|
Name |
Accession |
Description |
Interval |
E-value |
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
1-1065 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1926.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 1 MPKRDDIQKILVIGSGAIVIGQGCEFDYSGAQGLKALREEGYETVLINSNPATIMTDPESADRTYIEPLTPEYLEKVIAA 80
Cdd:PRK05294 1 MPKRTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 81 ERPQAVLPTLGGQTALNLTVAAAERGVFKKHGVEVLGANLETIRKAEDRQLFKAAMQKIGLDLPRSVVVTDATDLKPVAR 160
Cdd:PRK05294 81 ERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 161 ELGFPVIVRASFTLGGTGGGIAYHFDELRHRVHRALEASPVKKVLLEESVIGWKEYELEVMRDRKDNFVVICSIENLDPM 240
Cdd:PRK05294 161 EIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 241 GVHTGDSVTVAPAQTLTDRQYQEMRDEAKRIVSEIGVETGGCNIQFAVDPRDGRRVVIEINPRVSRSSALASKATGFPIA 320
Cdd:PRK05294 241 GVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVETGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 321 RIAAKLAVGYALDELPNDITKATLACFEPAIDYIVTKAPRFATEKF--GEFPLDTAMKSVGEAMAVGRTFKESLQKALRG 398
Cdd:PRK05294 321 KVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFpgADRRLGTQMKSVGEVMAIGRTFEESLQKALRS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 399 LESGKKGLEGR--EDLDDETLLQRVAGPSSARLYHVATALERGLSVERIAEVSKIDPWFLNELKEIKDFEKTLAAS--PL 474
Cdd:PRK05294 401 LEIGVTGLDEDlfEEESLEELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENglPL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 475 DAEILRAAKRLGFSDAQLARCQGKSEAEIRARRVRLGIRPSYKLIDTCAGEFPSSTPYFYSTYENAGDFLPaaAGKKRVV 554
Cdd:PRK05294 481 DAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNP--SDRKKVL 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 555 ILGSGPNRIGQGIEFDYCCVQASKALRELGWQSVMVNCNPETVSTDYDASDRLYFEPLTFEDVMEIIDVEKPDGVIVQFG 634
Cdd:PRK05294 559 VLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFG 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 635 GQTPLNLAAQLAKARVPILGTQPAAIDMAEDRRLFGAALKKLKILSPESGIARTAAQALKIARRIGYPVMVRPSYVLGGR 714
Cdd:PRK05294 639 GQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGR 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 715 MMEIVYDDAALLDYSERARKASLHPSLLVDRFLADAAELDVDAVCDGKDVWIAGVMEHIEEAGVHSGDSACSLPSHSLPP 794
Cdd:PRK05294 719 AMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICDGEDVLIGGIMEHIEEAGVHSGDSACSLPPQTLSE 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 795 SVLAVVREHTRRLALHLKVRGLINIQYAVKDGAVYVLEANPRASRTVPFVSKATGLPVARIATWVMMGKTLKKLvppAAL 874
Cdd:PRK05294 799 EIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAEL---GYT 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 875 KGAEPPYTATKEAVMPFIKFPGVDPRLGPEMKSTGEVMGLDADFPRSFAKSQEAAGLSLPTSGSVFVSVRDEDKPVLLHV 954
Cdd:PRK05294 876 KGLIPPYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSGTVFLSVRDRDKEEVVEL 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 955 ARALRQMGFTLVATRNTADFLERYGLPTGRVAKIGEGKPDVVDLLRQRGLSLVINTPSGKRARTDGYSIRRTALELDIPC 1034
Cdd:PRK05294 956 AKRLLELGFKILATSGTAKFLREAGIPVELVNKVHEGRPHIVDLIKNGEIDLVINTPTGRQAIRDGFSIRRAALEYKVPY 1035
|
1050 1060 1070
....*....|....*....|....*....|.
gi 1084961178 1035 ITNIRSVNAAVHAIAVLQGATMSVKPLQEHY 1065
Cdd:PRK05294 1036 ITTLAGARAAVKAIEALKFGELEVRSLQEYH 1066
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
2-1048 |
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: 1546.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 2 PKRDDIQKILVIGSGAIVIGQGCEFDYSGAQGLKALREEGYETVLINSNPATIMTDPESADRTYIEPLTPEYLEKVIAAE 81
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 82 RPQAVLPTLGGQTALNLTVAAAERGVFKKHGVEVLGANLETIRKAEDRQLFKAAMQKIGLDLPRSVVVTDATDLKPVARE 161
Cdd:TIGR01369 81 RPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 162 LGFPVIVRASFTLGGTGGGIAYHFDELRHRVHRALEASPVKKVLLEESVIGWKEYELEVMRDRKDNFVVICSIENLDPMG 241
Cdd:TIGR01369 161 IGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 242 VHTGDSVTVAPAQTLTDRQYQEMRDEAKRIVSEIGVEtGGCNIQFAVDPRDGRRVVIEINPRVSRSSALASKATGFPIAR 321
Cdd:TIGR01369 241 VHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIE-GGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 322 IAAKLAVGYALDELPNDITKATLACFEPAIDYIVTKAPRFATEKFGEFP--LDTAMKSVGEAMAVGRTFKESLQKALRGL 399
Cdd:TIGR01369 320 VAAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDrkLGTQMKSVGEVMAIGRTFEEALQKALRSL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 400 ESGKKGLEG--REDLDDETLLQRVAGPSSARLYHVATALERGLSVERIAEVSKIDPWFLNELKEIKDFEKTLA---ASPL 474
Cdd:TIGR01369 400 EIGATGFDLpdREVEPDEDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEevkLTDL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 475 DAEILRAAKRLGFSDAQLARCQGKSEAEIRARRVRLGIRPSYKLIDTCAGEFPSSTPYFYSTYENAGDFLPAAAgKKRVV 554
Cdd:TIGR01369 480 DPELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTD-KKKVL 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 555 ILGSGPNRIGQGIEFDYCCVQASKALRELGWQSVMVNCNPETVSTDYDASDRLYFEPLTFEDVMEIIDVEKPDGVIVQFG 634
Cdd:TIGR01369 559 VLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFG 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 635 GQTPLNLAAQLAKARVPILGTQPAAIDMAEDRRLFGAALKKLKILSPESGIARTAAQALKIARRIGYPVMVRPSYVLGGR 714
Cdd:TIGR01369 639 GQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGR 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 715 MMEIVYDDAALLDYSERARKASLHPSLLVDRFLADAAELDVDAVCDGKDVWIAGVMEHIEEAGVHSGDSACSLPSHSLPP 794
Cdd:TIGR01369 719 AMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSA 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 795 SVLAVVREHTRRLALHLKVRGLINIQYAVKDGAVYVLEANPRASRTVPFVSKATGLPVARIATWVMMGKTLKKLVPpaaL 874
Cdd:TIGR01369 799 EIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGV---G 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 875 KGAEPPYTATKEAVMPFIKFPGVDPRLGPEMKSTGEVMGLDADFPRSFAKSQEAAGLSLPTSGSVFVSVRDEDKPVLLHV 954
Cdd:TIGR01369 876 KEKEPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDL 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 955 ARALRQMGFTLVATRNTADFLERYGLPTGRVAKIGEGKPDVVDLLRQRGLSLVINTPS-GKRARTDGYSIRRTALELDIP 1033
Cdd:TIGR01369 956 ARKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEGRPNILDLIKNGEIELVINTTSkGAGTATDGYKIRREALDYGVP 1035
|
1050
....*....|....*
gi 1084961178 1034 CITNIRSVNAAVHAI 1048
Cdd:TIGR01369 1036 LITTLNTAEAFAEAL 1050
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
1-1066 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1456.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 1 MPKRDDIQKILVIGSGAIVIGQGCEFDYSGAQGLKALREEGYETVLINSNPATIMTDPESADRTYIEPLTPEYLEKVIAA 80
Cdd:PRK12815 1 MPKDTDIQKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 81 ERPQAVLPTLGGQTALNLTVAAAERGVFKKHGVEVLGANLETIRKAEDRQLFKAAMQKIGLDLPRSVVVTDATDLKPVAR 160
Cdd:PRK12815 81 EKPDALLATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 161 ELGFPVIVRASFTLGGTGGGIAYHFDELRHRVHRALEASPVKKVLLEESVIGWKEYELEVMRDRKDNFVVICSIENLDPM 240
Cdd:PRK12815 161 KIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 241 GVHTGDSVTVAPAQTLTDRQYQEMRDEAKRIVSEIGVeTGGCNIQFAVDPRDGRRVVIEINPRVSRSSALASKATGFPIA 320
Cdd:PRK12815 241 GIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGV-VGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 321 RIAAKLAVGYALDELPNDITKATLACFEPAIDYIVTKAPRFATEKFG--EFPLDTAMKSVGEAMAVGRTFKESLQKALRG 398
Cdd:PRK12815 320 KIAAKLAVGYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGyaDRTLGTQMKATGEVMAIGRNFESAFQKALRS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 399 LESGKKGLEGREDL---DDETLLQRVAGPSSARLYHVATALERGLSVERIAEVSKIDPWFLNELKEIKDFEKTLAA--SP 473
Cdd:PRK12815 400 LEIKRNGLSLPIELsgkSDEELLQDLRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEdgLD 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 474 LDAEILRAAKRLGFSDAQLARCQGKSEAEIRARRVRLGIRPSYKLIDTCAGEFPSSTPYFYSTYENAGDFLPAAAgKKRV 553
Cdd:PRK12815 480 LSADLLRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGESEAEPSSE-KKKV 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 554 VILGSGPNRIGQGIEFDYCCVQASKALRELGWQSVMVNCNPETVSTDYDASDRLYFEPLTFEDVMEIIDVEKPDGVIVQF 633
Cdd:PRK12815 559 LILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIVQF 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 634 GGQTPLNLAAQLAKARVPILGTQPAAIDMAEDRRLFGAALKKLKILSPESGIARTAAQALKIARRIGYPVMVRPSYVLGG 713
Cdd:PRK12815 639 GGQTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGG 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 714 RMMEIVYDDAALLDYSERArKASLHPsLLVDRFLaDAAELDVDAVCDGKDVWIAGVMEHIEEAGVHSGDSACSLPSHSLP 793
Cdd:PRK12815 719 QGMAVVYDEPALEAYLAEN-ASQLYP-ILIDQFI-DGKEYEVDAISDGEDVTIPGIIEHIEQAGVHSGDSIAVLPPQSLS 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 794 PSVLAVVREHTRRLALHLKVRGLINIQYAVKDGAVYVLEANPRASRTVPFVSKATGLPVARIATWVMMGKTLKKLVPPAA 873
Cdd:PRK12815 796 EEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLAELGYPNG 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 874 LkGAEPPYTATKEAVMPFIKFPGVDPRLGPEMKSTGEVMGLDADFPRSFAKSQEAAGLSLPTSGSVFVSVRDEDKPVLLH 953
Cdd:PRK12815 876 L-WPGSPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGTIFISVRDEDKPEVTK 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 954 VARALRQMGFTLVATRNTADFLERYGLPTGRVAKIGEGKPDVVDLLRQRGLSLVINTPSGKRARTDGYSIRRTALELDIP 1033
Cdd:PRK12815 955 LARRFAQLGFKLLATEGTANWLAEEGITTGVVEKVQEGSPSLLERIKQHRIVLVVNTSLSDSASEDAIKIRDEALSTHIP 1034
|
1050 1060 1070
....*....|....*....|....*....|...
gi 1084961178 1034 CITNIRSVNAAVHAIAVLQGATMSVKPLQEHYK 1066
Cdd:PRK12815 1035 VFTELETAQAFLQVLESLALTTQPIQELQEKHK 1067
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
3-1065 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 1401.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 3 KRDDIQKILVIGSGAIVIGQGCEFDYSGAQGLKALREEGYETVLINSNPATIMTDPESADRTYIEPLTPEYLEKVIAAER 82
Cdd:PLN02735 19 KRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 83 PQAVLPTLGGQTALNLTVAAAERGVFKKHGVEVLGANLETIRKAEDRQLFKAAMQKIGLDLPRSVVVTDATDLKPVAREL 162
Cdd:PLN02735 99 PDALLPTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 163 G-FPVIVRASFTLGGTGGGIAYHFDELRHRVHRALEASPVKKVLLEESVIGWKEYELEVMRDRKDNFVVICSIENLDPMG 241
Cdd:PLN02735 179 GeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 242 VHTGDSVTVAPAQTLTDRQYQEMRDEAKRIVSEIGVETGGCNIQFAVDPRDGRRVVIEINPRVSRSSALASKATGFPIAR 321
Cdd:PLN02735 259 VHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVECGGSNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 322 IAAKLAVGYALDELPNDITKATLACFEPAIDYIVTKAPRFATEKF-GEFP-LDTAMKSVGEAMAVGRTFKESLQKALRGL 399
Cdd:PLN02735 339 MAAKLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFpGSQPiLTTQMKSVGEAMALGRTFQESFQKALRSL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 400 ESGKKGL----EGREDLDDETLLQRVAGPSSARLYHVATALERGLSVERIAEVSKIDPWFLNELKEIKDFEKTLAA---S 472
Cdd:PLN02735 419 ETGFSGWgcakVKELDWDWEQLKYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSrslS 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 473 PLDAEILRAAKRLGFSDAQLARCQGKSEAEIRARRVRLGIRPSYKLIDTCAGEFPSSTPYFYSTYEnaGDFLPAAAGKKR 552
Cdd:PLN02735 499 ELSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYD--GECESAPTNKKK 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 553 VVILGSGPNRIGQGIEFDYCCVQASKALRELGWQSVMVNCNPETVSTDYDASDRLYFEPLTFEDVMEIIDVEKPDGVIVQ 632
Cdd:PLN02735 577 VLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQ 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 633 FGGQTPLNLAAQLAKA-------------RVPILGTQPAAIDMAEDRRLFGAALKKLKILSPESGIARTAAQALKIARRI 699
Cdd:PLN02735 657 FGGQTPLKLALPIQKYldknpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKRI 736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 700 GYPVMVRPSYVLGGRMMEIVYDDAALLDYSERARKASLHPSLLVDRFLADAAELDVDAVCDGK-DVWIAGVMEHIEEAGV 778
Cdd:PLN02735 737 GYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALADSEgNVVIGGIMEHIEQAGV 816
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 779 HSGDSACSLPSHSLPPSVLAVVREHTRRLALHLKVRGLINIQYAV-KDGAVYVLEANPRASRTVPFVSKATGLPVARIAT 857
Cdd:PLN02735 817 HSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAItPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYAS 896
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 858 WVMMGKTLKKLvppAALKGAEPPYTATKEAVMPFIKFPGVDPRLGPEMKSTGEVMGLDADFPRSFAKSQEAAGLSLPTSG 937
Cdd:PLN02735 897 LVMSGKSLKDL---GFTEEVIPAHVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLPLSG 973
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 938 SVFVSVRDEDKPVLLHVARALRQMGFTLVATRNTADFLERYGLPTGRVAKIGEGKPDVVDLLRQRGLSLVINTPSGKRA- 1016
Cdd:PLN02735 974 TVFISLNDLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVLKLHEGRPHAGDMLANGQIQLMVITSSGDALd 1053
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*....
gi 1084961178 1017 RTDGYSIRRTALELDIPCITNIRSVNAAVHAIAVLQGATMSVKPLQEHY 1065
Cdd:PLN02735 1054 QKDGRQLRRMALAYKVPIITTVAGALATAQAVKSLKECPIEMIALQDFF 1102
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
556-1070 |
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: 734.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 556 LGSGPNRIGQGIEFDYCCVQASKALRELGWQSVMVNCNPETVSTDYDASDRLYFEPLTFEDVMEIIDVEKPDGVIVQFGG 635
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 636 QTPLNLAAQLAKAR----VPILGTQPAAIDMAEDRRLFGAALKKLKILSPESGIARTAAQALKIARRIGYPVMVRPSYVL 711
Cdd:COG0458 81 QTALNLAVELEEAGilegVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 712 GGRMMEIVYDDAALLDYSERARKASLHPSLLVDRFLADAAELDVDAVCDGKD-VWIAGVMEHIEEAGVHSGDSACSLPSH 790
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDnVIIVGIMEHIEPAGVHSGDSICVAPPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 791 SLPPSVLAVVREHTRRLALHLKVRGLINIQYAVKDGAVYVLEANPRASRTVPFVSKATGLPVARIATWVMMGKTLKKLVP 870
Cdd:COG0458 241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 871 PaalKGAEP--PYTATKEAVMPFIKFPGVDPRLGPEMKSTGEVMGLDADFPRSFAKSQEAAGLSLPtsGSVFVS-VRDED 947
Cdd:COG0458 321 D---TGFEPtlDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLP--GTVLLSlVADDD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 948 KPVLLHVARALRQMGFTLVATRNTADFLERYGLPTGRVAKIGEGKPDVVDLLRQRGLSLVINTPSGKRARTDGYSIRRTA 1027
Cdd:COG0458 396 KEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVINTLLGAKSLGDSDGIIRRA 475
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1084961178 1028 LELDIPCITNIRSVNAAVHAIAVLQGATMSVKPLQEHYKSLPY 1070
Cdd:COG0458 476 LAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYE 518
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
13-556 |
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: 701.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 13 IGSGAIVIGQGCEFDYSGAQGLKALREEGYETVLINSNPATIMTDPESADRTYIEPLTPEYLEKVIAAERPQAVLPTLGG 92
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 93 QTALNLTVAAAERGVFKkhGVEVLGANLETIRKAEDRQLFKAAMQKIGLDLPRSVVVTDATDLKPVARELGFPVIVRASF 172
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 173 TLGGTGGGIAYHFDELRHRVHRALEASPVKKVLLEESVIGWKEYELEVMRDRKDNFVVICSIENLDPMGVHTGDSVTVAP 252
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 253 AQTLTDRQYQEMRDEAKRIVSEIGVEtGGCNIQFAVDprDGRRVVIEINPRVSRSSALASKATGFPIARIAAKLAVGYAL 332
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVV-GLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 333 DELPNDiTKatlacFEPAIDYIVTKAPRFATEKFGEFP--LDTAMKSVGEAMAVGRTFKESLQKALRGLESGKKG--LEG 408
Cdd:COG0458 316 DELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDpvLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLLS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 409 REDLDDETLLQRVAgPSSARLYHVATALERGLSVERIAEVSKIDPWFLNELKEIKDFEKTLAASPLDAEILRAAKRLGFS 488
Cdd:COG0458 390 LVADDDKEEALLLA-RRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVINTLLGAKSLGDS 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1084961178 489 DAQLARCQGKSEAEIRARRVRLGIRPSYKLIDTCAGEFPSSTPYFYSTYENAGDFLPAAAGKKRVVIL 556
Cdd:COG0458 469 DGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
128-333 |
2.48e-74 |
|
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: 244.52 E-value: 2.48e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 128 DRQLFKAAMQKIGLDLPRS--VVVTDATDLKPVARELGFPVIVRASFTLGGTGGGIAYHFDELRHRVHRALEASPV---- 201
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGtaGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 202 KKVLLEESVIGWKEYELEVMRDRKDNFVVICSIENLDPMgvHTGDSVTVAPAQTLTDRQYQEMRDEAKRIVSEIGVEtGG 281
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYV-GA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1084961178 282 CNIQFAVDPRDGRRVVIEINPRVSRSSALASKATGFPIARIAAKLAVGYALD 333
Cdd:pfam02786 158 GTVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
417-537 |
2.07e-55 |
|
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: 187.66 E-value: 2.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 417 LLQRVAGPSSARLYHVATALERGLSVERIAEVSKIDPWFLNELKEIKDFEKTLAA---SPLDAEILRAAKRLGFSDAQLA 493
Cdd:smart01096 1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKgglDELDADLLRKAKRLGFSDRQIA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1084961178 494 RCQGKSEAEIRARRVRLGIRPSYKLIDTCAGEFPSSTPYFYSTY 537
Cdd:smart01096 81 KLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
937-1045 |
8.10e-44 |
|
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: 154.17 E-value: 8.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 937 GSVFVSVRDEDKPVLLHVARALRQMGFTLVATRNTADFLERYGLPTGRVAKIGEGKPDVVDLLRQRGLSLVINTPSGKRA 1016
Cdd:cd01424 1 GTVFISVADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEGRPNIVDLIKNGEIQLVINTPSGKRA 80
|
90 100
....*....|....*....|....*....
gi 1084961178 1017 RTDGYSIRRTALELDIPCITNIRSVNAAV 1045
Cdd:cd01424 81 IRDGFSIRRAALEYKVPYFTTLDTARAAV 109
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
665-865 |
9.06e-35 |
|
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: 132.04 E-value: 9.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 665 DRRLFGAALKKLKILSPESGIAR--TAAQALKIARRIGYPVMVRPSYVLGGRMMEIVYDDAALLDYSERARKAS----LH 738
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 739 PSLLVDRFLADAAELDVDAVCDGKD-VWIAGVMEHIEEagVHSGDSACSLPSHSLPPSVLAVVREHTRRLALHLKVRGLI 817
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGnCITVCNRECSDQ--RRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1084961178 818 NIQYAV--KDGAVYVLEANPRASRTVPFVSKATGLPVARIATWVMMGKTL 865
Cdd:pfam02786 159 TVEFALdpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
117-329 |
3.00e-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: 118.05 E-value: 3.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 117 GANLETIRKAEDRQLFKAAMQKIGLDLPRSVVVTDATDLKPVARELGFPVIVRASFTLGGTGGGIAYHFDELRHRVHRAL 196
Cdd:COG0439 43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEAR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 197 E----ASPVKKVLLEESVIGwKEYELEVM-RDRKdnfVVICSI---ENLDPMGVHTGDsvtVAPAQtLTDRQYQEMRDEA 268
Cdd:COG0439 123 AeakaGSPNGEVLVEEFLEG-REYSVEGLvRDGE---VVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELV 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084961178 269 KRIVSEIGVETGGCNIQFAVDPrDGRRVVIEINPRVS--RSSALASKATGFPIARIAAKLAVG 329
Cdd:COG0439 195 ARALRALGYRRGAFHTEFLLTP-DGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALG 256
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
424-494 |
1.05e-28 |
|
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: 109.77 E-value: 1.05e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084961178 424 PSSARLYHVATALERGLSVERIAEVSKIDPWFLNELKEIKDFEKTLAA--SPLDAEILRAAKRLGFSDAQLAR 494
Cdd:pfam02787 6 PTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEagLDLDAELLREAKRLGFSDRQIAK 78
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
951-1036 |
4.99e-23 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 214855 [Multi-domain] Cd Length: 91 Bit Score: 94.08 E-value: 4.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 951 LLHVARALRQMGFTLVATRNTADFLERYGLPTGR--VAKIGEGKPDVVDLLRQRGLSLVINTPSG--KRARTDGYSIRRT 1026
Cdd:smart00851 2 LVEFAKRLAELGFELLATGGTAKFLREAGLPVVKtlHPKVHGGIPQILDLIKNGEIDLVINTLYPfeAQAHEDGYSIRRA 81
|
90
....*....|
gi 1084961178 1027 ALELDIPCIT 1036
Cdd:smart00851 82 AENIDIPGPT 91
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
951-1036 |
2.41e-22 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 460462 [Multi-domain] Cd Length: 93 Bit Score: 92.17 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 951 LLHVARALRQMGFTLVATRNTADFLERYGLP-TGRVAKIGEGKPD----VVDLLRQRGLSLVINTPSGKRART-DGYSIR 1024
Cdd:pfam02142 2 LVELAKALVELGFELLATGGTAKFLREAGIPvTEVVEKTGEGRPGgrvqIGDLIKNGEIDLVINTLYPFKATVhDGYAIR 81
|
90
....*....|..
gi 1084961178 1025 RTALELDIPCIT 1036
Cdd:pfam02142 82 RAAENIDIPGPT 93
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
36-329 |
6.59e-21 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 96.15 E-value: 6.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 36 ALREEGYETVLINSNPATIMTDPESADRTYIEPLTP-------EYLEKVIAAERPQAVLPTlgGQTALNLTVAAAERgvF 108
Cdd:COG3919 23 SLGEAGVRVIVVDRDPLGPAARSRYVDEVVVVPDPGddpeafvDALLELAERHGPDVLIPT--GDEYVELLSRHRDE--L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 109 KKHgVEVLGANLETIRKAEDRQLFKAAMQKIGLDLPRSVVVTDATDLKPVARELGFPVIVRAS--------FTLGGTGGG 180
Cdd:COG3919 99 EEH-YRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGFPVVVKPAdsvgydelSFPGKKKVF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 181 IAYHFDELRHRVHRALEASPvkKVLLEESVIGWKEYE--LEVMRDRKDNFVVICSIENL--DPMGVHTGDSVTVAPaqtl 256
Cdd:COG3919 178 YVDDREELLALLRRIAAAGY--ELIVQEYIPGDDGEMrgLTAYVDRDGEVVATFTGRKLrhYPPAGGNSAARESVD---- 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084961178 257 tdrqYQEMRDEAKRIVSEIGVeTGGCNIQFAVDPRDGRRVVIEINPRVSRSSALASKAtGFPIARIAAKLAVG 329
Cdd:COG3919 252 ----DPELEEAARRLLEALGY-HGFANVEFKRDPRDGEYKLIEINPRFWRSLYLATAA-GVNFPYLLYDDAVG 318
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
617-863 |
1.51e-19 |
|
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: 89.55 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 617 VMEIIDVEKPDGVIvqFGGQTPLNLAAQLAKA-RVPilGTQPAAIDMAEDRRLFGAALKKLKILSPESGIARTAAQALKI 695
Cdd:COG0439 9 AAELARETGIDAVL--SESEFAVETAAELAEElGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 696 ARRIGYPVMVRPSYVLGGRMMEIVYDDAALLDYSERARK----ASLHPSLLVDRFLaDAAELDVDAVCDGKDVWIAGVME 771
Cdd:COG0439 85 AEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAeakaGSPNGEVLVEEFL-EGREYSVEGLVRDGEVVVCSITR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 772 HIeEAGVHSGDSACSLPShSLPPSVLAVVREHTRRLALHLKV-RGLINIQYAV-KDGAVYVLEANPRAS--RTVPFVSKA 847
Cdd:COG0439 164 KH-QKPPYFVELGHEAPS-PLPEELRAEIGELVARALRALGYrRGAFHTEFLLtPDGEPYLIEINARLGgeHIPPLTELA 241
|
250
....*....|....*.
gi 1084961178 848 TGLPVARIATWVMMGK 863
Cdd:COG0439 242 TGVDLVREQIRLALGE 257
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
9-317 |
2.89e-15 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 78.39 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 9 KILVIGSGAivigqgcefdysGAQGLKALREEGyetvlinsNPATIM-TDPES-------ADRTYIEP--LTPEYLEKVI 78
Cdd:PRK12767 3 NILVTSAGR------------RVQLVKALKKSL--------LKGRVIgADISElapalyfADKFYVVPkvTDPNYIDRLL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 79 ---AAERPQAVLPTlggqTALNLTVAAAERGVFKKHGVEVLGANLETIRKAEDRQLFKAAMQKIGLDLPRSVVVTDATDL 155
Cdd:PRK12767 63 dicKKEKIDLLIPL----IDPELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 156 KPV--ARELGFPVIVRASFTLGGTGGGIAYHFDELRHrvhralEASPVKKVLLEESVIGwKEYELEVMRDRKDNFVVICS 233
Cdd:PRK12767 139 KAAlaKGELQFPLFVKPRDGSASIGVFKVNDKEELEF------LLEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVISIVP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 234 IENLDPMGVHTGDSVTVApaqtltdrqYQEMRDEAKRIVSEIGvETGGCNIQFAVdpRDGRRVVIEINPRVSRSSALASK 313
Cdd:PRK12767 212 RKRIEVRAGETSKGVTVK---------DPELFKLAERLAEALG-ARGPLNIQCFV--TDGEPYLFEINPRFGGGYPLSYM 279
|
....
gi 1084961178 314 AtGF 317
Cdd:PRK12767 280 A-GA 282
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
938-1039 |
1.66e-14 |
|
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: 70.79 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 938 SVFVSVRDEDKPVLLHVARALRQMGFTLVATRNTADFLERYGLPTGRVAK-IGEGKPDV---VDLLRQRGLSLVINTPS- 1012
Cdd:cd01423 2 GILISIGSYSKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWpSEEPQNDKpslRELLAEGKIDLVINLPSn 81
|
90 100
....*....|....*....|....*...
gi 1084961178 1013 -GKRARTDGYSIRRTALELDIPCITNIR 1039
Cdd:cd01423 82 rGKRVLDNDYVMRRAADDFAVPLITNPK 109
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
21-302 |
2.15e-13 |
|
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: 72.06 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 21 GQGCEFD---YSGAQGLKALREEGYETVLINSNPATIMTDpesadrtyiepltpeylekvIAAERPQAVLPTLGGQTALN 97
Cdd:COG1181 9 GRSAEREvslKSGRAVAAALDKAGYDVVPIGIDVEDLPAA--------------------LKELKPDVVFPALHGRGGED 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 98 LTVaaaeRGVFKKHGVEVLGANLETIRKAEDRQLFKAAMQKIGLDLPRSVVVT--DATDLKPVARELGFPVIVRASFtlG 175
Cdd:COG1181 69 GTI----QGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRrgELADLEAIEEELGLPLFVKPAR--E 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 176 GTGGGI--AYHFDELRHRVHRALEASPvkKVLLEESVIGwKEYELEVMRDrkDNFVVICSIEnLDPMGV--------HTG 245
Cdd:COG1181 143 GSSVGVskVKNAEELAAALEEAFKYDD--KVLVEEFIDG-REVTVGVLGN--GGPRALPPIE-IVPENGfydyeakyTDG 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1084961178 246 DSVTVAPAQtLTDRQYQEMRDEAKRIVSEIGVEtGGCNIQFAVDPrDGRRVVIEINP 302
Cdd:COG1181 217 GTEYICPAR-LPEELEERIQELALKAFRALGCR-GYARVDFRLDE-DGEPYLLEVNT 270
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
681-865 |
3.54e-12 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 70.06 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 681 PESGIArTAAQALKIARRIGYPVMVRPSYVLGGRMMEIVYDDAALLDY----SERARKASLHPSLLVDRFLADAAELDVD 756
Cdd:PRK06111 134 ITTNLE-DAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTKAfesnKKRAANFFGNGEMYIEKYIEDPRHIEIQ 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 757 AVCDGKDvwiagvmeHIeeagVHSGDSACSL-----------PSHSLPPSVLAVVREHTRRLALHLKVRGLINIQYAVKD 825
Cdd:PRK06111 213 LLADTHG--------NT----VYLWERECSVqrrhqkvieeaPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDE 280
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1084961178 826 GA-VYVLEANPRASRTVPFVSKATGLPVA----RIAtwvmMGKTL 865
Cdd:PRK06111 281 QKnFYFLEMNTRLQVEHPVTEEITGIDLVeqqlRIA----AGEKL 321
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
615-843 |
2.16e-11 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 66.45 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 615 EDVMEIIDVEKPDGVIVqfGGQTPLNLAAQ----LAKARVPILGTQPAAIDMAEDRRLFGAALKKLKILSPESGIARTAA 690
Cdd:PRK12767 59 DRLLDICKKEKIDLLIP--LIDPELPLLAQnrdrFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 691 QALKI--ARRIGYPVMVRPSYVLGGRMMEIVYDDAALLDYserarkASLHPSLLVDRFLADAaELDVDAVCD--GKDVWI 766
Cdd:PRK12767 137 DFKAAlaKGELQFPLFVKPRDGSASIGVFKVNDKEELEFL------LEYVPNLIIQEFIEGQ-EYTVDVLCDlnGEVISI 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084961178 767 AgVMEHIEeagVHSG--DSACSLPSHslppsvlaVVREHTRRLALHLKVRGLINIQYAVKDGAVYVLEANPRASRTVPF 843
Cdd:PRK12767 210 V-PRKRIE---VRAGetSKGVTVKDP--------ELFKLAERLAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPL 276
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
939-1037 |
8.21e-11 |
|
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: 60.22 E-value: 8.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 939 VFVSVRDEDKPVLLHVARALRQMGFTLVATRNTADFLERYGLPTGRVAKIGE-GKPDVVDLLRQRGL-SLVINTPSGKRA 1016
Cdd:cd00532 2 VFLSVSDHVKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRHEdGEPTVDAAIAEKGKfDVVINLRDPRRD 81
|
90 100
....*....|....*....|....
gi 1084961178 1017 RT---DGYSIRRTALELDIPCITN 1037
Cdd:cd00532 82 RCtdeDGTALLRLARLYKIPVTTP 105
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
9-340 |
3.77e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 63.46 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 9 KILVIGSGAIVIgqgcefdysgaQGLKALREEGYETVLINSNPATIMTDPESADRTYI---EPLTPEYL--EKVI-AAER 82
Cdd:PRK08654 4 KILIANRGEIAI-----------RVMRACRELGIKTVAVYSEADKNALFVKYADEAYPigpAPPSKSYLniERIIdVAKK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 83 P--QAVLPTLGgqtalnltvAAAERGVF----KKHGVEVLGANLETIRKAEDRQLFKAAMQKIGLD-LP-RSVVVTDATD 154
Cdd:PRK08654 73 AgaDAIHPGYG---------FLAENPEFakacEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPvLPgTEEGIEDIEE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 155 LKPVARELGFPVIVRASFTLGGTGGGIAYHFDELRhrvhRALEASpvKK----------VLLEESVIGWKEYELEVMRDR 224
Cdd:PRK08654 144 AKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELE----DAIEST--QSiaqsafgdstVFIEKYLEKPRHIEIQILADK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 225 KDNFVVI----CSI----ENLdpmgvhtgdsVTVAPAQTLTDRQYQEMRDEAKRIVSEIGVETGGcNIQFAVDprDGRRV 296
Cdd:PRK08654 218 HGNVIHLgdreCSIqrrhQKL----------IEEAPSPIMTPELRERMGEAAVKAAKAINYENAG-TVEFLYS--NGNFY 284
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1084961178 297 VIEINPRVSRSSALASKATGFPIARIAAKLAVGYALDELPNDIT 340
Cdd:PRK08654 285 FLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELSFKQEDIT 328
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
642-854 |
1.07e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 62.08 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 642 AAQLAKARVPILGTQPAAI----DMAEDRRLfgAALKKLKILSPESGIARTAAQALKIARRIGYPVMVRPSYVLGGRMME 717
Cdd:PRK12833 95 AEAVEAAGLIFVGPDAQTIrtmgDKARARRT--ARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIR 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 718 IVYDDAAL---LDYSERARKASL-HPSLLVDRFLADAAELDVDAVCDGKDVwiagvmehieeagVHSGDSACSL------ 787
Cdd:PRK12833 173 VAHDAAQLaaeLPLAQREAQAAFgDGGVYLERFIARARHIEVQILGDGERV-------------VHLFERECSLqrrrqk 239
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084961178 788 -----PSHSLPPSVLAVVREHTRRLALHLKVRGLINIQYAVKD--GAVYVLEANPRASRTVPFVSKATGLPVAR 854
Cdd:PRK12833 240 ileeaPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDarGEFYFIEMNTRIQVEHPVTEAITGIDLVQ 313
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
110-335 |
2.50e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 60.89 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 110 KHGVEVLGANLETIRKAEDRQLFKAAMQKIGLDL-PRSV-VVTDATDLKPVARELGFPVIVRAsfTLGGTGGGIAYHFD- 186
Cdd:PRK07178 96 ERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVtPGSEgNLADLDEALAEAERIGYPVMLKA--TSGGGGRGIRRCNSr 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 187 -ELRHRVHRAL-EASPV---KKVLLEESVIGWKEYELEVMRDRKDNFVVI----CSIENldpmgvHTGDSVTVAPAQTLT 257
Cdd:PRK07178 174 eELEQNFPRVIsEATKAfgsAEVFLEKCIVNPKHIEVQILADSHGNVVHLferdCSIQR------RNQKLIEIAPSPQLT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 258 DRQYQEMRDEAKRIVSEIGVETGGcNIQFAVDpRDGRRVVIEINPRVSRSSALASKATGFPIA----RIAAKLAVGYALD 333
Cdd:PRK07178 248 PEQRAYIGDLAVRAAKAVGYENAG-TVEFLLD-ADGEVYFMEMNTRVQVEHTITEEITGIDIVreqiRIASGLPLSYKQE 325
|
..
gi 1084961178 334 EL 335
Cdd:PRK07178 326 DI 327
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
121-304 |
1.05e-08 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 58.55 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 121 ETIRKAEDRQLFKAAMQKIGLDLPRSVVVTDATDLKPVARELGFPVIVRASfTLG--GTGGGIAYHFDELRhrvhRALEA 198
Cdd:COG0026 82 EALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTR-RGGydGKGQVVIKSAADLE----AAWAA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 199 SPVKKVLLEESV-IgwkEYELEVM--RDRKDNFVVICSIENldpmgVHTGD--SVTVAPAQtLTDRQYQEMRDEAKRIVS 273
Cdd:COG0026 157 LGGGPCILEEFVpF---ERELSVIvaRSPDGEVATYPVVEN-----VHRNGilDESIAPAR-ISEALAAEAEEIAKRIAE 227
|
170 180 190
....*....|....*....|....*....|.
gi 1084961178 274 EIGVeTGGCNIQFAVDpRDGRRVVIEINPRV 304
Cdd:COG0026 228 ALDY-VGVLAVEFFVT-KDGELLVNEIAPRP 256
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
112-304 |
1.94e-08 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 58.61 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 112 GVEVLGANLETIRKAEDRQLFKAAMQKIGLD-LPRSVV-VTDATDLKPVARELGFPVIVRASftLGGTGGG--IAYHFDE 187
Cdd:PRK12999 103 GITFIGPTAEVLRLLGDKVAARNAAIKAGVPvIPGSEGpIDDIEEALEFAEEIGYPIMLKAS--AGGGGRGmrIVRSEEE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 188 LRHRVHRAL-EA-----SPvkKVLLEESVIGWKEYELEVMRDRKDNFVVI----CS--------IEnldpmgvhtgdsvt 249
Cdd:PRK12999 181 LEEAFERAKrEAkaafgND--EVYLEKYVENPRHIEVQILGDKHGNVVHLyerdCSvqrrhqkvVE-------------- 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1084961178 250 VAPAQTLTDRQYQEMRDEAKRIVSEIGVEtGGCNIQFAVDPrDGRRVVIEINPRV 304
Cdd:PRK12999 245 IAPAPGLSEELRERICEAAVKLARAVGYV-NAGTVEFLVDA-DGNFYFIEVNPRI 297
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
34-327 |
2.40e-08 |
|
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: 56.87 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 34 LKALREEGYETVLINsnpatimtdpesADRTYIEPLTPEYLEKVIAAERPQAVLP-TLGGQTALNLTVAAAERGVFkkhg 112
Cdd:COG0189 20 IEAAQRRGHEVEVID------------PDDLTLDLGRAPELYRGEDLSEFDAVLPrIDPPFYGLALLRQLEAAGVP---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 113 veVLGaNLETIRKAEDRQLFKAAMQKIGLDLPRSVVVTDATDLKPVARELGFPVIVRasfTLGGTGG-GI--AYHFDELR 189
Cdd:COG0189 84 --VVN-DPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLK---PLDGSGGrGVflVEDEDALE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 190 HrVHRALEASPVKKVLLEESVIGWKEYEL--EVMRDRkdnfvVICSIeNLDPMG------VHTGDSVTvapAQTLTDrqy 261
Cdd:COG0189 158 S-ILEALTELGSEPVLVQEFIPEEDGRDIrvLVVGGE-----PVAAI-RRIPAEgefrtnLARGGRAE---PVELTD--- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084961178 262 qEMRDEAKRIVSEIGVETGGcnIQFAVDprDGRRVVIEINPrvsrSSALA--SKATGFPIA-RIAAKLA 327
Cdd:COG0189 225 -EERELALRAAPALGLDFAG--VDLIED--DDGPLVLEVNV----TPGFRglERATGVDIAeAIADYLE 284
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
117-305 |
1.26e-07 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 56.01 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 117 GANLETIRKAEDRQLFKAAMQKIGLDLPRSVVVTDATDLKPVARELGFPVIVRASFTLGGTGGGIAYHFDELRHRVHRAL 196
Cdd:PRK02186 96 AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALR 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 197 EASpVKKVLLEESVIGwKEYELEVMRDRKDNFVVICSIENLDPMGvHTGDSVTVAPAQtLTDRQYQEMRDEAKRIVSEIG 276
Cdd:PRK02186 176 RAG-TRAALVQAYVEG-DEYSVETLTVARGHQVLGITRKHLGPPP-HFVEIGHDFPAP-LSAPQRERIVRTVLRALDAVG 251
|
170 180
....*....|....*....|....*....
gi 1084961178 277 VETGGCNIQFAVdpRDGRRVVIEINPRVS 305
Cdd:PRK02186 252 YAFGPAHTELRV--RGDTVVIIEINPRLA 278
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
119-304 |
1.60e-07 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 54.77 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 119 NLETIRKAEDRQLFKAAMQKIGLDLPRSVVVTDATDLKPVARELGFPVIVRASfTLG--GTGGGIAYHFDELRHrVHRAL 196
Cdd:PRK06019 91 GPDALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTR-RGGydGKGQWVIRSAEDLEA-AWALL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 197 EASPvkkVLLEESV-IgwkEYELEVM--RDRKDNFVVICSIENldpmgVHTGD--SVTVAPAQtLTDRQYQEMRDEAKRI 271
Cdd:PRK06019 169 GSVP---CILEEFVpF---EREVSVIvaRGRDGEVVFYPLVEN-----VHRNGilRTSIAPAR-ISAELQAQAEEIASRI 236
|
170 180 190
....*....|....*....|....*....|....*....
gi 1084961178 272 VSE---IGVetggcniqFAV---DPRDGRRVVIEINPRV 304
Cdd:PRK06019 237 AEEldyVGV--------LAVeffVTGDGELLVNEIAPRP 267
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
7-339 |
2.39e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 54.72 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 7 IQKILVIGSGAIVIgqgcefdysgaQGLKALREEGYETVLINSNpatimTDPES-----ADRTY-IEPLTPE--YL--EK 76
Cdd:PRK05586 2 FKKILIANRGEIAV-----------RIIRACREMGIETVAVYSE-----ADKDAlhvqlADEAVcIGPASSKdsYLniQN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 77 VIAA---ERPQAVLPTLGgqtalnltvAAAERGVF----KKHGVEVLGANLETIRKAEDRQLFKAAMQKIGLDL-PRSV- 147
Cdd:PRK05586 66 IISAtvlTGAQAIHPGFG---------FLSENSKFakmcKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVvPGSEg 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 148 VVTDATDLKPVARELGFPVIVRASFTLGGTGGGIAYHFDELRHRVHRA-LEASPV---KKVLLEESVIGWKEYELEVMRD 223
Cdd:PRK05586 137 EIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAkSEAKAAfgdDSMYIEKFIENPKHIEFQILGD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 224 RKDNFVVI----CSIENLDPMGVHTgdsvtvAPAQTLTDRQYQEMRDEAKRIVSEIGVETGGcNIQFAVDpRDGRRVVIE 299
Cdd:PRK05586 217 NYGNVVHLgerdCSLQRRNQKVLEE------APSPVMTEELRKKMGEIAVKAAKAVNYKNAG-TIEFLLD-KDGNFYFME 288
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1084961178 300 INPRVSRSSALASKATGFPIARIAAKLAVGYALDELPNDI 339
Cdd:PRK05586 289 MNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLSIKQEDI 328
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
642-918 |
3.37e-07 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 54.47 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 642 AAQLAKaRVPILGTQPAAIDMAEDRRLFGAALKKLKILSPESGIARTAAQALKIARRIGYPVMVRPSYVLGGRMMEIVYD 721
Cdd:PRK02186 85 ASEVAR-RLGLPAANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCAS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 722 DAALLDYSERARKAsLHPSLLVDRFLaDAAELDVDAVCDGKDVWIAGVMEHIEEAGVHSGDSACSLPSHSLPPSVLAVVR 801
Cdd:PRK02186 164 VAEAAAHCAALRRA-GTRAALVQAYV-EGDEYSVETLTVARGHQVLGITRKHLGPPPHFVEIGHDFPAPLSAPQRERIVR 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 802 EHTRRL-ALHLKVrGLINIQYAVKDGAVYVLEANPR-ASRTVP-FVSKATGLPVAR--IATWVMMGKTlkkLVPPAALKG 876
Cdd:PRK02186 242 TVLRALdAVGYAF-GPAHTELRVRGDTVVIIEINPRlAGGMIPvLLEEAFGVDLLDhvIDLHLGVAAF---ADPTAKRYG 317
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1084961178 877 AEPPYTATKEAVMPFIKFPGVDPRLGPE-----MKSTGEVMGLDADF 918
Cdd:PRK02186 318 AIRFVLPARSGVLRGLLFLPDDIAARPElrfhpLKQPGDALRLEGDF 364
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
149-304 |
4.00e-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: 54.32 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 149 VTDATDLKPVARELGFPVIVRASftLGGTGGG--IAYHFDELRHRVHRAL-EAspvKK------VLLEESVIGWKEYELE 219
Cdd:COG1038 141 VDDLEEALAFAEEIGYPVMLKAA--AGGGGRGmrVVRSEEELEEAFESARrEA---KAafgddeVFLEKYIERPKHIEVQ 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 220 VMRDRKDNFVVI----CS--------IEnldpmgvhtgdsvtVAPAQTLTDRQYQEMRDEAKRIVSEIG------VEtgg 281
Cdd:COG1038 216 ILGDKHGNIVHLferdCSvqrrhqkvVE--------------IAPAPNLDEELREAICEAAVKLAKAVGyvnagtVE--- 278
|
170 180
....*....|....*....|...
gi 1084961178 282 cniqFAVDpRDGRRVVIEINPRV 304
Cdd:COG1038 279 ----FLVD-DDGNFYFIEVNPRI 296
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
684-836 |
1.31e-06 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 52.33 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 684 GIARTAAQALKIARRIGYPVMVRPSYVLGGRMMEIVYDDAALLDYSERAR---KASLH-PSLLVDRFLADAAELDVDAVC 759
Cdd:COG4770 136 GPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARreaKAAFGdDRVYLEKYIERPRHIEVQVLA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 760 DGK-DVWIAGVME------H---IEEAgvhsgdsacslPSHSLPPSVLAVVREHTRRLALHLKVRGLINIQYAV-KDGAV 828
Cdd:COG4770 216 DKHgNVVHLGERDcsiqrrHqkvIEEA-----------PSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVdADGNF 284
|
....*...
gi 1084961178 829 YVLEANPR 836
Cdd:COG4770 285 YFLEMNTR 292
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
684-850 |
1.48e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 52.02 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 684 GIARTAAQALKIARRIGYPVMVRPSYVLGGRMMEIVYDDAALLDYSERARKASL----HPSLLVDRFLADAAELDVDAVC 759
Cdd:PRK05586 136 GEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKaafgDDSMYIEKFIENPKHIEFQILG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 760 DGkdvwiagvMEHIeeagVHSGDSACSLPSHS---LPPSVLAVVREHTRR----------LALHLKVRGLINIQYAvKDG 826
Cdd:PRK05586 216 DN--------YGNV----VHLGERDCSLQRRNqkvLEEAPSPVMTEELRKkmgeiavkaaKAVNYKNAGTIEFLLD-KDG 282
|
170 180
....*....|....*....|....
gi 1084961178 827 AVYVLEANPRASRTVPFVSKATGL 850
Cdd:PRK05586 283 NFYFMEMNTRIQVEHPITEMITGV 306
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
34-339 |
4.27e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 50.41 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 34 LKALREEGYETVLINSNpatimTDPES-----ADRTYI---EPLTPEYL--EKVIAAER---PQAVLPTLGgqtALNLTV 100
Cdd:PRK06111 18 IRTCQKLGIRTVAIYSE-----ADRDAlhvkmADEAYLiggPRVQESYLnlEKIIEIAKktgAEAIHPGYG---LLSENA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 101 AAAERgvFKKHGVEVLGANLETIRKAEDRQLFKAAMQKIGLD-LP-RSVVVTDATDLKPVARELGFPVIVRASFTLGGTG 178
Cdd:PRK06111 90 SFAER--CKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPvVPgITTNLEDAEEAIAIARQIGYPVMLKASAGGGGIG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 179 GGIAYHFDELRhrvhRALEASPVK--------KVLLEESVIGWKEYELEVMRDRKDNFVVI----CSIENldpmgvHTGD 246
Cdd:PRK06111 168 MQLVETEQELT----KAFESNKKRaanffgngEMYIEKYIEDPRHIEIQLLADTHGNTVYLwereCSVQR------RHQK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 247 SVTVAPAQTLTDRQYQEMRDEAKRIVSEIGVETGGcNIQFAVDPrDGRRVVIEINPRVSRSSALASKATGFPIARIAAKL 326
Cdd:PRK06111 238 VIEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAG-TIEFLVDE-QKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRI 315
|
330
....*....|...
gi 1084961178 327 AVGYALDELPNDI 339
Cdd:PRK06111 316 AAGEKLSFTQDDI 328
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
111-304 |
6.37e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 49.80 E-value: 6.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 111 HGVEVLGANLETIRKAEDRQLFKAAMQKIGLDL-PRSV-VVTDATDLKPVARELGFPVIVRAsfTLGGTGGGI--AYHFD 186
Cdd:PRK08591 98 SGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVvPGSDgPVDDEEEALAIAKEIGYPVIIKA--TAGGGGRGMrvVRTEA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 187 ELRHRVHRA-LEASPV---KKVLLEESVIGWKEYELEVMRDRKDNFVVI----CSI---------Enldpmgvhtgdsvt 249
Cdd:PRK08591 176 ELEKAFSMArAEAKAAfgnPGVYMEKYLENPRHIEIQVLADGHGNAIHLgerdCSLqrrhqkvleE-------------- 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1084961178 250 vAPAQTLTDRQYQEMRDEAKRIVSEIGVETGGcNIQFAVDpRDGRRVVIEINPRV 304
Cdd:PRK08591 242 -APSPAITEELRRKIGEAAVKAAKAIGYRGAG-TIEFLYE-KNGEFYFIEMNTRI 293
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
1-339 |
1.39e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 48.98 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 1 MPKRddIQKILVIGSGAIVIgqgcefdysgaQGLKALREEGYETVL------INSNPA-----TIMTDPESADRTYIEPl 69
Cdd:PRK12833 1 MPSR--IRKVLVANRGEIAV-----------RIIRAARELGMRTVAacsdadRDSLAArmadeAVHIGPSHAAKSYLNP- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 70 tpeylEKVIAAER---PQAVLPTLGGqTALNLTVAAAergvFKKHGVEVLGANLETIR----KAEDRQLFKAAMQKIgld 142
Cdd:PRK12833 67 -----AAILAAARqcgADAIHPGYGF-LSENAAFAEA----VEAAGLIFVGPDAQTIRtmgdKARARRTARRAGVPT--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 143 LPRSV-VVTDATDLKPVARELGFPVIVRASFTLGGTGGGIAYHFDELRHRVHRA-LEASPV---KKVLLEESVIGWKEYE 217
Cdd:PRK12833 134 VPGSDgVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAELPLAqREAQAAfgdGGVYLERFIARARHIE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 218 LEVMRDRKDN---FVVICSIENldpmgvHTGDSVTVAPAQTLTDRQYQEMRDEAKRIVSEIGVETGGcNIQFAVDPRDGR 294
Cdd:PRK12833 214 VQILGDGERVvhlFERECSLQR------RRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAG-TLEYLFDDARGE 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1084961178 295 RVVIEINPRVSRSSALASKATGFPIARIAAKLAVGYALDELPNDI 339
Cdd:PRK12833 287 FYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLRFAQGDI 331
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
112-339 |
1.44e-05 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 49.04 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 112 GVEVLGANLETIRKAEDRQLFKAAMQKIGLDL-PRSVVVTDAT--DLKPVARELGFPVIVRASFtlGGTGGGIAYHFDEl 188
Cdd:PRK08463 98 GIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIvPGTEKLNSESmeEIKIFARKIGYPVILKASG--GGGGRGIRVVHKE- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 189 rHRVHRALEASPVK--------KVLLEESVIGWKEYELEVMRDRKDNFVVI----CSIENldpmgvHTGDSVTVAPAQTL 256
Cdd:PRK08463 175 -EDLENAFESCKREalayfnndEVFMEKYVVNPRHIEFQILGDNYGNIIHLcerdCSIQR------RHQKVIEIAPCPSI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 257 TDRQYQEMRDEAKRIVSEIGVETGGcNIQFAVDPRDgRRVVIEINPRVSRSSALASKATGFPIARIAAKLAVGYALDELP 336
Cdd:PRK08463 248 SDNLRKTMGVTAVAAAKAVGYTNAG-TIEFLLDDYN-RFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEILDLEQ 325
|
...
gi 1084961178 337 NDI 339
Cdd:PRK08463 326 SDI 328
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
133-235 |
3.12e-05 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 46.10 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 133 KAAMQKIGLDLPRSVVVTDATDLKPVARELGFPVIV-RASFTLGGTG--GGI--AYHFDELRHRVHRAL----------- 196
Cdd:pfam08442 8 KEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYVvKAQVLAGGRGkaGGVklAKSPEEAKEVAKEMLgknlvtkqtgp 87
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1084961178 197 EASPVKKVLLEESVIGWKEYELEVMRDRKDN-FVVICSIE 235
Cdd:pfam08442 88 DGQPVNKVLVEEALDIKKEYYLSIVLDRASKgPVIIASTE 127
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
109-332 |
3.89e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 47.43 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 109 KKHGVEVLGANLETIRKAEDRQLFKAAMQKIGLD-LPRSV-VVTDATDLKPVARELGFPVIVRASFTLGGTGGGIAYHFD 186
Cdd:PRK08462 98 SHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPvIPGSDgALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDES 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 187 ELRHRV----HRALEASPVKKVLLEESVIGWKEYELEVMRDRKDNFVVI----CSIENldpmgvHTGDSVTVAPAQTLTD 258
Cdd:PRK08462 178 DLENLYlaaeSEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAVVLDE 251
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084961178 259 RQYQEMRDEAKRIVSEIGVETGGcNIQFAVDpRDGRRVVIEINPRVSRSSALASKATGFPIARIAAKLAVGYAL 332
Cdd:PRK08462 252 KTRERLHETAIKAAKAIGYEGAG-TFEFLLD-SNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL 323
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
654-725 |
4.37e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 47.10 E-value: 4.37e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084961178 654 GTQPAAIDMAEDRRLFGAALKKLKI-LSPES-GIARTAAQALKIARRIGYPVMVRPSYVLGGRMMEIVYDDAAL 725
Cdd:PRK08591 104 GPSAETIRLMGDKVTAKATMKKAGVpVVPGSdGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAEL 177
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
686-836 |
4.93e-05 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 47.44 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 686 ARTAAQALKIARRIGYPVMVRPSYVLGGRMMEIVYDDAALLDYSERAR---KASL-HPSLLVDRFLADAaeldvdavcdg 761
Cdd:PRK12999 142 IDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKreaKAAFgNDEVYLEKYVENP----------- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 762 kdvwiagvmEHIE------EAG--VHSGDSACSL-----------PSHSLPPSVLAVVREHTRRLALHLKVRGLINIQYA 822
Cdd:PRK12999 211 ---------RHIEvqilgdKHGnvVHLYERDCSVqrrhqkvveiaPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFL 281
|
170
....*....|....*
gi 1084961178 823 V-KDGAVYVLEANPR 836
Cdd:PRK12999 282 VdADGNFYFIEVNPR 296
|
|
| LysX_arch |
TIGR02144 |
Lysine biosynthesis enzyme LysX; The family of proteins found in this equivalog include the ... |
657-730 |
7.02e-05 |
|
Lysine biosynthesis enzyme LysX; The family of proteins found in this equivalog include the characterized LysX from Thermus thermophilus, which is part of a well-organized lysine biosynthesis gene cluster. LysX is believed to carry out an ATP-dependent acylation of the amino group of alpha-aminoadipate in the prokaryotic version of the fungal AAA lysine biosynthesis pathway. No species having a sequence in this equivalog contains the elements of the more common diaminopimelate lysine biosythesis pathway, and none has been shown to be a lysine auxotroph. These sequences have mainly recieved the name of the related enzyme, "ribosomal protein S6 modification protein RimK". RimK has been characterized in E. coli, and acts by ATP-dependent condensation of S6 with glutamate residues.
Pssm-ID: 273994 [Multi-domain] Cd Length: 280 Bit Score: 45.85 E-value: 7.02e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084961178 657 PAAIDMAEDRRLFGAALKKLKILSPESGIARTAAQALKIARRIGYPVMVRPSYVLGGRMMEIVYDDAALLDYSE 730
Cdd:TIGR02144 79 SHAIEACGDKIFTYLKLAKAGVPTPRTYLAFDREAALKAAEALGYPVVLKPVIGSWGRLVAKVRDRDEAEALLE 152
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
687-733 |
9.36e-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: 9.36e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1084961178 687 RTAAQALKIARRIGYPVMVRPSYVLGGRMMEIVYDDAALLDYSERAR 733
Cdd:COG1038 142 DDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESAR 188
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
619-855 |
2.67e-04 |
|
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: 44.52 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 619 EIIDVEKPDGVIVQFGGQTPLNLAAQLAkARVPILGTQPAAIDMAEDRRLFGAALKKLKILSPESgiartaaqaLKIARR 698
Cdd:COG2232 67 ELAAADDPDGLVYGSGFENFPELLERLA-RRLPLLGNPPEVVRRVKDPLRFFALLDELGIPHPET---------RFEPPP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 699 IGYPVMVRPSYVLGGRmmeivyddaalldyseRARKASLHPSLLVDRFLADAAE---LDVDAVCDGKDVWIAGVME-HIE 774
Cdd:COG2232 137 DPGPWLVKPIGGAGGW----------------HIRPADSEAPPAPGRYFQRYVEgtpASVLFLADGSDARVLGFNRqLIG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 775 EAGVH----SGdsaCSLPSHsLPPSVLAVVREHTRRLALHLKVRGLINIQYAVKDGAVYVLEANPRASRTVPFVSKATGL 850
Cdd:COG2232 201 PAGERpfryGG---NIGPLA-LPPALAEEMRAIAEALVAALGLVGLNGVDFILDGDGPYVLEVNPRPQASLDLYEDATGG 276
|
....*
gi 1084961178 851 PVARI 855
Cdd:COG2232 277 NLFDA 281
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
29-301 |
3.27e-04 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 43.95 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 29 SGAQGLKALREEGYETVLINsnpatimTDPESADRtyiepltpeylekvIAAERPQAVLPTLGG--------QTALNL-- 98
Cdd:PRK01372 24 SGAAVLAALREAGYDAHPID-------PGEDIAAQ--------------LKELGFDRVFNALHGrggedgtiQGLLELlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 99 ---TvaaaergvfkkhGVEVLGANLeTIRKAEDRQLFKAAmqkiGLDLPRSVVVTDATDLKPVARELGFPVIVRASftLG 175
Cdd:PRK01372 83 ipyT------------GSGVLASAL-AMDKLRTKLVWQAA----GLPTPPWIVLTREEDLLAAIDKLGLPLVVKPA--RE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 176 GTGGGIAYHFDELRHRVHRALEASPVKKVLLEESVIGwKEYELEVMRDRkdnfvVICSIEnLDPMGV--------HTGDS 247
Cdd:PRK01372 144 GSSVGVSKVKEEDELQAALELAFKYDDEVLVEKYIKG-RELTVAVLGGK-----ALPVIE-IVPAGEfydyeakyLAGGT 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1084961178 248 VTVAPAQtLTDRQYQEMRDEAKRIVSEIGVEtGGCNIQFAVDpRDGRRVVIEIN 301
Cdd:PRK01372 217 QYICPAG-LPAEIEAELQELALKAYRALGCR-GWGRVDFMLD-EDGKPYLLEVN 267
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
690-835 |
7.10e-04 |
|
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: 42.79 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 690 AQALKIARRIGYPVMVRP-----SyvLGgrmMEIVYDDAALLDYSERARKasLHPSLLVDRFLaDAAELDVdAVCDGKDV 764
Cdd:COG1181 122 ADLEAIEEELGLPLFVKParegsS--VG---VSKVKNAEELAAALEEAFK--YDDKVLVEEFI-DGREVTV-GVLGNGGP 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084961178 765 WIAGVMEHIEEAGV-------HSGDSACSLPShSLPPSVLAVVREHTRRLALHLKVRGLINIQYAV-KDGAVYVLEANP 835
Cdd:COG1181 193 RALPPIEIVPENGFydyeakyTDGGTEYICPA-RLPEELEERIQELALKAFRALGCRGYARVDFRLdEDGEPYLLEVNT 270
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
691-734 |
8.65e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 43.05 E-value: 8.65e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1084961178 691 QALKIARRIGYPVMVRPSYVLGGRMMEIVYDDAALLDYSERARK 734
Cdd:PRK08654 143 EAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIESTQS 186
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
610-855 |
1.18e-03 |
|
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: 41.95 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 610 EPLTFEDVMEIIdvEKPDGVIVQF-GGQTPLNLAAQLAKARVPILgTQPAAIDMAEDRRLFGAALKKLKILSPESGIART 688
Cdd:TIGR00768 35 INLTFNEGPRAL--AELDVVIVRIvSMFRGLAVLRYLESLGVPVI-NSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 689 AAQALKIARRIGYPVMVRPSYVLGGRMMEIVYDDAALLDYSERARK-ASLHPSLLVDRFLADAAELDVDAVCDGKDVwiA 767
Cdd:TIGR00768 112 PEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQAAESLLEHFEQlNGPQNLFLVQEYIKKPGGRDIRVFVVGDEV--V 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 768 GVMEHIEEAG----VHSGDSA--CSLpshslppsvlavvREHTRRLAlhLKVRGLINIQYA------VKDGAVyVLEANP 835
Cdd:TIGR00768 190 AAIYRITSGHwrsnLARGGKAepCSL-------------TEEIEELA--IKAAKALGLDVAgvdlleSEDGLL-VNEVNA 253
|
250 260
....*....|....*....|..
gi 1084961178 836 rasrTVPF--VSKATGLPVARI 855
Cdd:TIGR00768 254 ----NPEFknSVKTTGVNIAGK 271
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
663-836 |
3.42e-03 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 39.29 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 663 AEDRRLFGAALKKLKILSPEsgiarTAAQAlkIARRIGYPVMVRPSYVLGGrmmeivydDAALLDYSERARKASLHPsLL 742
Cdd:pfam02655 1 ASDKLKTYKALKNAGVPTPE-----TLQAE--ELLREEKKYVVKPRDGCGG--------EGVRKVENGREDEAFIEN-VL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084961178 743 VDRFLaDAAELDVDAVCDGKDVWIAGV-MEHIEEAGVHSGDSACSLPS-HSLPPSVLAVVREHTRRLAlhlKVRGLINIQ 820
Cdd:pfam02655 65 VQEFI-EGEPLSVSLLSDGEKALPLSVnRQYIDNGGSGFVYAGNVTPSrTELKEEIIELAEEVVECLP---GLRGYVGVD 140
|
170
....*....|....*.
gi 1084961178 821 YAVKDGAVYVLEANPR 836
Cdd:pfam02655 141 LVLKDNEPYVIEVNPR 156
|
|
| |
