|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
391-1377 |
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: 1630.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 391 PPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPD 470
Cdd:TIGR01369 4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 471 GVLLTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGY 550
Cdd:TIGR01369 84 AILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 551 PVLVRAAFALGGLGSGFASNREELSALVAPAFAHT--SQVLVDKSLKGWKEIEYEVVRDAYGNCVT-------------- 614
Cdd:TIGR01369 164 PVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITvcnmenfdpmgvht 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 615 -------------------------------------------------YYIIEVNARLSRSSALASKATGYPLAYVAAK 645
Cdd:TIGR01369 244 gdsivvapsqtltdkeyqmlrdasikiirelgieggcnvqfalnpdsgrYYVIEVNPRVSRSSALASKATGYPIAKVAAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 646 LALGIPLPELRNSVTGGT-AAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENC 724
Cdd:TIGR01369 324 LAVGYTLDELKNPVTGTTpASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 725 VGFDHT---VKPVSD--MELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHRGQPLPPDL 799
Cdd:TIGR01369 404 TGFDLPdreVEPDEDlwRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTDLDPEL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 800 LQQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRT-PHVLVLGSG 878
Cdd:TIGR01369 484 LRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDkKKVLVLGSG 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 879 VYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPN 958
Cdd:TIGR01369 564 PNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPL 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 959 NMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVA 1038
Cdd:TIGR01369 644 NLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1039 YTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVASDGVVAAIAISEHVENAGVHSGDATLVTPPQDITAKTLER 1118
Cdd:TIGR01369 724 YNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDR 803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1119 IKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVG--LMTGSGVV 1196
Cdd:TIGR01369 804 IKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGvgKEKEPKYV 883
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1197 GVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIGSYKNKSELLPTVRLLESLG 1276
Cdd:TIGR01369 884 AVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLAEKG 963
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1277 YSLYASLGTADFYTEHGVKVTAVDWHFEEAvdgecppqRSILEQLAEKNFELVINLSMRGAGgrrlssFVTKGYRTRRLA 1356
Cdd:TIGR01369 964 YKLYATEGTAKFLGEAGIKPELVLKVSEGR--------PNILDLIKNGEIELVINTTSKGAG------TATDGYKIRREA 1029
|
1050 1060
....*....|....*....|.
gi 578803167 1357 ADFSVPLIIDIKCTKLFVEAL 1377
Cdd:TIGR01369 1030 LDYGVPLITTLNTAEAFAEAL 1050
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
394-1377 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1281.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 394 RKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVL 473
Cdd:PRK05294 8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 474 LTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVL 553
Cdd:PRK05294 88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 554 VRAAFALGGLGSGFASNREELSALVAPAFAH--TSQVLVDKSLKGWKEIEYEVVRDAYGNCVT----------------- 614
Cdd:PRK05294 168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLspVTEVLIEESLLGWKEYEYEVMRDKNDNCIIvcsienidpmgvhtgds 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 615 -----------------------------------------------YYIIEVNARLSRSSALASKATGYPLAYVAAKLA 647
Cdd:PRK05294 248 itvapaqtltdkeyqmlrdasiaiireigvetggcnvqfalnpkdgrYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 648 LGIPLPELRNSVTGGT-AAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCVG 726
Cdd:PRK05294 328 VGYTLDEIKNDITGKTpASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 727 FDHTVKPVSDME-----LETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHrGQPLPPDLLQ 801
Cdd:PRK05294 408 LDEDLFEEESLEelreeLKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKEN-GLPLDAELLR 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 802 QAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRTPHVLVLGSGVYR 881
Cdd:PRK05294 487 EAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVLGSGPNR 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 882 IGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNNMA 961
Cdd:PRK05294 567 IGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPLKLA 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 962 MALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTD 1041
Cdd:PRK05294 647 KALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDE 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1042 GDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVaSDGVVAAIA-ISEHVENAGVHSGDATLVTPPQDITAKTLERIK 1120
Cdd:PRK05294 727 EELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAI-CDGEDVLIGgIMEHIEEAGVHSGDSACSLPPQTLSEEIIEEIR 805
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1121 AIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVGLMTG--SGVVGV 1198
Cdd:PRK05294 806 EYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGliPPYVAV 885
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1199 KVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKK-NILLTIgSYKNKSELLPTVRLLESLGY 1277
Cdd:PRK05294 886 KEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSV-RDRDKEEVVELAKRLLELGF 964
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1278 SLYASLGTADFYTEHGVKVTAVDWHFEEAVDgecppqrsILEQLAEKNFELVINlSMRGAGGRRlssfvtKGYRTRRLAA 1357
Cdd:PRK05294 965 KILATSGTAKFLREAGIPVELVNKVHEGRPH--------IVDLIKNGEIDLVIN-TPTGRQAIR------DGFSIRRAAL 1029
|
1050 1060
....*....|....*....|
gi 578803167 1358 DFSVPLIIDIKCTKLFVEAL 1377
Cdd:PRK05294 1030 EYKVPYITTLAGARAAVKAI 1049
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
1397-1743 |
0e+00 |
|
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.
Pssm-ID: 238641 [Multi-domain] Cd Length: 344 Bit Score: 631.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1397 KLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASS 1476
Cdd:cd01316 1 RTIRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1477 ENAGTLGTVAGSAAGLKLYLNETFSELRLDSVVQWMEHFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKE 1556
Cdd:cd01316 81 TNAATVGELASEAVGLKFYLNETFSTLILDKITAWASHFNAWPSTKPIVTHAKSQTLAAVLLLASLHNRSIHICHVSSKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1557 EILLIKAAKARGLPVTCEVAPHHLFLSHDDLERlgpGKGEVRPELGSRQDVEALWENMAVIDCFASDHAPHTLEEKCGSR 1636
Cdd:cd01316 161 EINLIRLAKARGLKVTCEVSPHHLFLSQDDLPR---GQYEVRPFLPTREDQEALWENLDYIDCFATDHAPHTLAEKTGNK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1637 PPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKV 1716
Cdd:cd01316 238 PPPGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFNLPPQSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKV 317
|
330 340
....*....|....*....|....*..
gi 578803167 1717 KGTVRRVVLRGEVAYIDGQVLVPPGYG 1743
Cdd:cd01316 318 KGKVQRVVLRGETAFIDGEIVAPPGFG 344
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
875-1377 |
1.87e-175 |
|
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: 546.78 E-value: 1.87e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 875 LGSGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGG 954
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 955 QLPNNMAMALHRQQ----CRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVL 1030
Cdd:COG0458 81 QTALNLAVELEEAGilegVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1031 SGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVaSDGV--VAAIAISEHVENAGVHSGDATLVTPP 1108
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVV-RDGEdnVIIVGIMEHIEPAGVHSGDSICVAPP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1109 QDITAKTLERIKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVG 1188
Cdd:COG0458 240 QTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1189 LMTG----SGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKnILLTIGSYKNKSE 1264
Cdd:COG0458 320 NDTGfeptLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGT-VLLSLVADDDKEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1265 LLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEavdgecppQRSILEQLAEKNFELVINLSMRGAGGRRLSS 1344
Cdd:COG0458 399 ALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEG--------RPIIVDEIELEEIILVINTLLGAKSLGDSDG 470
|
490 500 510
....*....|....*....|....*....|....*....
gi 578803167 1345 F------VTKGYRTRRLAADFSVPLIIDIKCTKLFVEAL 1377
Cdd:COG0458 471 IirralaAKVPYVTTLAAAAAAALAIKAVETEAGEFEEA 509
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
1-355 |
5.50e-160 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 496.91 E-value: 5.50e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1 MAALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDemdefglckWFESSG 80
Cdd:PRK12564 4 KAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNRE---------DFESDR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 81 IHVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQNGTEPSSLP-----FLDPNA 155
Cdd:PRK12564 75 PHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLekaraFPGLLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 156 RPLVPEVSIKTPRVFNTGGA---PRILALDCGLKYNQIRCLCQRGAEVTVVPWD---HALDSQEYEGLFLSNGPGDPASY 229
Cdd:PRK12564 155 LDLVKEVSTKEPYPWPGPGGelkYKVVAIDFGVKRNILRELAERGCRVTVVPATttaEEILALNPDGVFLSNGPGDPAAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 230 PSVVSTLSRVLSEPnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWA 309
Cdd:PRK12564 235 DYAIEMIRELLEKK--IPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLE 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 578803167 310 PLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLE 355
Cdd:PRK12564 313 VTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVE 358
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
2-359 |
2.37e-158 |
|
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: 492.14 E-value: 2.37e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2 AALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDemdefglckWFESSGI 81
Cdd:TIGR01368 1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDE---------DAESKGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 82 HVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVqngTEPSSLPFL------DPNA 155
Cdd:TIGR01368 72 HVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVIS---TEDSNDEELvekarvSPDI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 156 RP--LVPEVSIKTPRVFN--TGGAPRILALDCGLKYNQIRCLCQRGAEVTVVPWDHALDS-QEYE--GLFLSNGPGDPAS 228
Cdd:TIGR01368 149 TGinLVAEVSTKEPYTWGqrGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEiKKYNpdGIFLSNGPGDPAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 229 YPSVVSTLSRVLSEpnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPA-D 307
Cdd:TIGR01368 229 VEPAIETIRKLLEK---IPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAgD 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 578803167 308 WAPLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVKE 359
Cdd:TIGR01368 306 LEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
2-358 |
1.48e-154 |
|
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: 481.83 E-value: 1.48e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2 AALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDemdefglckWFESSGI 81
Cdd:COG0505 5 ALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDE---------DFESDRP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 82 HVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQNGTEPSSL-------PFLDPn 154
Cdd:COG0505 76 WVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELlekaraaPGMEG- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 155 aRPLVPEVSIKTPRVF--NTGGAPRILALDCGLKYNQIRCLCQRGAEVTVVPWDHALD---SQEYEGLFLSNGPGDPASY 229
Cdd:COG0505 155 -LDLVKEVSTKEPYEWteAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEeilALNPDGVFLSNGPGDPAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 230 PSVVSTLSRVLSEpnPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPA-DW 308
Cdd:COG0505 234 DYAIETIRELLGK--GIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDL 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 578803167 309 APLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVK 358
Cdd:COG0505 312 EVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
|
|
| PyrB |
COG0540 |
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; ... |
1873-2178 |
2.85e-140 |
|
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; Aspartate carbamoyltransferase, catalytic subunit is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440306 [Multi-domain] Cd Length: 306 Bit Score: 439.10 E-value: 2.85e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1873 HSLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEAT 1952
Cdd:COG0540 1 MSFKMRHLLSIEDLSREEIEELLDTAEEFKEVLRPIKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSAST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1953 SSVQKGESLADSVQTMSCY-ADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITM 2031
Cdd:COG0540 81 SSVSKGESLADTIRTLEAYgADAIVIRHPQEGAARLLAEHVDVPVINAGDGAHEHPTQALLDLYTIREEFGRLDGLKVAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2032 VGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLrMPPTVRAFVAsrgtkqEEFESIEEALPDTDVLYMTRIQKERFGSTQ- 2110
Cdd:COG0540 161 VGDLKHSRVARSNIKALSKLGAEVTLVAPPTL-LPEEIEELGV------EVTTDLDEALPDADVVYMLRIQKERFTDGLf 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803167 2111 -EYEACFGQFILTPHIMTRAKKKMVVMH--PMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGR 2178
Cdd:COG0540 234 pSYREYKRSYGLTAERLALAKPDAIVMHpgPRNRGVEIDSDVDDTPRSVIFEQVTNGVAVRMALLYLLLGG 304
|
|
| pyrB |
PRK00856 |
aspartate carbamoyltransferase catalytic subunit; |
1874-2178 |
9.88e-128 |
|
aspartate carbamoyltransferase catalytic subunit;
Pssm-ID: 234849 [Multi-domain] Cd Length: 305 Bit Score: 403.68 E-value: 9.88e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1874 SLVGQHILSVQQFTKDQMSHLFNVAHTLR-MMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEAT 1952
Cdd:PRK00856 2 PLKMKHLLSIEDLSREEIELLLDTAEEFKeVLRREVKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSAST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1953 SSVQKGESLADSVQTMSCY-ADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITM 2031
Cdd:PRK00856 82 SSVSKGETLADTIRTLSAMgADAIVIRHPQSGAARLLAESSDVPVINAGDGSHQHPTQALLDLLTIREEFGRLEGLKVAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2032 VGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLrMPPTVRAFvasrgtkqEEFESIEEALPDTDVLYMTRIQKERFG---- 2107
Cdd:PRK00856 162 VGDIKHSRVARSNIQALTRLGAEVRLIAPPTL-LPEGMPEY--------GVHTDLDEVIEDADVVMMLRVQKERMDggll 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803167 2108 -STQEYeacFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGR 2178
Cdd:PRK00856 233 pSYEEY---KRSYGLTAERLALAKPDAIVMHPGPvnRGVEIASDVADGPQSVIFEQVTNGVAVRMAVLELLLGG 303
|
|
| asp_carb_tr |
TIGR00670 |
aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB ... |
1879-2177 |
5.46e-111 |
|
aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB encodes the catalytic chain of aspartate carbamoyltransferase, an enzyme of pyrimidine biosynthesis, which organizes into trimers. In some species, including E. coli and the Archaea but excluding Bacillus subtilis, a regulatory subunit PyrI is also present in an allosterically regulated hexameric holoenzyme. Several molecular weight classes of ATCase are described in MEDLINE:96303527 and often vary within taxa. PyrB and PyrI are fused in Thermotoga maritima.Ornithine carbamoyltransferases are in the same superfamily and form an outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273209 [Multi-domain] Cd Length: 301 Bit Score: 355.51 E-value: 5.46e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1879 HILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEA-TSSVQK 1957
Cdd:TIGR00670 2 HLISISDLSREEIELLLETARELEQVLNGKEPLKLLKGKILANLFFEPSTRTRLSFETAMKRLGGSVVNFSDSeTSSVAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1958 GESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKH 2037
Cdd:TIGR00670 82 GETLADTIKTLSGYVDAIVIRHPLEGAARLAAEVSEVPVINAGDGSNQHPTQTLLDLYTIYEEFGRLDGLKIALVGDLKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2038 GRTVHSLACLLTQYRVSLRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEACFG 2117
Cdd:TIGR00670 162 GRTVHSLAEALTRFGVEVYLISPEELRMPKEILEELKAKGIKVRETESLEEVIDEADVLYVTRIQKERFPDPEEYEKVKG 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2118 QFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2177
Cdd:TIGR00670 242 SYGITLERLEAAKKGVIIMHPLPRVDEIDPSVDDTPHAKYFKQAFNGVPVRMALLALLLG 301
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
1374-1747 |
6.31e-105 |
|
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439814 [Multi-domain] Cd Length: 439 Bit Score: 344.00 E-value: 6.31e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1374 VEALGQIGPAPPLKVHVDCmtSQKLVrLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPAL 1453
Cdd:COG0044 25 IAAIGPDLAAPEAAEVIDA--TGLLV-LPGLIDLHVHLREPGLEHKEDIETGTRAAAAGGVTTVVDMPNTNPVTDTPEAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1454 ALAQKLAEAGARCDFALFLGASSENAGTL----GTVAGSAAGLKLYLNETFSELRLD----------------------- 1506
Cdd:COG0044 102 EFKLARAEEKALVDVGPHGALTKGLGENLaelgALAEAGAVAFKVFMGSDDGNPVLDdgllrraleyaaefgalvavhae 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1507 --SVVQWM---EHFETWPSHLPIV-AHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHL 1580
Cdd:COG0044 182 dpDLIRGGvmnEGKTSPRLGLKGRpAEAEEEAVARDIALAEETGARLHIVHVSTAEAVELIREAKARGLPVTAEVCPHHL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1581 FLSHDDLERLGPgKGEVRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCGSRP--PPGFPGLETMLPLLLT-AV 1655
Cdd:COG0044 262 TLTDEDLERYGT-NFKVNPPLRTEEDREALWEGLAdgTIDVIATDHAPHTLEEKELPFAeaPNGIPGLETALPLLLTeLV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1656 SEGRLSLDDLLQRLHHNPRRIFHLPP----QEDTY---VEVDLEHEWTI-PSHMpFSKAHWTPFEGQKVKGTVRRVVLRG 1727
Cdd:COG0044 341 HKGRLSLERLVELLSTNPARIFGLPRkgriAVGADadlVLFDPDAEWTVtAEDL-HSKSKNTPFEGRELTGRVVATIVRG 419
|
410 420
....*....|....*....|
gi 578803167 1728 EVAYIDGQVLVPPgYGQDVR 1747
Cdd:COG0044 420 RVVYEDGEVVGEP-RGRFLR 438
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
178-354 |
1.44e-97 |
|
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: 311.74 E-value: 1.44e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 178 ILALDCGLKYNQIRCLCQRGAEVTVVPWDHALD---SQEYEGLFLSNGPGDPASYPSVVSTLSRVLSEPnpRPVFGICLG 254
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEeilKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKK--IPIFGICLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 255 HQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWAPLFTNANDGSNEGIVHNSLPFFSVQ 334
Cdd:cd01744 79 HQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQ 158
|
170 180
....*....|....*....|
gi 578803167 335 FHPEHQAGPSDMELLFDIFL 354
Cdd:cd01744 159 FHPEASPGPHDTEYLFDEFL 178
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
1398-1733 |
5.29e-92 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 305.52 E-value: 5.29e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1398 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSE 1477
Cdd:TIGR00857 35 LLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNTKPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1478 NAGTLGT------VAGSAAGL----------KLYLNETfSELRLDSVVQWMEHFE---------------TWPSHLPIVA 1526
Cdd:TIGR00857 115 NQGKELTeayelkEAGAVGRMftddgsevqdILSMRRA-LEYAAIAGVPIALHAEdpdliyggvmhegpsAAQLGLPARP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1527 -HAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGpGKGEVRPELGSRQ 1605
Cdd:TIGR00857 194 pEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKITAEVTPHHLLLSEEDVARLD-GNGKVNPPLREKE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1606 DVEALWENMA--VIDCFASDHAPHTLEEKCGSRP--PPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLP- 1680
Cdd:TIGR00857 273 DRLALIEGLKdgIIDIIATDHAPHTLEEKTKEFAaaPPGIPGLETALPLLLQLLVKGLISLKDLIRMLSINPARIFGLPd 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 578803167 1681 --PQED----TYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYID 1733
Cdd:TIGR00857 353 kgTLEEgnpaDITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1398-1733 |
9.20e-87 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 290.94 E-value: 9.20e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1398 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIiDAPA-----LALAQK-------------- 1458
Cdd:PRK09357 49 LVVAPGLVDLHVHLREPGQEDKETIETGSRAAAAGGFTTVVAMPNTKPVI-DTPEvveyvLDRAKEaglvdvlpvgaitk 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1459 ------------LAEAGARC---DfalflGASSENAGTLGTVAGSAAGLKLYLNETFSELRL-------DSVVQWMEHFE 1516
Cdd:PRK09357 128 glageeltefgaLKEAGVVAfsdD-----GIPVQDARLMRRALEYAKALDLLIAQHCEDPSLteggvmnEGEVSARLGLP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1517 TWPshlpivAHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPgKGE 1596
Cdd:PRK09357 203 GIP------AVAEEVMIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYDP-NYK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1597 VRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCG--SRPPPGFPGLETMLPLLLTA-VSEGRLSLDDLLQRLHH 1671
Cdd:PRK09357 276 VNPPLRTEEDREALIEGLKdgTIDAIATDHAPHAREEKECefEAAPFGITGLETALSLLYTTlVKTGLLDLEQLLEKMTI 355
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803167 1672 NPRRIFHLPP------QEDTYVEVDLEHEWTI-PSHMpFSKAHWTPFEGQKVKGTVRRVVLRGEVAYID 1733
Cdd:PRK09357 356 NPARILGLPAgplaegEPADLVIFDPEAEWTVdGEDF-ASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| CPSase_sm_chain |
pfam00988 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
4-138 |
1.79e-75 |
|
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: 246.47 E-value: 1.79e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 4 LVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDEMdefglckwfESSGIHV 83
Cdd:pfam00988 1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDF---------ESDKIHV 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 578803167 84 AALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKL 138
Cdd:pfam00988 72 AGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
2-138 |
1.88e-71 |
|
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: 234.96 E-value: 1.88e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2 AALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDemdefglckWFESSGI 81
Cdd:smart01097 3 AYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDE---------DFESDKI 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 578803167 82 HVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKL 138
Cdd:smart01097 74 QVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
514-653 |
7.35e-58 |
|
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: 199.45 E-value: 7.35e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 514 DRRAFAARMAEIGEHVAPSEAA--NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREELSALVAPAFAHT------ 585
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGpvETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 586 SQVLVDKSLKGWKEIEYEVVRDAYGNCVT--------------------------------------------------- 614
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITvcnrecsdqrrtqksievapsqtltdeerqmlreaavkiarhlgyvgagtv 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 578803167 615 ----------YYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 653
Cdd:pfam02786 161 efaldpfsgeYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
736-858 |
3.83e-56 |
|
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: 190.74 E-value: 3.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 736 DMELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHRGQPLPPDLLQQAKCLGFSDKQIAL 815
Cdd:smart01096 2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIAK 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 578803167 816 AVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTY 858
Cdd:smart01096 82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| OTCace_N |
pfam02729 |
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain; |
1879-2019 |
3.84e-55 |
|
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;
Pssm-ID: 460665 [Multi-domain] Cd Length: 140 Bit Score: 188.79 E-value: 3.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1879 HILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKG 1958
Cdd:pfam02729 1 HFLSLEDLSREEIEALLDLAAELKEARKRGKKLPLLKGKTVALLFEEPSTRTRVSFEVAAKRLGGHVIYLSSSDIQLSSG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803167 1959 ESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGdGVGEHPTQALLDIFTIRE 2019
Cdd:pfam02729 81 ESLADTARVLSRYVDAIVIRHFGHEDLEELAEYASVPVINAG-GDHEHPTQALADLLTIRE 140
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
1250-1375 |
6.09e-43 |
|
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases (CPS), including ammonia-dependent CPS Type I, and glutamine-dependent CPS Type III. These are multidomain proteins, in which MGS is the C-terminal domain.
Pssm-ID: 238711 [Multi-domain] Cd Length: 116 Bit Score: 152.84 E-value: 6.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1250 KNILLTIGSYkNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGEcppqRSILEQLAEKNFELV 1329
Cdd:cd01423 1 KGILISIGSY-SKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQNDK----PSLRELLAEGKIDLV 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 578803167 1330 INLSMRGAGGRRLSsfvtkGYRTRRLAADFSVPLIIDIKCTKLFVE 1375
Cdd:cd01423 76 INLPSNRGKRVLDN-----DYVMRRAADDFAVPLITNPKCAKLFIE 116
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
1401-1729 |
9.95e-08 |
|
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.
Pssm-ID: 460401 [Multi-domain] Cd Length: 334 Bit Score: 56.36 E-value: 9.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1401 LPGLIDVHVHLR--------EPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDApalalaqkLAEAGARCDFALFL 1472
Cdd:pfam01979 3 LPGLIDAHVHLEmgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEA--------LLEAAEELPLGLRF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1473 GASSENAGTLGTVAGSAA-GLKLYLNETFSELRLDSVVQ-WMEHFETWpshlpivaHAEQQTVAAVLMVAQLTQRSVHIc 1550
Cdd:pfam01979 75 LGPGCSLDTDGELEGRKAlREKLKAGAEFIKGMADGVVFvGLAPHGAP--------TFSDDELKAALEEAKKYGLPVAI- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1551 HVAR-KEEILLIKAAKARG---------------LPVTCEVAPHHLFLSHDDLERLGPGKGEVR------PELGSRQDVE 1608
Cdd:pfam01979 146 HALEtKGEVEDAIAAFGGGiehgthlevaesgglLDIIKLILAHGVHLSPTEANLLAEHLKGAGvahcpfSNSKLRSGRI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1609 ALWE--NMAVIDCFASDHAPHTleekcgsRPPPGFPGLETMlpLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTy 1686
Cdd:pfam01979 226 ALRKalEDGVKVGLGTDGAGSG-------NSLNMLEELRLA--LELQFDPEGGLSPLEALRMATINPAKALGLDDKVGS- 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 578803167 1687 VEV----DLehewtipshMPFSKAHWTPFEGQKVKGTVRRVVLRGEV 1729
Cdd:pfam01979 296 IEVgkdaDL---------VVVDLDPLAAFFGLKPDGNVKKVIVKGKI 333
|
|
| KLF1_2_4_N |
cd21972 |
N-terminal domain of Kruppel-like factor (KLF) 1, KLF2, KLF4, and similar proteins; Kruppel ... |
1752-1877 |
5.98e-04 |
|
N-terminal domain of Kruppel-like factor (KLF) 1, KLF2, KLF4, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF1, KLF2, KLF4, and similar proteins.
Pssm-ID: 409230 [Multi-domain] Cd Length: 194 Bit Score: 43.05 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1752 GAVPQLPPSAPATSEmtTTPERPRRGIPGL-PDGRFHLPPRIHRASDPGLPAVFLRPGAGiPRGSRAWAEEPKEKSSRKV 1830
Cdd:cd21972 32 VTSDNDNPPPPDPAY--PPPESPESCSTVYdSDGCHPTPNAYCGPNGPGLPGHFLLAGNS-PNLGPKIKTENQEQACMPV 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803167 1831 AEPELM-----GTPDGTCYPPPP----------VPRQASPQNLGTPGLLHPQTSPLLHSLVG 1877
Cdd:cd21972 109 AGYSGHygprePQRVPPAPPPPQyaghfqyhghFNMFSPPLRANHPGMSTVMLTPLSTPPLG 170
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
391-1377 |
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: 1630.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 391 PPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPD 470
Cdd:TIGR01369 4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 471 GVLLTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGY 550
Cdd:TIGR01369 84 AILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 551 PVLVRAAFALGGLGSGFASNREELSALVAPAFAHT--SQVLVDKSLKGWKEIEYEVVRDAYGNCVT-------------- 614
Cdd:TIGR01369 164 PVIVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITvcnmenfdpmgvht 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 615 -------------------------------------------------YYIIEVNARLSRSSALASKATGYPLAYVAAK 645
Cdd:TIGR01369 244 gdsivvapsqtltdkeyqmlrdasikiirelgieggcnvqfalnpdsgrYYVIEVNPRVSRSSALASKATGYPIAKVAAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 646 LALGIPLPELRNSVTGGT-AAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENC 724
Cdd:TIGR01369 324 LAVGYTLDELKNPVTGTTpASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 725 VGFDHT---VKPVSD--MELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHRGQPLPPDL 799
Cdd:TIGR01369 404 TGFDLPdreVEPDEDlwRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTDLDPEL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 800 LQQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRT-PHVLVLGSG 878
Cdd:TIGR01369 484 LRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFTDkKKVLVLGSG 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 879 VYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPN 958
Cdd:TIGR01369 564 PNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPL 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 959 NMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVA 1038
Cdd:TIGR01369 644 NLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1039 YTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVASDGVVAAIAISEHVENAGVHSGDATLVTPPQDITAKTLER 1118
Cdd:TIGR01369 724 YNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDR 803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1119 IKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVG--LMTGSGVV 1196
Cdd:TIGR01369 804 IKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGvgKEKEPKYV 883
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1197 GVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIGSYKNKSELLPTVRLLESLG 1276
Cdd:TIGR01369 884 AVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLAEKG 963
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1277 YSLYASLGTADFYTEHGVKVTAVDWHFEEAvdgecppqRSILEQLAEKNFELVINLSMRGAGgrrlssFVTKGYRTRRLA 1356
Cdd:TIGR01369 964 YKLYATEGTAKFLGEAGIKPELVLKVSEGR--------PNILDLIKNGEIELVINTTSKGAG------TATDGYKIRREA 1029
|
1050 1060
....*....|....*....|.
gi 578803167 1357 ADFSVPLIIDIKCTKLFVEAL 1377
Cdd:TIGR01369 1030 LDYGVPLITTLNTAEAFAEAL 1050
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
394-1377 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1281.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 394 RKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVL 473
Cdd:PRK05294 8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 474 LTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVL 553
Cdd:PRK05294 88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 554 VRAAFALGGLGSGFASNREELSALVAPAFAH--TSQVLVDKSLKGWKEIEYEVVRDAYGNCVT----------------- 614
Cdd:PRK05294 168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLspVTEVLIEESLLGWKEYEYEVMRDKNDNCIIvcsienidpmgvhtgds 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 615 -----------------------------------------------YYIIEVNARLSRSSALASKATGYPLAYVAAKLA 647
Cdd:PRK05294 248 itvapaqtltdkeyqmlrdasiaiireigvetggcnvqfalnpkdgrYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 648 LGIPLPELRNSVTGGT-AAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCVG 726
Cdd:PRK05294 328 VGYTLDEIKNDITGKTpASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 727 FDHTVKPVSDME-----LETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHrGQPLPPDLLQ 801
Cdd:PRK05294 408 LDEDLFEEESLEelreeLKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKEN-GLPLDAELLR 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 802 QAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRTPHVLVLGSGVYR 881
Cdd:PRK05294 487 EAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVLGSGPNR 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 882 IGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNNMA 961
Cdd:PRK05294 567 IGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPLKLA 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 962 MALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTD 1041
Cdd:PRK05294 647 KALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDE 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1042 GDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVaSDGVVAAIA-ISEHVENAGVHSGDATLVTPPQDITAKTLERIK 1120
Cdd:PRK05294 727 EELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAI-CDGEDVLIGgIMEHIEEAGVHSGDSACSLPPQTLSEEIIEEIR 805
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1121 AIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVGLMTG--SGVVGV 1198
Cdd:PRK05294 806 EYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGliPPYVAV 885
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1199 KVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKK-NILLTIgSYKNKSELLPTVRLLESLGY 1277
Cdd:PRK05294 886 KEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSV-RDRDKEEVVELAKRLLELGF 964
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1278 SLYASLGTADFYTEHGVKVTAVDWHFEEAVDgecppqrsILEQLAEKNFELVINlSMRGAGGRRlssfvtKGYRTRRLAA 1357
Cdd:PRK05294 965 KILATSGTAKFLREAGIPVELVNKVHEGRPH--------IVDLIKNGEIDLVIN-TPTGRQAIR------DGFSIRRAAL 1029
|
1050 1060
....*....|....*....|
gi 578803167 1358 DFSVPLIIDIKCTKLFVEAL 1377
Cdd:PRK05294 1030 EYKVPYITTLAGARAAVKAI 1049
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
394-1385 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 940.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 394 RKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVL 473
Cdd:PRK12815 8 QKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAREKPDALL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 474 LTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVL 553
Cdd:PRK12815 88 ATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAEKIGFPII 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 554 VRAAFALGGLGSGFASNREELSALVAPAFA--HTSQVLVDKSLKGWKEIEYEVVRDAYGNCVT----------------- 614
Cdd:PRK12815 168 VRPAYTLGGTGGGIAENLEELEQLFKQGLQasPIHQCLLEESIAGWKEIEYEVMRDRNGNCITvcnmenidpvgihtgds 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 615 ----------------------------------------------YYIIEVNARLSRSSALASKATGYPLAYVAAKLAL 648
Cdd:PRK12815 248 ivvapsqtltddeyqmlrsaslkiisalgvvggcniqfaldpkskqYYLIEVNPRVSRSSALASKATGYPIAKIAAKLAV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 649 GIPLPELRNSVTGGT-AAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALR--MVDENCV 725
Cdd:PRK12815 328 GYTLNELKNPVTGLTyASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRslEIKRNGL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 726 GFDHTVKPVSDMEL----ETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHRGQpLPPDLLQ 801
Cdd:PRK12815 408 SLPIELSGKSDEELlqdlRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEDGLD-LSADLLR 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 802 QAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTH-DLTFRTPHVLVLGSGVY 880
Cdd:PRK12815 487 KVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGESEaEPSSEKKKVLILGSGPI 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 881 RIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNNM 960
Cdd:PRK12815 567 RIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIVQFGGQTAINL 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 961 AMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYT 1040
Cdd:PRK12815 647 AKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYD 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1041 DGDLERFLssAAAVSKEHPVVISKFIqEAKEIDVDAVaSDGVVAAIA-ISEHVENAGVHSGDATLVTPPQDITAKTLERI 1119
Cdd:PRK12815 727 EPALEAYL--AENASQLYPILIDQFI-DGKEYEVDAI-SDGEDVTIPgIIEHIEQAGVHSGDSIAVLPPQSLSEEQQEKI 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1120 KAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMG----EEVEPVGLMTGSGV 1195
Cdd:PRK12815 803 RDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGkslaELGYPNGLWPGSPF 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1196 VGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIGSYKNKSELLPTVRLLESL 1275
Cdd:PRK12815 883 IHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGTIFISVRDEDKPEVTKLARRFAQL 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1276 GYSLYASLGTADFYTEHGVKVTAVDWHFEEavdgecppQRSILEQLAEKNFELVINLSMRGAGGRrlssfvtKGYRTRRL 1355
Cdd:PRK12815 963 GFKLLATEGTANWLAEEGITTGVVEKVQEG--------SPSLLERIKQHRIVLVVNTSLSDSASE-------DAIKIRDE 1027
|
1050 1060 1070
....*....|....*....|....*....|
gi 578803167 1356 AADFSVPLIIDIKCTKLFVEALGQIGPAPP 1385
Cdd:PRK12815 1028 ALSTHIPVFTELETAQAFLQVLESLALTTQ 1057
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
394-1377 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 772.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 394 RKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVL 473
Cdd:PLN02735 24 KKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKERPDALL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 474 LTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLG-YPV 552
Cdd:PLN02735 104 PTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDIGeFPL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 553 LVRAAFALGGLGSGFASNREELSALVAPAFA--HTSQVLVDKSLKGWKEIEYEVVRDAYGNCVT---------------- 614
Cdd:PLN02735 184 IIRPAFTLGGTGGGIAYNKEEFETICKAGLAasITSQVLVEKSLLGWKEYELEVMRDLADNVVIicsienidpmgvhtgd 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 615 ------------------------------------------------YYIIEVNARLSRSSALASKATGYPLAYVAAKL 646
Cdd:PLN02735 264 sitvapaqtltdkeyqrlrdysvaiireigvecggsnvqfavnpvdgeVMIIEMNPRVSRSSALASKATGFPIAKMAAKL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 647 ALGIPLPELRNSVTGGT-AAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCV 725
Cdd:PLN02735 344 SVGYTLDQIPNDITLKTpASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSLETGFS 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 726 GFDhtVKPVSDME---------LETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHRGQPLP 796
Cdd:PLN02735 424 GWG--CAKVKELDwdweqlkykLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSLSELS 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 797 PDLLQQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRTPHVLVLG 876
Cdd:PLN02735 502 KDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPTNKKKVLILG 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 877 SGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQL 956
Cdd:PLN02735 582 GGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQFGGQT 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 957 PNNMAMALHRQ-------------QCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCV 1023
Cdd:PLN02735 662 PLKLALPIQKYldknpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKRIGYPVV 741
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1024 VRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVA-SDGVVAAIAISEHVENAGVHSGDA 1102
Cdd:PLN02735 742 VRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALAdSEGNVVIGGIMEHIEQAGVHSGDS 821
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1103 TLVTPPQDITAKTLERIKAIVHAVGQELQVTGPFNLQL-IAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMG 1181
Cdd:PLN02735 822 ACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASLVMSG 901
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1182 ---------EEVEPVGlmtgsgvVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNI 1252
Cdd:PLN02735 902 kslkdlgftEEVIPAH-------VSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLPLSGT 974
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1253 LLTIGSYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAV-DWHfeeavdgECPPQrsILEQLAEKNFELVIN 1331
Cdd:PLN02735 975 VFISLNDLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVlKLH-------EGRPH--AGDMLANGQIQLMVI 1045
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*.
gi 578803167 1332 LSMRGAGGRRlssfvtKGYRTRRLAADFSVPLIIDIKCTKLFVEAL 1377
Cdd:PLN02735 1046 TSSGDALDQK------DGRQLRRMALAYKVPIITTVAGALATAQAV 1085
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
1397-1743 |
0e+00 |
|
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.
Pssm-ID: 238641 [Multi-domain] Cd Length: 344 Bit Score: 631.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1397 KLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASS 1476
Cdd:cd01316 1 RTIRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1477 ENAGTLGTVAGSAAGLKLYLNETFSELRLDSVVQWMEHFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKE 1556
Cdd:cd01316 81 TNAATVGELASEAVGLKFYLNETFSTLILDKITAWASHFNAWPSTKPIVTHAKSQTLAAVLLLASLHNRSIHICHVSSKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1557 EILLIKAAKARGLPVTCEVAPHHLFLSHDDLERlgpGKGEVRPELGSRQDVEALWENMAVIDCFASDHAPHTLEEKCGSR 1636
Cdd:cd01316 161 EINLIRLAKARGLKVTCEVSPHHLFLSQDDLPR---GQYEVRPFLPTREDQEALWENLDYIDCFATDHAPHTLAEKTGNK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1637 PPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKV 1716
Cdd:cd01316 238 PPPGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFNLPPQSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKV 317
|
330 340
....*....|....*....|....*..
gi 578803167 1717 KGTVRRVVLRGEVAYIDGQVLVPPGYG 1743
Cdd:cd01316 318 KGKVQRVVLRGETAFIDGEIVAPPGFG 344
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
875-1377 |
1.87e-175 |
|
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: 546.78 E-value: 1.87e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 875 LGSGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGG 954
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 955 QLPNNMAMALHRQQ----CRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVL 1030
Cdd:COG0458 81 QTALNLAVELEEAGilegVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1031 SGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVaSDGV--VAAIAISEHVENAGVHSGDATLVTPP 1108
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVV-RDGEdnVIIVGIMEHIEPAGVHSGDSICVAPP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1109 QDITAKTLERIKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVG 1188
Cdd:COG0458 240 QTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1189 LMTG----SGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKnILLTIGSYKNKSE 1264
Cdd:COG0458 320 NDTGfeptLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGT-VLLSLVADDDKEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1265 LLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEavdgecppQRSILEQLAEKNFELVINLSMRGAGGRRLSS 1344
Cdd:COG0458 399 ALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEG--------RPIIVDEIELEEIILVINTLLGAKSLGDSDG 470
|
490 500 510
....*....|....*....|....*....|....*....
gi 578803167 1345 F------VTKGYRTRRLAADFSVPLIIDIKCTKLFVEAL 1377
Cdd:COG0458 471 IirralaAKVPYVTTLAAAAAAALAIKAVETEAGEFEEA 509
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
399-877 |
6.31e-166 |
|
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: 520.59 E-value: 6.31e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 399 LGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVLLTFGG 478
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 479 QTALNCGVELTKAGVLAryGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAF 558
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 559 ALGGLGSGFASNREELSALVAPAFAH--TSQVLVDKSLKGWKEIEYEVVRDAYGNCVT---------------------- 614
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVspDHPVLIDESLLGAKEIEVDVVRDGEDNVIIvgimehiepagvhsgdsicvap 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 615 ---------------------------------------YYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPEL 655
Cdd:COG0458 239 pqtlsdkeyqrlrdatlkiaralgvvglcniqfavddgrVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDEL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 656 RNSvTGgtaaFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDencVGFDHTV--KP 733
Cdd:COG0458 319 GND-TG----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLE---IGLPGTVllSL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 734 VSD-----MELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHrgqPLPPDLLQQAKCLGF 808
Cdd:COG0458 391 VADddkeeALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEI---ILVINTLLGAKSLGD 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803167 809 SDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRTPHVLVLGS 877
Cdd:COG0458 468 SDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
1-355 |
5.50e-160 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 496.91 E-value: 5.50e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1 MAALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDemdefglckWFESSG 80
Cdd:PRK12564 4 KAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNRE---------DFESDR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 81 IHVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQNGTEPSSLP-----FLDPNA 155
Cdd:PRK12564 75 PHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLekaraFPGLLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 156 RPLVPEVSIKTPRVFNTGGA---PRILALDCGLKYNQIRCLCQRGAEVTVVPWD---HALDSQEYEGLFLSNGPGDPASY 229
Cdd:PRK12564 155 LDLVKEVSTKEPYPWPGPGGelkYKVVAIDFGVKRNILRELAERGCRVTVVPATttaEEILALNPDGVFLSNGPGDPAAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 230 PSVVSTLSRVLSEPnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWA 309
Cdd:PRK12564 235 DYAIEMIRELLEKK--IPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLE 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 578803167 310 PLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLE 355
Cdd:PRK12564 313 VTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVE 358
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
2-359 |
2.37e-158 |
|
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: 492.14 E-value: 2.37e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2 AALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDemdefglckWFESSGI 81
Cdd:TIGR01368 1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDE---------DAESKGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 82 HVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVqngTEPSSLPFL------DPNA 155
Cdd:TIGR01368 72 HVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVIS---TEDSNDEELvekarvSPDI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 156 RP--LVPEVSIKTPRVFN--TGGAPRILALDCGLKYNQIRCLCQRGAEVTVVPWDHALDS-QEYE--GLFLSNGPGDPAS 228
Cdd:TIGR01368 149 TGinLVAEVSTKEPYTWGqrGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEiKKYNpdGIFLSNGPGDPAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 229 YPSVVSTLSRVLSEpnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPA-D 307
Cdd:TIGR01368 229 VEPAIETIRKLLEK---IPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAgD 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 578803167 308 WAPLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVKE 359
Cdd:TIGR01368 306 LEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
2-358 |
1.48e-154 |
|
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: 481.83 E-value: 1.48e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2 AALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDemdefglckWFESSGI 81
Cdd:COG0505 5 ALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDE---------DFESDRP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 82 HVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQNGTEPSSL-------PFLDPn 154
Cdd:COG0505 76 WVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELlekaraaPGMEG- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 155 aRPLVPEVSIKTPRVF--NTGGAPRILALDCGLKYNQIRCLCQRGAEVTVVPWDHALD---SQEYEGLFLSNGPGDPASY 229
Cdd:COG0505 155 -LDLVKEVSTKEPYEWteAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEeilALNPDGVFLSNGPGDPAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 230 PSVVSTLSRVLSEpnPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPA-DW 308
Cdd:COG0505 234 DYAIETIRELLGK--GIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDL 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 578803167 309 APLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVK 358
Cdd:COG0505 312 EVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
|
|
| PyrB |
COG0540 |
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; ... |
1873-2178 |
2.85e-140 |
|
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; Aspartate carbamoyltransferase, catalytic subunit is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440306 [Multi-domain] Cd Length: 306 Bit Score: 439.10 E-value: 2.85e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1873 HSLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEAT 1952
Cdd:COG0540 1 MSFKMRHLLSIEDLSREEIEELLDTAEEFKEVLRPIKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSAST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1953 SSVQKGESLADSVQTMSCY-ADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITM 2031
Cdd:COG0540 81 SSVSKGESLADTIRTLEAYgADAIVIRHPQEGAARLLAEHVDVPVINAGDGAHEHPTQALLDLYTIREEFGRLDGLKVAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2032 VGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLrMPPTVRAFVAsrgtkqEEFESIEEALPDTDVLYMTRIQKERFGSTQ- 2110
Cdd:COG0540 161 VGDLKHSRVARSNIKALSKLGAEVTLVAPPTL-LPEEIEELGV------EVTTDLDEALPDADVVYMLRIQKERFTDGLf 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803167 2111 -EYEACFGQFILTPHIMTRAKKKMVVMH--PMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGR 2178
Cdd:COG0540 234 pSYREYKRSYGLTAERLALAKPDAIVMHpgPRNRGVEIDSDVDDTPRSVIFEQVTNGVAVRMALLYLLLGG 304
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
1398-1723 |
1.40e-128 |
|
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines.
Pssm-ID: 238627 [Multi-domain] Cd Length: 337 Bit Score: 407.55 E-value: 1.40e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1398 LVRLPGLIDVHVHLREPGGT-HKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASS 1476
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGGTtYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1477 EnaGTLGTVAGS----AAGLKLYLNETFSELRLDSVVQWMEHFETWPS-HLPIVAHAEqqtvaavlMVAQLTQ---RSVH 1548
Cdd:cd01302 81 G--DVTDELKKLfdagINSLKVFMNYYFGELFDVDDGTLMRTFLEIASrGGPVMVHAE--------RAAQLAEeagANVH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1549 ICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPgKGEVRPELGSRQDVEALWENMA--VIDCFASDHAP 1626
Cdd:cd01302 151 IAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGA-WGKVNPPLRSKEDREALWEGVKngKIDTIASDHAP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1627 HTLEEKC----GSRPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQED---------TYVEVDLEH 1693
Cdd:cd01302 230 HSKEEKEsgkdIWKAPPGFPGLETRLPILLTEGVKRGLSLETLVEILSENPARIFGLYPKGTiavgydadlVIVDPKKEW 309
|
330 340 350
....*....|....*....|....*....|
gi 578803167 1694 EWTIPSHMpfSKAHWTPFEGQKVKGTVRRV 1723
Cdd:cd01302 310 KVTAEEIE--SKADWTPFEGMEVTGKPVST 337
|
|
| pyrB |
PRK00856 |
aspartate carbamoyltransferase catalytic subunit; |
1874-2178 |
9.88e-128 |
|
aspartate carbamoyltransferase catalytic subunit;
Pssm-ID: 234849 [Multi-domain] Cd Length: 305 Bit Score: 403.68 E-value: 9.88e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1874 SLVGQHILSVQQFTKDQMSHLFNVAHTLR-MMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEAT 1952
Cdd:PRK00856 2 PLKMKHLLSIEDLSREEIELLLDTAEEFKeVLRREVKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSAST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1953 SSVQKGESLADSVQTMSCY-ADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITM 2031
Cdd:PRK00856 82 SSVSKGETLADTIRTLSAMgADAIVIRHPQSGAARLLAESSDVPVINAGDGSHQHPTQALLDLLTIREEFGRLEGLKVAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2032 VGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLrMPPTVRAFvasrgtkqEEFESIEEALPDTDVLYMTRIQKERFG---- 2107
Cdd:PRK00856 162 VGDIKHSRVARSNIQALTRLGAEVRLIAPPTL-LPEGMPEY--------GVHTDLDEVIEDADVVMMLRVQKERMDggll 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803167 2108 -STQEYeacFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGR 2178
Cdd:PRK00856 233 pSYEEY---KRSYGLTAERLALAKPDAIVMHPGPvnRGVEIASDVADGPQSVIFEQVTNGVAVRMAVLELLLGG 303
|
|
| PLN02527 |
PLN02527 |
aspartate carbamoyltransferase |
1878-2177 |
7.53e-127 |
|
aspartate carbamoyltransferase
Pssm-ID: 178142 [Multi-domain] Cd Length: 306 Bit Score: 401.43 E-value: 7.53e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1878 QHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEA--TSSV 1955
Cdd:PLN02527 1 SDVIEAQQFDREMLELLFEVAREMEKVERGSPGSQMLKGYLMATLFYEPSTRTRLSFESAMKRLGGEVLTTENAgeFSSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1956 QKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDL 2035
Cdd:PLN02527 81 AKGETLEDTIRTVEGYSDIIVLRHFESGAARRAAATAEIPVINAGDGPGQHPTQALLDVYTIQREIGRLDGIKVGLVGDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2036 KHGRTVHSLACLLTQYR-VSLRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFG-STQEYE 2113
Cdd:PLN02527 161 ANGRTVRSLAYLLAKYEdVKIYFVAPDVVKMKDDIKDYLTSKGVEWEESSDLMEVASKCDVLYQTRIQRERFGeRIDLYE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803167 2114 ACFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2177
Cdd:PLN02527 241 AARGKYIVDKKVMDVLPKHAVVMHPLPRLDEITTDVDSDPRAAYFRQAKNGLFIRMALLKLLLG 304
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
4-360 |
1.60e-126 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 402.35 E-value: 1.60e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 4 LVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDEmdefglckwFESSGIHV 83
Cdd:PRK12838 5 LILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINADD---------YESKQPQV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 84 AALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQNGTEPSSLPF----LDPNarpLV 159
Cdd:PRK12838 76 KGVIVYELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASITTTDDAHAFDQIkalvLPKN---VV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 160 PEVSIKTPRVFNTGGaPRILALDCGLKYNQIRCLCQRGAEVTVVPWD---HALDSQEYEGLFLSNGPGDPASYPSVVSTL 236
Cdd:PRK12838 153 AQVSTKEPYTYGNGG-KHVALIDFGYKKSILRSLSKRGCKVTVLPYDtslEEIKNLNPDGIVLSNGPGDPKELQPYLPEI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 237 SRVLSEpnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSL-PADWAPLFTNA 315
Cdd:PRK12838 232 KKLISS---YPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVDEDSLdGTPLSVRFFNV 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 578803167 316 NDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVKEA 360
Cdd:PRK12838 309 NDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMMEKA 353
|
|
| asp_carb_tr |
TIGR00670 |
aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB ... |
1879-2177 |
5.46e-111 |
|
aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB encodes the catalytic chain of aspartate carbamoyltransferase, an enzyme of pyrimidine biosynthesis, which organizes into trimers. In some species, including E. coli and the Archaea but excluding Bacillus subtilis, a regulatory subunit PyrI is also present in an allosterically regulated hexameric holoenzyme. Several molecular weight classes of ATCase are described in MEDLINE:96303527 and often vary within taxa. PyrB and PyrI are fused in Thermotoga maritima.Ornithine carbamoyltransferases are in the same superfamily and form an outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273209 [Multi-domain] Cd Length: 301 Bit Score: 355.51 E-value: 5.46e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1879 HILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEA-TSSVQK 1957
Cdd:TIGR00670 2 HLISISDLSREEIELLLETARELEQVLNGKEPLKLLKGKILANLFFEPSTRTRLSFETAMKRLGGSVVNFSDSeTSSVAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1958 GESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKH 2037
Cdd:TIGR00670 82 GETLADTIKTLSGYVDAIVIRHPLEGAARLAAEVSEVPVINAGDGSNQHPTQTLLDLYTIYEEFGRLDGLKIALVGDLKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2038 GRTVHSLACLLTQYRVSLRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEACFG 2117
Cdd:TIGR00670 162 GRTVHSLAEALTRFGVEVYLISPEELRMPKEILEELKAKGIKVRETESLEEVIDEADVLYVTRIQKERFPDPEEYEKVKG 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2118 QFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2177
Cdd:TIGR00670 242 SYGITLERLEAAKKGVIIMHPLPRVDEIDPSVDDTPHAKYFKQAFNGVPVRMALLALLLG 301
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
1374-1747 |
6.31e-105 |
|
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439814 [Multi-domain] Cd Length: 439 Bit Score: 344.00 E-value: 6.31e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1374 VEALGQIGPAPPLKVHVDCmtSQKLVrLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPAL 1453
Cdd:COG0044 25 IAAIGPDLAAPEAAEVIDA--TGLLV-LPGLIDLHVHLREPGLEHKEDIETGTRAAAAGGVTTVVDMPNTNPVTDTPEAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1454 ALAQKLAEAGARCDFALFLGASSENAGTL----GTVAGSAAGLKLYLNETFSELRLD----------------------- 1506
Cdd:COG0044 102 EFKLARAEEKALVDVGPHGALTKGLGENLaelgALAEAGAVAFKVFMGSDDGNPVLDdgllrraleyaaefgalvavhae 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1507 --SVVQWM---EHFETWPSHLPIV-AHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHL 1580
Cdd:COG0044 182 dpDLIRGGvmnEGKTSPRLGLKGRpAEAEEEAVARDIALAEETGARLHIVHVSTAEAVELIREAKARGLPVTAEVCPHHL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1581 FLSHDDLERLGPgKGEVRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCGSRP--PPGFPGLETMLPLLLT-AV 1655
Cdd:COG0044 262 TLTDEDLERYGT-NFKVNPPLRTEEDREALWEGLAdgTIDVIATDHAPHTLEEKELPFAeaPNGIPGLETALPLLLTeLV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1656 SEGRLSLDDLLQRLHHNPRRIFHLPP----QEDTY---VEVDLEHEWTI-PSHMpFSKAHWTPFEGQKVKGTVRRVVLRG 1727
Cdd:COG0044 341 HKGRLSLERLVELLSTNPARIFGLPRkgriAVGADadlVLFDPDAEWTVtAEDL-HSKSKNTPFEGRELTGRVVATIVRG 419
|
410 420
....*....|....*....|
gi 578803167 1728 EVAYIDGQVLVPPgYGQDVR 1747
Cdd:COG0044 420 RVVYEDGEVVGEP-RGRFLR 438
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
178-354 |
1.44e-97 |
|
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: 311.74 E-value: 1.44e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 178 ILALDCGLKYNQIRCLCQRGAEVTVVPWDHALD---SQEYEGLFLSNGPGDPASYPSVVSTLSRVLSEPnpRPVFGICLG 254
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEeilKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKK--IPIFGICLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 255 HQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWAPLFTNANDGSNEGIVHNSLPFFSVQ 334
Cdd:cd01744 79 HQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQ 158
|
170 180
....*....|....*....|
gi 578803167 335 FHPEHQAGPSDMELLFDIFL 354
Cdd:cd01744 159 FHPEASPGPHDTEYLFDEFL 178
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
1401-1727 |
7.64e-93 |
|
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.
Pssm-ID: 238643 [Multi-domain] Cd Length: 361 Bit Score: 306.18 E-value: 7.64e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1401 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGAS-SENA 1479
Cdd:cd01318 5 LPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGVTgSEDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1480 GTLgtVAGSAAGLKLYLNETFSELRLDsvvqwMEHFETWPSH--LPIVAHAEQQT------------------------- 1532
Cdd:cd01318 85 EEL--DKAPPAGYKIFMGDSTGDLLDD-----EETLERIFAEgsVLVTFHAEDEDrlrenrkelkgesahprirdaeaaa 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1533 --VAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARglpVTCEVAPHHLFLSHDDLERLGpGKGEVRPELGSRQDVEAL 1610
Cdd:cd01318 158 vaTARALKLARRHGARLHICHVSTPEELKLIKKAKPG---VTVEVTPHHLFLDVEDYDRLG-TLGKVNPPLRSREDRKAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1611 WENMA--VIDCFASDHAPHTLEEKCGSRP--PPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLP---PQE 1683
Cdd:cd01318 234 LQALAdgRIDVIASDHAPHTLEEKRKGYPaaPSGIPGVETALPLMLTLVNKGILSLSRVVRLTSHNPARIFGIKnkgRIA 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 578803167 1684 DTY----VEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRG 1727
Cdd:cd01318 314 EGYdadlTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| PRK08192 |
PRK08192 |
aspartate carbamoyltransferase; Provisional |
1877-2177 |
3.68e-92 |
|
aspartate carbamoyltransferase; Provisional
Pssm-ID: 169269 [Multi-domain] Cd Length: 338 Bit Score: 303.19 E-value: 3.68e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1877 GQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVL-SFSEATSSV 1955
Cdd:PRK08192 5 GSHILSVNQLDRDAIQRIFNVADRMEPYALREKRTRVLEGAILGNLFFEPSTRTRVSFGCAFNLLGGHVReTTGMASSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1956 QKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREEL----GTVNGMTITM 2031
Cdd:PRK08192 85 SKGESLYDTARVLSTYSDVIAMRHPDAGSVKEFAEGSRVPVINGGDGSNEHPTQALLDLFTIQKELahagRGIDGMHIAM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2032 VGDLKHGRTVHSLACLLTQY-RVSLRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQ 2110
Cdd:PRK08192 165 VGDLKFGRTVHSLSRLLCMYkNVSFTLVSPKELAMPDYVISDIENAGHKITITDQLEGNLDKADILYLTRIQEERFPSQE 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803167 2111 EYEACFGQFILTPHIMTR-AKKKMVVMHPMPR-----VNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2177
Cdd:PRK08192 245 EANKYRGKFRLNQSIYTQhCKSNTVIMHPLPRdsraqANELDNDLNSHPNLAIFRQADNGLLIRMALFALTLG 317
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
1398-1733 |
5.29e-92 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 305.52 E-value: 5.29e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1398 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSE 1477
Cdd:TIGR00857 35 LLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNTKPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1478 NAGTLGT------VAGSAAGL----------KLYLNETfSELRLDSVVQWMEHFE---------------TWPSHLPIVA 1526
Cdd:TIGR00857 115 NQGKELTeayelkEAGAVGRMftddgsevqdILSMRRA-LEYAAIAGVPIALHAEdpdliyggvmhegpsAAQLGLPARP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1527 -HAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGpGKGEVRPELGSRQ 1605
Cdd:TIGR00857 194 pEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKITAEVTPHHLLLSEEDVARLD-GNGKVNPPLREKE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1606 DVEALWENMA--VIDCFASDHAPHTLEEKCGSRP--PPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLP- 1680
Cdd:TIGR00857 273 DRLALIEGLKdgIIDIIATDHAPHTLEEKTKEFAaaPPGIPGLETALPLLLQLLVKGLISLKDLIRMLSINPARIFGLPd 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 578803167 1681 --PQED----TYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYID 1733
Cdd:TIGR00857 353 kgTLEEgnpaDITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| PRK11891 |
PRK11891 |
aspartate carbamoyltransferase; Provisional |
1878-2177 |
8.06e-87 |
|
aspartate carbamoyltransferase; Provisional
Pssm-ID: 183362 [Multi-domain] Cd Length: 429 Bit Score: 291.38 E-value: 8.06e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1878 QHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEAT-SSVQ 1956
Cdd:PRK11891 88 PQLLSVDQFSRDSVEALFRVADVMQPIARRQKISRVLEGAVLGNLFFEASTRTRVSFGAAFCRLGGSVCDTTGFTfSSMA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1957 KGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREE---LG-TVNGMTITMV 2032
Cdd:PRK11891 168 KGESIYDTSRVMSGYVDALVIRHPEQGSVAEFARATNLPVINGGDGPGEHPSQALLDLYTIQREfsrLGkIVDGAHIALV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2033 GDLKHGRTVHSLACLLTQYR-VSLRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGStQE 2111
Cdd:PRK11891 248 GDLKYGRTVHSLVKLLALYRgLKFTLVSPPTLEMPAYIVEQISRNGHVIEQTDDLAAGLRGADVVYATRIQKERFAD-ES 326
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803167 2112 YEACFGQFILTPHIMTRA-KKKMVVMHPMPR-----VNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2177
Cdd:PRK11891 327 FEGYTPDFQINQALVDAVcKPDTLIMHPLPRdsrpgANDLSTDLNRDPRLAIFRQTDNGIPVRMAIFAVLLG 398
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1398-1733 |
9.20e-87 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 290.94 E-value: 9.20e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1398 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIiDAPA-----LALAQK-------------- 1458
Cdd:PRK09357 49 LVVAPGLVDLHVHLREPGQEDKETIETGSRAAAAGGFTTVVAMPNTKPVI-DTPEvveyvLDRAKEaglvdvlpvgaitk 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1459 ------------LAEAGARC---DfalflGASSENAGTLGTVAGSAAGLKLYLNETFSELRL-------DSVVQWMEHFE 1516
Cdd:PRK09357 128 glageeltefgaLKEAGVVAfsdD-----GIPVQDARLMRRALEYAKALDLLIAQHCEDPSLteggvmnEGEVSARLGLP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1517 TWPshlpivAHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPgKGE 1596
Cdd:PRK09357 203 GIP------AVAEEVMIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYDP-NYK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1597 VRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCG--SRPPPGFPGLETMLPLLLTA-VSEGRLSLDDLLQRLHH 1671
Cdd:PRK09357 276 VNPPLRTEEDREALIEGLKdgTIDAIATDHAPHAREEKECefEAAPFGITGLETALSLLYTTlVKTGLLDLEQLLEKMTI 355
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803167 1672 NPRRIFHLPP------QEDTYVEVDLEHEWTI-PSHMpFSKAHWTPFEGQKVKGTVRRVVLRGEVAYID 1733
Cdd:PRK09357 356 NPARILGLPAgplaegEPADLVIFDPEAEWTVdGEDF-ASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
2-358 |
2.87e-85 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 285.15 E-value: 2.87e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2 AALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDEmdefglckwFESSGI 81
Cdd:CHL00197 7 AILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLED---------IESVKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 82 HVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLG-------------KLVQNGTEPSSL 148
Cdd:CHL00197 78 QVKGIIAKNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGcisnqnlnlsylrAKIKESPHMPSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 149 PFLDPNARPLVPEVSIKTPRVFN--------TGGAPRILALDCGLKYNQIRCLCQRGAEVTVVPWDHALD---SQEYEGL 217
Cdd:CHL00197 158 DLIPRVTTSSYYEWDEKSHPSFYladnkrphSSYQLKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQdilSYQPDGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 218 FLSNGPGDPASYPSVVSTLSRVLSEPnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLvgSGRCFLTSQNHGF 297
Cdd:CHL00197 238 LLSNGPGDPSAIHYGIKTVKKLLKYN--IPIFGICMGHQILSLALEAKTFKLKFGHRGLNHPSGL--NQQVEITSQNHGF 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803167 298 AVETDSLPADWAPL-FTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVK 358
Cdd:CHL00197 314 AVNLESLAKNKFYItHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIK 375
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
2-350 |
4.45e-76 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 259.91 E-value: 4.45e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2 AALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDemDEfglckwfESSGI 81
Cdd:PLN02771 57 ARLVLEDGSVWKAKSFGARGTQVGEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFD--DE-------ESRQC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 82 HVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLV--QNGTEPSSLPF---LDPNAR 156
Cdd:PLN02771 128 FLAGLVIRSLSISTSNWRCTKTLGDYLAERNIMGIYDVDTRAITRRLREDGSLIGVLSteDSKTDEELLKMsrsWDIVGI 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 157 PLVPEVSIKTPRV----------FNTGGAP----RILALDCGLKYNQIRCLCQRGAEVTVVP--WDhALDSQEY--EGLF 218
Cdd:PLN02771 208 DLISGVSCKSPYEwvdktnpewdFNTNSRDgesyHVIAYDFGIKHNILRRLASYGCKITVVPstWP-ASEALKMkpDGVL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 219 LSNGPGDPASYPSVVSTLSRVLSEPnprPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFA 298
Cdd:PLN02771 287 FSNGPGDPSAVPYAVETVKELLGKV---PVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYA 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 578803167 299 VETDSLPADWAPLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLF 350
Cdd:PLN02771 364 VDPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQYHPEASPGPHDSDNAF 415
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
1401-1740 |
6.29e-76 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 258.54 E-value: 6.29e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1401 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFAL-FLGASseNA 1479
Cdd:PRK04250 46 LPGLIDVHVHLRDFEESYKETIESGTKAALHGGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALnFLIAG--NC 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1480 GTLGTVagSAAGLKLYLNETFSELRLDSvvqWMEHFETWPSHLPIVAH--------------AEQQTVAAVLMVAQLTQR 1545
Cdd:PRK04250 124 EKAEEI--KADFYKIFMGASTGGIFSEN---FEVDYACAPGIVSVHAEdpelirefperppeAEVVAIERALEAGKKLKK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1546 SVHICHVARKEEILLIKaaKARGLPVTCEVAPHHLFLSHDDLERlGPgKGEVRPELGSRQDVEALWENMAVIDCFASDHA 1625
Cdd:PRK04250 199 PLHICHISTKDGLKLIL--KSNLPWVSFEVTPHHLFLTRKDYER-NP-LLKVYPPLRSEEDRKALWENFSKIPIIASDHA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1626 PHTLEEKcgSRPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPP------QEDTYVEVDLEHEWTIPS 1699
Cdd:PRK04250 275 PHTLEDK--EAGAAGIPGLETEVPLLLDAANKGMISLFDIVEKMHDNPARIFGIKNygieegNYANFAVFDMKKEWTIKA 352
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 578803167 1700 HMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPP 1740
Cdd:PRK04250 353 EELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEIIGKP 393
|
|
| CPSase_sm_chain |
pfam00988 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
4-138 |
1.79e-75 |
|
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: 246.47 E-value: 1.79e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 4 LVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDEMdefglckwfESSGIHV 83
Cdd:pfam00988 1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDF---------ESDKIHV 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 578803167 84 AALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKL 138
Cdd:pfam00988 72 AGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
1401-1747 |
1.96e-72 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 250.34 E-value: 1.96e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1401 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGAS----- 1475
Cdd:PRK02382 53 LPGGIDVHVHFREPGYTHKETWYTGSRSAAAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVTgnwdp 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1476 -----SENAGTLGTV--AGSAAGLKLYLnETFSEL-----RLDSVV--------------QWMEHFETWPSHLPI-VAHA 1528
Cdd:PRK02382 133 leslwERGVFALGEIfmADSTGGMGIDE-ELFEEAlaeaaRLGVLAtvhaededlfdelaKLLKGDADADAWSAYrPAAA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1529 EQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKarglpVTCEVAPHHLFLSHDDLERLGPgKGEVRPELGSRQDVE 1608
Cdd:PRK02382 212 EAAAVERALEVASETGARIHIAHISTPEGVDAARREG-----ITCEVTPHHLFLSRRDWERLGT-FGKMNPPLRSEKRRE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1609 ALWE--NMAVIDCFASDHAPHTLEEKCGS--RPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQ-- 1682
Cdd:PRK02382 286 ALWErlNDGTIDVVASDHAPHTREEKDADiwDAPSGVPGVETMLPLLLAAVRKNRLPLERVRDVTAANPARIFGLDGKgr 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803167 1683 -EDTY----VEVDLEHEWTIPSHMPFSKAHWTPFEGqkVKGTVRRVVL-RGEVAYIDGQVLVPPGYGQDVR 1747
Cdd:PRK02382 366 iAEGYdadlVLVDPDAAREIRGDDLHSKAGWTPFEG--MEGVFPELTMvRGTVVWDGDDINAKRGRGEFLR 434
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
2-138 |
1.88e-71 |
|
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: 234.96 E-value: 1.88e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2 AALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDemdefglckWFESSGI 81
Cdd:smart01097 3 AYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDE---------DFESDKI 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 578803167 82 HVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKL 138
Cdd:smart01097 74 QVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1379-1736 |
4.82e-71 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 246.12 E-value: 4.82e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1379 QIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPalALAQK 1458
Cdd:PRK07575 33 AIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREPGLEHKEDLFTASRACAKGGVTSFLEMPNTKPLTTTQA--ALDDK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1459 LAEAGARC--DFALFLGASSENAGTLGTVAGsAAGLKLYLNETFSELRLDSVVQWMEHF-ETwpsHLPIVAHAEQQTV-- 1533
Cdd:PRK07575 111 LARAAEKCvvNYGFFIGATPDNLPELLTANP-TCGIKIFMGSSHGPLLVDEEAALERIFaEG---TRLIAVHAEDQARir 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1534 ---------------------AAVLMVAQLT-------QRSVHICHVARKEEILLIKAAKarGLPVTCEVAPHHLFLSHD 1585
Cdd:PRK07575 187 arraefagisdpadhsqiqdeEAALLATRLAlklskkyQRRLHILHLSTAIEAELLRQDK--PSWVTAEVTPQHLLLNTD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1586 DLERLGPgKGEVRPELGSRQDVEALWENM--AVIDCFASDHAPHTLEEKCGSRP--PPGFPGLETMLPLLLTAVSEGRLS 1661
Cdd:PRK07575 265 AYERIGT-LAQMNPPLRSPEDNEALWQALrdGVIDFIATDHAPHTLEEKAQPYPnsPSGMPGVETSLPLMLTAAMRGKCT 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1662 LDDLLQRLHHNPRRIFHLP------PQEDT-YVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDG 1734
Cdd:PRK07575 344 VAQVVRWMSTAVARAYGIPnkgriaPGYDAdLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRG 423
|
..
gi 578803167 1735 QV 1736
Cdd:PRK07575 424 QV 425
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
1366-1747 |
5.81e-70 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 242.90 E-value: 5.81e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1366 DIKCTKLFVEALGQIGPAPPLKVhVDCmtsQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRP 1445
Cdd:PRK09060 24 DIGIRDGRIAAIGDLSGASAGEV-IDC---RGLHVLPGVIDSQVHFREPGLEHKEDLETGSRAAVLGGVTAVFEMPNTNP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1446 PIIDAPALALAQKLAEAGARCDFALFLGASSENAGTLGTV--AGSAAGLKLYLNETFSELRLD---SVVQWME------- 1513
Cdd:PRK09060 100 LTTTAEALADKLARARHRMHCDFAFYVGGTRDNADELAELerLPGCAGIKVFMGSSTGDLLVEddeGLRRILRngrrraa 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1514 -HFE---------------TWPSHlPIVAHAEqqtvAAVLM------VAQLTQRSVHICHVARKEEILLIKAAKARglpV 1571
Cdd:PRK09060 180 fHSEdeyrlrerkglrvegDPSSH-PVWRDEE----AALLAtrrlvrLARETGRRIHVLHVSTAEEIDFLADHKDV---A 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1572 TCEVAPHHLFLSHDDL-ERLGpGKGEVRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKcgSRP----PPGFPGL 1644
Cdd:PRK09060 252 TVEVTPHHLTLAAPECyERLG-TLAQMNPPIRDARHRDGLWRGVRqgVVDVLGSDHAPHTLEEK--AKPypasPSGMTGV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1645 ETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQ--------EDTYVeVDLEHEWTIPSHMPFSKAHWTPFEGQKV 1716
Cdd:PRK09060 329 QTLVPIMLDHVNAGRLSLERFVDLTSAGPARIFGIAGKgriavgydADFTI-VDLKRRETITNEWIASRCGWTPYDGKEV 407
|
410 420 430
....*....|....*....|....*....|.
gi 578803167 1717 KGTVRRVVLRGEVAYIDGQVLVPPGyGQDVR 1747
Cdd:PRK09060 408 TGWPVGTIVRGQRVMWDGELVGPPT-GEPVR 437
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
1390-1723 |
8.36e-70 |
|
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.
Pssm-ID: 238642 [Multi-domain] Cd Length: 374 Bit Score: 240.22 E-value: 8.36e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1390 VDCmtsQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIiDAPAL--ALAQKLAEAGARCD 1467
Cdd:cd01317 5 IDA---EGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVI-DNPAVveLLKNRAKDVGIVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1468 FAL------FLGASSENAGTL---GTVAGSAAGLKLYLNETfselrLDSVVQWMEHFEtwpshLPIVAH----------- 1527
Cdd:cd01317 81 LPIgaltkgLKGEELTEIGELleaGAVGFSDDGKPIQDAEL-----LRRALEYAAMLD-----LPIIVHpedpslagggv 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1528 ------------------AEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLER 1589
Cdd:cd01317 151 mnegkvasrlglpgippeAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDDEALES 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1590 LGPGkGEVRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCgsRP----PPGFPGLETMLPLLLT-AVSEGRLSL 1662
Cdd:cd01317 231 YDTN-AKVNPPLRSEEDREALIEALKdgTIDAIASDHAPHTDEEKD--LPfaeaPPGIIGLETALPLLWTlLVKGGLLTL 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803167 1663 DDLLQRLHHNPRRIFHLPPQEDTYVE------VDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRV 1723
Cdd:cd01317 308 PDLIRALSTNPAKILGLPPGRLEVGApadlvlFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
1398-1740 |
6.86e-64 |
|
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.
Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 225.63 E-value: 6.86e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1398 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFALFLGASS 1476
Cdd:cd01315 48 LVVMPGLIDTHVHINEPGRTEWEGFETGTKAAAAGGITTIIDMPlNSIPPTTTVENLEAKLEAAQGKLHVDVGFWGGLVP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1477 EN---------AGTLG---TVAGSAAGL-----KLYLNETFSEL-RLDSVVqwMEHFE------------------TWPS 1520
Cdd:cd01315 128 GNldqlrpldeAGVVGfkcFLCPSGVDEfpavdDEQLEEAMKELaKTGSVL--AVHAEnpeitealqeqakakgkrDYRD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1521 HL---PIVAhaEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPgKGEV 1597
Cdd:cd01315 206 YLasrPVFT--EVEAIQRILLLAKETGCRLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDVPDGGT-EFKC 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1598 RPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCGSRPP-----PGFPGLETMLPLLLT-AVSEGRLSLDDLLQRL 1669
Cdd:cd01315 283 APPIRDAANQEQLWEALEngDIDMVVSDHSPCTPELKLLGKGDffkawGGISGLQLGLPVMLTeAVNKRGLSLEDIARLM 362
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803167 1670 HHNPRRIFHLPPQEDT--------YVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPP 1740
Cdd:cd01315 363 CENPAKLFGLSHQKGRiavgydadFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDGEVVGEP 441
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
179-355 |
7.14e-61 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 207.09 E-value: 7.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 179 LALDCGL--KYNQIRCLCQRGAEVTVVPWDH---ALDSQEYEGLFLSNGPGDPASYPSVVSTLSRVLsePNPRPVFGICL 253
Cdd:pfam00117 1 LLIDNGDsfTYNLARALRELGVEVTVVPNDTpaeEILEENPDGIILSGGPGSPGAAGGAIEAIREAR--ELKIPILGICL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 254 GHQLLALAIGAKTYKM-RYGNRGHNQPC------LLVGSGRCFLTSQNHGFAVETDSLPADWAPLFTNANDGSNEGIVHN 326
Cdd:pfam00117 79 GHQLLALAFGGKVVKAkKFGHHGKNSPVgddgcgLFYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHK 158
|
170 180
....*....|....*....|....*....
gi 578803167 327 SLPFFSVQFHPEHQAGPSDMELLFDIFLE 355
Cdd:pfam00117 159 KLPIFGVQFHPESILTPHGPEILFNFFIK 187
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
514-653 |
7.35e-58 |
|
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: 199.45 E-value: 7.35e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 514 DRRAFAARMAEIGEHVAPSEAA--NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREELSALVAPAFAHT------ 585
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGpvETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 586 SQVLVDKSLKGWKEIEYEVVRDAYGNCVT--------------------------------------------------- 614
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITvcnrecsdqrrtqksievapsqtltdeerqmlreaavkiarhlgyvgagtv 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 578803167 615 ----------YYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLP 653
Cdd:pfam02786 161 efaldpfsgeYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| ArgF |
COG0078 |
Ornithine carbamoyltransferase [Amino acid transport and metabolism]; Ornithine ... |
1874-2178 |
1.47e-56 |
|
Ornithine carbamoyltransferase [Amino acid transport and metabolism]; Ornithine carbamoyltransferase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 439848 [Multi-domain] Cd Length: 310 Bit Score: 199.51 E-value: 1.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1874 SLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATS 1953
Cdd:COG0078 2 NLKGRHFLSLLDLTPEELRALLDLAAELKAKRKAGIPHRPLKGKTLAMIFEKPSTRTRVSFEVGMAQLGGHAIYLDPGDS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1954 SVQKGESLADSVQTMSCYADVVVLR-HPQPGAVELaAKHCRRPVINA-GDgvGEHPTQALLDIFTIREELGTVNGMTITM 2031
Cdd:COG0078 82 QLGRGESIKDTARVLSRYVDGIMIRtFGHETLEEL-AKYAGVPVINGlTD--LFHPCQALADLLTIREHFGKLKGLKVAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2032 VGDlkhGRTV-HSLACLLTQYRVSLRYVAPPSLRMPPTV----RAFVASRGTKQEEFESIEEALPDTDVLY------MTR 2100
Cdd:COG0078 159 VGD---GNNVaNSLLLAAAKLGMDVRIATPEGYEPDPEIvakaKEIAAESGGSITITHDPAEAVKGADVVYtdvwvsMGQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2101 iQKERfgstQEYEACFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEV-DSdPRAAYFRQAENGMYIRMALLATVLG 2177
Cdd:COG0078 236 -EEEA----EERIKAFKPYQVNEELMALAKPDAIFMHCLPahRGEEVTDEViDG-PQSVVFDEAENRLHAQKALLAWLLG 309
|
.
gi 578803167 2178 R 2178
Cdd:COG0078 310 G 310
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
736-858 |
3.83e-56 |
|
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: 190.74 E-value: 3.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 736 DMELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHRGQPLPPDLLQQAKCLGFSDKQIAL 815
Cdd:smart01096 2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIAK 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 578803167 816 AVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTY 858
Cdd:smart01096 82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| OTCace_N |
pfam02729 |
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain; |
1879-2019 |
3.84e-55 |
|
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;
Pssm-ID: 460665 [Multi-domain] Cd Length: 140 Bit Score: 188.79 E-value: 3.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1879 HILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKG 1958
Cdd:pfam02729 1 HFLSLEDLSREEIEALLDLAAELKEARKRGKKLPLLKGKTVALLFEEPSTRTRVSFEVAAKRLGGHVIYLSSSDIQLSSG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803167 1959 ESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGdGVGEHPTQALLDIFTIRE 2019
Cdd:pfam02729 81 ESLADTARVLSRYVDAIVIRHFGHEDLEELAEYASVPVINAG-GDHEHPTQALADLLTIRE 140
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
1401-1736 |
1.57e-54 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 198.17 E-value: 1.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1401 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSENAG 1480
Cdd:PRK09236 53 LPGMIDDQVHFREPGLTHKGDIASESRAAVAGGITSFMEMPNTNPPTTTLEALEAKYQIAAQRSLANYSFYFGATNDNLD 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1481 TLGTV-AGSAAGLKLY---------------LNETFSELRL---------DSVVQWMEHF-ETWPSHLPIVAHAEQQTVA 1534
Cdd:PRK09236 133 EIKRLdPKRVCGVKVFmgastgnmlvdnpetLERIFRDAPTliathcedtPTIKANLAKYkEKYGDDIPAEMHPLIRSAE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1535 AVL----MVAQLTQRS---VHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGpGKGEVRPELGSRQDV 1607
Cdd:PRK09236 213 ACYksssLAVSLAKKHgtrLHVLHISTAKELSLFENGPLAEKRITAEVCVHHLWFDDSDYARLG-NLIKCNPAIKTASDR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1608 EALWENMA--VIDCFASDHAPHTLEEKCGS--RPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLppQE 1683
Cdd:PRK09236 292 EALRQALAddRIDVIATDHAPHTWEEKQGPyfQAPSGLPLVQHALPALLELVHEGKLSLEKVVEKTSHAPAILFDI--KE 369
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803167 1684 DTY---------VEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQV 1736
Cdd:PRK09236 370 RGFiregywadlVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHNGQL 431
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
1401-1748 |
1.07e-52 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 192.99 E-value: 1.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1401 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFALFLGASSENA 1479
Cdd:PRK06189 53 FPGMIDVHVHFNEPGRTHWEGFATGSAALAAGGCTTYFDMPlNSIPPTVTREALDAKAELARQKSAVDFALWGGLVPGNL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1480 GTLGTVA-GSAAGLKLYLNETFSE-----------------LRLDSVVQWMEHFETWPSHLPIVAHAEQQT--------- 1532
Cdd:PRK06189 133 EHLRELAeAGVIGFKAFMSNSGTDefrssddltlyegmkeiAALGKILALHAESDALTRHLTTQARQQGKTdvrdylesr 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1533 -----VAAV---LMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPgKGEVRPELGSR 1604
Cdd:PRK06189 213 pvvaeLEAVqraLLYAQETGCPLHFVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDFERIGA-VAKCAPPLRSR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1605 QDVEALWENMAV--IDCFASDHAPHTLEEKCGS---RPPPGFPGLETMLPLLLT-AVSEGRLSLDDLLQRLHHNPRRIFH 1678
Cdd:PRK06189 292 SQKEELWRGLLAgeIDMISSDHSPCPPELKEGDdffLVWGGISGGQSTLLVMLTeGYIERGIPLETIARLLATNPAKRFG 371
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803167 1679 LPP-------QEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVlVPPGYGQDVRK 1748
Cdd:PRK06189 372 LPQkgrlevgADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEV-FPPPRGQLLRP 447
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
1398-1740 |
6.59e-48 |
|
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ring-opening hydrolysis. The seed members of this model are all in the vicinity of other genes involved in the processes of xanthine/urate/allantoin catabolism. Although not included in the seed, many eukaryotic homologs of this family are included above the trusted cutoff. Below the noise cutoff are related hydantoinases.
Pssm-ID: 163175 [Multi-domain] Cd Length: 443 Bit Score: 178.73 E-value: 6.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1398 LVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFALFLGASS 1476
Cdd:TIGR03178 47 LVVFPGVVDTHVHINEPGRTEWEGFETGTRAAAAGGITTYIDMPlNSIPATTTRASLEAKFEAAKGKLAVDVGFWGGLVP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1477 ENAGTLGTVAGSAA-GLKLYLN----ETFSELRLDSVVQWME-----------HFETwPSHL-----------PIVAH-- 1527
Cdd:TIGR03178 127 YNLDDLRELDEAGVvGFKAFLSpsgdDEFPHVDDWQLYKGMRelarlgqlllvHAEN-PAITsalgeeappqgGVGADay 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1528 -------AEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPgKGEVRPE 1600
Cdd:TIGR03178 206 lasrpvfAEVEAIRRTLALAKVTGCRVHVVHLSSAEAVELITEAKQEGLDVTVETCPHYLTLTAEEVPDGGT-LAKCAPP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1601 LGSRQDVEALWENMA--VIDCFASDHAPHTLEEKC--------GsrpppGFPGLETMLPLLLTAVSEGR-LSLDDLLQRL 1669
Cdd:TIGR03178 285 IRDLANQEGLWEALLngLIDCVVSDHSPCTPDLKRagdffkawG-----GIAGLQSTLDVMFDEAVQKRgLPLEDIARLM 359
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578803167 1670 HHNPRRIFHLP------PQEDT-YVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPP 1740
Cdd:TIGR03178 360 ATNPAKRFGLAqkgriaPGKDAdFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQFIGAP 437
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
1401-1741 |
2.61e-47 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 175.33 E-value: 2.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1401 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALaqKLAE--AGARCDFALFLGA--SS 1476
Cdd:PRK00369 46 LPGAIDLHVHLRGLKLSYKEDVASGTSEAAYGGVTLVADMPNTIPPLNTPEAITE--KLAEleYYSRVDYFVYSGVtkDP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1477 ENAGTLGTvagsaAGLKLYLNETfseLRLDSVVQWMEhfetwpSHLPIVAHAEQQTV--------------AAVLMVAQL 1542
Cdd:PRK00369 124 EKVDKLPI-----AGYKIFPEDL---EREETFRVLLK------SRKLKILHPEVPLAlksnrklrrncwyeIAALYYVKD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1543 TQRsVHICHVARKEEILLikaAKARGLpvTCEVAPHHLFLshddlERLGPGKGEVRPELGSRQDVEALWENMAVIDCFAS 1622
Cdd:PRK00369 190 YQN-VHITHASNPRTVRL---AKELGF--TVDITPHHLLV-----NGEKDCLTKVNPPIRDINERLWLLQALSEVDAIAS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1623 DHAPHTLEEKCGSRP--PPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPpqeDTYVEVDLEHEWTIPS- 1699
Cdd:PRK00369 259 DHAPHSSFEKLQPYEvcPPGIAALSFTPPFIYTLVSKGILSIDRAVELISTNPARILGIP---YGEIKEGYRANFTVIQf 335
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 578803167 1700 -----HMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPG 1741
Cdd:PRK00369 336 edwrySTKYSKVIETPLDGFELKASVYATIVQGKLAYLEGEVFPVKG 382
|
|
| pyrB |
PRK13814 |
aspartate carbamoyltransferase; |
1879-2178 |
3.17e-46 |
|
aspartate carbamoyltransferase;
Pssm-ID: 139876 [Multi-domain] Cd Length: 310 Bit Score: 169.90 E-value: 3.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1879 HILSVQQFTKDQMSHLFNVA-HTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQK 1957
Cdd:PRK13814 7 HLLNMRSLTRDHIEKLIQRAnYFLTQGMEKNSVFETLKGHVVANLFFEPSTRTRNSFEIAAKRLGAMVLNPNLKISAISK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1958 GESLADSVQTMSCYA-DVVVLRHPQPGAVELAAKHCRRPV-INAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDL 2035
Cdd:PRK13814 87 GETLFDTIKTLEAMGvYFFIVRHSENETPEQIAKQLSSGVvINAGDGNHQHPSQALIDLMTIKQHKPHWNKLCVTIIGDI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2036 KHGRTVHSLA-CLLTQYRVSLRYVAPPSLrMPPTVrafvasRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEA 2114
Cdd:PRK13814 167 RHSRVANSLMdGLVTMGVPEIRLVGPSSL-LPDKV------GNDSIKKFTELKPSLLNSDVIVTLRLQKERHDNSVDIDA 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578803167 2115 CFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGR 2178
Cdd:PRK13814 240 FRGSFRLTPEKLYSAKPDAIVMHPGPvnREVEINSDVADNQQSVILQQVRNGVAMRMAVLELFLLR 305
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
1401-1748 |
5.65e-46 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 171.96 E-value: 5.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1401 LPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSENAG 1480
Cdd:PRK01211 45 LPAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMPNNNIPIKDYNAFSDKLGRVAPKAYVDFSLYSMETGNNAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1481 TLGTVagsAAGLKLYLNETFSELRLDSVVQWMEHFETwpSHLPIVAHAEQQ------------------------TVAAV 1536
Cdd:PRK01211 125 ILDER---SIGLKVYMGGTTNTNGTDIEGGEIKKINE--ANIPVFFHAELSeclrkhqfesknlrdhdlarpiecEIKAV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1537 LMVAQLTQRSVHICHVARKEEIllikaakargLPVTCEVAPHHLFLsHDDLErLGpGKGEVRPELGSRQDVEALWENM-- 1614
Cdd:PRK01211 200 KYVKNLDLKTKIIAHVSSIDVI----------GRFLREVTPHHLLL-NDDMP-LG-SYGKVNPPLRDRWTQERLLEEYis 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1615 AVIDCFASDHAPHTLEEKCG-SRPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQ--EDTY----V 1687
Cdd:PRK01211 267 GRFDILSSDHAPHTEEDKQEfEYAKSGIIGVETRVPLFLALVKKKILPLDVLYKTAIERPASLFGIKKGkiEEGYdadfM 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803167 1688 EVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTvRRVVLRGEVAyIDGQVLVPPGYGQDVRK 1748
Cdd:PRK01211 347 AFDFTNIKKINDKRLHSKCPVSPFNGFDAIFP-SHVIMRGEVV-IDNYELISERTGKFVPK 405
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
1376-1743 |
1.53e-44 |
|
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.
Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 168.94 E-value: 1.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1376 ALGQ-IGPAPPLKVhVDCmtSQKLVrLPGLIDVHVHLREP--GGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPA 1452
Cdd:cd01314 28 AIGPnLEAPGGVEV-IDA--TGKYV-LPGGIDPHTHLELPfmGTVTADDFESGTRAAAAGGTTTIIDFAIPNKGQSLLEA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1453 LALAQKLAEAGARCDFALFLGASSENAGT---LGTVAgsAAGL---KLYLneTFSELRLDSVVQWMEHFETWPSH--LPI 1524
Cdd:cd01314 104 VEKWRGKADGKSVIDYGFHMIITDWTDSVieeLPELV--KKGIssfKVFM--AYKGLLMVDDEELLDVLKRAKELgaLVM 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1525 VaHAEQQTVAAVL--------------------------------MVAQLTQRSVHICHVARKEEILLIKAAKARGLPVT 1572
Cdd:cd01314 180 V-HAENGDVIAELqkkllaqgktgpeyhalsrppeveaeataraiRLAELAGAPLYIVHVSSKEAADEIARARKKGLPVY 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1573 CEVAPHHLFLSHDDLERLGP-GKGEV-RPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCGSRP-----PPGFPG 1643
Cdd:cd01314 259 GETCPQYLLLDDSDYWKDWFeGAKYVcSPPLRPKEDQEALWDGLSsgTLQTVGSDHCPFNFAQKARGKDdftkiPNGVPG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1644 LETMLPLLLTA-VSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVE--------VDLEHEWTIPSHMPFSKAHWTPFEGQ 1714
Cdd:cd01314 339 VETRMPLLWSEgVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVgsdadlviWDPNAEKTISADTHHHNVDYNIFEGM 418
|
410 420
....*....|....*....|....*....
gi 578803167 1715 KVKGTVRRVVLRGEVAYIDGQVLVPPGYG 1743
Cdd:cd01314 419 KVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| PRK00779 |
PRK00779 |
ornithine carbamoyltransferase; Provisional |
1874-2176 |
1.52e-43 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 234835 [Multi-domain] Cd Length: 304 Bit Score: 161.80 E-value: 1.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1874 SLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATS 1953
Cdd:PRK00779 1 MLMGRHFLSLDDLSPEELEELLDLAAELKKKRKAGEPHPPLKGKTLAMIFEKPSTRTRVSFEVGMAQLGGHAIFLSPRDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1954 SVQKGESLADSVQTMSCYADVVVLR-HPQPGAVELaAKHCRRPVINA-GDgvGEHPTQALLDIFTIREELGTVNGMTITM 2031
Cdd:PRK00779 81 QLGRGEPIEDTARVLSRYVDAIMIRtFEHETLEEL-AEYSTVPVINGlTD--LSHPCQILADLLTIYEHRGSLKGLKVAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2032 VGDlkhGRTV-HSLACLLTQYRVSLRYVAPPSLRMPPTVRAFVA-SRGTKQEEFESIEEALPDTDVLY------Mtriqk 2103
Cdd:PRK00779 158 VGD---GNNVaNSLLLAAALLGFDLRVATPKGYEPDPEIVEKIAkETGASIEVTHDPKEAVKGADVVYtdvwvsM----- 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578803167 2104 erfGSTQEYE---ACFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVL 2176
Cdd:PRK00779 230 ---GQEAEAEerlKAFAPYQVNEELMALAKPDAIFMHCLPahRGEEVTDEVIDGPQSVVWDEAENRLHAQKALLAWLL 304
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
1250-1375 |
6.09e-43 |
|
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases (CPS), including ammonia-dependent CPS Type I, and glutamine-dependent CPS Type III. These are multidomain proteins, in which MGS is the C-terminal domain.
Pssm-ID: 238711 [Multi-domain] Cd Length: 116 Bit Score: 152.84 E-value: 6.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1250 KNILLTIGSYkNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGEcppqRSILEQLAEKNFELV 1329
Cdd:cd01423 1 KGILISIGSY-SKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQNDK----PSLRELLAEGKIDLV 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 578803167 1330 INLSMRGAGGRRLSsfvtkGYRTRRLAADFSVPLIIDIKCTKLFVE 1375
Cdd:cd01423 76 INLPSNRGKRVLDN-----DYVMRRAADDFAVPLITNPKCAKLFIE 116
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
1379-1748 |
2.56e-42 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 162.56 E-value: 2.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1379 QIGP--APPLKVHV-DCmtSQKLVrLPGLIDVHVHLREP--GGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPAL 1453
Cdd:TIGR02033 28 AVGDnlIPPDAVEViDA--TGKYV-LPGGIDVHTHLEMPfgGTTTADDFFTGTKAAAAGGTTTIIDFVVPEKGSSLTEAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1454 ALAQKLAEAGARCDFALFLGASSENAGTLG-----TVAGSAAGLKLY-------------LNETFSELR----------- 1504
Cdd:TIGR02033 105 ETWHEKAEGKSVIDYGFHMDITHWNDSVLEehipeVKEEGINSFKVFmayknllmvddeeLFEILKRLKelgallqvhae 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1505 ----LDSVVQWM-EHFETWPSHLPIV--AHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAP 1577
Cdd:TIGR02033 185 ngdiIAELQARMlAQGITGPEYHALSrpPELEAEAVARAITLAALADAPLYVVHVSTKDAADEIAQARKKGQPVFGETCP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1578 HHLFLSHDDLERLG--PGKGEVRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCG------SRPPPGFPGLETM 1647
Cdd:TIGR02033 265 QYLVLDDTHYDKPGfeGAKYVCSPPLREPEDQDALWSALSsgALQTVGSDHCTFNFAQKKAigkddfTKIPNGGPGVEER 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1648 LPLLLTA-VSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVE--------VDLEHEWTIPSHMPFSKAHWTPFEGQKVKG 1718
Cdd:TIGR02033 345 MSLLFDEgVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVgsdadiviWDPNRTTVISAETHHSNADYNPFEGFKVRG 424
|
410 420 430
....*....|....*....|....*....|
gi 578803167 1719 TVRRVVLRGEVAYIDGQVLVPPGYGQDVRK 1748
Cdd:TIGR02033 425 APVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
1379-1720 |
4.40e-41 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 158.23 E-value: 4.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1379 QIGPAPPLKVHVDCmtsQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIiDAPAL--ALA 1456
Cdd:PRK07369 37 HIDPIPPDTQIIDA---SGLILGPGLVDLYSHSGEPGFEERETLASLAAAAAAGGFTRVAILPDTFPPL-DNPATlaRLQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1457 QKLAE-AGARCDF--ALFLGASSENAGTLGT-----VAGSAAGLKLylnETFSELR--LDSVVQWMEHFETWPSHL---- 1522
Cdd:PRK07369 113 QQAQQiPPVQLHFwgALTLGGQGKQLTELAElaaagVVGFTDGQPL---ENLALLRrlLEYLKPLGKPVALWPCDRslag 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1523 ----------------PIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDD 1586
Cdd:PRK07369 190 ngvmregllalrlglpGDPASAETTALAALLELVAAIGTPVHLMRISTARSVELIAQAKARGLPITASTTWMHLLLDTEA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1587 LERLGPgkgEVR--PELGSRQDVEALWENM--AVIDCFASDHAPHTLEEKCG--SRPPPGFPGLETMLPLLL-TAVSEGR 1659
Cdd:PRK07369 270 LASYDP---NLRldPPLGNPSDRQALIEGVrtGVIDAIAIDHAPYTYEEKTVafAEAPPGAIGLELALPLLWqNLVETGE 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803167 1660 LSLDDLLQRLHHNPRRIFHLPP------QEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTV 1720
Cdd:PRK07369 347 LSALQLWQALSTNPARCLGQEPpslapgQPAELILFDPQKTWTVSAQTLHSLSRNTPWLGQTLKGRV 413
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
1397-1754 |
9.16e-41 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 158.03 E-value: 9.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1397 KLVrLPGLIDVHVHLREP-GGTH-KEDFASGTAAALAGGITMVC--AMPNTRPPIIDApaLALAQKLAEAGARCD--FAL 1470
Cdd:PRK08323 45 KYV-MPGGIDPHTHMEMPfGGTVsSDDFETGTRAAACGGTTTIIdfALQPKGQSLREA--LEAWHGKAAGKAVIDygFHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1471 FLGASSENAGT-LGTVAgsAAG---LKLYLN-------------ETFSELR-LDSVVqwMEHFE---------------- 1516
Cdd:PRK08323 122 IITDWNEVVLDeMPELV--EEGitsFKLFMAykgalmldddellRALQRAAeLGALP--MVHAEngdaiaylqakllaeg 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1517 -TWPSHLPIV--AHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPG 1593
Cdd:PRK08323 198 kTGPEYHALSrpPEVEGEATNRAIMLAELAGAPLYIVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWF 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1594 KGEVR---PELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCG------SRPPPGFPGLETMLPLLLTA-VSEGRLS 1661
Cdd:PRK08323 278 EGAKYvmsPPLRDKEHQDALWRGLQdgDLQVVATDHCPFCFEQKKQlgrgdfTKIPNGTPGVEDRMPLLFSEgVMTGRIT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1662 LDDLLQRLHHNPRRIFHLPPQEDTyVEV---------DLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYI 1732
Cdd:PRK08323 358 LNRFVELTSTNPAKIFGLYPRKGT-IAVgadadiviwDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVE 436
|
410 420
....*....|....*....|..
gi 578803167 1733 DGQVLVPPGYGQDVRKWPQGAV 1754
Cdd:PRK08323 437 DGEFRGKAGHGRFLKRKPFQAV 458
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
1397-1783 |
2.58e-38 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 151.39 E-value: 2.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1397 KLVrLPGLIDVHVHLREPGGT---HKEDFASGTAAALAGGITMVC--AMPNTRPPIIDApaLALAQKLAEAGARCDFALF 1471
Cdd:PRK13404 50 RLV-LPGGVDSHCHIDQPSGDgimMADDFYTGTVSAAFGGTTTVIpfAAQHRGQSLREA--VEDYHRRAAGKAVIDYAFH 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1472 LGASSENAGTLG-----TVAGSAAGLKLYLneTFSELRLDS-------------------------VVQWM-----EHFE 1516
Cdd:PRK13404 127 LIVADPTEEVLTeelpaLIAQGYTSFKVFM--TYDDLKLDDrqildvlavarrhgamvmvhaenhdMIAWLtkrllAAGL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1517 TWPSH----LPIVAHAEQQTVAAVLmvAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERlgP 1592
Cdd:PRK13404 205 TAPKYhaisRPMLAEREATHRAIAL--AELVDVPILIVHVSGREAAEQIRRARGRGLKIFAETCPQYLFLTAEDLDR--P 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1593 G----KGEVRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCGSRP----------PPGFPGLETMLPLLLTA-V 1655
Cdd:PRK13404 281 GmegaKYICSPPPRDKANQEAIWNGLAdgTFEVFSSDHAPFRFDDTDGKLAaganpsfkaiANGIPGIETRLPLLFSEgV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1656 SEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYV---EVDL-----EHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRG 1727
Cdd:PRK13404 361 VKGRISLNRFVALTSTNPAKLYGLYPRKGAIAigaDADIaiwdpDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRG 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 578803167 1728 EVAYIDGQVLVPPGYGQDVRKwpqgavpqlppsapatsemtTTPERPRRGIPGLPD 1783
Cdd:PRK13404 441 RVVVEDGELVAERGSGQFLAR--------------------SLPDRARPNGRLEPE 476
|
|
| OTCace |
pfam00185 |
Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain; |
2028-2175 |
3.01e-38 |
|
Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain;
Pssm-ID: 425511 [Multi-domain] Cd Length: 154 Bit Score: 140.82 E-value: 3.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2028 TITMVGDlKHGRTVHSLACLLTQYRVSLRYVAPPSLRMPPTV----RAFVASRGTKQEEFESIEEALPDTDVLYMTRIQ- 2102
Cdd:pfam00185 1 KIAYVGD-GHNNVAHSLIIAAAKLGMDVRLATPKGYPPDPEVldkaKKIAEKSGGSIEITDDPAEAVKGADVVYTDVWQs 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803167 2103 ----KERFgstQEYEAcFGQFILTPHIMTRAKKKMVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATV 2175
Cdd:pfam00185 80 mgqeKERE---ERLKA-FKPYQVNEELMKLAKKDAIFMHCLPahRGEEVTDDVFDGPRSVVFDQAENRLHAQKALLALL 154
|
|
| pyrB |
PRK13376 |
bifunctional aspartate carbamoyltransferase catalytic subunit/aspartate carbamoyltransferase ... |
1874-2177 |
7.68e-35 |
|
bifunctional aspartate carbamoyltransferase catalytic subunit/aspartate carbamoyltransferase regulatory subunit; Provisional
Pssm-ID: 237369 [Multi-domain] Cd Length: 525 Bit Score: 141.82 E-value: 7.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1874 SLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLD---ILKGKV-MASMFYEVSTRTSSSFA-AAMARLGGAVLSF 1948
Cdd:PRK13376 4 DFLGRTLAVIEDLSVEEQLFLYEKTRELKQRWYEGEDVSefrIKKRDVgIYIVFVEPSTRTKESFInAAKFHKNVKVNIF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1949 SEATSSVQKGESLADSVQTMSCYAD--VVVLRHPQPG--------AVELAAKH-CRRPV-INAGDGVGEHPTQALLDIFT 2016
Cdd:PRK13376 84 DSEHSSFNKQESYTDTFNMLTGYSDysIFIVRTRLEGvcrlleekVSEFASRNgIEVPAfINAGDGKHEHPTQELLDEFT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2017 IREELGTVNG-MTITMVGDLKHGRTVHSLACLLTQYR-VSLRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTD 2094
Cdd:PRK13376 164 FLEQNNFDNSfIHIALVGDLLHGRTVHSKVNGLKIFKnVKVDLIAPEELAMPEHYVEKMKKNGFEVRIFSSIEEYLSQKD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2095 VL---YMTRIQKERFGStqeyeacfgQFILTPHIMTRA---KKKMV--------VMHPMPRVN---EISVEVDSDPRAAY 2157
Cdd:PRK13376 244 VAkiwYFTRLQLERMGE---------DILEKEHILRKAvtfRKEFLdklpegvkFYHPLPRHKvypTIPTFLDTLPLNGW 314
|
330 340
....*....|....*....|
gi 578803167 2158 FRQAENGMYIRMALLATVLG 2177
Cdd:PRK13376 315 ETQAINGYWVRIVLLSMLGG 334
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
738-814 |
2.76e-33 |
|
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: 124.03 E-value: 2.76e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803167 738 ELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHrGQPLPPDLLQQAKCLGFSDKQIA 814
Cdd:pfam02787 2 ELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEA-GLDLDAELLREAKRLGFSDRQIA 77
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
1380-1731 |
6.80e-33 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 134.03 E-value: 6.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1380 IGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIiDAPALA----- 1454
Cdd:PRK07627 33 IGQAPAGFNADKTIDASGLIVCPGLVDLSARLREPGYEYKATLESEMAAAVAGGVTSLVCPPDTDPVL-DEPGLVemlkf 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1455 LAQKLAEAGARCDFALFLGASSENAGTL------GTVAGSAAGLKLylnetfselrLDSVVQW--MEH-----FETWPSH 1521
Cdd:PRK07627 112 RARNLNQAHVYPLGALTVGLKGEVLTEMvelteaGCVGFSQANVPV----------VDTQVLLraLQYastfgFTVWLRP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1522 LPI------VAH----------------AEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHH 1579
Cdd:PRK07627 182 LDAflgrggVAAsgavasrlglsgvpvaAETIALHTIFELMRVTGARVHLARLSSAAGVALVRAAKAEGLPVTCDVGVNH 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1580 LFLSHDDLERLGPgKGEVRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKC--GSRPPPGFPGLETMLPLLLTAV 1655
Cdd:PRK07627 262 VHLIDVDIGYFDS-QFRLDPPLRSQRDREAIRAALAdgTIDAICSDHTPVDDDEKLlpFAEATPGATGLELLLPLTLKWA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1656 SEGRLSLDDLLQRLHHNPRRIFHLPPQE-------DTYVeVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGE 1728
Cdd:PRK07627 341 DEAKVPLARALARITSAPARVLGLPAGRlaegapaDLCV-FDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLVAGQ 419
|
...
gi 578803167 1729 VAY 1731
Cdd:PRK07627 420 VAF 422
|
|
| PLN02342 |
PLN02342 |
ornithine carbamoyltransferase |
1836-2177 |
1.66e-32 |
|
ornithine carbamoyltransferase
Pssm-ID: 177976 [Multi-domain] Cd Length: 348 Bit Score: 131.07 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1836 MGTPDGTCYPPPPVPRQASPQNlGTPGLLHPQTSPLLHSLVG----QHILSVQQFTKDQMSHLFNVAHTLRMMVQK-ERS 1910
Cdd:PLN02342 1 MFFSLRRARSPSAVSSSSRARR-GLVVCAASSSAAAPSPIKGkskpKHFLHIDDFDKEEILGLLDRAKEVKALLKSgDRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1911 LDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVVVLR---HPQpgAVEL 1987
Cdd:PLN02342 80 FQPFKGKSMAMIFTKPSMRTRVSFETGFFLLGGHALYLGPDDIQLGKREETRDIARVLSRYNDIIMARvfaHQD--VLDL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1988 aAKHCRRPVINAGDGVgEHPTQALLDIFTIREELGTVNGMTITMVGDlkHGRTVHSLACLLTQYRVSLRYVAPPSLRMPP 2067
Cdd:PLN02342 158 -AEYSSVPVINGLTDY-NHPCQIMADALTIIEHIGRLEGTKVVYVGD--GNNIVHSWLLLAAVLPFHFVCACPKGYEPDA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2068 TVrafvaSRGTKQEEFESIE------EALPDTDVLY------MTriQKErfgstqEYE---ACFGQFILTPHIMTRAKKK 2132
Cdd:PLN02342 234 KT-----VEKARAAGISKIEitndpaEAVKGADVVYtdvwasMG--QKE------EAEkrkKAFQGFQVNEALMKLAGPQ 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 578803167 2133 MVVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2177
Cdd:PLN02342 301 AYFMHCLPaeRGVEVTDGVMEAPNSIVFPQAENRMHAQNAIMLHQLG 347
|
|
| PLN02795 |
PLN02795 |
allantoinase |
1399-1734 |
7.04e-31 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 129.51 E-value: 7.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1399 VRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFALFLGASSE 1477
Cdd:PLN02795 96 VVMPGLIDVHVHLNEPGRTEWEGFPTGTKAAAAGGITTLVDMPlNSFPSTTSVETLELKIEAAKGKLYVDVGFWGGLVPE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1478 NA------------GTLG----------------TVAGSAAGLK---------LYLNETFSELRLDSVVQ-----WMEHF 1515
Cdd:PLN02795 176 NAhnasvleelldaGALGlksfmcpsgindfpmtTATHIKAALPvlakygrplLVHAEVVSPVESDSRLDadprsYSTYL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1516 ETWPshlpivAHAEQQTVAAVLMVAQLTQR-------SVHICHVARKEEIL-LIKAAKARGLPVTCEVAPHHLFLSHDDL 1587
Cdd:PLN02795 256 KSRP------PSWEQEAIRQLLEVAKDTRPggvaegaHVHIVHLSDAESSLeLIKEAKAKGDSVTVETCPHYLAFSAEEI 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1588 erlgpGKGEVR----PELGSRQDVEALWENMA--VIDCFASDHAPHT-----LEEKCGSRPPPGFPGLETMLPLLLTAVS 1656
Cdd:PLN02795 330 -----PDGDTRykcaPPIRDAANRELLWKALLdgDIDMLSSDHSPSPpdlklLEEGNFLRAWGGISSLQFVLPATWTAGR 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1657 EGRLSLDDLLQRLHHNPRRIFHLP------PQEDTYVEV-DLEHEWTIPSHMPFSKAH--WTPFEGQKVKGTVRRVVLRG 1727
Cdd:PLN02795 405 AYGLTLEQLARWWSERPAKLAGLDskgaiaPGKDADIVVwDPEAEFVLDESYPIYHKHksLSPYLGTKLSGKVIATFVRG 484
|
....*..
gi 578803167 1728 EVAYIDG 1734
Cdd:PLN02795 485 NLVFLEG 491
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
1390-1731 |
7.15e-30 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 125.15 E-value: 7.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1390 VDCmtsQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPpIIDAPAL---------------- 1453
Cdd:PRK09059 51 VDC---AGKAVAPGLVDARVFVGEPGAEHRETIASASRAAAAGGVTSIIMMPDTDP-VIDDVALvefvkrtardtaivni 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1454 ----ALAQKLA-----------EAGARC----------------------DFALFLGASSENAgTLGtvagsAAGLklyL 1496
Cdd:PRK09059 127 hpaaAITKGLAgeemtefgllrAAGAVAftdgrrsvantqvmrraltyarDFDAVIVHETRDP-DLG-----GNGV---M 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1497 NETFselrldsvvqwmehFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVA 1576
Cdd:PRK09059 198 NEGL--------------FASWLGLSGIPREAEVIPLERDLRLAALTRGRYHAAQISCAESAEALRRAKDRGLKVTAGVS 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1577 PHHLFLSHDDLerlgpgkGEVR------PELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKcgsRPP-----PGFPG 1643
Cdd:PRK09059 264 INHLSLNENDI-------GEYRtffklsPPLRTEDDRVAMVEAVAsgTIDIIVSSHDPQDVDTK---RLPfseaaAGAIG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1644 LETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLP-------PQEDTYVeVDLEHEWTIPSHMPFSKAHWTPFEGQKV 1716
Cdd:PRK09059 334 LETLLAAALRLYHNGEVPLLRLIEALSTRPAEIFGLPagtlkpgAPADIIV-IDLDEPWVVDPEDLKSRSKNTPFEEARF 412
|
410
....*....|....*
gi 578803167 1717 KGTVRRVVLRGEVAY 1731
Cdd:PRK09059 413 QGRVVRTIVAGKTVY 427
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
1391-1731 |
1.74e-29 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 124.20 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1391 DCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMP-NTRPPIIDAPALALAQKLAEAGARCDFA 1469
Cdd:PRK08044 42 EVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPlNQLPATVDRASIELKFDAAKGKLTIDAA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1470 LFLGASSENAGTLGTV-AGSAAGLKLYL--------NETFSELRLDSVVQWME-----------HFETWP--SHLPIVAH 1527
Cdd:PRK08044 122 QLGGLVSYNLDRLHELdEVGVVGFKCFVatcgdrgiDNDFRDVNDWQFYKGAQklgelgqpvlvHCENALicDELGEEAK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1528 AEQQTVAA-----------------VLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERL 1590
Cdd:PRK08044 202 REGRVTAHdyvasrpvfteveairrVLYLAKVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1591 GPgKGEVRPELGSRQDVEALWENM--AVIDCFASDHAPHTLEEKCGS--RPPPGFPGLETMLPLLL-TAVSEGRLSLDDL 1665
Cdd:PRK08044 282 GT-LAKCSPPIRDLENQKGMWEKLfnGEIDCLVSDHSPCPPEMKAGNimEAWGGIAGLQNCMDVMFdEAVQKRGMSLPMF 360
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578803167 1666 LQRLHHNPRRIFHL-------PPQEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAY 1731
Cdd:PRK08044 361 GKLMATNAADIFGLqqkgriaPGKDADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIY 433
|
|
| PRK14805 |
PRK14805 |
ornithine carbamoyltransferase; Provisional |
1878-2177 |
3.42e-26 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 237819 [Multi-domain] Cd Length: 302 Bit Score: 111.32 E-value: 3.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1878 QHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSldILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQK 1957
Cdd:PRK14805 2 KHLLSIKELTQQQLLDLLALAKTIKANPAEYRQ--ALAGKSVVMLFEKPSLRTRVSFDIGINKLGGHCLYLDQQNGALGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1958 GESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVgEHPTQALLDIFTIREELGTVNGMTITMVGDlkh 2037
Cdd:PRK14805 80 RESVADFAANLSCWADAIVARVFSHSTIEQLAEHGSVPVINALCDL-YHPCQALADFLTLAEQFGDVSKVKLAYVGD--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2038 GRTV-HSL----ACLLTQYRVslryVAPPSLRMPPTV----RAFVASRGTKQEEFESIeEALPDTDVLYM-TRIQKERFG 2107
Cdd:PRK14805 156 GNNVtHSLmygaAILGATMTV----ICPPGHFPDGQIvaeaQELAAKSGGKLVLTSDI-EAIEGHDAIYTdTWISMGDDT 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803167 2108 STQEYEACFGQFILTPHIMTRAKKKMvVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLG 2177
Cdd:PRK14805 231 PLAEIKAKFAPYQVNKALMEKAGATF-VMHCQPahRGVEITSEVMDGEGSLILQQAENRMHAQNAVLVTLLS 301
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
966-1184 |
1.06e-23 |
|
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: 102.64 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 966 RQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLE 1045
Cdd:COG0439 36 AEELGLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1046 RFL----SSAAAVSKEHPVVISKFIqEAKEIDVDAVASDGVVAAIAISEHvENAGVHSGDATLVTPPqDITAKTLERIKA 1121
Cdd:COG0439 116 AALaearAEAKAGSPNGEVLVEEFL-EGREYSVEGLVRDGEVVVCSITRK-HQKPPYFVELGHEAPS-PLPEELRAEIGE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803167 1122 IVHAVGQELQV-TGPFNLQ-LIAKDDQLKVIECNVRVS--RSFPFVSKTLGVDLVALATRVIMGEEV 1184
Cdd:COG0439 193 LVARALRALGYrRGAFHTEfLLTPDGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEPR 259
|
|
| PRK02102 |
PRK02102 |
ornithine carbamoyltransferase; Validated |
1875-2177 |
1.64e-23 |
|
ornithine carbamoyltransferase; Validated
Pssm-ID: 179366 [Multi-domain] Cd Length: 331 Bit Score: 104.20 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1875 LVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSS 1954
Cdd:PRK02102 5 LKGRSFLKLLDFTPEEIEYLIDLSIELKAAKKAGIEHQYLEGKNIALIFEKTSTRTRCAFEVAAIDLGAHVTYLGPNDSQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1955 VQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVgEHPTQALLDIFTIREELGTVNGMTITMVGD 2034
Cdd:PRK02102 85 LGKKESIEDTARVLGRMYDGIEYRGFKQEIVEELAKYSGVPVWNGLTDE-WHPTQMLADFMTMKEHFGPLKGLKLAYVGD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2035 lkhGR--TVHSL---ACLLTqyrVSLRYVAPPSLRMPPTV----RAFVASRGTKQEEFESIEEALPDTDVLYmTRI---- 2101
Cdd:PRK02102 164 ---GRnnMANSLmvgGAKLG---MDVRICAPKELWPEEELvalaREIAKETGAKITITEDPEEAVKGADVIY-TDVwvsm 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2102 --QKERfgstQEYEACFGQFILTPHIMTR-AKKKMVVMHPMP-----------------RVNEISV--EVDSDPRAAYFR 2159
Cdd:PRK02102 237 geEDEW----EERIKLLKPYQVNMDLMKAtGNPDVIFMHCLPafhdtetkvgkeiaekyGLKGLEVtdEVFESKYSIVFD 312
|
330
....*....|....*...
gi 578803167 2160 QAENGMYIRMALLATVLG 2177
Cdd:PRK02102 313 EAENRMHTIKAVMVATLG 330
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
187-338 |
7.71e-23 |
|
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: 97.99 E-value: 7.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 187 YNQIRCLCQRGAEVTVVPWDHALDSQE----YEGLFLSNGPGDPASYPSVVSTLSRVLSEpnpRPVFGICLGHQLLALAI 262
Cdd:cd01743 12 YNLVQYLRELGAEVVVVRNDEITLEELellnPDAIVISPGPGHPEDAGISLEIIRALAGK---VPILGVCLGHQAIAEAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 263 GAKTYKMRYGNRG------HNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWapLFTNANDgsnEGIV----HNSLPFFS 332
Cdd:cd01743 89 GGKVVRAPEPMHGktseihHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPDLL--EVTASTE---DGVImalrHRDLPIYG 163
|
....*.
gi 578803167 333 VQFHPE 338
Cdd:cd01743 164 VQFHPE 169
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
1404-1676 |
6.03e-22 |
|
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 98.17 E-value: 6.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1404 LIDVHVHLREPGGTH------------------KEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGAR 1465
Cdd:cd01292 1 FIDTHVHLDGSALRGtrlnlelkeaeelspedlYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1466 CDFALFLGASSENAGTLGTV------------AGSAAGLKLYLNETFSELRLDSVvqwMEHFETWPSH-LPIVAHAEQQT 1532
Cdd:cd01292 81 IRVVLGLGIPGVPAAVDEDAealllellrrglELGAVGLKLAGPYTATGLSDESL---RRVLEEARKLgLPVVIHAGELP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1533 VA--AVLMVAQLTQR--SVHICHVARKEEILLIKAAKArglPVTCEVAPHHLFLSHDDlerlgpgkgevrpelgsRQDVE 1608
Cdd:cd01292 158 DPtrALEDLVALLRLggRVVIGHVSHLDPELLELLKEA---GVSLEVCPLSNYLLGRD-----------------GEGAE 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803167 1609 ALWENMA--VIDCFASDHAPHTLEekcgsrpppgfpglETMLPLLLTAVSEGRL--SLDDLLQRLHHNPRRI 1676
Cdd:cd01292 218 ALRRLLElgIRVTLGTDGPPHPLG--------------TDLLALLRLLLKVLRLglSLEEALRLATINPARA 275
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
985-1182 |
2.18e-21 |
|
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: 94.68 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 985 RFKFSRLLDTIGISQPQW--RELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKE----H 1058
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGtaGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAafgnP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1059 PVVISKFIQEAKEIDVDAVAsDGVVAAIAISEhVENA-GVHSGDATLVTPPQDITAKTLERIKAIVHAVGQELQVTGPFN 1137
Cdd:pfam02786 82 QVLVEKSLKGPKHIEYQVLR-DAHGNCITVCN-RECSdQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 578803167 1138 LQLI--AKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGE 1182
Cdd:pfam02786 160 VEFAldPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGY 206
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
1264-1364 |
8.53e-19 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 460462 [Multi-domain] Cd Length: 93 Bit Score: 82.92 E-value: 8.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1264 ELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEA-VDGECppqrSILEQLAEKNFELVINLSMRGAGGRRl 1342
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTGEGrPGGRV----QIGDLIKNGEIDLVINTLYPFKATVH- 75
|
90 100
....*....|....*....|..
gi 578803167 1343 ssfvtKGYRTRRLAADFSVPLI 1364
Cdd:pfam02142 76 -----DGYAIRRAAENIDIPGP 92
|
|
| PRK04284 |
PRK04284 |
ornithine carbamoyltransferase; Provisional |
1874-2178 |
9.37e-19 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 235269 [Multi-domain] Cd Length: 332 Bit Score: 89.80 E-value: 9.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1874 SLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATS 1953
Cdd:PRK04284 3 NLRNRSFLTLLDFTPKEIEYLLDLSEDLKRAKYAGIEVQKLKGKNIALIFEKDSTRTRCAFEVAAYDQGAHVTYLGPTGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1954 SVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINaGDGVGEHPTQALLDIFTIREEL-GTVNGMTITMV 2032
Cdd:PRK04284 83 QMGKKESTKDTARVLGGMYDGIEYRGFSQRTVETLAEYSGVPVWN-GLTDEDHPTQVLADFLTAKEHLkKPYKDIKFTYV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2033 GDlkhGRTVHSLACLLTQYRVSLRY--VAPPSLRMPPTV----RAFVASRGTKQEEFESIEEALPDTDVLYM-------- 2098
Cdd:PRK04284 162 GD---GRNNVANALMQGAAIMGMDFhlVCPKELNPDDELlnkcKEIAAETGGKITITDDIDEGVKGSDVIYTdvwvsmge 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2099 -TRIQKERFGSTQEYEacfgqfiLTPHIMTRAKKKMVV-MHPMPRVN-------------------EISVEVDSDPRAAY 2157
Cdd:PRK04284 239 pDEVWEERIKLLKPYQ-------VNKEMMKKTGNPNAIfEHCLPSFHdldtkvgkeifekyglkemEVTDEVFESKASVV 311
|
330 340
....*....|....*....|.
gi 578803167 2158 FRQAENGMYIRMALLATVLGR 2178
Cdd:PRK04284 312 FDEAENRMHTIKAVMVATLGE 332
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
177-351 |
8.88e-17 |
|
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: 81.53 E-value: 8.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 177 RILALDCGLKYNQI-----RCLCQRGAEVTVV--------PWDHALDsqEYEGLFLSNGPG---DPASYPSVVSTLSRVL 240
Cdd:COG0518 1 KILILDHDPFGGQYpgliaRRLREAGIELDVLrvyageilPYDPDLE--DPDGLILSGGPMsvyDEDPWLEDEPALIREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 241 SEPNpRPVFGICLGHQLLALAIGAKTYKMRYGNRG------HNQPCLLVGSGRCFLTSQNHGFAVetDSLPADWAPLFTN 314
Cdd:COG0518 79 FELG-KPVLGICYGAQLLAHALGGKVEPGPGREIGwapvelTEADPLFAGLPDEFTVWMSHGDTV--TELPEGAEVLASS 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 578803167 315 ANDgSNEGIVHNSlPFFSVQFHPEhqAGPSDMELLFD 351
Cdd:COG0518 156 DNC-PNQAFRYGR-RVYGVQFHPE--VTHTMMEAWLE 188
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
963-1186 |
3.81e-16 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 81.85 E-value: 3.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 963 ALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQT--VGYPCVVRPSYVLSGAAMNVAYT 1040
Cdd:PRK12767 90 RFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKgeLQFPLFVKPRDGSASIGVFKVND 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1041 DGDLERFLSSAAavskehPVVISKFIQEaKEIDVDA-VASDGVVAAIAISEHVEnagVHSGDATlvtppQDITAKTLERI 1119
Cdd:PRK12767 170 KEELEFLLEYVP------NLIIQEFIEG-QEYTVDVlCDLNGEVISIVPRKRIE---VRAGETS-----KGVTVKDPELF 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803167 1120 KAIVHaVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFvSKTLGVDLVALATRVIMGEEVEP 1186
Cdd:PRK12767 235 KLAER-LAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPL-SYMAGANEPDWIIRNLLGGENEP 299
|
|
| PRK12562 |
PRK12562 |
ornithine carbamoyltransferase subunit F; Provisional |
1872-2178 |
4.71e-16 |
|
ornithine carbamoyltransferase subunit F; Provisional
Pssm-ID: 105755 Cd Length: 334 Bit Score: 82.03 E-value: 4.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1872 LHSLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEA 1951
Cdd:PRK12562 1 MSGFYKKHFLKLLDFTPAELNSLLQLAAKLKADKKNGKEVARLTGKNIALIFEKDSTRTRCSFEVAAYDQGARVTYLGPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1952 TSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINaGDGVGEHPTQALLDIFTIREEL--GTVNGMTI 2029
Cdd:PRK12562 81 GSQIGHKESIKDTARVLGRMYDGIQYRGHGQEVVETLAEYAGVPVWN-GLTNEFHPTQLLADLLTMQEHLpgKAFNEMTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2030 TMVGDLKH--GRTVHSLACLLTqyrVSLRYVAP----PSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLY------ 2097
Cdd:PRK12562 160 VYAGDARNnmGNSMLEAAALTG---LDLRLVAPqacwPEASLVAECSALAQKHGGKITLTEDIAAGVKGADFIYtdvwvs 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2098 MTRIQK---ERFGSTQEYEACFGQFILT--PHI------------MTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQ 2160
Cdd:PRK12562 237 MGEPKEkwaERIALLRGYQVNSKMMALTgnPQVkflhclpafhddQTTLGKKMAKEFGLHGGMEVTDEVFESPASIVFDQ 316
|
330
....*....|....*...
gi 578803167 2161 AENGMYIRMALLATVLGR 2178
Cdd:PRK12562 317 AENRMHTIKAVMVATLAK 334
|
|
| PRK03515 |
PRK03515 |
ornithine carbamoyltransferase subunit I; Provisional |
1878-2176 |
2.02e-15 |
|
ornithine carbamoyltransferase subunit I; Provisional
Pssm-ID: 179587 [Multi-domain] Cd Length: 336 Bit Score: 79.76 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1878 QHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQK 1957
Cdd:PRK03515 7 RHFLRLLDFTPAELNSLLQLAAKLKADKKNGKEEQKLTGKNIALIFEKDSTRTRCSFEVAAYDQGARVTYLGPSGSQIGH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1958 GESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINagdGVGE--HPTQALLDIFTIREEL--GTVNGMTITMVG 2033
Cdd:PRK03515 87 KESIKDTARVLGRMYDGIQYRGYGQEIVETLAEYAGVPVWN---GLTNefHPTQLLADLLTMQEHLpgKAFNEMTLAYAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2034 DLKH--GRTVHSLACLLTqyrVSLRYVAP----PSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYM--------- 2098
Cdd:PRK03515 164 DARNnmGNSLLEAAALTG---LDLRLVAPkacwPEAALVTECRALAQKNGGNITLTEDIAEGVKGADFIYTdvwvsmgep 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2099 TRIQKERFGSTQEYEACFGQFILT--PHI------------MTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENG 2164
Cdd:PRK03515 241 KEVWAERIALLRPYQVNSKMMQLTgnPQVkflhclpafhddQTTLGKKMAEEYGLHGGMEVTDEVFESAHSIVFDQAENR 320
|
330
....*....|...
gi 578803167 2165 MY-IRMALLATVL 2176
Cdd:PRK03515 321 LHtIKAVMVATLS 333
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
187-338 |
2.06e-15 |
|
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: 76.62 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 187 YNQIRCLCQRGAEVTVVPWDH----ALDSQEYEGLFLSNGPGDPASYP---SVVSTLSRVLsepnprPVFGICLGHQLLA 259
Cdd:COG0512 12 YNLVQYLGELGAEVVVVRNDEitleEIEALAPDGIVLSPGPGTPEEAGislEVIRAFAGKI------PILGVCLGHQAIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 260 LAIGAKTYKMRY------------GN---RGHNQPcLLVgsGRcfltsqNHGFAVETDSLPAD-----WAPlftnanDGS 319
Cdd:COG0512 86 EAFGGKVVRAPEpmhgktspithdGSglfAGLPNP-FTA--TR------YHSLVVDRETLPDElevtaWTE------DGE 150
|
170
....*....|....*....
gi 578803167 320 NEGIVHNSLPFFSVQFHPE 338
Cdd:COG0512 151 IMGIRHRELPIEGVQFHPE 169
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
187-338 |
3.21e-14 |
|
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: 73.28 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 187 YNQIRCLCQRGAEVtVVPWDHALDSQEYEGL---FLSNGPGdpASYPSVVSTLSRVLSEPNPR-PVFGICLGHQLLALAI 262
Cdd:TIGR00566 13 YNLVQYFCELGAEV-VVKRNDSLTLQEIEALlplLIVISPG--PCTPNEAGISLEAIRHFAGKlPILGVCLGHQAMGQAF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 263 GAKTYKMRYGNRGHNQPCLLVGSGRC------FLTSQNHGFAVETDSLPADWAPLFTNANDGSNEGIVHNSLPFFSVQFH 336
Cdd:TIGR00566 90 GGDVVRANTVMHGKTSEIEHNGAGIFrglfnpLTATRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQFH 169
|
..
gi 578803167 337 PE 338
Cdd:TIGR00566 170 PE 171
|
|
| PRK01713 |
PRK01713 |
ornithine carbamoyltransferase; Provisional |
1874-2176 |
3.73e-14 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 167263 [Multi-domain] Cd Length: 334 Bit Score: 76.18 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1874 SLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATS 1953
Cdd:PRK01713 4 NLKNRHLLSLVNHTEREIKYLLDLSRDLKRAKYAGTEQQRLKGKNIALIFEKTSTRTRCAFEVAAYDQGAQVTYIDPNSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1954 SVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINagdGVGE--HPTQALLDIFTIREELGT-VNGMTIT 2030
Cdd:PRK01713 84 QIGHKESMKDTARVLGRMYDAIEYRGFKQSIVNELAEYAGVPVFN---GLTDefHPTQMLADVLTMIENCDKpLSEISYV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2031 MVGDLKHGRTvHSLACLLTQYRVSLRYVAPPSL----RMPPTVRAFVASRGTKQEEFESIEEALPDTDVlymtrIQKERF 2106
Cdd:PRK01713 161 YIGDARNNMG-NSLLLIGAKLGMDVRICAPKALlpeaSLVEMCEKFAKESGARITVTDDIDKAVKGVDF-----VHTDVW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2107 GSTQEYEACFGQFI-------LTPHIMTR-AKKKMVVMHPMPRVN---------------------EISVEVDSDPRAAY 2157
Cdd:PRK01713 235 VSMGEPLETWGERIkllmpyqVTPELMKRtGNPKVKFMHCLPAFHnsetkvgrqiaekypelangiEVTEDVFESPMNIA 314
|
330
....*....|....*....
gi 578803167 2158 FRQAENGMYIRMALLATVL 2176
Cdd:PRK01713 315 FEQAENRMHTIKAVMVASL 333
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
866-1187 |
5.77e-14 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 76.12 E-value: 5.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 866 TFRTPHVLVLGSgvyrigssvefDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLY------FDEISF-EVVMD 938
Cdd:COG3919 2 MTMRFRVVVLGG-----------DINALAVARSLGEAGVRVIVVDRDPLGPAARSRYVDEVVvvpdpgDDPEAFvDALLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 939 IYELENPEGVILSMGGQLpnnMAMALHRQQ----CRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQF 1014
Cdd:COG3919 71 LAERHGPDVLIPTGDEYV---ELLSRHRDEleehYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1015 CQTVGYPCVVRPSYvlSGAAMNV----------AYTDGDLERFLSSAAAVskEHPVVISKFI--QEAKEIDVDA-VASDG 1081
Cdd:COG3919 148 AEDLGFPVVVKPAD--SVGYDELsfpgkkkvfyVDDREELLALLRRIAAA--GYELIVQEYIpgDDGEMRGLTAyVDRDG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1082 VVAAIAISEHV----ENAGVHSgdATLVTPPQDItaktLERIKAIVHAVGqelqVTGPFNLQLI--AKDDQLKVIECNVR 1155
Cdd:COG3919 224 EVVATFTGRKLrhypPAGGNSA--ARESVDDPEL----EEAARRLLEALG----YHGFANVEFKrdPRDGEYKLIEINPR 293
|
330 340 350
....*....|....*....|....*....|..
gi 578803167 1156 VSRSFPFVSKTlGVDLVALATRVIMGEEVEPV 1187
Cdd:COG3919 294 FWRSLYLATAA-GVNFPYLLYDDAVGRPLEPV 324
|
|
| PRK14804 |
PRK14804 |
ornithine carbamoyltransferase; Provisional |
1878-2176 |
8.45e-14 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 173265 [Multi-domain] Cd Length: 311 Bit Score: 74.68 E-value: 8.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1878 QHILSVQQFTKDQMSHLFNVAhtlrMMVQKERS--LDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSV 1955
Cdd:PRK14804 7 KHLISWEDWSDSEILDLLDFA----VHVKKNRVnyAGHMSGRSLAMLFQKTSTRTRVSFEVAMTEMGGHGIYLDWMASNF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1956 QkgesLAD---SVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGeHPTQALLDIFTIREELGTV--NGMTIT 2030
Cdd:PRK14804 83 Q----LSDidlEARYLSRNVSVIMARLKKHEDLLVMKNGSQVPVINGCDNMF-HPCQSLADIMTIALDSPEIplNQKQLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2031 MVGdlKHGRTVHSLACLLTQYRVSLRYVAPPSLR---MPPTV-RAfvASRGTKQEEfESIEEALPDTDVLYMTRIQKERF 2106
Cdd:PRK14804 158 YIG--VHNNVVNSLIGITAALGIHLTLVTPIAAKeniHAQTVeRA--KKKGTLSWE-MNLHKAVSHADYVYTDTWLDMEF 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803167 2107 GSTQEYEACFGQFI--LTPH-----IMTRAKKKmvVMHPMP--RVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVL 2176
Cdd:PRK14804 233 FNDPSYADKKKQRMelMMPYqinssLMEKTNAK--VMHDMPihAGYEITREVVLSDRSIIFQQAENRLDAQKAVILKLL 309
|
|
| PRK04523 |
PRK04523 |
N-acetylornithine carbamoyltransferase; Reviewed |
1878-2178 |
8.82e-14 |
|
N-acetylornithine carbamoyltransferase; Reviewed
Pssm-ID: 235304 [Multi-domain] Cd Length: 335 Bit Score: 74.78 E-value: 8.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1878 QHILSVQQFTKDQMSHLFNVAHTLRmmvQKERSlDILKGKVMASMFYEVSTRTSSSFAAAMARLGG-AV----------L 1946
Cdd:PRK04523 4 KHFLNTQDWSRAELDALLTQAAAFK---RNKLG-SALKGKSIALVFFNPSLRTRTSFELGAFQLGGhAVvlqpgkdawpI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1947 SFSEATssVQKG---ESLADSVQTMSCYADVVVLR----------HPQPGAVELAAKHCRRPVINAGDGVgeHPTQALLD 2013
Cdd:PRK04523 80 EFELGA--VMDGeteEHIREVARVLSRYVDLIGVRafpkfvdwskDRQDQVLNSFAKYSTVPVINMETIT--HPCQELAH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2014 IFTIREELG-TVNGMTI------------TMVGD------LKHGRTVhSLACLLTQYRVSLRYVAppslrmppTVRAFVA 2074
Cdd:PRK04523 156 ALALQEHFGtTLRGKKYvltwtyhpkplnTAVANsalliaTRLGMDV-TLLCPTPDYILDERYMD--------WAEQNAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 2075 SRGTKQEEFESIEEALPDTDVLYM----TRIQKERFGSTQEYEACFGQFILTPHIMTRAKKKmVVMH--PMPRVNEISVE 2148
Cdd:PRK04523 227 ESGGSLTVSHDIDSAYAGADVVYAkswgALPFFGNWEPEKPIRDQYQHFIVDERKMALTNNG-VFSHclPLRRNVKVTDA 305
|
330 340 350
....*....|....*....|....*....|
gi 578803167 2149 VDSDPRAAYFRQAENGMYIRMALLATVLGR 2178
Cdd:PRK04523 306 VMDSPNCIAIDEAENRLHVQKAIMAALASQ 335
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
177-338 |
1.02e-12 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 69.31 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 177 RILALDC--GLKYNQIRCLCQRGAEVTVV------PWDHALDSQEYEGLFLSNGPGDP----ASYPSVVSTLSRVLsepn 244
Cdd:PRK07765 2 RILVVDNydSFVFNLVQYLGQLGVEAEVWrnddprLADEAAVAAQFDGVLLSPGPGTPeragASIDMVRACAAAGT---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 245 prPVFGICLGHQLLALAIGA-----------KTYKMRYGNRGhnqpcLLVGSGRCFLTSQNHGFAVETDSLPADwapLFT 313
Cdd:PRK07765 78 --PLLGVCLGHQAIGVAFGAtvdrapellhgKTSSVHHTGVG-----VLAGLPDPFTATRYHSLTILPETLPAE---LEV 147
|
170 180
....*....|....*....|....*....
gi 578803167 314 NANDGSneGIV----HNSLPFFSVQFHPE 338
Cdd:PRK07765 148 TARTDS--GVImavrHRELPIHGVQFHPE 174
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
187-338 |
1.24e-12 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 68.62 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 187 YN---QIRCLcqrGAEVTVVPWDhALDSQEYE-----GLFLSNGPGDPA---SYPSVVSTLSRVLsepnprPVFGICLGH 255
Cdd:PRK05670 13 YNlvqYLGEL---GAEVVVYRND-EITLEEIEalnpdAIVLSPGPGTPAeagISLELIREFAGKV------PILGVCLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 256 QLLALAIGA-----------KTYKMRygnrgHNQPCLLVGSGRCFLTSQNHGFAVETDSLPADwapLFTNA--NDGSNEG 322
Cdd:PRK05670 83 QAIGEAFGGkvvrakeimhgKTSPIE-----HDGSGIFAGLPNPFTVTRYHSLVVDRESLPDC---LEVTAwtDDGEIMG 154
|
170
....*....|....*.
gi 578803167 323 IVHNSLPFFSVQFHPE 338
Cdd:PRK05670 155 VRHKELPIYGVQFHPE 170
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
187-355 |
1.38e-12 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 68.35 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 187 YNQIRCLCQRGAEVtVVPWDHALDSQEYEGL-----FLSNGPGDPASYPSVVSTLSRVLSEpnpRPVFGICLGHQLLALA 261
Cdd:PRK06774 13 YNLYQYFCELGTEV-MVKRNDELQLTDIEQLapshlVISPGPCTPNEAGISLAVIRHFADK---LPILGVCLGHQALGQA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 262 IGAKTYKMRYGNRG------HNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWAPLFTNANDGSNE---GIVHNSLPFFS 332
Cdd:PRK06774 89 FGARVVRARQVMHGktsaicHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTAWSERGGEMDeimGIRHRTLPLEG 168
|
170 180
....*....|....*....|...
gi 578803167 333 VQFHPEHQAGPSDMELLfDIFLE 355
Cdd:PRK06774 169 VQFHPESILSEQGHQLL-DNFLK 190
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
1264-1364 |
1.42e-12 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 214855 [Multi-domain] Cd Length: 91 Bit Score: 65.19 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1264 ELLPTVRLLESLGYSLYASLGTADFYTEHGVKV--TAVDWHFEEavdgecppQRSILEQLAEKNFELVINLSMRGAggrr 1341
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPVvkTLHPKVHGG--------IPQILDLIKNGEIDLVINTLYPFE---- 68
|
90 100
....*....|....*....|...
gi 578803167 1342 lSSFVTKGYRTRRLAADFSVPLI 1364
Cdd:smart00851 69 -AQAHEDGYSIRRAAENIDIPGP 90
|
|
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
1401-1715 |
1.45e-12 |
|
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in the pyrimidine biosynthesis. In contrast to the large polyfunctional CAD proteins of higher organisms, this group of DHOases is monofunctional and mainly dimeric.
Pssm-ID: 238619 Cd Length: 335 Bit Score: 71.16 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1401 LPGLIDVHVHLREpgGTHKEDFASGTAAALAGGITMvcamPNTRPPIIDAP-ALALAQKLAEAGARCDF----ALFLGAS 1475
Cdd:cd01294 3 IPRPDDMHLHLRD--GAMLKLVLPYTARGFSRAIVM----PNLKPPVTTTAdALAYRERILAADPGPNFtplmTLYLTEN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1476 -SENAGTLGTVAGSAAGLKLYLN--ETFSELRLDSVVQWMEHFETWPSH-LPIVAHAEQQTVAAVLM---------VAQL 1542
Cdd:cd01294 77 tTPEELREAKKKGGIRGVKLYPAgaTTNSQGGVTDLEKIYPVLEAMQKLgMPLLVHGEVPDFKIDVLdreakfipvLEPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1543 TQR----SVHICHVARKEEILLIKAAKARglpVTCEVAPHHLFLSHDDLerLGPGKGEV---RPELGSRQDVEALwENMA 1615
Cdd:cd01294 157 AQRfpklKIVLEHITTADAVEYVKSCNEN---VAATITPHHLLLTRDDL--LGGGLNPHlycKPVAKRPEDREAL-RKAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1616 VIDC----FASDHAPHTLEEKcgsRPPPGFPGLET---MLPLLLTAVSEGRlSLDDLLQRLHHNPRRIFHLPPQEDTYVE 1688
Cdd:cd01294 231 TSGHpkffLGSDSAPHPKSNK---ESSCGCAGIFSapiALPYLAEVFEEHN-ALDKLEAFASDNGPNFYGLPPNKKTITL 306
|
330 340
....*....|....*....|....*..
gi 578803167 1689 VdlEHEWTIPSHMPFSKAHWTPFEGQK 1715
Cdd:cd01294 307 V--KEPWKVPEKIPFGNNGVVPFRAGE 331
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
178-338 |
1.68e-12 |
|
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: 68.11 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 178 ILALDCGLKYNQI--RCLCQRGAEVTVVPWDHALD---SQEYEGLFLSNGPGdpasypsvvSTLSRVLSEPNPR------ 246
Cdd:TIGR00888 1 ILVLDFGSQYTQLiaRRLRELGVYSELVPNTTPLEeirEKNPKGIILSGGPS---------SVYAENAPRADEKifelgv 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 247 PVFGICLGHQLLALAIG---AKTYKMRYGN---RGHNQPCLLVGSGRCFLTSQNHGFAVEtdSLPADWAPLFTNANdGSN 320
Cdd:TIGR00888 72 PVLGICYGMQLMAKQLGgevGRAEKREYGKaelEILDEDDLFRGLPDESTVWMSHGDKVK--ELPEGFKVLATSDN-CPV 148
|
170
....*....|....*...
gi 578803167 321 EGIVHNSLPFFSVQFHPE 338
Cdd:TIGR00888 149 AAMAHEEKPIYGVQFHPE 166
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
172-338 |
2.81e-12 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 72.26 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 172 TGGAPRILALDCGLKY-----NQIRclcQRGAEVTVVPWDHA---LDSQEYEGLFLSNGPGDPASY--PSVVST-LSRVL 240
Cdd:PRK13566 523 VGEGKRVLLVDHEDSFvhtlaNYFR---QTGAEVTTVRYGFAeemLDRVNPDLVVLSPGPGRPSDFdcKATIDAaLARNL 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 241 sepnprPVFGICLGHQLLALAIGAKTYKMRYGNRG------HNQPC-LLVGSGRCFLTSQNHGFAVETDSLPADwaplFT 313
Cdd:PRK13566 600 ------PIFGVCLGLQAIVEAFGGELGQLAYPMHGkpsrirVRGPGrLFSGLPEEFTVGRYHSLFADPETLPDE----LL 669
|
170 180
....*....|....*....|....*...
gi 578803167 314 N---ANDGSNEGIVHNSLPFFSVQFHPE 338
Cdd:PRK13566 670 VtaeTEDGVIMAIEHKTLPVAAVQFHPE 697
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
996-1156 |
7.39e-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: 7.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 996 GISQPQWRELSDLESARQFCQTVGYPCVV---RPSYvlSGAAMNVAYTDGDLERFLSSAAAVskehPVVISKFIQEAKEI 1072
Cdd:pfam02222 4 GLPTPRFMAAESLEELIEAGQELGYPCVVkarRGGY--DGKGQYVVRSEADLPQAWEELGDG----PVIVEEFVPFDREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1073 DVDAVAS-DGVVAAIAISEHVEnagvHSGDATLVTPPQDITAKTLERIKAIVHAVGQELQVTGPFNLQL-IAKDDQLKVI 1150
Cdd:pfam02222 78 SVLVVRSvDGETAFYPVVETIQ----EDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELfVTEDGDLLIN 153
|
....*.
gi 578803167 1151 ECNVRV 1156
Cdd:pfam02222 154 ELAPRP 159
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
460-651 |
1.88e-11 |
|
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: 66.82 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 460 VTQVIRNERPDGVLltfggqtALNCGVELTKAGVLARYGVRvlGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLE 539
Cdd:COG0439 9 AAELARETGIDAVL-------SESEFAVETAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 540 QAQAAAERLGYPVLVRAAFALGGLGSGFASNREELSALVA------PAFAHTSQVLVDKSLKGwKEIEYEV--------- 604
Cdd:COG0439 80 EALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAearaeaKAGSPNGEVLVEEFLEG-REYSVEGlvrdgevvv 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 605 -----------------------------------VRDA-----YGNCVTY-----------YIIEVNARLS--RSSALA 631
Cdd:COG0439 159 csitrkhqkppyfvelgheapsplpeelraeigelVARAlralgYRRGAFHteflltpdgepYLIEINARLGgeHIPPLT 238
|
250 260
....*....|....*....|
gi 578803167 632 SKATGYPLAYVAAKLALGIP 651
Cdd:COG0439 239 ELATGVDLVREQIRLALGEP 258
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
190-340 |
3.69e-11 |
|
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: 64.19 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 190 IRCLCQRGAEVTVVPW---DHALDSQEYEGLFLSNGPGDP--ASYPSVVST---LSRVLSEPnpRPVFGICLGHQLLALA 261
Cdd:cd01741 20 LREAGAETIEIDVVDVyagELLPDLDDYDGLVILGGPMSVdeDDYPWLKKLkelIRQALAAG--KPVLGICLGHQLLARA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 262 IGAKTYKMRYG----------NRGHNQPCLLVGSGRCFLTSQNHGFAVEtdSLPADWAPLFTNAnDGSNEGIVHNSLpFF 331
Cdd:cd01741 98 LGGKVGRNPKGweigwfpvtlTEAGKADPLFAGLPDEFPVFHWHGDTVV--ELPPGAVLLASSE-ACPNQAFRYGDR-AL 173
|
....*....
gi 578803167 332 SVQFHPEHQ 340
Cdd:cd01741 174 GLQFHPEER 182
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
209-338 |
4.25e-11 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 63.99 E-value: 4.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 209 LDSQE-YEGLFLSNGPGDPASYPSVVSTLSRVLSEpnpRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGR 287
Cdd:PRK06895 38 LDEVEnFSHILISPGPDVPRAYPQLFAMLERYHQH---KSILGVCLGHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSP 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803167 288 CF--LTSQ-----NHGFAVETDSLPAdwaPLFTNANdgSNEGIV----HNSLPFFSVQFHPE 338
Cdd:PRK06895 115 LFdgLPEEfniglYHSWAVSEENFPT---PLEITAV--CDENVVmamqHKTLPIYGVQFHPE 171
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
187-338 |
5.24e-11 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 64.13 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 187 YNQIRCLCQRGAEVTVVPWDHaLDSQEYEGL-----FLSNGPGDPASYPSVVSTLSRVLSEpnpRPVFGICLGHQLLALA 261
Cdd:PRK08857 13 YNLYQYFCELGAQVKVVRNDE-IDIDGIEALnpthlVISPGPCTPNEAGISLQAIEHFAGK---LPILGVCLGHQAIAQV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 262 IGAKTYKMRYGNRG------HNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWA-PLFTNANDGSNE---GIVHNSLPFF 331
Cdd:PRK08857 89 FGGQVVRARQVMHGktspirHTGRSVFKGLNNPLTVTRYHSLVVKNDTLPECFElTAWTELEDGSMDeimGFQHKTLPIE 168
|
....*..
gi 578803167 332 SVQFHPE 338
Cdd:PRK08857 169 AVQFHPE 175
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
178-338 |
6.85e-11 |
|
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: 63.32 E-value: 6.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 178 ILALDCGLKYNQ-----IRCLcqrGAEVTVVPWDHALDS---QEYEGLFLSNGPgdpasypsvvstlSRVLSEPNPR--- 246
Cdd:cd01742 1 ILILDFGSQYTHliarrVREL---GVYSEILPNTTPLEEiklKNPKGIILSGGP-------------SSVYEEDAPRvdp 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 247 -------PVFGICLGHQLLALAIGAKTYKMRYGNRGHNQpCLLVGSGRCF--LTSQ-----NHGFAVETdsLPADWAPLF 312
Cdd:cd01742 65 eifelgvPVLGICYGMQLIAKALGGKVERGDKREYGKAE-IEIDDSSPLFegLPDEqtvwmSHGDEVVK--LPEGFKVIA 141
|
170 180
....*....|....*....|....*.
gi 578803167 313 TNANDGsNEGIVHNSLPFFSVQFHPE 338
Cdd:cd01742 142 SSDNCP-VAAIANEEKKIYGVQFHPE 166
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
924-1174 |
1.60e-10 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 64.19 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 924 DRLYFDEISFEVVMDIYELENPEGVILsmgGQLPNNMAMA----LHRQQCRVLGtSPEAIDSAENRFKFSRLLDTIGISQ 999
Cdd:COG0189 36 DDLTLDLGRAPELYRGEDLSEFDAVLP---RIDPPFYGLAllrqLEAAGVPVVN-DPEAIRRARDKLFTLQLLARAGIPV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1000 PQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEhPVVISKFIQEAKEIDVDAVAS 1079
Cdd:COG0189 112 PPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEALTELGSE-PVLVQEFIPEEDGRDIRVLVV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1080 DG-VVAAIA-ISEHVENAG-VHSGDATLvtpPQDITAKTLERIKAIVHAVGqeLQVTGpfnLQLIAKDDQLKVIECNVRV 1156
Cdd:COG0189 191 GGePVAAIRrIPAEGEFRTnLARGGRAE---PVELTDEERELALRAAPALG--LDFAG---VDLIEDDDGPLVLEVNVTP 262
|
250
....*....|....*...
gi 578803167 1157 srSFPFVSKTLGVDLVAL 1174
Cdd:COG0189 263 --GFRGLERATGVDIAEA 278
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
1401-1731 |
9.33e-10 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 63.18 E-value: 9.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1401 LPGLIDVHVHLREPGGTHKeDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQK---------------LAEAGAR 1465
Cdd:PRK08417 29 LPALVDLNVSLKNDSLSSK-NLKSLENECLKGGVGSIVLYPDSTPAIDNEIALELINSaqrelpmqifpsiraLDEDGKL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1466 CDFALFL--GA------SSENAGTLGTVAGSAAGLK--LYLNETFSELRlDSVVqwMEHFETWPS-HLP-IVAHAEQQTV 1533
Cdd:PRK08417 108 SNIATLLkkGAkalelsSDLDANLLKVIAQYAKMLDvpIFCRCEDSSFD-DSGV--MNDGELSFElGLPgIPSIAETKEV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1534 AAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPgKGEVRPELGSRQDVEALWEN 1613
Cdd:PRK08417 185 AKMKELAKFYKNKVLFDTLALPRSLELLDKFKSEGEKLLKEVSIHHLILDDSACENFNT-AAKLNPPLRSKEDRLALLEA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1614 M--AVIDCFASDHAPHTLEEKCGS--RPPPGFPGLETMLPLLLT-AVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDT--- 1685
Cdd:PRK08417 264 LkeGKIDFLTSLHSAKSNSKKDLAfdEAAFGIDSICEYFSLCYTyLVKEGIITWSELSRFTSYNPAQFLGLNSGEIEvgk 343
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 578803167 1686 ---YVEVDLEHEWTIPSHMPfskahwtPFEGQKVKGTVRRVVLRGEVAY 1731
Cdd:PRK08417 344 eadLVLFDPNESTIIDDNFS-------LYSGDELYGKIEAVIIKGKLYL 385
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
247-338 |
1.54e-09 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 62.81 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 247 PVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSG------RCFLTSQNHGFAVETDSLPADWAPLfTNANDGSN 320
Cdd:PRK14607 75 PILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGlfrgipNPTVATRYHSLVVEEASLPECLEVT-AKSDDGEI 153
|
90
....*....|....*...
gi 578803167 321 EGIVHNSLPFFSVQFHPE 338
Cdd:PRK14607 154 MGIRHKEHPIFGVQFHPE 171
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
1251-1364 |
2.98e-09 |
|
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate synthetase (CSP). CSP, a CarA and CarB heterodimer, catalyzes the production of carbamoyl phosphate which is subsequently employed in the metabolic pathways responsible for the synthesis of pyrimidine nucleotides or arginine. The MGS-like domain is the C-terminal domain of CarB and appears to play a regulatory role in CPS function by binding allosteric effector molecules, including UMP and ornithine.
Pssm-ID: 238712 [Multi-domain] Cd Length: 110 Bit Score: 56.33 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1251 NILLTIgSYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEavdgecppQRSILEQLAEKNFELVI 1330
Cdd:cd01424 2 TVFISV-ADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEG--------RPNIVDLIKNGEIQLVI 72
|
90 100 110
....*....|....*....|....*....|....
gi 578803167 1331 NlsmrGAGGRRlssFVTKGYRTRRLAADFSVPLI 1364
Cdd:cd01424 73 N----TPSGKR---AIRDGFSIRRAALEYKVPYF 99
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
395-654 |
7.08e-09 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 59.90 E-value: 7.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 395 KVLILGSGGlsigqagefdysGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLP-IT-PHYVTQVI---RNERP 469
Cdd:PRK12767 3 NILVTSAGR------------RVQLVKALKKSLLKGRVIGADISELAPALYFADKFYVVPkVTdPNYIDRLLdicKKEKI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 470 DGVLLTFGgqtalncgVELtkaGVLARY-------GVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQ 542
Cdd:PRK12767 71 DLLIPLID--------PEL---PLLAQNrdrfeeiGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 543 AA--AERLGYPVLVRAAFALGGLGSGFASNREELSalvaPAFAHTSQVLVDKSLKGwKEIEYEVVRDAYGNCV------- 613
Cdd:PRK12767 140 AAlaKGELQFPLFVKPRDGSASIGVFKVNDKEELE----FLLEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVIsivprkr 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 614 ---------------------------------------------TYYIIEVNARLSrssalaskaTGYPLAYVA----- 643
Cdd:PRK12767 215 ievragetskgvtvkdpelfklaerlaealgargplniqcfvtdgEPYLFEINPRFG---------GGYPLSYMAganep 285
|
330
....*....|....*
gi 578803167 644 ----AKLALGIPLPE 654
Cdd:PRK12767 286 dwiiRNLLGGENEPI 300
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
1383-1750 |
7.35e-09 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 60.63 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1383 APPLKVHVDCMT---SQKLVrLPGLIDVHVHLREP--GGTHKEDFASGTAAALAGGITMvcampntrppIID-------- 1449
Cdd:PLN02942 36 APNLKVPDDVRVidaTGKFV-MPGGIDPHTHLAMPfmGTETIDDFFSGQAAALAGGTTM----------HIDfvipvngn 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1450 -APALALAQKLAEAGArCDFALFLGAS------SENAGTLGTVAGSAAgLKLYLNETFSELRLDSVVqwMEHFETWPS-- 1520
Cdd:PLN02942 105 lLAGYEAYEKKAEKSC-MDYGFHMAITkwddtvSRDMETLVKEKGINS-FKFFMAYKGSLMVTDELL--LEGFKRCKSlg 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1521 HLPIVaHAEQ--------------------------------QTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARG 1568
Cdd:PLN02942 181 ALAMV-HAENgdavfegqkrmielgitgpeghalsrppllegEATARAIRLAKFVNTPLYVVHVMSIDAMEEIARARKSG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1569 LPVTCEVAPHHLFLshDDLERLGP-----GKGEVRPELGSRQDVEALWENMA--VIDCFASDHAPHTLEEKCGSRP---- 1637
Cdd:PLN02942 260 QRVIGEPVVSGLVL--DDSKLWDPdftiaSKYVMSPPIRPAGHGKALQAALSsgILQLVGTDHCPFNSTQKAFGKDdfrk 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1638 -PPGFPGLETMLPLLL-TAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVE--------VDLEHEWTIPSHMPFSKAH 1707
Cdd:PLN02942 338 iPNGVNGIEERMHLVWdTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAgsdadiiiLNPNSTFTISAKTHHSRID 417
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 578803167 1708 WTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPGYGQDVRKWP 1750
Cdd:PLN02942 418 TNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPP 460
|
|
| PRK07200 |
PRK07200 |
aspartate/ornithine carbamoyltransferase family protein; Validated |
1887-2097 |
8.23e-09 |
|
aspartate/ornithine carbamoyltransferase family protein; Validated
Pssm-ID: 235961 [Multi-domain] Cd Length: 395 Bit Score: 60.14 E-value: 8.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1887 TKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQ 1966
Cdd:PRK07200 30 TPDELKAVLDVADALRALREENISTKVFNSGLGISVFRDNSTRTRFSYASACNLLGLEVQDLDEGKSQIAHGETVRETAN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1967 TMSCYADVVVLR------------HPQPGAVELAAKHC---RRP-VINAGDGVgEHPTQALLDIFTIREELGTVN---GM 2027
Cdd:PRK07200 110 MISFMADVIGIRddmyigkgnaymREVGAAVDDGYKQGvlpQRPtLVNLQCDI-DHPTQSMADLLHLIEHFGGLEnlkGK 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578803167 2028 TITMVGDL--KHGRTV---HSLACLLTQYRVSLRYVAPPSLRMPPTV----RAFVASRGTKQEEFESIEEALPDTDVLY 2097
Cdd:PRK07200 189 KIAMTWAYspSYGKPLsvpQGIIGLMTRFGMDVTLAHPEGYDLMPEVvevaKKNAKASGGSFRQVNSMEEAFKDADIVY 267
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
187-362 |
1.21e-08 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 57.12 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 187 YNQIRCLCQRGAEVtVVPWDHALDSQEYEGL---FLSNGPGdPASYPSVVSTLSRVLSEPNPRPVFGICLGHQLLALAIG 263
Cdd:PRK07649 13 FNLVQFLGELGQEL-VVKRNDEVTISDIENMkpdFLMISPG-PCSPNEAGISMEVIRYFAGKIPIFGVCLGHQSIAQVFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 264 A---KTYKMRYGNRG---HNQPCLLVGSGRCFLTSQNHGFAVETDSLPaDWAPLFTNANDGSNEGIVHNSLPFFSVQFHP 337
Cdd:PRK07649 91 GevvRAERLMHGKTSlmhHDGKTIFSDIPNPFTATRYHSLIVKKETLP-DCLEVTSWTEEGEIMAIRHKTLPIEGVQFHP 169
|
170 180
....*....|....*....|....*
gi 578803167 338 EHQAGPSDMELLFDiFLETVKEATA 362
Cdd:PRK07649 170 ESIMTSHGKELLQN-FIRKYSPSVT 193
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
498-613 |
1.89e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 59.27 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 498 GVRVLGTPVETIELTEDRraFAAR--MAEIGEHVAP--SEAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREE 573
Cdd:PRK06111 99 GIVFIGPSADIIAKMGSK--IEARraMQAAGVPVVPgiTTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQE 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 578803167 574 LSAlvapAFAHTSQ----------VLVDKSLKGWKEIEYEVVRDAYGNCV 613
Cdd:PRK06111 177 LTK----AFESNKKraanffgngeMYIEKYIEDPRHIEIQLLADTHGNTV 222
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
247-338 |
2.02e-08 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 56.01 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 247 PVFGICLGHQLLALAIGAKTYKMRYGNRG--------HNQPclLVGSGRCFLTSQNHgfAVETDSLPADWAPLFTNANDG 318
Cdd:PRK00758 69 PILGICLGHQLIAKAFGGEVGRGEYGEYAlveveildEDDI--LKGLPPEIRVWASH--ADEVKELPDGFEILARSDICE 144
|
90 100
....*....|....*....|
gi 578803167 319 sNEGIVHNSLPFFSVQFHPE 338
Cdd:PRK00758 145 -VEAMKHKEKPIYGVQFHPE 163
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
498-613 |
2.58e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 58.84 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 498 GVRVLGTPVETIELTEDRRAFAARMAEIGEHVAP--SEAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREEL- 574
Cdd:PRK08654 99 GIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPgtEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELe 178
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 578803167 575 ------SALVAPAFAhTSQVLVDKSLKGWKEIEYEVVRDAYGNCV 613
Cdd:PRK08654 179 daiestQSIAQSAFG-DSTVFIEKYLEKPRHIEIQILADKHGNVI 222
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
491-616 |
4.07e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 58.19 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 491 AGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAAN--SLEQAQAAAERLGYPVLVRAAFALGGLGSGFA 568
Cdd:PRK07178 91 AEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNlaDLDEALAEAERIGYPVMLKATSGGGGRGIRRC 170
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 578803167 569 SNREELS-------ALVAPAFAhTSQVLVDKSLKGWKEIEYEVVRDAYGNCVTYY 616
Cdd:PRK07178 171 NSREELEqnfprviSEATKAFG-SAEVFLEKCIVNPKHIEVQILADSHGNVVHLF 224
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
1401-1729 |
9.95e-08 |
|
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.
Pssm-ID: 460401 [Multi-domain] Cd Length: 334 Bit Score: 56.36 E-value: 9.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1401 LPGLIDVHVHLR--------EPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDApalalaqkLAEAGARCDFALFL 1472
Cdd:pfam01979 3 LPGLIDAHVHLEmgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEA--------LLEAAEELPLGLRF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1473 GASSENAGTLGTVAGSAA-GLKLYLNETFSELRLDSVVQ-WMEHFETWpshlpivaHAEQQTVAAVLMVAQLTQRSVHIc 1550
Cdd:pfam01979 75 LGPGCSLDTDGELEGRKAlREKLKAGAEFIKGMADGVVFvGLAPHGAP--------TFSDDELKAALEEAKKYGLPVAI- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1551 HVAR-KEEILLIKAAKARG---------------LPVTCEVAPHHLFLSHDDLERLGPGKGEVR------PELGSRQDVE 1608
Cdd:pfam01979 146 HALEtKGEVEDAIAAFGGGiehgthlevaesgglLDIIKLILAHGVHLSPTEANLLAEHLKGAGvahcpfSNSKLRSGRI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1609 ALWE--NMAVIDCFASDHAPHTleekcgsRPPPGFPGLETMlpLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTy 1686
Cdd:pfam01979 226 ALRKalEDGVKVGLGTDGAGSG-------NSLNMLEELRLA--LELQFDPEGGLSPLEALRMATINPAKALGLDDKVGS- 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 578803167 1687 VEV----DLehewtipshMPFSKAHWTPFEGQKVKGTVRRVVLRGEV 1729
Cdd:pfam01979 296 IEVgkdaDL---------VVVDLDPLAAFFGLKPDGNVKKVIVKGKI 333
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
187-338 |
1.24e-07 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 53.97 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 187 YNQIRCLCQRGAEVTVVPWDH----ALDSQEYEGLFLSNGPGDPASypsvvSTLSR-VLSEPNPR-PVFGICLGHQLLAL 260
Cdd:CHL00101 13 YNLVQSLGELNSDVLVCRNDEidlsKIKNLNIRHIIISPGPGHPRD-----SGISLdVISSYAPYiPILGVCLGHQSIGY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 261 AIGAKTYKMRYGNRG------HNQPCLLVGSGRCFLTSQNHGFAVETDSLPadwAPLFTNA--NDGSNEGIVHNSLPF-F 331
Cdd:CHL00101 88 LFGGKIIKAPKPMHGktskiyHNHDDLFQGLPNPFTATRYHSLIIDPLNLP---SPLEITAwtEDGLIMACRHKKYKMlR 164
|
....*..
gi 578803167 332 SVQFHPE 338
Cdd:CHL00101 165 GIQFHPE 171
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
391-661 |
2.04e-07 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 55.70 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 391 PPPRKVLILGS--GGLSIgqagefdysgsqaIKALKEENIQTLLInpniATVQTSQGL----ADKVYFLPITPH------ 458
Cdd:COG3919 3 TMRFRVVVLGGdiNALAV-------------ARSLGEAGVRVIVV----DRDPLGPAArsryVDEVVVVPDPGDdpeafv 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 459 -YVTQVIRNERPDgVLLTFGGQTALncgveltkagVLARY------GVRVLGTPVETIELTEDRRAFAARMAEIGEHVAP 531
Cdd:COG3919 66 dALLELAERHGPD-VLIPTGDEYVE----------LLSRHrdeleeHYRLPYPDADLLDRLLDKERFYELAEELGVPVPK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 532 SEAANSLEQAQAAAERLGYPVLVRAA--------FALGGLGSGFASNREELSALVAPAFA------------------HT 585
Cdd:COG3919 135 TVVLDSADDLDALAEDLGFPVVVKPAdsvgydelSFPGKKKVFYVDDREELLALLRRIAAagyelivqeyipgddgemRG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 586 SQVLVDKS-----------LKGW--------------------------KEIEY------EVVRDAYGNcvTYYIIEVNA 622
Cdd:COG3919 215 LTAYVDRDgevvatftgrkLRHYppaggnsaaresvddpeleeaarrllEALGYhgfanvEFKRDPRDG--EYKLIEINP 292
|
330 340 350
....*....|....*....|....*....|....*....
gi 578803167 623 RLSRSSALASKAtGYPLAYVAAKLALGIPLPELRNSVTG 661
Cdd:COG3919 293 RFWRSLYLATAA-GVNFPYLLYDDAVGRPLEPVPAYREG 330
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
216-338 |
2.75e-07 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 53.65 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 216 GLFLSNGPGDPASypSVVStLSRVLSEPNPRPVFGICLGHQLLALAIGAKTYKMRYG-NRGHNQPC---------LLVGS 285
Cdd:PLN02335 65 GVLISPGPGTPQD--SGIS-LQTVLELGPLVPLFGVCMGLQCIGEAFGGKIVRSPFGvMHGKSSPVhydekgeegLFSGL 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 578803167 286 GRCFLTSQNHGFAVETDSLPADWAPLFTNANDGSNEGIVHNSLPFFS-VQFHPE 338
Cdd:PLN02335 142 PNPFTAGRYHSLVIEKDTFPSDELEVTAWTEDGLIMAARHRKYKHIQgVQFHPE 195
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
190-263 |
4.69e-07 |
|
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: 50.29 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 190 IRCLCQRGAEVTVVPWDH-----ALDSQEYEGLFLSNGPGDP---ASYPSVVSTLSRVLSepNPRPVFGICLGHQLLALA 261
Cdd:cd01653 18 LDALREAGAEVDVVSPDGgpvesDVDLDDYDGLILPGGPGTPddlARDEALLALLREAAA--AGKPILGICLGAQLLVLG 95
|
..
gi 578803167 262 IG 263
Cdd:cd01653 96 VQ 97
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
247-353 |
7.59e-07 |
|
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: 153216 [Multi-domain] Cd Length: 189 Bit Score: 51.81 E-value: 7.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 247 PVFGICLGHQLLALAIGAKTYkmrygnrghnqPCLLVGSgrcfltsqNHGFAVetDSLPADWAPLFTnANDGSNEGIVHN 326
Cdd:cd01745 102 PILGICRGMQLLNVALGGTLY-----------QDIRVNS--------LHHQAI--KRLADGLRVEAR-APDGVIEAIESP 159
|
90 100
....*....|....*....|....*....
gi 578803167 327 SLPF-FSVQFHPE-HQAGPSDMELLFDIF 353
Cdd:cd01745 160 DRPFvLGVQWHPEwLADTDPDSLKLFEAF 188
|
|
| PRK06849 |
PRK06849 |
hypothetical protein; Provisional |
969-1156 |
2.53e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235876 [Multi-domain] Cd Length: 389 Bit Score: 52.36 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 969 CRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQF-CQTVGYPCVVRPSYVLSGAAMNVAYTdgdlERF 1047
Cdd:PRK06849 101 CEVLHFDFELLLLLHNKWEFAEQARSLGLSVPKTYLITDPEAIRNFmFKTPHTPYVLKPIYSRFVRRVDLLPK----EAA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1048 LSSaAAVSKEHPVVISKFIQeAKEIDVDAVASDGVVAAIA--ISEHVENAGVHSGDATLVTPpqditaktleRIKAIVHA 1125
Cdd:PRK06849 177 LKE-LPISKDNPWVMQEFIQ-GKEYCSYSIVRSGELRAHScyKPEYCAGSGAQIAFQPINHP----------RIEEFVTH 244
|
170 180 190
....*....|....*....|....*....|..
gi 578803167 1126 VGQELQVTGPFNLQLI-AKDDQLKVIECNVRV 1156
Cdd:PRK06849 245 FVKELNYTGQISFDFIeTENGDAYPIECNPRT 276
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
190-258 |
3.59e-06 |
|
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: 47.20 E-value: 3.59e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578803167 190 IRCLCQRGAEVTVVPWDH-----ALDSQEYEGLFLSNGPGDP---ASYPSVVSTLSRVLSepNPRPVFGICLGHQLL 258
Cdd:cd03128 18 LDALREAGAEVDVVSPDGgpvesDVDLDDYDGLILPGGPGTPddlAWDEALLALLREAAA--AGKPVLGICLGAQLL 92
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
493-613 |
4.19e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 51.67 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 493 VLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAP-SEAA-NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASN 570
Cdd:PRK08462 96 ICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPgSDGAlKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVED 175
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 578803167 571 REEL--SALVAPAFAHTS----QVLVDKSLKGWKEIEYEVVRDAYGNCV 613
Cdd:PRK08462 176 ESDLenLYLAAESEALSAfgdgTMYMEKFINNPRHIEVQILGDKHGNVI 224
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
187-338 |
1.33e-05 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 47.99 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 187 YNQIRCLCQRGAEVTVVPWDH----ALDSQEYEGLFLSNGPGDPASypSVVStLSRVLSEPNPRPVFGICLGHQLLALAI 262
Cdd:PRK08007 13 WNLYQYFCELGADVLVKRNDAltlaDIDALKPQKIVISPGPCTPDE--AGIS-LDVIRHYAGRLPILGVCLGHQAMAQAF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 263 GA---KTYKMRYGNRG---HNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWAplfTNANDGSNE--GIVHNSLPFFSVQ 334
Cdd:PRK08007 90 GGkvvRAAKVMHGKTSpitHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFE---VTAWSETREimGIRHRQWDLEGVQ 166
|
....
gi 578803167 335 FHPE 338
Cdd:PRK08007 167 FHPE 170
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
247-338 |
1.39e-05 |
|
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: 48.41 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 247 PVFGICLGHQLLALAIGAKTY---KMRYGNRGHNQPC----------LLVGSGRCF--LTSQN-------HGFAVetDSL 304
Cdd:pfam07722 107 PILGICRGFQLLNVALGGTLYqdiQEQPGFTDHREHCqvapyapshaVNVEPGSLLasLLGSEefrvnslHHQAI--DRL 184
|
90 100 110
....*....|....*....|....*....|....*.
gi 578803167 305 PADWAPLFTnANDGSNEGIVHNSLPFF--SVQFHPE 338
Cdd:pfam07722 185 APGLRVEAV-APDGTIEAIESPNAKGFalGVQWHPE 219
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
498-613 |
1.95e-05 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 50.14 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 498 GVRVLGTPVETIELTEDRraFAARMA--EIGEHVAPS--EAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREE 573
Cdd:PRK12999 103 GITFIGPTAEVLRLLGDK--VAARNAaiKAGVPVIPGseGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEE 180
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 578803167 574 LSALVAPA-------FAhTSQVLVDKSLKGWKEIEYEVVRDAYGNCV 613
Cdd:PRK12999 181 LEEAFERAkreakaaFG-NDEVYLEKYVENPRHIEVQILGDKHGNVV 226
|
|
| guaA |
PRK00074 |
GMP synthase; Reviewed |
177-338 |
2.98e-05 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 48.89 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 177 RILALDCGLKYNQ-----IRCL---CQrgaevtVVPWDHALDS-QEYE--GLFLSNGPgdpASypsvvstlsrVLSEPNP 245
Cdd:PRK00074 5 KILILDFGSQYTQliarrVRELgvySE------IVPYDISAEEiRAFNpkGIILSGGP---AS----------VYEEGAP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 246 R----------PVFGICLGHQLLALAIGAK---TYKMRYGN---RGHNQPCLLVGSGRCFLTSQNHGFAVETdsLPADWA 309
Cdd:PRK00074 66 RadpeifelgvPVLGICYGMQLMAHQLGGKverAGKREYGRaelEVDNDSPLFKGLPEEQDVWMSHGDKVTE--LPEGFK 143
|
170 180
....*....|....*....|....*....
gi 578803167 310 PLFTNANdGSNEGIVHNSLPFFSVQFHPE 338
Cdd:PRK00074 144 VIASTEN-CPIAAIANEERKFYGVQFHPE 171
|
|
| GATase1_Glutamyl_Hydrolase |
cd01747 |
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ... |
247-341 |
3.44e-05 |
|
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: 47.70 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 247 PVFGICLGHQLLAL----------AIGAKTYKMRYGNRGHNQPCLLVGS----------GRCFlTSQNHGFAVETDSLP- 305
Cdd:cd01747 94 PVWGTCLGFELLTYltsgetllleATEATNSALPLNFTEDALQSRLFKRfppdllkslaTEPL-TMNNHRYGISPENFTe 172
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 578803167 306 ----ADWAP-LFTNANDGSNEGIV---HNSLPFFSVQFHPEHQA 341
Cdd:cd01747 173 ngllSDFFNvLTTNDDWNGVEFIStveAYKYPIYGVQWHPEKNA 216
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
990-1122 |
4.48e-05 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 47.79 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 990 RLLDTIGISQPQWRELS--DLESARQFCQTVGYPCVVRPsyVLSGAA--MNVAYTDGDLERFLSSAAAVSkeHPVVISKF 1065
Cdd:COG1181 101 RVLAAAGLPTPPYVVLRrgELADLEAIEEELGLPLFVKP--AREGSSvgVSKVKNAEELAAALEEAFKYD--DKVLVEEF 176
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578803167 1066 IqEAKEIDVdAVASDGVVAAIAISEHVENAGV-------HSGDATLVTPPqDITAKTLERIKAI 1122
Cdd:COG1181 177 I-DGREVTV-GVLGNGGPRALPPIEIVPENGFydyeakyTDGGTEYICPA-RLPEELEERIQEL 237
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
991-1179 |
7.85e-05 |
|
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: 45.77 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 991 LLDTIGISQPQW-------RELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLssAAAVSKEHPVVIS 1063
Cdd:pfam07478 1 LLKAAGLPVVPFvtftradWKLNPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAI--EEAFQYDEKVLVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1064 KFIqEAKEIDVdAVASDGVVAAIAISEHVENAGV------HSGDATLVTPPQDITAKTLERIKAIVHAVGQELQVTG--- 1134
Cdd:pfam07478 79 EGI-EGREIEC-AVLGNEDPEVSPVGEIVPSGGFydyeakYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRGlar 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578803167 1135 -PFNLQliaKDDQLKVIECN-----VRVSRsFPFVSKTLGVDLVALATRVI 1179
Cdd:pfam07478 157 vDFFLT---EDGEIVLNEVNtipgfTSISM-FPKLAAAAGVSFPDLVDQLI 203
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
502-613 |
9.06e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 47.40 E-value: 9.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 502 LGTPVETIELTEDRRAFAARMAEIGEHVAP-SEAA-NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREEL----- 574
Cdd:PRK05586 103 IGPDSETIELMGNKSNAREIMIKAGVPVVPgSEGEiENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELikafn 182
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 578803167 575 --SALVAPAFAHTSqVLVDKSLKGWKEIEYEVVRDAYGNCV 613
Cdd:PRK05586 183 taKSEAKAAFGDDS-MYIEKFIENPKHIEFQILGDNYGNVV 222
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
522-601 |
1.21e-04 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 46.65 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 522 MAEIGEHVAPSEAANSLEQA----QAAAERLGYPVLVRAAfalgGLGSGF----ASNREELSALVAPAFAHTSQVLVDKS 593
Cdd:PRK01966 131 LAAAGIPVAPYVVLTRGDWEeaslAEIEAKLGLPVFVKPA----NLGSSVgiskVKNEEELAAALDLAFEYDRKVLVEQG 206
|
....*...
gi 578803167 594 LKGwKEIE 601
Cdd:PRK01966 207 IKG-REIE 213
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
395-601 |
2.28e-04 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 45.48 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 395 KVLILgSGGLSigqaGEFD---YSGSQAIKALKEENIQtllinpniatvqtsqgladkVYFLPITPHYVTQVIRNERPDG 471
Cdd:COG1181 2 RVAVL-FGGRS----AEREvslKSGRAVAAALDKAGYD--------------------VVPIGIDVEDLPAALKELKPDV 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 472 VLLtfggqtALNC--GVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANS--LEQAQAAAER 547
Cdd:COG1181 57 VFP------ALHGrgGEDGTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRgeLADLEAIEEE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578803167 548 LGYPVLVRAAFAlgglGSGF----ASNREELSALVAPAFAHTSQVLVDKSLKGwKEIE 601
Cdd:COG1181 131 LGLPLFVKPARE----GSSVgvskVKNAEELAAALEEAFKYDDKVLVEEFIDG-REVT 183
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
498-576 |
2.29e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 46.29 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 498 GVRVLGTPVETIELTEDRrAFAARMA-EIGEHVAPSEAA--NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREEL 574
Cdd:PRK12833 102 GLIFVGPDAQTIRTMGDK-ARARRTArRAGVPTVPGSDGvvASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQL 180
|
..
gi 578803167 575 SA 576
Cdd:PRK12833 181 AA 182
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
536-601 |
2.92e-04 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 44.23 E-value: 2.92e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 536 NSLEQAQAAAERLGYPVLVRAAfalgGLGSGF----ASNREELSALVAPAFAHTSQVLVDKSLKGwKEIE 601
Cdd:pfam07478 23 NPKEWCAQVEEALGYPVFVKPA----RLGSSVgvskVESREELQAAIEEAFQYDEKVLVEEGIEG-REIE 87
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
498-613 |
2.98e-04 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 45.57 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 498 GVRVLGTPVETIELTEDRRAFAARMAEIGEHVAP-SEAAN--SLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREEL 574
Cdd:PRK08463 98 GIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPgTEKLNseSMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDL 177
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 578803167 575 SALV------APAFAHTSQVLVDKSLKGWKEIEYEVVRDAYGNCV 613
Cdd:PRK08463 178 ENAFesckreALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNII 222
|
|
| PRK14570 |
PRK14570 |
D-alanyl-alanine synthetase A; Provisional |
1016-1080 |
4.77e-04 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173034 [Multi-domain] Cd Length: 364 Bit Score: 44.82 E-value: 4.77e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578803167 1016 QTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVskEHPVVISKFIqEAKEIDVDAVASD 1080
Cdd:PRK14570 168 EVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKY--DLTVVIEKFI-EAREIECSVIGNE 229
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
972-1078 |
5.54e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 44.97 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 972 LGTSPEAIDSAENRFKFSRLLDTIGISQPQWRE--LSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLS 1049
Cdd:PRK08654 103 IGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEegIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIE 182
|
90 100 110
....*....|....*....|....*....|...
gi 578803167 1050 S----AAAVSKEHPVVISKFIQEAKEIDVDAVA 1078
Cdd:PRK08654 183 StqsiAQSAFGDSTVFIEKYLEKPRHIEIQILA 215
|
|
| KLF1_2_4_N |
cd21972 |
N-terminal domain of Kruppel-like factor (KLF) 1, KLF2, KLF4, and similar proteins; Kruppel ... |
1752-1877 |
5.98e-04 |
|
N-terminal domain of Kruppel-like factor (KLF) 1, KLF2, KLF4, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF1, KLF2, KLF4, and similar proteins.
Pssm-ID: 409230 [Multi-domain] Cd Length: 194 Bit Score: 43.05 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1752 GAVPQLPPSAPATSEmtTTPERPRRGIPGL-PDGRFHLPPRIHRASDPGLPAVFLRPGAGiPRGSRAWAEEPKEKSSRKV 1830
Cdd:cd21972 32 VTSDNDNPPPPDPAY--PPPESPESCSTVYdSDGCHPTPNAYCGPNGPGLPGHFLLAGNS-PNLGPKIKTENQEQACMPV 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578803167 1831 AEPELM-----GTPDGTCYPPPP----------VPRQASPQNLGTPGLLHPQTSPLLHSLVG 1877
Cdd:cd21972 109 AGYSGHygprePQRVPPAPPPPQyaghfqyhghFNMFSPPLRANHPGMSTVMLTPLSTPPLG 170
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
529-596 |
7.78e-04 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 43.95 E-value: 7.78e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 529 VAPSEAANSLEQAQAAAERLGYPVLVRAafALGG--LGSGFASNREELSALVAPAFAHTSQVLVDKSLKG 596
Cdd:PRK01372 113 TPPWIVLTREEDLLAAIDKLGLPLVVKP--AREGssVGVSKVKEEDELQAALELAFKYDDEVLVEKYIKG 180
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
975-1149 |
1.40e-03 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 43.22 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 975 SPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVV---RPSY------VLSGAAmnvaytdgDLE 1045
Cdd:PRK06019 91 GPDALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLktrRGGYdgkgqwVIRSAE--------DLE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1046 RFLSSAAAVskehPVVISKFIQEAKEIDVDAVAS-DGVVAAIAIsehVENagVHSG---DATLVtpPQDITAKTLERIKA 1121
Cdd:PRK06019 163 AAWALLGSV----PCILEEFVPFEREVSVIVARGrDGEVVFYPL---VEN--VHRNgilRTSIA--PARISAELQAQAEE 231
|
170 180
....*....|....*....|....*....
gi 578803167 1122 IVHAVGQELQVTGPFNLQL-IAKDDQLKV 1149
Cdd:PRK06019 232 IASRIAEELDYVGVLAVEFfVTGDGELLV 260
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
973-1212 |
1.46e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 43.68 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 973 GTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPsyVLSGAAMNVAYTDGDLERFLSSAA 1052
Cdd:PRK02186 96 AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKP--RMGSGSVGVRLCASVAEAAAHCAA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1053 AVSKEHPVVISKFIQEAKEIDVDAVASDGVVAAIAISE-------HVENAGvHSGDATLVTPPQDITAKTLERikaIVHA 1125
Cdd:PRK02186 174 LRRAGTRAALVQAYVEGDEYSVETLTVARGHQVLGITRkhlgpppHFVEIG-HDFPAPLSAPQRERIVRTVLR---ALDA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1126 VGQELqvtGPFNLQLIAKDDQLKVIECNVRVSRSF-P-FVSKTLGVDLVALATRVIMGEEVEPVGLMTGSGVVGVKVPQF 1203
Cdd:PRK02186 250 VGYAF---GPAHTELRVRGDTVVIIEINPRLAGGMiPvLLEEAFGVDLLDHVIDLHLGVAAFADPTAKRYGAIRFVLPAR 326
|
....*....
gi 578803167 1204 SfSRLAGAD 1212
Cdd:PRK02186 327 S-GVLRGLL 334
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
507-613 |
1.66e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 43.25 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 507 ETIELTEDRRAFAARMAEIGEHVAP-SEAA-NSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREELsalvAPAFAH 584
Cdd:PRK08591 108 ETIRLMGDKVTAKATMKKAGVPVVPgSDGPvDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAEL----EKAFSM 183
|
90 100 110
....*....|....*....|....*....|....*....
gi 578803167 585 TSQ----------VLVDKSLKGWKEIEYEVVRDAYGNCV 613
Cdd:PRK08591 184 ARAeakaafgnpgVYMEKYLENPRHIEIQVLADGHGNAI 222
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
507-647 |
1.69e-03 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 43.14 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 507 ETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAFalGGL-GSG--FASNREELSALVApAFA 583
Cdd:COG0026 82 EALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRR--GGYdGKGqvVIKSAADLEAAWA-ALG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 584 HTSQVL---VDkslkgwkeIEYE----VVRDAYGNCVTYYIIE------------VNARLsrSSALASKATGYplayvAA 644
Cdd:COG0026 159 GGPCILeefVP--------FERElsviVARSPDGEVATYPVVEnvhrngildesiAPARI--SEALAAEAEEI-----AK 223
|
...
gi 578803167 645 KLA 647
Cdd:COG0026 224 RIA 226
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
507-615 |
2.01e-03 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 42.83 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 507 ETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAFaLG--GLGSGFASNREELSALVApAFAH 584
Cdd:PRK06019 93 DALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTRR-GGydGKGQWVIRSAEDLEAAWA-LLGS 170
|
90 100 110
....*....|....*....|....*....|....*
gi 578803167 585 TSQVlvdksLKGWKEIEYE----VVRDAYGNCVTY 615
Cdd:PRK06019 171 VPCI-----LEEFVPFEREvsviVARGRDGEVVFY 200
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1005-1186 |
5.09e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 41.65 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1005 LSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLER-FL---SSAAAVSKEHPVVISKFIQEAKEIDVDAVAsD 1080
Cdd:PRK08462 140 LKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENlYLaaeSEALSAFGDGTMYMEKFINNPRHIEVQILG-D 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1081 GVVAAIAISEhvENAGVHSGDATLV--TPPQDITAKTLER-----IKAiVHAVGQELQVTGPFnlqLIAKDDQLKVIECN 1153
Cdd:PRK08462 219 KHGNVIHVGE--RDCSLQRRHQKLIeeSPAVVLDEKTRERlhetaIKA-AKAIGYEGAGTFEF---LLDSNLDFYFMEMN 292
|
170 180 190
....*....|....*....|....*....|...
gi 578803167 1154 VRVSRSFPFVSKTLGVDLVALATRVIMGEEVEP 1186
Cdd:PRK08462 293 TRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPS 325
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
1380-1568 |
7.86e-03 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 41.10 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1380 IGPAPPLKV-----HVDCmtSQKLVrLPGLIDVHVHLREPGGTHKEDFASGT---------------AAALAGGITMVCA 1439
Cdd:COG1228 41 VGPAADLAVpagaeVIDA--TGKTV-LPGLIDAHTHLGLGGGRAVEFEAGGGitptvdlvnpadkrlRRALAAGVTTVRD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578803167 1440 MPNTRPPIIDAPA------LALAQKLAEAGArcdFALFLGASSENAGTLG-----TVAGSAAGLKLYLNETFSELRLDSV 1508
Cdd:COG1228 118 LPGGPLGLRDAIIagesklLPGPRVLAAGPA---LSLTGGAHARGPEEARaalreLLAEGADYIKVFAEGGAPDFSLEEL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578803167 1509 VQWMEhfETWPSHLPIVAHAEQQtvAAVLMVAQLTQRSV-HICHVArkEEIllIKAAKARG 1568
Cdd:COG1228 195 RAILE--AAHALGLPVAAHAHQA--DDIRLAVEAGVDSIeHGTYLD--DEV--ADLLAEAG 247
|
|
| |
