741 VDNLRR-YMHT---AVQASPEHPILIDKFLDEAIEIDVDALCDGTEAViggimehieeagIHSGDSACSLPPYS---ISR 813
Cdd:PRK08462 176 ESDLENlYLAAeseALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNV------------IHVGERDCSLQRRHqklIEE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 814 EIADEIRRQTKMMALELNVRGLMNVQY---------AIKDDVIYILEVNPRASRTAPFVSKATGRPLAKLAARIMSGKTL 884
Cdd:PRK08462 244 SPAVVLDEKTRERLHETAIKAAKAIGYegagtfeflLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL 323
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
112-304 |
1.32e-07 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 55.91 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 112 GVELIGAKLPAIKMAEDRTLFKEAMQRINL-TVPRS-GLAHNHAEAMEIIKEIGFPAIIRPSftLGGTGGG--IAYNMEE 187
Cdd:PRK12999 103 GITFIGPTAEVLRLLGDKVAARNAAIKAGVpVIPGSeGPIDDIEEALEFAEEIGYPIMLKAS--AGGGGRGmrIVRSEEE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 188 Y-EKMSVAGIEA-----SPtsEILIEESVIGWKEYELEVMRDTADNVVII----CS--------IEnfdpmgvhtgdsit 249
Cdd:PRK12999 181 LeEAFERAKREAkaafgND--EVYLEKYVENPRHIEVQILGDKHGNVVHLyerdCSvqrrhqkvVE-------------- 244
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500471923 250 VAPAQTLTDKEYQILRDASLKIIREIG----------VDTggsniqfginprDGRLVVIEMNPRV 304
Cdd:PRK12999 245 IAPAPGLSEELRERICEAAVKLARAVGyvnagtveflVDA------------DGNFYFIEVNPRI 297
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
660-885 |
1.40e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 55.42 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 660 LAVSLEKAGVPIIGTSPDAIDRAEDRERFQEMLHKLGLR-QPENGTA-RSFEEAEKVADRIGYPVVVRPSYVLGGRAMEI 737
Cdd:PRK06111 91 FAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPvVPGITTNlEDAEEAIAIARQIGYPVMLKASAGGGGIGMQL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 738 VYDVDNLRRYMHT----AVQASPEHPILIDKFLDEAIEIDVDALCDGTEAViggimehieeagIHSGDSACSL------- 806
Cdd:PRK06111 171 VETEQELTKAFESnkkrAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNT------------VYLWERECSVqrrhqkv 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 807 ----PPYSISREIADEIRRQTKMMALELNVRGLMNVQYAI-KDDVIYILEVNPRASRTAPFVSKATGRPLAKLAARIMSG 881
Cdd:PRK06111 239 ieeaPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVdEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAG 318
|
....
gi 500471923 882 KTLR 885
Cdd:PRK06111 319 EKLS 322
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
109-304 |
8.24e-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: 53.54 E-value: 8.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 109 EKYGVELIGAKLPAIKMAEDRTLFKEAMQRINL-TVPRS-GLAHNHAEAMEIIKEIGFPAIIRPSftLGGTGGG--IAYN 184
Cdd:COG1038 99 EEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVpVIPGTeGPVDDLEEALAFAEEIGYPVMLKAA--AGGGGRGmrVVRS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 185 MEEYEK-MSVAGIEA-----SPtsEILIEESVIGWKEYELEVMRDTADNVVII----CS--------IEnfdpmgvhtgd 246
Cdd:COG1038 177 EEELEEaFESARREAkaafgDD--EVFLEKYIERPKHIEVQILGDKHGNIVHLferdCSvqrrhqkvVE----------- 243
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500471923 247 sitVAPAQTLTDKEYQILRDASLKIIREIG----------VDtggsniqfginpRDGRLVVIEMNPRV 304
Cdd:COG1038 244 ---IAPAPNLDEELREAICEAAVKLAKAVGyvnagtveflVD------------DDGNFYFIEVNPRI 296
|
|
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
957-1008 |
9.74e-07 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 52.79 E-value: 9.74e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 500471923 957 ISVrdADKKHIVSAAKKLYDNGFELVATRGTAAYLQEKGIPVLVVNKV------LEGR 1008
Cdd:PRK00881 9 ISV--SDKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVtgfpeiLDGR 64
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
109-402 |
1.24e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 52.34 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 109 EKYGVELIGAKLPAIKMAEDRTLFKEAMQRINLTV---PRSGLAhNHAEAMEIIKEIGFPAIIRPSFTLGGTGGGIAYNM 185
Cdd:PRK06111 96 KEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVvpgITTNLE-DAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 186 EEYEKmSVAGIEASPTS-----EILIEESVIGWKEYELEVMRDTADNVVII----CSIENfdpmgvHTGDSITVAPAQTL 256
Cdd:PRK06111 175 QELTK-AFESNKKRAANffgngEMYIEKYIEDPRHIEIQLLADTHGNTVYLwereCSVQR------RHQKVIEEAPSPFL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 257 TDKEYQILRDASLKIIREIGVdTGGSNIQFGINPrDGRLVVIEMNPRVSRSSALASKATGFPIA----KIAAKLAVGYTL 332
Cdd:PRK06111 248 DEETRKAMGERAVQAAKAIGY-TNAGTIEFLVDE-QKNFYFLEMNTRLQVEHPVTEEITGIDLVeqqlRIAAGEKLSFTQ 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 333 DEITND-------ITRETPACFEPT----IDYVVTKVPRFTFEKFPAADATLTTQMKS-VGEVMAIGRTFKESLQKAIRS 400
Cdd:PRK06111 326 DDIKRSghaievrIYAEDPKTFFPSpgkiTDLTLPGGEGVRHDHAVENGVTVTPFYDPmIAKLIAHGETREEAISRLHDA 405
|
..
gi 500471923 401 LE 402
Cdd:PRK06111 406 LE 407
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
35-179 |
1.62e-06 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 51.09 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 35 KALKEEGFQVVLLNsnpatimtdpdfADRTYIEPVTPEILAMIIEKERPDAVLPTlggQTALNTAVAVAESgvLEKYGVE 114
Cdd:COG0189 21 EAAQRRGHEVEVID------------PDDLTLDLGRAPELYRGEDLSEFDAVLPR---IDPPFYGLALLRQ--LEAAGVP 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500471923 115 LIGaKLPAIKMAEDRTLFKEAMQRINLTVPRSGLAHNHAEAMEIIKEIGFPAIIRPsftLGGTGG 179
Cdd:COG0189 84 VVN-DPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKP---LDGSGG 144
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
570-885 |
1.83e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 51.64 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 570 KKIMIlgggPNRiGQgiefdyCCVHGVFALAEDGYETIMVNCNPETVSTDYDTSDRLYF---EPLT-YEDVLNIVELEKP 645
Cdd:PRK07178 3 KKILI----ANR-GE------IAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSigaDPLAgYLNPRRLVNLAVE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 646 EGVIVQFGGQTPL----KLAVSLEKAGVPIIGTSPDAIDRAEDRERFQEMLHKLGLrqP----ENGTARSFEEAEKVADR 717
Cdd:PRK07178 72 TGCDALHPGYGFLsenaELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGV--PvtpgSEGNLADLDEALAEAER 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 718 IGYPVVVRPSYVLGGRAMEIVYDVDNLR----RYMHTAVQA--SPEhpILIDKFLDEAIEIDVDALCDGTEAViggimeh 791
Cdd:PRK07178 150 IGYPVMLKATSGGGGRGIRRCNSREELEqnfpRVISEATKAfgSAE--VFLEKCIVNPKHIEVQILADSHGNV------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 792 ieeagIHSGDSACslppySISR------EIA-----DEIRRQTkmmALELNVRGLMNVQYA---------IKDDVIYILE 851
Cdd:PRK07178 221 -----VHLFERDC-----SIQRrnqkliEIApspqlTPEQRAY---IGDLAVRAAKAVGYEnagtvefllDADGEVYFME 287
|
330 340 350
....*....|....*....|....*....|....
gi 500471923 852 VNPRASRTAPFVSKATGRPLAKLAARIMSGKTLR 885
Cdd:PRK07178 288 MNTRVQVEHTITEEITGIDIVREQIRIASGLPLS 321
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
1-346 |
1.89e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 51.68 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 1 MPKRtdIKKILIIGAGPI---VIGQACEFDYSGTQACKALKEEGFQVVLLNSnpaTIMTDPDFADRTYIEPvtpEILAMI 77
Cdd:PRK12833 1 MPSR--IRKVLVANRGEIavrIIRAARELGMRTVAACSDADRDSLAARMADE---AVHIGPSHAAKSYLNP---AAILAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 78 IEKERPDAVLPTLGgqtALNTAVAVAESgvLEKYGVELIGAKLPAIKMAEDRTLFKEAMQRINL-TVPRS-GLAHNHAEA 155
Cdd:PRK12833 73 ARQCGADAIHPGYG---FLSENAAFAEA--VEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVpTVPGSdGVVASLDAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 156 MEIIKEIGFPAIIRPSFTLGGTGGGIAYNMEEY-EKMSVAGIEASP---TSEILIEESVIGWKEYELEVMRDTADNVVII 231
Cdd:PRK12833 148 LEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLaAELPLAQREAQAafgDGGVYLERFIARARHIEVQILGDGERVVHLF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 232 ---CSIENfdpmgvHTGDSITVAPAQTLTDKEYQILRDASLKIIREIGVDTGGSnIQFGINPRDGRLVVIEMNPRVSRSS 308
Cdd:PRK12833 228 ereCSLQR------RRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGT-LEYLFDDARGEFYFIEMNTRIQVEH 300
|
330 340 350
....*....|....*....|....*....|....*...
gi 500471923 309 ALASKATGFPIAKIAAKLAVGYTLDEITNDITRETPAC 346
Cdd:PRK12833 301 PVTEAITGIDLVQEMLRIADGEPLRFAQGDIALRGAAL 338
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
682-855 |
2.02e-06 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 48.92 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 682 AEDRERFQEMLHKLGLRQPENGTARSFEEAEKvadrigyPVVVRPSYVLGGRAMEIVYDVDNLRRYMHtavqaspehPIL 761
Cdd:pfam02655 1 ASDKLKTYKALKNAGVPTPETLQAEELLREEK-------KYVVKPRDGCGGEGVRKVENGREDEAFIE---------NVL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 762 IDKFLdEAIEIDVDALCDGTEAVIGGI-MEHIEEAGIHSGDSACSLP-PYSISREIADEIRRQTKmmALElNVRGLMNVQ 839
Cdd:pfam02655 65 VQEFI-EGEPLSVSLLSDGEKALPLSVnRQYIDNGGSGFVYAGNVTPsRTELKEEIIELAEEVVE--CLP-GLRGYVGVD 140
|
170
....*....|....*.
gi 500471923 840 YAIKDDVIYILEVNPR 855
Cdd:pfam02655 141 LVLKDNEPYVIEVNPR 156
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
665-889 |
3.05e-06 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 51.68 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 665 EKAGVPIIGTSPDAIDRAEDRERFQEMLHKLGLrqP----ENGTARSFEEAEKVADRIGYPVVVRPSYVLGGRAMEIVYD 740
Cdd:PRK12999 100 AEAGITFIGPTAEVLRLLGDKVAARNAAIKAGV--PvipgSEGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 741 VDNLRRYMHTAV---QAS---PEhpILIDKFLDEAIEIDVDALCDGTeaviGGIMeHIEEAgihsgDsaCSL-------- 806
Cdd:PRK12999 178 EEELEEAFERAKreaKAAfgnDE--VYLEKYVENPRHIEVQILGDKH----GNVV-HLYER-----D--CSVqrrhqkvv 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 807 ---PPYSISREIADEIRRQTKMMALELNVRGLMNVQYAIKDDV-IYILEVNPRASrtapfVSKA-----TGRPLAKLAAR 877
Cdd:PRK12999 244 eiaPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGnFYFIEVNPRIQ-----VEHTvteevTGIDIVQSQIL 318
|
250
....*....|..
gi 500471923 878 IMSGKTLRELGI 889
Cdd:PRK12999 319 IAEGATLHDLEI 330
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
29-301 |
3.20e-06 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 50.11 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 29 SGTQACKALKEEGFQVVLLnsnpatimtDPDfadrtyiepvtpEILAMIIEKERPDAVLPTLGG--------QTALNT-A 99
Cdd:PRK01372 24 SGAAVLAALREAGYDAHPI---------DPG------------EDIAAQLKELGFDRVFNALHGrggedgtiQGLLELlG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 100 VAVAESGVLEKygveligaklpAIKMAEDRTlfKEAMQRINLTVPRSGLAHNHAEAMEIIKEIGFPAIIRPSftLGGTGG 179
Cdd:PRK01372 83 IPYTGSGVLAS-----------ALAMDKLRT--KLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKPA--REGSSV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 180 GIaYNMEEYEKMSVAGIEASPT-SEILIEESVIGwKEYELEVMRDTADNVVIICSIENFdpm--gvHTGDSITVAPAQtL 256
Cdd:PRK01372 148 GV-SKVKEEDELQAALELAFKYdDEVLVEKYIKG-RELTVAVLGGKALPVIEIVPAGEFydyeakyLAGGTQYICPAG-L 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 500471923 257 TDKEYQILRDASLKIIREIGVdTGGSNIQFGINpRDGRLVVIEMN 301
Cdd:PRK01372 225 PAEIEAELQELALKAYRALGC-RGWGRVDFMLD-EDGKPYLLEVN 267
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
664-806 |
3.37e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 50.96 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 664 LEKAGVPIIGTSPDAIDRAEDRERFQEMLHKLGLrqP----ENGTARSFEEAEKVADRIGYPVVVRPSYVLGGRAMEIVY 739
Cdd:PRK08591 95 CEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGV--PvvpgSDGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVR 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500471923 740 DVDNLRRYMHTAVQ---ASPEHPIL-IDKFLDEAIEIDVDALCDGTEAViggimehieeagIHSGDSACSL 806
Cdd:PRK08591 173 TEAELEKAFSMARAeakAAFGNPGVyMEKYLENPRHIEIQVLADGHGNA------------IHLGERDCSL 231
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
62-301 |
4.00e-06 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 50.06 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 62 DRTYIEPVTPEILAMIIEKeRPDAVLPTLGGQTALNTAVAvaesGVLEKYGVELIGAKLPAIKMAEDRTLFKEAMQRINL 141
Cdd:PRK14569 37 DAVGVDASGKELVAKLLEL-KPDKCFVALHGEDGENGRVS----ALLEMLEIKHTSSSMKSSVITMDKMISKEILMHHRM 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 142 TVPRSGLAHNHAEAMEiikEIGFPAIIRPSftlgGTGGGIA-YNMEEYEKMSVAGIEASPTSEILIEESVIGwKEYELEV 220
Cdd:PRK14569 112 PTPMAKFLTDKLVAED---EISFPVAVKPS----SGGSSIAtFKVKSIQELKHAYEEASKYGEVMIEQWVTG-KEITVAI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 221 MRDTADNVVIICSIENF-DPMGVHTGDSITVAPAQTLTDKEYQIlRDASLKIIREIGVdTGGSNIQFGINPRdGRLVVIE 299
Cdd:PRK14569 184 VNDEVYSSVWIEPQNEFyDYESKYSGKSIYHSPSGLCEQKELEV-RQLAKKAYDLLGC-SGHARVDFIYDDR-GNFYIME 260
|
..
gi 500471923 300 MN 301
Cdd:PRK14569 261 IN 262
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
79-327 |
4.19e-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: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 79 EKERPDAVLPTlGGQTALNTAVAVAesgvLEKYGVELIGAKLpAIKMAEDRTLFKEAMQRINLTVPRSGLAHNHAEAMEI 158
Cdd:TIGR00768 45 ALAELDVVIVR-IVSMFRGLAVLRY----LESLGVPVINSSD-AILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 159 IKEIGFPAIIRPSFtlGGTGGGIAYNMEEYEKMSVAGI---EASPTSEILIEESVigwKEYELEVMRDTADNVVIICSIE 235
Cdd:TIGR00768 119 IEEIGFPVVLKPVF--GSWGRGVSLARDRQAAESLLEHfeqLNGPQNLFLVQEYI---KKPGGRDIRVFVVGDEVVAAIY 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 236 NFDPMG----VHTGDSITVAPaqtLTDKEYQIlrdaSLKIIREIGVDTGGSNIqfgINPRDGrLVVIEMNPRVSRSSalA 311
Cdd:TIGR00768 194 RITSGHwrsnLARGGKAEPCS---LTEEIEEL----AIKAAKALGLDVAGVDL---LESEDG-LLVNEVNANPEFKN--S 260
|
250
....*....|....*.
gi 500471923 312 SKATGFPIAKIAAKLA 327
Cdd:TIGR00768 261 VKTTGVNIAGKLLDYI 276
|
|
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
957-1008 |
5.08e-06 |
|
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: 50.41 E-value: 5.08e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 500471923 957 ISVrdADKKHIVSAAKKLYDNGFELVATRGTAAYLQEKGIPVLVVNKV------LEGR 1008
Cdd:COG0138 8 ISV--SDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVtgfpeiLDGR 63
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
674-728 |
6.60e-06 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 50.15 E-value: 6.60e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 500471923 674 TSPDAIDRAEDRERFQEMLHKLGLRQPENGTARSFEEAEKVADRIGYPVVVRPSY 728
Cdd:PRK14016 204 TSAIAVDIACDKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPLD 258
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
684-861 |
3.53e-05 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 47.03 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 684 DRERFQEMLHKLGLRQPENGTARSFEEAEKVADRIGYPVVVRPsyVLGGR--AMEIVYDVDNLRrymhTAVQASPEHP-- 759
Cdd:PRK01372 98 DKLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKP--AREGSsvGVSKVKEEDELQ----AALELAFKYDde 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 760 ILIDKFLdEAIEIDVdalcdgteAVIGG----IMEhIE--------EAGIHSGDSACSLPPysisrEIADEIRRQTKMMA 827
Cdd:PRK01372 172 VLVEKYI-KGRELTV--------AVLGGkalpVIE-IVpagefydyEAKYLAGGTQYICPA-----GLPAEIEAELQELA 236
|
170 180 190
....*....|....*....|....*....|....*....
gi 500471923 828 LE----LNVRGLMNVQYAIKDD-VIYILEVNprasrTAP 861
Cdd:PRK01372 237 LKayraLGCRGWGRVDFMLDEDgKPYLLEVN-----TQP 270
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
668-881 |
4.39e-05 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 47.53 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 668 GVPiiGTSPDAIDRAEDRERFQEMLHKLGLRQPENGTARSFEEAEKVADRIGYPVVVRPSYVLGGRAMEIVYDVDNLrrY 747
Cdd:PRK02186 93 GLP--AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEA--A 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 748 MHTAVQASPEHP-ILIDKFLDEAiEIDVDALCDGTEAVIGGIME-------HIEEAGiHSGDSACSLPpysiSRE-IADE 818
Cdd:PRK02186 169 AHCAALRRAGTRaALVQAYVEGD-EYSVETLTVARGHQVLGITRkhlgpppHFVEIG-HDFPAPLSAP----QRErIVRT 242
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500471923 819 IRRQTKMMALELnvrGLMNVQYAIKDDVIYILEVNPR-ASRTAP-FVSKATGRPLAKLAARIMSG 881
Cdd:PRK02186 243 VLRALDAVGYAF---GPAHTELRVRGDTVVIIEINPRlAGGMIPvLLEEAFGVDLLDHVIDLHLG 304
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
665-855 |
9.32e-05 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 46.61 E-value: 9.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 665 EKAGVPIIGTSPDAIDraedrerfqemlhklglrqpengtarSFEEAEKVADRIGYPVVVRPSYVLGGRAMEIVYDVDNL 744
Cdd:COG1038 127 IEAGVPVIPGTEGPVD--------------------------DLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEEL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 745 RRYMHTAVQ------ASPEhpILIDKFLDEAIEIDVDALCDGTeaviGGIMeHIEEAgihsgDsaCSL-----------P 807
Cdd:COG1038 181 EEAFESARReakaafGDDE--VFLEKYIERPKHIEVQILGDKH----GNIV-HLFER-----D--CSVqrrhqkvveiaP 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 500471923 808 PYSISREIADEIRRQTKMMALELNVRG------LMNvqyaiKDDVIYILEVNPR 855
Cdd:COG1038 247 APNLDEELREAICEAAVKLAKAVGYVNagtvefLVD-----DDGNFYFIEVNPR 295
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
694-855 |
9.60e-05 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 44.17 E-value: 9.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 694 KLGLRQPENGTARSFEEAEKVADRIGYPVVVRpSYVLG--GRAMEIVYDVDNLRrymhTAVQASPEHPILIDKFLD---E 768
Cdd:pfam02222 2 KLGLPTPRFMAAESLEELIEAGQELGYPCVVK-ARRGGydGKGQYVVRSEADLP----QAWEELGDGPVIVEEFVPfdrE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 769 AIEIDVDALcDGtEAVIGGIMEHIEEAGIhsgdsaC--SLPPYSISREIADEIRRQTKMMALELNVRGLMNVQYAIKDD- 845
Cdd:pfam02222 77 LSVLVVRSV-DG-ETAFYPVVETIQEDGI------CrlSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELFVTEDg 148
|
170
....*....|
gi 500471923 846 VIYILEVNPR 855
Cdd:pfam02222 149 DLLINELAPR 158
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
109-339 |
1.01e-04 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 46.34 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 109 EKYGVELIGAKLPAIKMAEDRTLFKEAMQRINL-TVPrsGLAHNHAEAMEIIKE----IGFPAIIRPSFTLGGTGGGIAY 183
Cdd:PRK08463 95 EDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIpIVP--GTEKLNSESMEEIKIfarkIGYPVILKASGGGGGRGIRVVH 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 184 NMEEYEKMSVAGIEASPT----SEILIEESVIGWKEYELEVMRDTADNVVII----CSIENfdpmgvHTGDSITVAPAQT 255
Cdd:PRK08463 173 KEEDLENAFESCKREALAyfnnDEVFMEKYVVNPRHIEFQILGDNYGNIIHLcerdCSIQR------RHQKVIEIAPCPS 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 256 LTDKEYQILRDASLKIIREIGVDTGGSnIQFGINPRDgRLVVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLDEI 335
Cdd:PRK08463 247 ISDNLRKTMGVTAVAAAKAVGYTNAGT-IEFLLDDYN-RFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEILDLE 324
|
....
gi 500471923 336 TNDI 339
Cdd:PRK08463 325 QSDI 328
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
122-220 |
1.35e-04 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 45.92 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 122 AIKMAEDRTLFKEAMQRINLTVPRSGLAHNHAEAMEIIKEIGFPAIIRPSFtlGGTGGGIAYNMEEYEKMSVAGIEASP- 200
Cdd:PRK14016 208 AVDIACDKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPLD--GNHGRGVTVNITTREEIEAAYAVASKe 285
|
90 100
....*....|....*....|
gi 500471923 201 TSEILIEESVIGwKEYELEV 220
Cdd:PRK14016 286 SSDVIVERYIPG-KDHRLLV 304
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
162-303 |
3.75e-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: 42.27 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 162 IGFPAIIRPSFTLGGTGGGIAYNMEEYEK--------MSVA----GIEASPTSEILIEESVIGwKEYELEVMRDTADNVV 229
Cdd:pfam13535 1 IPYPCVIKPSVGFFSVGVYKINNREEWKAafaaireeIEQWkemyPEAVVDGGSFLVEEYIEG-EEFAVDAYFDENGEPV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500471923 230 IICSIENFDPMGVHTGDSITVAPAQTLTDKEYQILrDASLKIIREIGVDTGGSNIQFGINpRDGRLVVIEMNPR 303
Cdd:pfam13535 80 ILNILKHDFASSEDVSDRIYVTSASIIRETQAAFT-EFLKRINALLGLKNFPVHIELRVD-EDGQIIPIEVNPL 151
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
633-744 |
8.77e-04 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 43.26 E-value: 8.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 633 YEDVLNIVELEKPEGVIVQFGGQTPL----KLAVSLEKAGVPIIGTSPDAIDRAEDRERFQEMLHKLGL-----RQPENg 703
Cdd:PRK08463 59 YLDVKRIVEIAKACGADAIHPGYGFLsenyEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIpivpgTEKLN- 137
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 500471923 704 tARSFEEAEKVADRIGYPVVVRPSYVLGGRAMEIVYDVDNL 744
Cdd:PRK08463 138 -SESMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDL 177
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
61-170 |
1.30e-03 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 42.43 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 61 ADRTYIEPVT-PEILAMIIEKERPDAVLPTLggqTALNTAVAVAesgvLEKYGVELI-GAKlpAIKMAEDRtlfkEAMQR 138
Cdd:PRK09288 53 AHRSHVIDMLdGDALRAVIEREKPDYIVPEI---EAIATDALVE----LEKEGFNVVpTAR--ATRLTMNR----EGIRR 119
|
90 100 110
....*....|....*....|....*....|....*..
gi 500471923 139 I---NLTVPRS--GLAHNHAEAMEIIKEIGFPAIIRP 170
Cdd:PRK09288 120 LaaeELGLPTSpyRFADSLEELRAAVEEIGYPCVVKP 156
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
709-880 |
8.20e-03 |
|
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: 38.84 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 709 EEAEKVADRIGYPVVVRPSyVLGGR-AMEIVYDVDNLRRYMHTAVQASPEhpILIDKFLdEAIEIDVDALCDGTEaVIGG 787
Cdd:pfam07478 26 EWCAQVEEALGYPVFVKPA-RLGSSvGVSKVESREELQAAIEEAFQYDEK--VLVEEGI-EGREIECAVLGNEDP-EVSP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500471923 788 IMEHIEEAGI------HSGDSACSLPPYSISREIADEIRRQTKMMALELNVRGLMNVQYAI-KDDVIYILEVNPRASRTA 860
Cdd:pfam07478 101 VGEIVPSGGFydyeakYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRGLARVDFFLtEDGEIVLNEVNTIPGFTS 180
|
170 180
....*....|....*....|....
gi 500471923 861 ----PFVSKATGRPLAKLAARIMS 880
Cdd:pfam07478 181 ismfPKLAAAAGVSFPDLVDQLIE 204
|
|
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
690-724 |
9.63e-03 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 40.11 E-value: 9.63e-03
10 20 30
....*....|....*....|....*....|....*
gi 500471923 690 EMLHKLGLRQPENGTARSFEEAEKVADRIGYPVVV 724
Cdd:COG1042 495 ALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVL 529
|
|
| |
