|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
346-1276 |
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: 1517.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 346 PKKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADMVYFLPLTPEYVEQVIKSERPNGV 425
Cdd:TIGR01369 6 IKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPDAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 426 LLTFGGQTALNCGVELEKTGIFKKYNVKVMGTPIQSIIETEDRKIFSDRVAEIGEKVAPSVAVYSIRQALDAAEKLEYPV 505
Cdd:TIGR01369 86 LPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYPV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 506 MARAAFSLGGLGSGFANNKEELEVLAKQALAHS--NQLIIDKSLRGWKEVEYEVVRDAYDNCITVCNMENLDPLGIHTGE 583
Cdd:TIGR01369 166 IVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHTGD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 584 SIVVAPSQTLSNREYNMLRTTAIKVIRHFGVIGECNIQYALNPESDQYYIIEVNARLSRSSALASKATGYPLAYVAAKLS 663
Cdd:TIGR01369 246 SIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 664 LAIPLPSIKNSVTGVTTACFEPSLDYCVVKMPRWDLAKFVRVSKTIGSSMKSVGEVMAIGRNFEEAFQKALRMVDENVNG 743
Cdd:TIGR01369 326 VGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 744 FDPYIKPVK-----EEELIEATDKRMFVLAAAIKANYTIEKLYQLTKIDPWFLNKMKNIID-YMNLLESRGNNLNRTVLL 817
Cdd:TIGR01369 406 FDLPDREVEpdedlWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDlEEELEEVKLTDLDPELLR 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 818 EAKKLGFSDRQIASAIKSTDLVVRHEREELNVVPFVKQIDTVAGEWPASTNYLYLTYNATSHDIEFLGNFTIVV-GSGVY 896
Cdd:TIGR01369 486 RAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKKKVLVlGSGPN 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 897 RIGSSVEFDWCAVGCLRELRKLGRQTIMINYNPETVSTDYDMCDRLYFEEISLETVMDIYQIENADGIILSMGGQLPNNI 976
Cdd:TIGR01369 566 RIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPLNL 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 977 AMDLHRQQARVLGTSPDSIDNAENRFKFSRMLDRKGILQPRWKELTDLKAAIEFCEEVGYPCLVRPSYVLSGAAMNVAYS 1056
Cdd:TIGR01369 646 AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYN 725
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1057 NQDLETYLNAASLVSKEYPVVISKFLQEAKEIDVDAVAADGEILCMAVSEHVENAGVHSGDATLVTPPQDINAETLLKIK 1136
Cdd:TIGR01369 726 EEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDRIK 805
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1137 EIARDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAVIGMPVEPVEVL--HGCGKVGV 1214
Cdd:TIGR01369 806 DIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGVGkeKEPKYVAV 885
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 86450111 1215 KVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMMSTGFQIPKKAILLSIGSFK 1276
Cdd:TIGR01369 886 KEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDK 947
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
347-1272 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1319.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 347 KKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADMVYFLPLTPEYVEQVIKSERPNGVL 426
Cdd:PRK05294 8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 427 LTFGGQTALNCGVELEKTGIFKKYNVKVMGTPIQSIIETEDRKIFSDRVAEIGEKVAPSVAVYSIRQALDAAEKLEYPVM 506
Cdd:PRK05294 88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 507 ARAAFSLGGLGSGFANNKEELEVLAKQALAHS--NQLIIDKSLRGWKEVEYEVVRDAYDNCITVCNMENLDPLGIHTGES 584
Cdd:PRK05294 168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLSpvTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 585 IVVAPSQTLSNREYNMLRTTAIKVIRHFGVI-GECNIQYALNPESDQYYIIEVNARLSRSSALASKATGYPLAYVAAKLS 663
Cdd:PRK05294 248 ITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 664 LAIPLPSIKNSVTGVTTACFEPSLDYCVVKMPRWDLAKFVRVSKTIGSSMKSVGEVMAIGRNFEEAFQKALRMVDENVNG 743
Cdd:PRK05294 328 VGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 744 FDPYIKPVK-----EEELIEATDKRMFVLAAAIKANYTIEKLYQLTKIDPWFLNKMKNIIDYMNLLESRGNNLNRTVLLE 818
Cdd:PRK05294 408 LDEDLFEEEsleelREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLPLDAELLRE 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 819 AKKLGFSDRQIASAIKSTDLVVRHEREELNVVPFVKQIDTVAGEWPASTNYLYLTYNATSHDIEFLGNFTIVVGSGVYRI 898
Cdd:PRK05294 488 AKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVLGSGPNRI 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 899 GSSVEFDWCAVGCLRELRKLGRQTIMINYNPETVSTDYDMCDRLYFEEISLETVMDIYQIENADGIILSMGGQLPNNIAM 978
Cdd:PRK05294 568 GQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPLKLAK 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 979 DLHRQQARVLGTSPDSIDNAENRFKFSRMLDRKGILQPRWKELTDLKAAIEFCEEVGYPCLVRPSYVLSGAAMNVAYSNQ 1058
Cdd:PRK05294 648 ALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDEE 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1059 DLETYLNAASLVSKEYPVVISKFLQEAKEIDVDAVaADGE-ILCMAVSEHVENAGVHSGDATLVTPPQDINAETLLKIKE 1137
Cdd:PRK05294 728 ELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAI-CDGEdVLIGGIMEHIEEAGVHSGDSACSLPPQTLSEEIIEEIRE 806
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1138 IARDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAVIGMPVEPVEVLHGC--GKVGVK 1215
Cdd:PRK05294 807 YTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGLipPYVAVK 886
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*...
gi 86450111 1216 VPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMMSTGFQIPKK-AILLSI 1272
Cdd:PRK05294 887 EAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSV 944
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
352-893 |
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: 642.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 352 LGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADMVYFLPLTPEYVEQVIKSERPNGVLLTFGG 431
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 432 QTALNCGVELEKTGIFKkyNVKVMGTPIQSIIETEDRKIFSDRVAEIGEKVAPSVAVYSIRQALDAAEKLEYPVMARAAF 511
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 512 SLGGLGSGFANNKEELEVLAKQALAHS--NQLIIDKSLRGWKEVEYEVVRDAYDNCITVCNMENLDPLGIHTGESIVVAP 589
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSpdHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 590 SQTLSNREYNMLRTTAIKVIRHFGVIGECNIQYALNpeSDQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLAIPLP 669
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 670 SIKNSvTGvttacFEPSLDYCVVKMPRWDLAKFVRVSKTIGSSMKSVGEVMAIGRNFEEAFQKALRMVDENVNG--FDPY 747
Cdd:COG0458 317 ELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLLSL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 748 IKPVKEEE--LIEATDKRMFVLAAAIKANYTIEKLYQLTKIDPWFLNKMKNIIDymNLLESRGNNLNRTVLLEAKKLGFS 825
Cdd:COG0458 391 VADDDKEEalLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIV--DEIELEEIILVINTLLGAKSLGDS 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86450111 826 DRQIASAIKSTDLVVRHEREELNVVPFVKQIDTVAGEWPASTNYLYLTYNATSHDIEFLGNFTIVVGS 893
Cdd:COG0458 469 DGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
1-312 |
2.18e-130 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 404.46 E-value: 2.18e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1 QILVLTYPLIGNYGVPSEKeldefglpkhFEwSSGISVAGLVVGELCTTPSHWRQTKTLSKWMEIEGVPGISDIDTRELT 80
Cdd:PRK12564 51 QIVTFTYPLIGNYGVNRED----------FE-SDRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 81 KKIRENGTVLGRITYNLPNP---KDDLKLTdPNL--RNLVAECSVIKPVVY---NPKGWPKICAIDCGLKLNQIRCFVAR 152
Cdd:PRK12564 120 RKLREKGAMKGVIATEDFDAeelLEKARAF-PGLlgLDLVKEVSTKEPYPWpgpGGELKYKVVAIDFGVKRNILRELAER 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 153 GARVELVPWNHS------LNPnefDGLFISNGPGDPVVCKNTVIEIQKVLKSsDKPIFGICLGHQLLSTAIGCKTFKMKY 226
Cdd:PRK12564 199 GCRVTVVPATTTaeeilaLNP---DGVFLSNGPGDPAALDYAIEMIRELLEK-KIPIFGICLGHQLLALALGAKTYKMKF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 227 GNRGHNLPCIHHGTGRCFMTSQNHGFAVESSTLPSDWEPLFTNANDNTNEGIIHKTKPYLSVQFHPEHTAGPEDLEMLFD 306
Cdd:PRK12564 275 GHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFD 354
|
....*.
gi 86450111 307 IFLETI 312
Cdd:PRK12564 355 EFVELM 360
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
1-314 |
6.48e-127 |
|
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273580 [Multi-domain] Cd Length: 357 Bit Score: 395.07 E-value: 6.48e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1 QILVLTYPLIGNYGVPsekeldefglPKHFEwSSGISVAGLVVGELCTTPSHWRQTKTLSKWMEIEGVPGISDIDTRELT 80
Cdd:TIGR01368 47 QIVVFTYPLIGNYGVN----------DEDAE-SKGIHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 81 KKIRENGTVLGRITYNLPNPKDDLKLT--DPNLR--NLVAECSVIKPVVYNPKGWP--KICAIDCGLKLNQIRCFVARGA 154
Cdd:TIGR01368 116 KKIREKGTMKGVISTEDSNDEELVEKArvSPDITgiNLVAEVSTKEPYTWGQRGGKgkRVVVIDFGVKRNILRRLVKRGC 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 155 RVELVPWNHS------LNPnefDGLFISNGPGDPVVCKNTVIEIQKVLksSDKPIFGICLGHQLLSTAIGCKTFKMKYGN 228
Cdd:TIGR01368 196 EVTVVPYDTDaeeikkYNP---DGIFLSNGPGDPAAVEPAIETIRKLL--EKIPIFGICLGHQLLALAFGAKTYKMKFGH 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 229 RGHNLPCIHHGTGRCFMTSQNHGFAVESSTLPS-DWEPLFTNANDNTNEGIIHKTKPYLSVQFHPEHTAGPEDLEMLFDI 307
Cdd:TIGR01368 271 RGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAgDLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDE 350
|
....*..
gi 86450111 308 FLETIKD 314
Cdd:TIGR01368 351 FIDLMKK 357
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
1-313 |
1.53e-124 |
|
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 388.99 E-value: 1.53e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1 QILVLTYPLIGNYGVPSEkeldefglpkHFEwSSGISVAGLVVGELCTTPSHWRQTKTLSKWMEIEGVPGISDIDTRELT 80
Cdd:COG0505 51 QIVTFTYPHIGNYGVNDE----------DFE-SDRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 81 KKIRENGTVLGRITYNLPNPKDDLKL----TDPNLRNLVAECSVIKPVVY--NPKGWPKICAIDCGLKLNQIRCFVARGA 154
Cdd:COG0505 120 RHLREKGAMKGVISTGDLDIEELLEKaraaPGMEGLDLVKEVSTKEPYEWteAPGAGFHVVALDFGVKRNILRELAERGC 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 155 RVELVPWNHS------LNPnefDGLFISNGPGDPVVCKNTVIEIQKVLKSsDKPIFGICLGHQLLSTAIGCKTFKMKYGN 228
Cdd:COG0505 200 RVTVVPATTSaeeilaLNP---DGVFLSNGPGDPAALDYAIETIRELLGK-GIPIFGICLGHQLLALALGAKTYKLKFGH 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 229 RGHNLPCIHHGTGRCFMTSQNHGFAVESSTLP-SDWEPLFTNANDNTNEGIIHKTKPYLSVQFHPEHTAGPEDLEMLFDI 307
Cdd:COG0505 276 RGANHPVKDLETGRVEITSQNHGFAVDEDSLPaTDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDR 355
|
....*.
gi 86450111 308 FLETIK 313
Cdd:COG0505 356 FIELME 361
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
467-669 |
2.20e-95 |
|
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: 304.23 E-value: 2.20e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 467 DRKIFSDRVAEIGEKVAPSVAVY--SIRQALDAAEKLEYPVMARAAFSLGGLGSGFANNKEELEVLAKQALAHS------ 538
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 539 NQLIIDKSLRGWKEVEYEVVRDAYDNCITVCNMENLDPLgiHTGESIVVAPSQTLSNREYNMLRTTAIKVIRHFGVIGEC 618
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 86450111 619 NIQYALNPESDQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLAIPLP 669
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
134-309 |
1.07e-94 |
|
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.
Pssm-ID: 153215 [Multi-domain] Cd Length: 178 Bit Score: 300.95 E-value: 1.07e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 134 ICAIDCGLKLNQIRCFVARGARVELVPWNHSLNPN---EFDGLFISNGPGDPVVCKNTVIEIQKVLKSsDKPIFGICLGH 210
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEIlklDPDGIFLSNGPGDPALLDEAIKTVRKLLGK-KIPIFGICLGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 211 QLLSTAIGCKTFKMKYGNRGHNLPCIHHGTGRCFMTSQNHGFAVESSTLPSDWEPLFTNANDNTNEGIIHKTKPYLSVQF 290
Cdd:cd01744 80 QLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159
|
170
....*....|....*....
gi 86450111 291 HPEHTAGPEDLEMLFDIFL 309
Cdd:cd01744 160 HPEASPGPHDTEYLFDEFL 178
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
137-310 |
1.56e-59 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 202.47 E-value: 1.56e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 137 IDCGL--KLNQIRCFVARGARVELVPWNHSLN---PNEFDGLFISNGPGDPVVCKNTVIEIQKVLKSsDKPIFGICLGHQ 211
Cdd:pfam00117 3 IDNGDsfTYNLARALRELGVEVTVVPNDTPAEeilEENPDGIILSGGPGSPGAAGGAIEAIREAREL-KIPILGICLGHQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 212 LLSTAIGCKTFKMK-YGNRGHNLPCIH------HGTGRCFMTSQNHGFAVESSTLPSDWEPLFTNANDNTNEGIIHKTKP 284
Cdd:pfam00117 82 LLALAFGGKVVKAKkFGHHGKNSPVGDdgcglfYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKLP 161
|
170 180
....*....|....*....|....*.
gi 86450111 285 YLSVQFHPEHTAGPEDLEMLFDIFLE 310
Cdd:pfam00117 162 IFGVQFHPESILTPHGPEILFNFFIK 187
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
753-874 |
3.59e-52 |
|
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: 178.80 E-value: 3.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 753 EEELIEATDKRMFVLAAAIKANYTIEKLYQLTKIDPWFLNKMKNIIDYMNLLESRG-NNLNRTVLLEAKKLGFSDRQIAS 831
Cdd:smart01096 2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGlDELDADLLRKAKRLGFSDRQIAK 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 86450111 832 AIKSTDLVVRHEREELNVVPFVKQIDTVAGEWPASTNYLYLTY 874
Cdd:smart01096 82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-93 |
1.23e-37 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses 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 synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.
Pssm-ID: 198165 [Multi-domain] Cd Length: 130 Bit Score: 137.51 E-value: 1.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1 QILVLTYPLIGNYGVPSEKeldefglpkhFEwSSGISVAGLVVGELCTTPSHWRQTKTLSKWMEIEGVPGISDIDTRELT 80
Cdd:smart01097 49 QIVVFTYPLIGNYGVNDED----------FE-SDKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALT 117
|
90
....*....|...
gi 86450111 81 KKIRENGTVLGRI 93
Cdd:smart01097 118 RKLREKGAMKGVI 130
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
346-1276 |
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: 1517.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 346 PKKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADMVYFLPLTPEYVEQVIKSERPNGV 425
Cdd:TIGR01369 6 IKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPDAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 426 LLTFGGQTALNCGVELEKTGIFKKYNVKVMGTPIQSIIETEDRKIFSDRVAEIGEKVAPSVAVYSIRQALDAAEKLEYPV 505
Cdd:TIGR01369 86 LPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYPV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 506 MARAAFSLGGLGSGFANNKEELEVLAKQALAHS--NQLIIDKSLRGWKEVEYEVVRDAYDNCITVCNMENLDPLGIHTGE 583
Cdd:TIGR01369 166 IVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHTGD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 584 SIVVAPSQTLSNREYNMLRTTAIKVIRHFGVIGECNIQYALNPESDQYYIIEVNARLSRSSALASKATGYPLAYVAAKLS 663
Cdd:TIGR01369 246 SIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 664 LAIPLPSIKNSVTGVTTACFEPSLDYCVVKMPRWDLAKFVRVSKTIGSSMKSVGEVMAIGRNFEEAFQKALRMVDENVNG 743
Cdd:TIGR01369 326 VGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 744 FDPYIKPVK-----EEELIEATDKRMFVLAAAIKANYTIEKLYQLTKIDPWFLNKMKNIID-YMNLLESRGNNLNRTVLL 817
Cdd:TIGR01369 406 FDLPDREVEpdedlWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDlEEELEEVKLTDLDPELLR 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 818 EAKKLGFSDRQIASAIKSTDLVVRHEREELNVVPFVKQIDTVAGEWPASTNYLYLTYNATSHDIEFLGNFTIVV-GSGVY 896
Cdd:TIGR01369 486 RAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDKKKVLVlGSGPN 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 897 RIGSSVEFDWCAVGCLRELRKLGRQTIMINYNPETVSTDYDMCDRLYFEEISLETVMDIYQIENADGIILSMGGQLPNNI 976
Cdd:TIGR01369 566 RIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPLNL 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 977 AMDLHRQQARVLGTSPDSIDNAENRFKFSRMLDRKGILQPRWKELTDLKAAIEFCEEVGYPCLVRPSYVLSGAAMNVAYS 1056
Cdd:TIGR01369 646 AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYN 725
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1057 NQDLETYLNAASLVSKEYPVVISKFLQEAKEIDVDAVAADGEILCMAVSEHVENAGVHSGDATLVTPPQDINAETLLKIK 1136
Cdd:TIGR01369 726 EEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDRIK 805
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1137 EIARDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAVIGMPVEPVEVL--HGCGKVGV 1214
Cdd:TIGR01369 806 DIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGVGkeKEPKYVAV 885
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 86450111 1215 KVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMMSTGFQIPKKAILLSIGSFK 1276
Cdd:TIGR01369 886 KEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDK 947
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
347-1272 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1319.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 347 KKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADMVYFLPLTPEYVEQVIKSERPNGVL 426
Cdd:PRK05294 8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 427 LTFGGQTALNCGVELEKTGIFKKYNVKVMGTPIQSIIETEDRKIFSDRVAEIGEKVAPSVAVYSIRQALDAAEKLEYPVM 506
Cdd:PRK05294 88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 507 ARAAFSLGGLGSGFANNKEELEVLAKQALAHS--NQLIIDKSLRGWKEVEYEVVRDAYDNCITVCNMENLDPLGIHTGES 584
Cdd:PRK05294 168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLSpvTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 585 IVVAPSQTLSNREYNMLRTTAIKVIRHFGVI-GECNIQYALNPESDQYYIIEVNARLSRSSALASKATGYPLAYVAAKLS 663
Cdd:PRK05294 248 ITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 664 LAIPLPSIKNSVTGVTTACFEPSLDYCVVKMPRWDLAKFVRVSKTIGSSMKSVGEVMAIGRNFEEAFQKALRMVDENVNG 743
Cdd:PRK05294 328 VGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 744 FDPYIKPVK-----EEELIEATDKRMFVLAAAIKANYTIEKLYQLTKIDPWFLNKMKNIIDYMNLLESRGNNLNRTVLLE 818
Cdd:PRK05294 408 LDEDLFEEEsleelREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLPLDAELLRE 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 819 AKKLGFSDRQIASAIKSTDLVVRHEREELNVVPFVKQIDTVAGEWPASTNYLYLTYNATSHDIEFLGNFTIVVGSGVYRI 898
Cdd:PRK05294 488 AKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVLGSGPNRI 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 899 GSSVEFDWCAVGCLRELRKLGRQTIMINYNPETVSTDYDMCDRLYFEEISLETVMDIYQIENADGIILSMGGQLPNNIAM 978
Cdd:PRK05294 568 GQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPLKLAK 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 979 DLHRQQARVLGTSPDSIDNAENRFKFSRMLDRKGILQPRWKELTDLKAAIEFCEEVGYPCLVRPSYVLSGAAMNVAYSNQ 1058
Cdd:PRK05294 648 ALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDEE 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1059 DLETYLNAASLVSKEYPVVISKFLQEAKEIDVDAVaADGE-ILCMAVSEHVENAGVHSGDATLVTPPQDINAETLLKIKE 1137
Cdd:PRK05294 728 ELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAI-CDGEdVLIGGIMEHIEEAGVHSGDSACSLPPQTLSEEIIEEIRE 806
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1138 IARDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAVIGMPVEPVEVLHGC--GKVGVK 1215
Cdd:PRK05294 807 YTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGLipPYVAVK 886
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*...
gi 86450111 1216 VPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMMSTGFQIPKK-AILLSI 1272
Cdd:PRK05294 887 EAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSV 944
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
347-1266 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1024.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 347 KKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADMVYFLPLTPEYVEQVIKSERPNGVL 426
Cdd:PRK12815 8 QKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAREKPDALL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 427 LTFGGQTALNCGVELEKTGIFKKYNVKVMGTPIQSIIETEDRKIFSDRVAEIGEKVAPSVAVYSIRQALDAAEKLEYPVM 506
Cdd:PRK12815 88 ATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAEKIGFPII 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 507 ARAAFSLGGLGSGFANNKEELEVLAKQALAHS--NQLIIDKSLRGWKEVEYEVVRDAYDNCITVCNMENLDPLGIHTGES 584
Cdd:PRK12815 168 VRPAYTLGGTGGGIAENLEELEQLFKQGLQASpiHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPVGIHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 585 IVVAPSQTLSNREYNMLRTTAIKVIRHFGVIGECNIQYALNPESDQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSL 664
Cdd:PRK12815 248 IVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAKIAAKLAV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 665 AIPLPSIKNSVTGVTTACFEPSLDYCVVKMPRWDLAKFVRVSKTIGSSMKSVGEVMAIGRNFEEAFQKALRMVDENVNGF 744
Cdd:PRK12815 328 GYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRSLEIKRNGL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 745 DPYIK--PVKEEELIE----ATDKRMFVLAAAIKANYTIEKLYQLTKIDPWFLNKMKNIIDYMNLLESRGNNLNRTVLLE 818
Cdd:PRK12815 408 SLPIElsGKSDEELLQdlrhPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEDGLDLSADLLRK 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 819 AKKLGFSDRQIASAIKSTDLVVRHEREELNVVPFVKQIDTVAGEWPASTNYLYLTYNATShDIEFLGN--FTIVVGSGVY 896
Cdd:PRK12815 488 VKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGES-EAEPSSEkkKVLILGSGPI 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 897 RIGSSVEFDWCAVGCLRELRKLGRQTIMINYNPETVSTDYDMCDRLYFEEISLETVMDIYQIENADGIILSMGGQLPNNI 976
Cdd:PRK12815 567 RIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIVQFGGQTAINL 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 977 AMDLHRQQARVLGTSPDSIDNAENRFKFSRMLDRKGILQPRWKELTDLKAAIEFCEEVGYPCLVRPSYVLSGAAMNVAYS 1056
Cdd:PRK12815 647 AKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYD 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1057 NQDLETYLNAAslVSKEYPVVISKFLqEAKEIDVDAVaADGE-ILCMAVSEHVENAGVHSGDATLVTPPQDINAETLLKI 1135
Cdd:PRK12815 727 EPALEAYLAEN--ASQLYPILIDQFI-DGKEYEVDAI-SDGEdVTIPGIIEHIEQAGVHSGDSIAVLPPQSLSEEQQEKI 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1136 KEIARDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAVIGMPVE----PVEVLHGCGK 1211
Cdd:PRK12815 803 RDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLAelgyPNGLWPGSPF 882
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*
gi 86450111 1212 VGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMMSTGFQIPKK 1266
Cdd:PRK12815 883 IHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSY 937
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
347-1265 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 857.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 347 KKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADMVYFLPLTPEYVEQVIKSERPNGVL 426
Cdd:PLN02735 24 KKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKERPDALL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 427 LTFGGQTALNCGVELEKTGIFKKYNVKVMGTPIQSIIETEDRKIFSDRVAEIGEKVAPSVAVYSIRQALDAAEKL-EYPV 505
Cdd:PLN02735 104 PTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDIgEFPL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 506 MARAAFSLGGLGSGFANNKEELEVLAKQALAHS--NQLIIDKSLRGWKEVEYEVVRDAYDNCITVCNMENLDPLGIHTGE 583
Cdd:PLN02735 184 IIRPAFTLGGTGGGIAYNKEEFETICKAGLAASitSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMGVHTGD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 584 SIVVAPSQTLSNREYNMLRTTAIKVIRHFGVigEC---NIQYALNPESDQYYIIEVNARLSRSSALASKATGYPLAYVAA 660
Cdd:PLN02735 264 SITVAPAQTLTDKEYQRLRDYSVAIIREIGV--ECggsNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAKMAA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 661 KLSLAIPLPSIKNSVTGVTTACFEPSLDYCVVKMPRWDLAKFVRVSKTIGSSMKSVGEVMAIGRNFEEAFQKALRMVDEN 740
Cdd:PLN02735 342 KLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSLETG 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 741 VNGFDPyiKPVKE---------EELIEATDKRMFVLAAAIKANYTIEKLYQLTKIDPWFLNKMKNIIDYMNLLESRG-NN 810
Cdd:PLN02735 422 FSGWGC--AKVKEldwdweqlkYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSlSE 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 811 LNRTVLLEAKKLGFSDRQIASAIKSTDLVVRHEREELNVVPFVKQIDTVAGEWPASTNYLYLTYNATSHDIEFLGNFTIV 890
Cdd:PLN02735 500 LSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPTNKKKVLI 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 891 VGSGVYRIGSSVEFDWCAVGCLRELRKLGRQTIMINYNPETVSTDYDMCDRLYFEEISLETVMDIYQIENADGIILSMGG 970
Cdd:PLN02735 580 LGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQFGG 659
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 971 QLPNNIAMDLHRQ-------------QARVLGTSPDSIDNAENRFKFSRMLDRKGILQPRWKELTDLKAAIEFCEEVGYP 1037
Cdd:PLN02735 660 QTPLKLALPIQKYldknpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKRIGYP 739
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1038 CLVRPSYVLSGAAMNVAYSNQDLETYLNAASLVSKEYPVVISKFLQEAKEIDVDAVA-ADGEILCMAVSEHVENAGVHSG 1116
Cdd:PLN02735 740 VVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALAdSEGNVVIGGIMEHIEQAGVHSG 819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1117 DATLVTPPQDINAETLLKIKEIARDLAALLDVTGPFNMQL-IAKNNELKVIECNVRVSRSFPFVSKTLNHDF-------V 1188
Cdd:PLN02735 820 DSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPSGEVYIIEANPRASRTVPFVSKAIGHPLakyaslvM 899
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86450111 1189 ATATRAVIGMPVEPVEvlhgcGKVGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMMSTGFQIPK 1265
Cdd:PLN02735 900 SGKSLKDLGFTEEVIP-----AHVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLPL 971
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
352-893 |
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: 642.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 352 LGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADMVYFLPLTPEYVEQVIKSERPNGVLLTFGG 431
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 432 QTALNCGVELEKTGIFKkyNVKVMGTPIQSIIETEDRKIFSDRVAEIGEKVAPSVAVYSIRQALDAAEKLEYPVMARAAF 511
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 512 SLGGLGSGFANNKEELEVLAKQALAHS--NQLIIDKSLRGWKEVEYEVVRDAYDNCITVCNMENLDPLGIHTGESIVVAP 589
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSpdHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 590 SQTLSNREYNMLRTTAIKVIRHFGVIGECNIQYALNpeSDQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLAIPLP 669
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 670 SIKNSvTGvttacFEPSLDYCVVKMPRWDLAKFVRVSKTIGSSMKSVGEVMAIGRNFEEAFQKALRMVDENVNG--FDPY 747
Cdd:COG0458 317 ELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLLSL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 748 IKPVKEEE--LIEATDKRMFVLAAAIKANYTIEKLYQLTKIDPWFLNKMKNIIDymNLLESRGNNLNRTVLLEAKKLGFS 825
Cdd:COG0458 391 VADDDKEEalLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIV--DEIELEEIILVINTLLGAKSLGDS 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86450111 826 DRQIASAIKSTDLVVRHEREELNVVPFVKQIDTVAGEWPASTNYLYLTYNATSHDIEFLGNFTIVVGS 893
Cdd:COG0458 469 DGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
891-1269 |
9.32e-155 |
|
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: 475.52 E-value: 9.32e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 891 VGSGVYRIGSSVEFDWCAVGCLRELRKLGRQTIMINYNPETVSTDYDMCDRLYFEEISLETVMDIYQIENADGIILSMGG 970
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 971 QLPNNIAMDLHRQQA----RVLGTSPDSIDNAENRFKFSRMLDRKGILQPRWKELTDLKAAIEFCEEVGYPCLVRPSYVL 1046
Cdd:COG0458 81 QTALNLAVELEEAGIlegvKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1047 SGAAMNVAYSNQDLETYLNAASLVSKEYPVVISKFLQEAKEIDVDAVA-ADGEILCMAVSEHVENAGVHSGDATLVTPPQ 1125
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRdGEDNVIIVGIMEHIEPAGVHSGDSICVAPPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1126 DINAETLLKIKEIARDLAALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPFVSKTLNHDFVATATRAVIGMPVEPVEV 1205
Cdd:COG0458 241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELGN 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86450111 1206 LHGC----GKVGVKVPQFSFSRLAGADVQLGVEMASTGEVACFGDNRYEAYLKAMMSTGFQIPKKAIL 1269
Cdd:COG0458 321 DTGFeptlDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGTVLL 388
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
1-312 |
2.18e-130 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 404.46 E-value: 2.18e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1 QILVLTYPLIGNYGVPSEKeldefglpkhFEwSSGISVAGLVVGELCTTPSHWRQTKTLSKWMEIEGVPGISDIDTRELT 80
Cdd:PRK12564 51 QIVTFTYPLIGNYGVNRED----------FE-SDRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 81 KKIRENGTVLGRITYNLPNP---KDDLKLTdPNL--RNLVAECSVIKPVVY---NPKGWPKICAIDCGLKLNQIRCFVAR 152
Cdd:PRK12564 120 RKLREKGAMKGVIATEDFDAeelLEKARAF-PGLlgLDLVKEVSTKEPYPWpgpGGELKYKVVAIDFGVKRNILRELAER 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 153 GARVELVPWNHS------LNPnefDGLFISNGPGDPVVCKNTVIEIQKVLKSsDKPIFGICLGHQLLSTAIGCKTFKMKY 226
Cdd:PRK12564 199 GCRVTVVPATTTaeeilaLNP---DGVFLSNGPGDPAALDYAIEMIRELLEK-KIPIFGICLGHQLLALALGAKTYKMKF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 227 GNRGHNLPCIHHGTGRCFMTSQNHGFAVESSTLPSDWEPLFTNANDNTNEGIIHKTKPYLSVQFHPEHTAGPEDLEMLFD 306
Cdd:PRK12564 275 GHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFD 354
|
....*.
gi 86450111 307 IFLETI 312
Cdd:PRK12564 355 EFVELM 360
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
1-314 |
6.48e-127 |
|
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273580 [Multi-domain] Cd Length: 357 Bit Score: 395.07 E-value: 6.48e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1 QILVLTYPLIGNYGVPsekeldefglPKHFEwSSGISVAGLVVGELCTTPSHWRQTKTLSKWMEIEGVPGISDIDTRELT 80
Cdd:TIGR01368 47 QIVVFTYPLIGNYGVN----------DEDAE-SKGIHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 81 KKIRENGTVLGRITYNLPNPKDDLKLT--DPNLR--NLVAECSVIKPVVYNPKGWP--KICAIDCGLKLNQIRCFVARGA 154
Cdd:TIGR01368 116 KKIREKGTMKGVISTEDSNDEELVEKArvSPDITgiNLVAEVSTKEPYTWGQRGGKgkRVVVIDFGVKRNILRRLVKRGC 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 155 RVELVPWNHS------LNPnefDGLFISNGPGDPVVCKNTVIEIQKVLksSDKPIFGICLGHQLLSTAIGCKTFKMKYGN 228
Cdd:TIGR01368 196 EVTVVPYDTDaeeikkYNP---DGIFLSNGPGDPAAVEPAIETIRKLL--EKIPIFGICLGHQLLALAFGAKTYKMKFGH 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 229 RGHNLPCIHHGTGRCFMTSQNHGFAVESSTLPS-DWEPLFTNANDNTNEGIIHKTKPYLSVQFHPEHTAGPEDLEMLFDI 307
Cdd:TIGR01368 271 RGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAgDLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDE 350
|
....*..
gi 86450111 308 FLETIKD 314
Cdd:TIGR01368 351 FIDLMKK 357
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
1-313 |
1.53e-124 |
|
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 388.99 E-value: 1.53e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1 QILVLTYPLIGNYGVPSEkeldefglpkHFEwSSGISVAGLVVGELCTTPSHWRQTKTLSKWMEIEGVPGISDIDTRELT 80
Cdd:COG0505 51 QIVTFTYPHIGNYGVNDE----------DFE-SDRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 81 KKIRENGTVLGRITYNLPNPKDDLKL----TDPNLRNLVAECSVIKPVVY--NPKGWPKICAIDCGLKLNQIRCFVARGA 154
Cdd:COG0505 120 RHLREKGAMKGVISTGDLDIEELLEKaraaPGMEGLDLVKEVSTKEPYEWteAPGAGFHVVALDFGVKRNILRELAERGC 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 155 RVELVPWNHS------LNPnefDGLFISNGPGDPVVCKNTVIEIQKVLKSsDKPIFGICLGHQLLSTAIGCKTFKMKYGN 228
Cdd:COG0505 200 RVTVVPATTSaeeilaLNP---DGVFLSNGPGDPAALDYAIETIRELLGK-GIPIFGICLGHQLLALALGAKTYKLKFGH 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 229 RGHNLPCIHHGTGRCFMTSQNHGFAVESSTLP-SDWEPLFTNANDNTNEGIIHKTKPYLSVQFHPEHTAGPEDLEMLFDI 307
Cdd:COG0505 276 RGANHPVKDLETGRVEITSQNHGFAVDEDSLPaTDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDR 355
|
....*.
gi 86450111 308 FLETIK 313
Cdd:COG0505 356 FIELME 361
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
1-313 |
2.82e-96 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 312.21 E-value: 2.82e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1 QILVLTYPLIGNYGVPsekeldefglPKHFEwSSGISVAGLVVGELCTTPSHWRQTKTLSKWMEIEGVPGISDIDTRELT 80
Cdd:PRK12838 49 QIVVFTYPLIGNYGIN----------ADDYE-SKQPQVKGVIVYELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 81 KKIRENGTVLGRITYNLPNPKDDLKLTDPNLRNLVAECSVIKPVVYNPKGwPKICAIDCGLKLNQIRCFVARGARVELVP 160
Cdd:PRK12838 118 KHIREKGTMKASITTTDDAHAFDQIKALVLPKNVVAQVSTKEPYTYGNGG-KHVALIDFGYKKSILRSLSKRGCKVTVLP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 161 WN------HSLNPnefDGLFISNGPGDPVVCKNTVIEIQKVLksSDKPIFGICLGHQLLSTAIGCKTFKMKYGNRGHNLP 234
Cdd:PRK12838 197 YDtsleeiKNLNP---DGIVLSNGPGDPKELQPYLPEIKKLI--SSYPILGICLGHQLIALALGADTEKLPFGHRGANHP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 235 CIHHGTGRCFMTSQNHGFAVESSTL-PSDWEPLFTNANDNTNEGIIHKTKPYLSVQFHPEHTAGPEDLEMLFDIFLETIK 313
Cdd:PRK12838 272 VIDLTTGRVWMTSQNHGYVVDEDSLdGTPLSVRFFNVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMME 351
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
467-669 |
2.20e-95 |
|
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: 304.23 E-value: 2.20e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 467 DRKIFSDRVAEIGEKVAPSVAVY--SIRQALDAAEKLEYPVMARAAFSLGGLGSGFANNKEELEVLAKQALAHS------ 538
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 539 NQLIIDKSLRGWKEVEYEVVRDAYDNCITVCNMENLDPLgiHTGESIVVAPSQTLSNREYNMLRTTAIKVIRHFGVIGEC 618
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 86450111 619 NIQYALNPESDQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLAIPLP 669
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
134-309 |
1.07e-94 |
|
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.
Pssm-ID: 153215 [Multi-domain] Cd Length: 178 Bit Score: 300.95 E-value: 1.07e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 134 ICAIDCGLKLNQIRCFVARGARVELVPWNHSLNPN---EFDGLFISNGPGDPVVCKNTVIEIQKVLKSsDKPIFGICLGH 210
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEIlklDPDGIFLSNGPGDPALLDEAIKTVRKLLGK-KIPIFGICLGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 211 QLLSTAIGCKTFKMKYGNRGHNLPCIHHGTGRCFMTSQNHGFAVESSTLPSDWEPLFTNANDNTNEGIIHKTKPYLSVQF 290
Cdd:cd01744 80 QLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159
|
170
....*....|....*....
gi 86450111 291 HPEHTAGPEDLEMLFDIFL 309
Cdd:cd01744 160 HPEASPGPHDTEYLFDEFL 178
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
332-735 |
1.21e-82 |
|
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: 293.44 E-value: 1.21e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 332 LTYTPTPESVIVGRPKKVLILGSGGLSIGQAGEFDYSGSQAIKALKEEKIQTILINPNIATVQTSKGLADMVYFLPLTPE 411
Cdd:TIGR01369 540 STYEGERDDVPFTDKKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFE 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 412 YVEQVIKSERPNGVLLTFGGQTALNCGVELEKTGifkkynVKVMGTPIQSIIETEDRKIFSDRVAEIGEKVAPSVAVYSI 491
Cdd:TIGR01369 620 DVMNIIELEKPEGVIVQFGGQTPLNLAKALEEAG------VPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSV 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 492 RQALDAAEKLEYPVMARAAFSLGGLGSGFANNKEELEVLAKQALAHSNQ--LIIDKSLRGWKEVEYEVVrdAYDNCITVC 569
Cdd:TIGR01369 694 EEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEhpVLIDKYLEDAVEVDVDAV--SDGEEVLIP 771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 570 N-MENLDPLGIHTGESIVVAPSQTLSNREYNMLRTTAIKVIRHFGVIGECNIQYALnpESDQYYIIEVNARLSRSSALAS 648
Cdd:TIGR01369 772 GiMEHIEEAGVHSGDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAV--KDGEVYVIEVNPRASRTVPFVS 849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 649 KATGYPLAYVAAKLSLAIPLPSIknsvtGVTtacFEPSLDYCVVKMPRWDLAKFVRVSKTIGSSMKSVGEVMAIGRNFEE 728
Cdd:TIGR01369 850 KATGVPLAKLAVRVMLGKKLEEL-----GVG---KEKEPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAE 921
|
....*..
gi 86450111 729 AFQKALR 735
Cdd:TIGR01369 922 AFLKAQL 928
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
1-321 |
8.08e-65 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 225.06 E-value: 8.08e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1 QILVLTYPLIGNYGVPSEKeldefglpkhFEwSSGISVAGLVVGELCTTPSHWRQTKTLSKWMEIEGVPGISDIDTRELT 80
Cdd:CHL00197 53 QIVTFTYPEIGNTGINLED----------IE-SVKIQVKGIIAKNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 81 KKIRENGTVLGRITYNLPNP-------KDDLKLTDPNLRNLVAECSVIKPVVYNPKGWP-------------KICAIDCG 140
Cdd:CHL00197 122 QHLRRFGTMNGCISNQNLNLsylrakiKESPHMPSSDLIPRVTTSSYYEWDEKSHPSFYladnkrphssyqlKIIVIDFG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 141 LKLNQIRCFVARGARVELVP-------WNhSLNPnefDGLFISNGPGDPVVCKNTVIEIQKVLKSSdKPIFGICLGHQLL 213
Cdd:CHL00197 202 VKYNILRRLKSFGCSITVVPatspyqdIL-SYQP---DGILLSNGPGDPSAIHYGIKTVKKLLKYN-IPIFGICMGHQIL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 214 STAIGCKTFKMKYGNRGhnlpcIHHGTG---RCFMTSQNHGFAVESSTLPSDwePLFT---NANDNTNEGIIHKTKPYLS 287
Cdd:CHL00197 277 SLALEAKTFKLKFGHRG-----LNHPSGlnqQVEITSQNHGFAVNLESLAKN--KFYIthfNLNDGTVAGISHSPKPYFS 349
|
330 340 350
....*....|....*....|....*....|....
gi 86450111 288 VQFHPEHTAGPEDLEMLFDIFLETIKdKLEGKKN 321
Cdd:CHL00197 350 VQYHPEASPGPHDADYLFEYFIEIIK-HSKSSKN 382
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
137-310 |
1.56e-59 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 202.47 E-value: 1.56e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 137 IDCGL--KLNQIRCFVARGARVELVPWNHSLN---PNEFDGLFISNGPGDPVVCKNTVIEIQKVLKSsDKPIFGICLGHQ 211
Cdd:pfam00117 3 IDNGDsfTYNLARALRELGVEVTVVPNDTPAEeilEENPDGIILSGGPGSPGAAGGAIEAIREAREL-KIPILGICLGHQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 212 LLSTAIGCKTFKMK-YGNRGHNLPCIH------HGTGRCFMTSQNHGFAVESSTLPSDWEPLFTNANDNTNEGIIHKTKP 284
Cdd:pfam00117 82 LLALAFGGKVVKAKkFGHHGKNSPVGDdgcglfYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKLP 161
|
170 180
....*....|....*....|....*.
gi 86450111 285 YLSVQFHPEHTAGPEDLEMLFDIFLE 310
Cdd:pfam00117 162 IFGVQFHPESILTPHGPEILFNFFIK 187
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
753-874 |
3.59e-52 |
|
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: 178.80 E-value: 3.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 753 EEELIEATDKRMFVLAAAIKANYTIEKLYQLTKIDPWFLNKMKNIIDYMNLLESRG-NNLNRTVLLEAKKLGFSDRQIAS 831
Cdd:smart01096 2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGlDELDADLLRKAKRLGFSDRQIAK 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 86450111 832 AIKSTDLVVRHEREELNVVPFVKQIDTVAGEWPASTNYLYLTY 874
Cdd:smart01096 82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
1-305 |
4.40e-49 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 180.56 E-value: 4.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1 QILVLTYPLIGNYGV-PSEKEldefglpkhfewSSGISVAGLVVGELCTTPSHWRQTKTLSKWMEIEGVPGISDIDTREL 79
Cdd:PLN02771 103 QFVLMTNPHIGNTGVnFDDEE------------SRQCFLAGLVIRSLSISTSNWRCTKTLGDYLAERNIMGIYDVDTRAI 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 80 TKKIRENGTVLGRITynlpnpKDDLKLTDPNLR----------NLVAECSVIKPVVYNPKGWP--------------KIC 135
Cdd:PLN02771 171 TRRLREDGSLIGVLS------TEDSKTDEELLKmsrswdivgiDLISGVSCKSPYEWVDKTNPewdfntnsrdgesyHVI 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 136 AIDCGLKLNQIRCFVARGARVELVP--WNHS----LNPnefDGLFISNGPGDPVVCKNTVIEIQKVLksSDKPIFGICLG 209
Cdd:PLN02771 245 AYDFGIKHNILRRLASYGCKITVVPstWPASealkMKP---DGVLFSNGPGDPSAVPYAVETVKELL--GKVPVFGICMG 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 210 HQLLSTAIGCKTFKMKYGNRGHNLPCIHHGTGRCFMTSQNHGFAVESSTLPSDWEPLFTNANDNTNEGIIHKTKPYLSVQ 289
Cdd:PLN02771 320 HQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQ 399
|
330
....*....|....*.
gi 86450111 290 FHPEHTAGPEDLEMLF 305
Cdd:PLN02771 400 YHPEASPGPHDSDNAF 415
|
|
| CPSase_sm_chain |
pfam00988 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-93 |
2.17e-39 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. 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 pfam00289. The small chain has a GATase domain in the carboxyl terminus. See pfam00117.
Pssm-ID: 460017 [Multi-domain] Cd Length: 126 Bit Score: 142.46 E-value: 2.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1 QILVLTYPLIGNYGVPSEkeldefglpkHFEwSSGISVAGLVVGELCTTPSHWRQTKTLSKWMEIEGVPGISDIDTRELT 80
Cdd:pfam00988 45 QIVVFTYPLIGNYGVNPE----------DFE-SDKIHVAGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALT 113
|
90
....*....|...
gi 86450111 81 KKIRENGTVLGRI 93
Cdd:pfam00988 114 RKIREKGAMKGVI 126
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
1-93 |
1.23e-37 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses 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 synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.
Pssm-ID: 198165 [Multi-domain] Cd Length: 130 Bit Score: 137.51 E-value: 1.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1 QILVLTYPLIGNYGVPSEKeldefglpkhFEwSSGISVAGLVVGELCTTPSHWRQTKTLSKWMEIEGVPGISDIDTRELT 80
Cdd:smart01097 49 QIVVFTYPLIGNYGVNDED----------FE-SDKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALT 117
|
90
....*....|...
gi 86450111 81 KKIRENGTVLGRI 93
Cdd:smart01097 118 RKLREKGAMKGVI 130
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
754-830 |
4.58e-34 |
|
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 460695 Cd Length: 79 Bit Score: 125.57 E-value: 4.58e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86450111 754 EELIEATDKRMFVLAAAIKANYTIEKLYQLTKIDPWFLNKMKNIIDYMNLLESRGNNLNRTVLLEAKKLGFSDRQIA 830
Cdd:pfam02787 1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAGLDLDAELLREAKRLGFSDRQIA 77
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
989-1200 |
4.54e-20 |
|
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: 91.47 E-value: 4.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 989 GTSPDSIDNAENRFKFSRMLDRKGILQPRWKELTDLKAAIEFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAAS 1068
Cdd:COG0439 43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEAR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1069 ----LVSKEYPVVISKFLqEAKEIDVDAVAADGEILCMAVSEHvENAGVHSGDATLVTPPqDINAETLLKIKEIARDLAA 1144
Cdd:COG0439 123 aeakAGSPNGEVLVEEFL-EGREYSVEGLVRDGEVVVCSITRK-HQKPPYFVELGHEAPS-PLPEELRAEIGELVARALR 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1145 LLDV-TGPFNMQ-LIAKNNELKVIECNVRVS--RSFPFVSKTLNHDFVATATRAVIGMPV 1200
Cdd:COG0439 200 ALGYrRGAFHTEfLLTPDGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEPR 259
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
153-293 |
1.44e-18 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.
Pssm-ID: 153214 [Multi-domain] Cd Length: 184 Bit Score: 84.89 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 153 GARVELVPwNHSLNPNE-----FDGLFISNGPGDPVVCKNTVIEIQKVLKssDKPIFGICLGHQLLSTAIGCKTFKMKYG 227
Cdd:cd01743 22 GAEVVVVR-NDEITLEElellnPDAIVISPGPGHPEDAGISLEIIRALAG--KVPILGVCLGHQAIAEAFGGKVVRAPEP 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86450111 228 NRGHNLPCIHHGTGRCFMTSQN------HGFAVESSTLPSDWEplFTNANDntnEGII----HKTKPYLSVQFHPE 293
Cdd:cd01743 99 MHGKTSEIHHDGSGLFKGLPQPftvgryHSLVVDPDPLPDLLE--VTASTE---DGVImalrHRDLPIYGVQFHPE 169
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
1023-1201 |
2.28e-18 |
|
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: 85.05 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1023 DLKAAIEFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASLVSKEYP----VVISKFLQEAKEIDVDaVAADGE 1098
Cdd:pfam02786 26 TEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSLKGPKHIEYQ-VLRDAH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1099 ILCMAVSEhVENA-GVHSGDATLVTPPQDINAETLLKIKEIARDLAALLDVTGPFNMQLI--AKNNELKVIECNVRVSRS 1175
Cdd:pfam02786 105 GNCITVCN-RECSdQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFAldPFSGEYYFIEMNTRLQVE 183
|
170 180
....*....|....*....|....*.
gi 86450111 1176 FPFVSKTLNHDFVATATRAVIGMPVE 1201
Cdd:pfam02786 184 HALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
133-296 |
7.54e-15 |
|
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440284 [Multi-domain] Cd Length: 225 Bit Score: 75.37 E-value: 7.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 133 KICAIDCG-------------LKLNQIRCFVARGARVELVPWNHSlnPNEFDGLFISNGPG---DPVVCKNTVIEIQKVL 196
Cdd:COG0518 1 KILILDHDpfggqypgliarrLREAGIELDVLRVYAGEILPYDPD--LEDPDGLILSGGPMsvyDEDPWLEDEPALIREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 197 KSSDKPIFGICLGHQLLSTAIGCKTFKMKYGNRG-------------HNLPcihhGTGRCFMTsqnHGFAVEssTLPSDW 263
Cdd:COG0518 79 FELGKPVLGICYGAQLLAHALGGKVEPGPGREIGwapvelteadplfAGLP----DEFTVWMS---HGDTVT--ELPEGA 149
|
170 180 190
....*....|....*....|....*....|...
gi 86450111 264 EPLFTNANDnTNEGIIHKtKPYLSVQFHPEHTA 296
Cdd:COG0518 150 EVLASSDNC-PNQAFRYG-RRVYGVQFHPEVTH 180
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
473-667 |
6.65e-14 |
|
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: 73.37 E-value: 6.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 473 DRVAEIGEKVAPSVAVYSIRQALDAAEKLEYPVMARAAFSLGGLGSGFANNKEELEVLAKQALAHSN------QLIIDKS 546
Cdd:COG0439 60 EALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKagspngEVLVEEF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 547 LRGwKEVEYEVVrdAYDNCITVCNM---ENLDPLGIHTGEsivVAPSQtLSNREYNMLRTTAIKVIRHFGVI-GECNIQY 622
Cdd:COG0439 140 LEG-REYSVEGL--VRDGEVVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELVARALRALGYRrGAFHTEF 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 86450111 623 ALNPEsDQYYIIEVNARLS--RSSALASKATGYPLAYVAAKLSLAIP 667
Cdd:COG0439 213 LLTPD-GEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEP 258
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
165-304 |
7.01e-14 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 75.91 E-value: 7.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 165 LNPnefDGLFISNGPGDPvvcKNTVIEIQKVLKSSDK-PIFGICLGHQLLSTAIGCKTFKMKYGNRGHNLPCIHHGTGrC 243
Cdd:PRK14607 43 LNP---SHIVISPGPGRP---EEAGISVEVIRHFSGKvPILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKG-L 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86450111 244 FMTSQN-------HGFAVESSTLPSDWEPLfTNANDNTNEGIIHKTKPYLSVQFHPEHTAGPEDLEML 304
Cdd:PRK14607 116 FRGIPNptvatryHSLVVEEASLPECLEVT-AKSDDGEIMGIRHKEHPIFGVQFHPESILTEEGKRIL 182
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
167-294 |
2.92e-13 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153212 [Multi-domain] Cd Length: 188 Bit Score: 69.58 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 167 PNEFDGLFISNGPGDPVVCKNTVIE-----IQKVLKSsDKPIFGICLGHQLLSTAIGCKTFKMKYG-----------NRG 230
Cdd:cd01741 44 LDDYDGLVILGGPMSVDEDDYPWLKklkelIRQALAA-GKPVLGICLGHQLLARALGGKVGRNPKGweigwfpvtltEAG 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86450111 231 HNLPcIHHGTGRCFMTSQNHGFAVESstLPSDWEPLFTNAnDNTNEGIIhKTKPYLSVQFHPEH 294
Cdd:cd01741 123 KADP-LFAGLPDEFPVFHWHGDTVVE--LPPGAVLLASSE-ACPNQAFR-YGDRALGLQFHPEE 181
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
153-293 |
4.15e-13 |
|
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440278 [Multi-domain] Cd Length: 189 Bit Score: 69.30 E-value: 4.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 153 GARVELVPwNHSLNPNE-----FDGLFISNGPGDPV---VCkntvIEIQKVLKSsDKPIFGICLGHQllstAIGcktfkM 224
Cdd:COG0512 22 GAEVVVVR-NDEITLEEiealaPDGIVLSPGPGTPEeagIS----LEVIRAFAG-KIPILGVCLGHQ----AIG-----E 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 225 KYGNRGHNLPCIHHGtgrcfMTSQ-------------N-------HGFAVESSTLPSDWEPlftNANDNTNE--GIIHKT 282
Cdd:COG0512 87 AFGGKVVRAPEPMHG-----KTSPithdgsglfaglpNpftatryHSLVVDRETLPDELEV---TAWTEDGEimGIRHRE 158
|
170
....*....|.
gi 86450111 283 KPYLSVQFHPE 293
Cdd:COG0512 159 LPIEGVQFHPE 169
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
348-659 |
1.23e-12 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 70.68 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 348 KVLILGSGGlsigqagefdysGSQAIKALKEEKIQTILINPNIATVQTSKGLADMVYFLP--LTPEYVEQVI---KSERP 422
Cdd:PRK12767 3 NILVTSAGR------------RVQLVKALKKSLLKGRVIGADISELAPALYFADKFYVVPkvTDPNYIDRLLdicKKEKI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 423 NGVLLTFGgqtalncgVELEKTGI----FKKYNVKVMGTPiQSIIET-EDRKIFSDRVAEIGEKVAPSVAVYSIRQAL-- 495
Cdd:PRK12767 71 DLLIPLID--------PELPLLAQnrdrFEEIGVKVLVSS-KEVIEIcNDKWLTYEFLKENGIPTPKSYLPESLEDFKaa 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 496 DAAEKLEYPVMARAAFSLGGLGSGFANNKEELEVLakqaLAHSNQLIIDKSLRGwKEVEYEVVRDAYDNCITVCNMENLD 575
Cdd:PRK12767 142 LAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFL----LEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVISIVPRKRIE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 576 PLGihtGESivvapSQTLSnREYNMLRTTAIKVIRHFGVIGECNIQYALNPesDQYYIIEVNARLSrssalaskaTGYPL 655
Cdd:PRK12767 217 VRA---GET-----SKGVT-VKDPELFKLAERLAEALGARGPLNIQCFVTD--GEPYLFEINPRFG---------GGYPL 276
|
....
gi 86450111 656 AYVA 659
Cdd:PRK12767 277 SYMA 280
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
165-304 |
1.60e-12 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 67.46 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 165 LNPnefDGLFISNGPGDPVVCKNTVIEIQKVlkSSDKPIFGICLGHQLLSTAIGC-----------KTFKMKYGNRGhnl 233
Cdd:PRK05670 42 LNP---DAIVLSPGPGTPAEAGISLELIREF--AGKVPILGVCLGHQAIGEAFGGkvvrakeimhgKTSPIEHDGSG--- 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86450111 234 pcIHHGTGRCFMTSQNHGFAVESSTLPSDWEPLFTnANDNTNEGIIHKTKPYLSVQFHPEHTAGPEDLEML 304
Cdd:PRK05670 114 --IFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAW-TDDGEIMGVRHKELPIYGVQFHPESILTEHGHKLL 181
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
1012-1156 |
4.30e-12 |
|
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: 65.74 E-value: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1012 GILQPRWKELTDLKAAIEFCEEVGYPCLV---RPSYvlSGAAMNVAYSNQDLETYLNAAslvsKEYPVVISKFLQEAKEI 1088
Cdd:pfam02222 4 GLPTPRFMAAESLEELIEAGQELGYPCVVkarRGGY--DGKGQYVVRSEADLPQAWEEL----GDGPVIVEEFVPFDREL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86450111 1089 DVDAV-AADGEILCMAVSEHVEnagvHSGDATLVTPPQDINAETLLKIKEIARDLAALLDVTGPFNMQL 1156
Cdd:pfam02222 78 SVLVVrSVDGETAFYPVVETIQ----EDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVEL 142
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
171-310 |
7.04e-12 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 65.64 E-value: 7.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 171 DGLFISNGPgdpvvckntviEIQKV------LKSSDKPIFGICLGHQLLSTAIGCKTFKMKYGNRG--------HNLPCI 236
Cdd:PRK00758 43 DGLILSGGP-----------DIERAgncpeyLKELDVPILGICLGHQLIAKAFGGEVGRGEYGEYAlveveildEDDILK 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86450111 237 hhGTGRCFMTSQNHgfAVESSTLPSDWEPLftnANDNT--NEGIIHKTKPYLSVQFHPE--HTagpEDLEMLFDIFLE 310
Cdd:PRK00758 112 --GLPPEIRVWASH--ADEVKELPDGFEIL---ARSDIceVEAMKHKEKPIYGVQFHPEvaHT---EYGEEIFKNFLE 179
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
144-293 |
8.70e-12 |
|
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase.
Pssm-ID: 273144 [Multi-domain] Cd Length: 188 Bit Score: 65.19 E-value: 8.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 144 NQIRCFVARGARVeLVPWNHSLNPNEFDGLF-----ISNGPGDPvvcKNTVIEIQKVLKSSDK-PIFGICLGHQLLSTAI 217
Cdd:TIGR00566 14 NLVQYFCELGAEV-VVKRNDSLTLQEIEALLpllivISPGPCTP---NEAGISLEAIRHFAGKlPILGVCLGHQAMGQAF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 218 GCKTFKMKYGNRGHNLPCIHHGTGRC------FMTSQNHGFAVESSTLPSDWEPLFTNANDNTNEGIIHKTKPYLSVQFH 291
Cdd:TIGR00566 90 GGDVVRANTVMHGKTSEIEHNGAGIFrglfnpLTATRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQFH 169
|
..
gi 86450111 292 PE 293
Cdd:TIGR00566 170 PE 171
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
173-310 |
1.95e-11 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 64.50 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 173 LFISNGPGDPvvcKNTVIEIQKVLKSSDK-PIFGICLGHQLLSTAIGCKTFKMKYGNRG------HNLPCIHHGTGRCFM 245
Cdd:PRK06774 47 LVISPGPCTP---NEAGISLAVIRHFADKlPILGVCLGHQALGQAFGARVVRARQVMHGktsaicHSGQGVFRGLNQPLT 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86450111 246 TSQNHGFAVESSTLPSDWE-PLFTNANDNTNE--GIIHKTKPYLSVQFHPEHTAGPEDLEMLfDIFLE 310
Cdd:PRK06774 124 VTRYHSLVIAADSLPGCFElTAWSERGGEMDEimGIRHRTLPLEGVQFHPESILSEQGHQLL-DNFLK 190
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
157-304 |
2.30e-11 |
|
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 129966 [Multi-domain] Cd Length: 188 Bit Score: 64.26 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 157 ELVPWNHSL------NPNefdGLFISNGPgDPVVCKNTVIEIQKVLKSsDKPIFGICLGHQLLSTAIGCKTFKMKYGNRG 230
Cdd:TIGR00888 26 ELVPNTTPLeeirekNPK---GIILSGGP-SSVYAENAPRADEKIFEL-GVPVLGICYGMQLMAKQLGGEVGRAEKREYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 231 H------NLPCIHHGTGRCFMTSQNHGFAVESstLPSDWEPLFTNANdNTNEGIIHKTKPYLSVQFHPEHTAGPEDLEML 304
Cdd:TIGR00888 101 KaeleilDEDDLFRGLPDESTVWMSHGDKVKE--LPEGFKVLATSDN-CPVAAMAHEEKPIYGVQFHPEVTHTEYGNELL 177
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
172-315 |
5.04e-11 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 64.05 E-value: 5.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 172 GLFISNGPGDPvvcKNTVIEIQKVLK-SSDKPIFGICLGHQLLSTAIGCKTFKMKYG-NRGHNLPCIH---------HGT 240
Cdd:PLN02335 65 GVLISPGPGTP---QDSGISLQTVLElGPLVPLFGVCMGLQCIGEAFGGKIVRSPFGvMHGKSSPVHYdekgeeglfSGL 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86450111 241 GRCFMTSQNHGFAVESSTLPSDWEPLFTNANDNTNEGIIHKTKPYLS-VQFHPEHTAGPEDLEMLFDiFLETIKDK 315
Cdd:PLN02335 142 PNPFTAGRYHSLVIEKDTFPSDELEVTAWTEDGLIMAARHRKYKHIQgVQFHPESIITTEGKTIVRN-FIKIIEKK 216
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
987-1178 |
8.51e-11 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 64.91 E-value: 8.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 987 VLGTSPDSIDNAENRFKFSRMLDRKGILQPRWKELTDLKAAIE--FCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYL 1064
Cdd:PRK12767 98 VLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAalAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1065 NAASlvskeyPVVISKFLQEaKEIDVDA-VAADGEILCMAVSEHVEnagVHSGDA-TLVTPPQDinaetllKIKEIARDL 1142
Cdd:PRK12767 178 EYVP------NLIIQEFIEG-QEYTVDVlCDLNGEVISIVPRKRIE---VRAGETsKGVTVKDP-------ELFKLAERL 240
|
170 180 190
....*....|....*....|....*....|....*.
gi 86450111 1143 AALLDVTGPFNMQLIAKNNELKVIECNVRVSRSFPF 1178
Cdd:PRK12767 241 AEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPL 276
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
164-293 |
1.24e-10 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 62.20 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 164 SLNPNEfdgLFISNGPGDPvvcKNTVIEIQKVLKSSDK-PIFGICLGHQLLSTAIGCKTFKMKYGNRGHNLPCIHhgTGR 242
Cdd:PRK08857 41 ALNPTH---LVISPGPCTP---NEAGISLQAIEHFAGKlPILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRH--TGR 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86450111 243 CFMTSQN--------HGFAVESSTLPSDWE-PLFTNANDNTNE---GIIHKTKPYLSVQFHPE 293
Cdd:PRK08857 113 SVFKGLNnpltvtryHSLVVKNDTLPECFElTAWTELEDGSMDeimGFQHKTLPIEAVQFHPE 175
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
169-293 |
1.55e-10 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 62.37 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 169 EFDGLFISNGPGDPV---VCkntvIEIQKVLKSSDKPIFGICLGHQLLSTAIGC-----------KTFKMKYGNRGhnlp 234
Cdd:PRK07765 46 QFDGVLLSPGPGTPEragAS----IDMVRACAAAGTPLLGVCLGHQAIGVAFGAtvdrapellhgKTSSVHHTGVG---- 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86450111 235 cIHHGTGRCFMTSQNHGFAVESSTLPSDWEplftnANDNTNEGII----HKTKPYLSVQFHPE 293
Cdd:PRK07765 118 -VLAGLPDPFTATRYHSLTILPETLPAELE-----VTARTDSGVImavrHRELPIHGVQFHPE 174
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
165-315 |
5.97e-10 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 60.20 E-value: 5.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 165 LNPnefDGLFISNGPGDPvvcKNTVIEIQKVLKSSDK-PIFGICLGHQLLSTAIGCKTFKM------KYGNRGHNLPCIH 237
Cdd:PRK07649 42 MKP---DFLMISPGPCSP---NEAGISMEVIRYFAGKiPIFGVCLGHQSIAQVFGGEVVRAerlmhgKTSLMHHDGKTIF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 238 HGTGRCFMTSQNHGFAVESSTLPSDWEplftnANDNTNEG----IIHKTKPYLSVQFHPEHTAGPEDLEMLFDiFLETIK 313
Cdd:PRK07649 116 SDIPNPFTATRYHSLIVKKETLPDCLE-----VTSWTEEGeimaIRHKTLPIEGVQFHPESIMTSHGKELLQN-FIRKYS 189
|
..
gi 86450111 314 DK 315
Cdd:PRK07649 190 PS 191
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
153-295 |
7.40e-10 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153213 [Multi-domain] Cd Length: 181 Bit Score: 59.47 E-value: 7.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 153 GARVELVPWNHSL---NPNEFDGLFISNGP------GDPVVCKntviEIQKVlkssDKPIFGICLGHQLLSTAIGCKTFK 223
Cdd:cd01742 22 GVYSEILPNTTPLeeiKLKNPKGIILSGGPssvyeeDAPRVDP----EIFEL----GVPVLGICYGMQLIAKALGGKVER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 224 MKYGNRGHNLPCIHHGTG---------RCFMtsqNHGFAVEssTLPSDWEPLFTNANdNTNEGIIHKTKPYLSVQFHPE- 293
Cdd:cd01742 94 GDKREYGKAEIEIDDSSPlfeglpdeqTVWM---SHGDEVV--KLPEGFKVIASSDN-CPVAAIANEEKKIYGVQFHPEv 167
|
...
gi 86450111 294 -HT 295
Cdd:cd01742 168 tHT 170
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
146-213 |
2.50e-09 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 56.07 E-value: 2.50e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86450111 146 IRCFVARGARVELVPWNHS-----LNPNEFDGLFISNGPGDPVVCKNTVIEIQKVLK--SSDKPIFGICLGHQLL 213
Cdd:cd01653 18 LDALREAGAEVDVVSPDGGpvesdVDLDDYDGLILPGGPGTPDDLARDEALLALLREaaAAGKPILGICLGAQLL 92
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
170-293 |
3.00e-09 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 57.82 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 170 FDGLFISNGPGDPVVCKNTVIEIQKVLKSsdKPIFGICLGHQLLstaigCKTFkmkyGNRGHNLPCIHHGTGRCFMTSQN 249
Cdd:PRK06895 44 FSHILISPGPDVPRAYPQLFAMLERYHQH--KSILGVCLGHQTL-----CEFF----GGELYNLNNVRHGQQRPLKVRSN 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 86450111 250 ----------------HGFAVESSTLPsdwEPLFTNA--NDNTNEGIIHKTKPYLSVQFHPE 293
Cdd:PRK06895 113 splfdglpeefniglyHSWAVSEENFP---TPLEITAvcDENVVMAMQHKTLPIYGVQFHPE 171
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
165-293 |
7.14e-09 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 57.05 E-value: 7.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 165 LNPNefdGLFISNGPGDPvvcKNTVIEIQkVLKS--SDKPIFGICLGHQLLSTAIGCKTFKMKYGNRGhNLPCIHHGTGR 242
Cdd:CHL00101 42 LNIR---HIIISPGPGHP---RDSGISLD-VISSyaPYIPILGVCLGHQSIGYLFGGKIIKAPKPMHG-KTSKIYHNHDD 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86450111 243 CFMTSQN-------HGFAVESSTLPSdwePLFTNAndNTNEGII----HKTKPYL-SVQFHPE 293
Cdd:CHL00101 114 LFQGLPNpftatryHSLIIDPLNLPS---PLEITA--WTEDGLImacrHKKYKMLrGIQFHPE 171
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
146-213 |
8.86e-09 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 53.74 E-value: 8.86e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86450111 146 IRCFVARGARVELVPWNHS-----LNPNEFDGLFISNGPGDPVVCKNTVIEIQKVLK--SSDKPIFGICLGHQLL 213
Cdd:cd03128 18 LDALREAGAEVDVVSPDGGpvesdVDLDDYDGLILPGGPGTPDDLAWDEALLALLREaaAAGKPVLGICLGAQLL 92
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
144-293 |
1.40e-08 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 56.08 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 144 NQIRCFVARGARVeLVPWNHSLNPNEFDGL-----FISNGPGDPvvcKNTVIEIQKVLKSSDK-PIFGICLGHQLLSTAI 217
Cdd:PRK08007 14 NLYQYFCELGADV-LVKRNDALTLADIDALkpqkiVISPGPCTP---DEAGISLDVIRHYAGRlPILGVCLGHQAMAQAF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 218 GCKTFKMKYGNRGHNLPCIHHGTG------RCFMTSQNHGFAVESSTLPSDWEplfTNANDNTNE--GIIHKTKPYLSVQ 289
Cdd:PRK08007 90 GGKVVRAAKVMHGKTSPITHNGEGvfrglaNPLTVTRYHSLVVEPDSLPACFE---VTAWSETREimGIRHRQWDLEGVQ 166
|
....
gi 86450111 290 FHPE 293
Cdd:PRK08007 167 FHPE 170
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
467-709 |
1.64e-08 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 58.40 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 467 DRKIFSDRVAEIGEKVAPSVAVYSIRQALDAAEKLEYPVMARAA--------FSLGGLGSGFANNKEELEVLAKQALAHS 538
Cdd:COG3919 117 DKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGFPVVVKPAdsvgydelSFPGKKKVFYVDDREELLALLRRIAAAG 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 539 NQLII-------DKSLRGwkeveYEVVRDAYDNCITVCNMENL--DPLGIhtGESIVVapsQTLSNREynmLRTTAIKVI 609
Cdd:COG3919 197 YELIVqeyipgdDGEMRG-----LTAYVDRDGEVVATFTGRKLrhYPPAG--GNSAAR---ESVDDPE---LEEAARRLL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 610 RHFGVIGECNIQYALNPESDQYYIIEVNARLSRSSALASKAtGYPLAYVAAKLSLAIPLPSIKNSVTGVTTACFEPSLDY 689
Cdd:COG3919 264 EALGYHGFANVEFKRDPRDGEYKLIEINPRFWRSLYLATAA-GVNFPYLLYDDAVGRPLEPVPAYREGVLWRVLPGDLLL 342
|
250 260
....*....|....*....|..
gi 86450111 690 CVVKMPRW--DLAKFVRVSKTI 709
Cdd:COG3919 343 RYLRDGELrkRLRELLRRGKVV 364
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
458-640 |
2.04e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 55.03 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 458 PIQSIIETEDRKIFSDR-VAEIGEKVAP--SVAVYSIRQALDAAEKLEYPVMARAAFSLGGLGSGFANNKEELEvlakQA 534
Cdd:PRK06111 105 PSADIIAKMGSKIEARRaMQAAGVPVVPgiTTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELT----KA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 535 LAhSNQ-----------LIIDKSLRGWKEVEYEVVRDAYDNCitvcnmenldplgIHTGE---SI------VV--APSQT 592
Cdd:PRK06111 181 FE-SNKkraanffgngeMYIEKYIEDPRHIEIQLLADTHGNT-------------VYLWErecSVqrrhqkVIeeAPSPF 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 86450111 593 LSNREYNMLRTTAIKVIRHFGVIGECNIQYaLNPESDQYYIIEVNARL 640
Cdd:PRK06111 247 LDEETRKAMGERAVQAAKAIGYTNAGTIEF-LVDEQKNFYFLEMNTRL 293
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
446-640 |
4.17e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 53.98 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 446 IFKKYNVKVMGTPIQSIIETEDRKIFSDRVAEIGEKVAPSV--AVYSIRQALDAAEKLEYPVMARAAFSLGGLGSGFANN 523
Cdd:PRK08462 96 ICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSdgALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVED 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 524 KEELE--VLAKQALAHS----NQLIIDKSLRGWKEVEYEVVRDAYDNCITV----CNMENldplgiHTGESIVVAPSQTL 593
Cdd:PRK08462 176 ESDLEnlYLAAESEALSafgdGTMYMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAVVL 249
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 86450111 594 SNREYNMLRTTAIKVIRHFGVIGECNIQYALNPESDqYYIIEVNARL 640
Cdd:PRK08462 250 DEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLD-FYFMEMNTRL 295
|
|
| PLN02889 |
PLN02889 |
oxo-acid-lyase/anthranilate synthase |
168-296 |
1.04e-06 |
|
oxo-acid-lyase/anthranilate synthase
Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 53.31 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 168 NEFDGLFISNGPGDPVVCKNTVIEIQKVLKSSDKPIFGICLGHQLL-----------STAIGCKTFKMKY-GNR-GHNLP 234
Cdd:PLN02889 130 KAFDNIVISPGPGSPTCPADIGICLRLLLECRDIPILGVCLGHQALgyvhgarivhaPEPVHGRLSEIEHnGCRlFDDIP 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 235 -------------------------------CIHHGTGRcFMTSQNHGF---AVESSTLPSDWEPLFTNANDNTNE---- 276
Cdd:PLN02889 210 sgrnsgfkvvryhslvidaeslpkelvpiawTSSSDTLS-FLESQKSGLvpdAYESQIGQSGSSDPFSSKLKNGTSwpss 288
|
170 180 190
....*....|....*....|....*....|..
gi 86450111 277 ------------GIIHKTKPYLSVQFHPEHTA 296
Cdd:PLN02889 289 hsermqngkilmGIMHSTRPHYGLQFHPESIA 320
|
|
| GATase1_Glutamyl_Hydrolase |
cd01747 |
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ... |
153-296 |
1.61e-06 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153218 [Multi-domain] Cd Length: 273 Bit Score: 51.17 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 153 GARVelVPWNHSLNPNEFDGLFIS-NG---PGDPVV-----CKNTVIEI-QKVLKSSDK----PIFGICLGHQLLS---- 214
Cdd:cd01747 33 GARV--VPIWINESEEYYDKLFKSiNGilfPGGAVDidtsgYARTAKIIyNLALERNDAgdyfPVWGTCLGFELLTylts 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 215 ----------------------TAIGCKTFKmkygnrghNLP--CIHHGTGRCFmTSQNHGFAV-----ESSTLPSDWEP 265
Cdd:cd01747 111 getllleateatnsalplnfteDALQSRLFK--------RFPpdLLKSLATEPL-TMNNHRYGIspenfTENGLLSDFFN 181
|
170 180 190
....*....|....*....|....*....|....*
gi 86450111 266 -LFTNANDNTNEGII---HKTKPYLSVQFHPEHTA 296
Cdd:cd01747 182 vLTTNDDWNGVEFIStveAYKYPIYGVQWHPEKNA 216
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
200-293 |
1.89e-06 |
|
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.
Pssm-ID: 429620 [Multi-domain] Cd Length: 219 Bit Score: 50.33 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 200 DKPIFGICLGHQLLSTAIGCKTF---KMKYGNRGHNLPC----------IHHGTGRCF--MTSQN-------HGFAVEss 257
Cdd:pfam07722 105 GKPILGICRGFQLLNVALGGTLYqdiQEQPGFTDHREHCqvapyapshaVNVEPGSLLasLLGSEefrvnslHHQAID-- 182
|
90 100 110
....*....|....*....|....*....|....*...
gi 86450111 258 TLPSDWEPLFTnANDNTNEGIIHK--TKPYLSVQFHPE 293
Cdd:pfam07722 183 RLAPGLRVEAV-APDGTIEAIESPnaKGFALGVQWHPE 219
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
991-1150 |
2.14e-06 |
|
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: 51.23 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 991 SPDSIDNAENRFKFSRMLDRKGILQPRWKELTDLKAAIEFCEEVGYPCLVRPS---------YVLSGAAmnvaysnqDLE 1061
Cdd:COG0026 80 GPEALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRrggydgkgqVVIKSAA--------DLE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1062 TYLNAASLVskeyPVVISKFLQEAKEIDVDAV-AADGEILCMAVsehVENagVH-SGDATLVTPPQDINAETLLKIKEIA 1139
Cdd:COG0026 152 AAWAALGGG----PCILEEFVPFERELSVIVArSPDGEVATYPV---VEN--VHrNGILDESIAPARISEALAAEAEEIA 222
|
170
....*....|.
gi 86450111 1140 RDLAALLDVTG 1150
Cdd:COG0026 223 KRIAEALDYVG 233
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
1011-1150 |
5.82e-06 |
|
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: 48.47 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1011 KGILQPRWKELTDLKAAiEFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAAslVSKEYPVVISKFLqEAKEIDV 1090
Cdd:pfam07478 13 VTFTRADWKLNPKEWCA-QVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEA--FQYDEKVLVEEGI-EGREIEC 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86450111 1091 dAVAADGEILCMAVSEHVENAGV------HSGDATLVTPPQDINAETLLKIKEIARDLAALLDVTG 1150
Cdd:pfam07478 89 -AVLGNEDPEVSPVGEIVPSGGFydyeakYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRG 153
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
448-572 |
1.52e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 49.21 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 448 KKYNVKVMGtPIQSIIETEDRKIFSDRV-AEIGEKVAPSV--AVYSIRQALDAAEKLEYPVMARAAFSLGGLGSGFANNK 524
Cdd:PRK08654 96 EKAGIVFIG-PSSDVIEAMGSKINAKKLmKKAGVPVLPGTeeGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSE 174
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 86450111 525 EELE--VLAKQALAHSN----QLIIDKSLRGWKEVEYEVVRDAYDNCITVCNME 572
Cdd:PRK08654 175 EELEdaIESTQSIAQSAfgdsTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRE 228
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
991-1169 |
1.86e-05 |
|
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: 48.11 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 991 SPDSIDNAENRFKFSRMLDRKGILQPRWKELTDLKAAIEFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASLV 1070
Cdd:TIGR00768 79 SSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQAAESLLEHFEQL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1071 SKEYPV-VISKFLQEAKEIDVDAVAADGEIL-CMA--VSEHVEnAGVHSGDATLVTPPQDINAETLLKIKEIARDLAALL 1146
Cdd:TIGR00768 159 NGPQNLfLVQEYIKKPGGRDIRVFVVGDEVVaAIYriTSGHWR-SNLARGGKAEPCSLTEEIEELAIKAAKALGLDVAGV 237
|
170 180
....*....|....*....|...
gi 86450111 1147 DvtgpfnmqLIAKNNELKVIECN 1169
Cdd:TIGR00768 238 D--------LLESEDGLLVNEVN 252
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
988-1094 |
1.91e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 48.83 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 988 LGTSPDSIDNAENRFKFSRMLDRKG--ILQPRWKELTDLKAAIEFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLN 1065
Cdd:PRK08654 103 IGPSSDVIEAMGSKINAKKLMKKAGvpVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIE 182
|
90 100 110
....*....|....*....|....*....|...
gi 86450111 1066 AASLVSKEY----PVVISKFLQEAKEIDVDAVA 1094
Cdd:PRK08654 183 STQSIAQSAfgdsTVFIEKYLEKPRHIEIQILA 215
|
|
| PfpI |
TIGR01382 |
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ... |
165-216 |
6.77e-05 |
|
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has been solved to 2 Angstrom resolution. It is an ATP-independent intracellular protease that crystallizes as a hexameric ring. Cys-101 is proposed as the active site residue in a catalytic triad with the adjacent His-102 and a Glu residue from an adjacent monomer. A member of this family from Bacillus subtilis, GSP18, has been shown to be expressed in response to several forms of stress. A role in the degradation of small peptides has been suggested. A closely related family consists of the thiamine biosynthesis protein ThiJ and its homologs. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273591 [Multi-domain] Cd Length: 166 Bit Score: 44.72 E-value: 6.77e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 86450111 165 LNPNEFDGLFISNGPGDPVVCKNT-VIEIQKVLKSSDKPIFGICLGHQLLSTA 216
Cdd:TIGR01382 56 VNPEEYDALVIPGGRAPEYLRLNNkAVRLVREFVEKGKPVAAICHGPQLLISA 108
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
490-640 |
7.92e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 46.63 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 490 SIRQALDAAEKLEYPVMARAAFSLGGLGSGFANNKEELE-----VLAKQALAH-SNQLIIDKSLRGWKEVEYEVVRDAYD 563
Cdd:PRK07178 139 DLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELEqnfprVISEATKAFgSAEVFLEKCIVNPKHIEVQILADSHG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 564 NCITV----CNMENldplgiHTGESIVVAPSQTLSNREYNMLRTTAIKVIRHFGVIGECNIQYALNPEsDQYYIIEVNAR 639
Cdd:PRK07178 219 NVVHLferdCSIQR------RNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDAD-GEVYFMEMNTR 291
|
.
gi 86450111 640 L 640
Cdd:PRK07178 292 V 292
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
487-739 |
1.44e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 45.86 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 487 AVYSIRQALDAAEKLEYPVMARAAFSLGGLGSGFANNKEELEVLAKQALAHS------NQLIIDKSLRGWKEVEYEVVRD 560
Cdd:PRK05586 137 EIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAkaafgdDSMYIEKFIENPKHIEFQILGD 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 561 AYDNCITV----CNMENldplgiHTGESIVVAPSQTLSNREYNMLRTTAIKVIRHFGVIGECNIQYALNpESDQYYIIEV 636
Cdd:PRK05586 217 NYGNVVHLgerdCSLQR------RNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLD-KDGNFYFMEM 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 637 NARLSRSSALASKATGYPLAY----VAAKLSLAIPLPSIKnsVTGVTTACFEPSLDYCVVKMPRWDLAKF--------VR 704
Cdd:PRK05586 290 NTRIQVEHPITEMITGVDLVKeqikIAYGEKLSIKQEDIK--INGHSIECRINAEDPKNGFMPCPGKIEElyipgglgVR 367
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 86450111 705 VSKTIGS---------SMksVGEVMAIGRNFEEAFQKALRMVDE 739
Cdd:PRK05586 368 VDSAVYSgytippyydSM--IGKLIVYGKDREEAIQKMKRALGE 409
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
487-640 |
1.63e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 45.56 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 487 AVYSIRQALDAAEKLEYPVMARAAFSLGGLGSGFANNKEELEVLAKQA-----LAHSN-QLIIDKSLRGWKEVEYEVVRD 560
Cdd:PRK08591 137 PVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMAraeakAAFGNpGVYMEKYLENPRHIEIQVLAD 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 561 AYDNcitvcnmenldplGIHTGE---SI------VV--APSQTLSNREYNMLRTTAIKVIRHFGVIGECNIQYaLNPESD 629
Cdd:PRK08591 217 GHGN-------------AIHLGErdcSLqrrhqkVLeeAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEF-LYEKNG 282
|
170
....*....|.
gi 86450111 630 QYYIIEVNARL 640
Cdd:PRK08591 283 EFYFIEMNTRI 293
|
|
| PRK14570 |
PRK14570 |
D-alanyl-alanine synthetase A; Provisional |
1032-1139 |
4.49e-04 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173034 [Multi-domain] Cd Length: 364 Bit Score: 44.05 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86450111 1032 EEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAAslVSKEYPVVISKFLqEAKEIDVDAVAAD-------GEILCMAV 1104
Cdd:PRK14570 168 EVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEA--FKYDLTVVIEKFI-EAREIECSVIGNEqikiftpGEIVVQDF 244
|
90 100 110
....*....|....*....|....*....|....*..
gi 86450111 1105 SEHVENA--GVHSGDATLVTPPQDINAETLLKIKEIA 1139
Cdd:PRK14570 245 IFYDYDAkySTIPGNSIVFNIPAHLDTKHLLDIKEYA 281
|
|
| PRK08250 |
PRK08250 |
glutamine amidotransferase; Provisional |
166-220 |
6.58e-04 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181323 [Multi-domain] Cd Length: 235 Bit Score: 42.65 E-value: 6.58e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86450111 166 NPNEFDGLFISNGPGDPVVCK------NTVIEIQKVLK--SSDKPIFGICLGHQLLSTAIGCK 220
Cdd:PRK08250 42 NADGFDLLIVMGGPQSPRTTReecpyfDSKAEQRLINQaiKAGKAVIGVCLGAQLIGEALGAK 104
|
|
| LysX_arch |
TIGR02144 |
Lysine biosynthesis enzyme LysX; The family of proteins found in this equivalog include the ... |
991-1064 |
7.85e-03 |
|
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: 39.69 E-value: 7.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86450111 991 SPDSIDNAENRFKFSRMLDRKGILQPRWKELTDLKAAIEFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYL 1064
Cdd:TIGR02144 78 SSHAIEACGDKIFTYLKLAKAGVPTPRTYLAFDREAALKAAEALGYPVVLKPVIGSWGRLVAKVRDRDEAEALL 151
|
|
| |
