|
Name |
Accession |
Description |
Interval |
E-value |
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
1-1109 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 2031.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 1 MPKRTDIQSILIIGAGPIIIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPITPEVVAKIIEK 80
Cdd:PRK05294 1 MPKRTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 81 ERPDALLPTMGGQTGLNTSLALADMGVLEKFGVELIGANREAIEMAEDRKLFREAMDRIGLENPKATIISApklengkyd 160
Cdd:PRK05294 81 ERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHS--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 161 isagVRQALIDLEHIGLPAIIRPAFTLGGTGGGVAYNRDDYEAIVRSGLDASPVAQVLIDESLLGWKEYEMEVVRDKADN 240
Cdd:PRK05294 152 ----MEEALEVAEEIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 241 AIIVCSIENVDPMGVHTGDSITVAPALTLTDKEYQIMRNGSIAVLREIGVETGGSNVQWAINPKDGRMVVIEMNPRVSRS 320
Cdd:PRK05294 228 CIIVCSIENIDPMGVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVETGGCNVQFALNPKDGRYIVIEMNPRVSRS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 321 SALASKATGFPIAKIAAKLAVGYTLDELDNDITKVTPASFEPTIDYVVTKIPRFAFEKFPGSKPELTTAMKSVGEAMAIG 400
Cdd:PRK05294 308 SALASKATGYPIAKVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 401 RTFHESVQKALASMETGLTGFDEIAIEGApDKAAVIKAISRQTPDRMRLIAQAMRHGLSDEEIVTATAFDPWFLARIREI 480
Cdd:PRK05294 388 RTFEESLQKALRSLEIGVTGLDEDLFEEE-SLEELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEI 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 481 VEAEAAIRKNGLPLDEKGLRKLKMMGFTDARLAKLTGRDEGQVRRARRNLGVTAVFKRIDTCAAEFEAQTPYMYSTYEvp 560
Cdd:PRK05294 467 VELEEELKENGLPLDAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYE-- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 561 amgdVECEARPSDRKKVVILGGGPNRIGQGIEFDYCCCHACFALTKAGYETIMINCNPETVSTDYDTSDRLYFEPLTLEH 640
Cdd:PRK05294 545 ----EECESNPSDRKKVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLED 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 641 VLEILRVEQDngtlHGVIVQFGGQTPLKLANALEAEGIPILGTTPDAIDLAEDRERFQQLLNDLELKQPVNGIASTEAQA 720
Cdd:PRK05294 621 VLEIIEKEKP----KGVIVQFGGQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEA 696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 721 FEIAGRVGYPLVIRPSYVLGGRAMEIVRDTEHLKRYITTAVTVSGDSPVLLDSYLSGAIEVDVDALSDGKTVHVAGIMQH 800
Cdd:PRK05294 697 LEVAEEIGYPVLVRPSYVLGGRAMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICDGEDVLIGGIMEH 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 801 IEEAGVHSGDSACSLPPYSLSRETVAELKAQTEKMALALGVVGLMNVQFAIKDGVIYVLEVNPRASRTVPFVAKATDSAI 880
Cdd:PRK05294 777 IEEAGVHSGDSACSLPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPL 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 881 ASIAARLMAGEPMANFPlraaYPEGVGPetplpfadpltladpntPWFSVKEAVLPFARFPGVDTLLGPEMRSTGEVMGW 960
Cdd:PRK05294 857 AKIAARVMLGKKLAELG----YTKGLIP-----------------PYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGI 915
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 961 DRNFPRAFLKAQMGAGTHLPESGRVFLSIKDADKsDDLANAARDLIAMGFTLVATRGTGAWLKEKGVEAEAVNKVYEGRP 1040
Cdd:PRK05294 916 DRTFGEAFAKAQLAAGNRLPTSGTVFLSVRDRDK-EEVVELAKRLLELGFKILATSGTAKFLREAGIPVELVNKVHEGRP 994
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502831299 1041 NIVDRLKNGDIALVFNTTDGNQSVSDSREIRAVALYDKIPYFTTAAASIAAVAAMKSRAEGEISVRPLQ 1109
Cdd:PRK05294 995 HIVDLIKNGEIDLVINTPTGRQAIRDGFSIRRAALEYKVPYITTLAGARAAVKAIEALKFGELEVRSLQ 1063
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
2-1084 |
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: 1506.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 2 PKRTDIQSILIIGAGPIIIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPITPEVVAKIIEKE 81
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 82 RPDALLPTMGGQTGLNTSLALADMGVLEKFGVELIGANREAIEMAEDRKLFREAMDRIGLENPKATIISApklengkydi 161
Cdd:TIGR01369 81 RPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHS---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 162 sagVRQALIDLEHIGLPAIIRPAFTLGGTGGGVAYNRDDYEAIVRSGLDASPVAQVLIDESLLGWKEYEMEVVRDKADNA 241
Cdd:TIGR01369 151 ---VEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNC 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 242 IIVCSIENVDPMGVHTGDSITVAPALTLTDKEYQIMRNGSIAVLREIGVEtGGSNVQWAINPKDGRMVVIEMNPRVSRSS 321
Cdd:TIGR01369 228 ITVCNMENFDPMGVHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIE-GGCNVQFALNPDSGRYYVIEVNPRVSRSS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 322 ALASKATGFPIAKIAAKLAVGYTLDELDNDITKVTPASFEPTIDYVVTKIPRFAFEKFPGSKPELTTAMKSVGEAMAIGR 401
Cdd:TIGR01369 307 ALASKATGYPIAKVAAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 402 TFHESVQKALASMETGLTGFDEIAIEGAPDKAaVIKAISRQTPDRMRLIAQAMRHGLSDEEIVTATAFDPWFLARIREIV 481
Cdd:TIGR01369 387 TFEEALQKALRSLEIGATGFDLPDREVEPDED-LWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 482 EAEAAIRKNGL-PLDEKGLRKLKMMGFTDARLAKLTGRDEGQVRRARRNLGVTAVFKRIDTCAAEFEAQTPYMYSTYEvp 560
Cdd:TIGR01369 466 DLEEELEEVKLtDLDPELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYE-- 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 561 amGDVEcEARPSDRKKVVILGGGPNRIGQGIEFDYCCCHACFALTKAGYETIMINCNPETVSTDYDTSDRLYFEPLTLEH 640
Cdd:TIGR01369 544 --GERD-DVPFTDKKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFED 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 641 VLEILRVEQdngtLHGVIVQFGGQTPLKLANALEAEGIPILGTTPDAIDLAEDRERFQQLLNDLELKQPVNGIASTEAQA 720
Cdd:TIGR01369 621 VMNIIELEK----PEGVIVQFGGQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEA 696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 721 FEIAGRVGYPLVIRPSYVLGGRAMEIVRDTEHLKRYITTAVTVSGDSPVLLDSYLSGAIEVDVDALSDGKTVHVAGIMQH 800
Cdd:TIGR01369 697 VEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEH 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 801 IEEAGVHSGDSACSLPPYSLSRETVAELKAQTEKMALALGVVGLMNVQFAIKDGVIYVLEVNPRASRTVPFVAKATDSAI 880
Cdd:TIGR01369 777 IEEAGVHSGDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPL 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 881 ASIAARLMAGEPMANFplraaypeGVGPETPLPFadpltladpntpwFSVKEAVLPFARFPGVDTLLGPEMRSTGEVMGW 960
Cdd:TIGR01369 857 AKLAVRVMLGKKLEEL--------GVGKEKEPKY-------------VAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGI 915
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 961 DRNFPRAFLKAQMGAGTHLPESGRVFLSIKDADKsDDLANAARDLIAMGFTLVATRGTGAWLKEKGVEAEAVNKVYEGRP 1040
Cdd:TIGR01369 916 GRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDK-EELLDLARKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEGRP 994
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*
gi 502831299 1041 NIVDRLKNGDIALVFNTTD-GNQSVSDSREIRAVALYDKIPYFTT 1084
Cdd:TIGR01369 995 NILDLIKNGEIELVINTTSkGAGTATDGYKIRREALDYGVPLITT 1039
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
580-1110 |
0e+00 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 722.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 580 LGGGPNRIGQGIEFDYCCCHACFALTKAGYETIMINCNPETVSTDYDTSDRLYFEPLTLEHVLEILRVEQDNGtlhgVIV 659
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDG----VIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 660 QFGGQTPLKLANALEA----EGIPILGTTPDAIDLAEDRERFQQLLNDLELKQPVNGIASTEAQAFEIAGRVGYPLVIRP 735
Cdd:COG0458 77 QFGGQTALNLAVELEEagilEGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 736 SYVLGGRAMEIVRDTEHLKRYITTAVTVSGDSPVLLDSYLSGAIEVDVDALSDGK-TVHVAGIMQHIEEAGVHSGDSACS 814
Cdd:COG0458 157 SYVLGGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEdNVIIVGIMEHIEPAGVHSGDSICV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 815 LPPYSLSRETVAELKAQTEKMALALGVVGLMNVQFAIKDGVIYVLEVNPRASRTVPFVAKATDSAIASIAARLMAGEPMA 894
Cdd:COG0458 237 APPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 895 NFPlraaYPEGVGPEtplpfadpltladpnTPWFSVKEAVLPFARFPGVDTLLGPEMRSTGEVMGWDRNFPRAFLKAQMG 974
Cdd:COG0458 317 ELG----NDTGFEPT---------------LDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 975 AGTHLPesGRVFLSIKDADKSDDLANAARDLIAMGFTLVATRGTGAWLKEKGVEAEAVNKVYEGRPNIVDRLKNGDIALV 1054
Cdd:COG0458 378 LEIGLP--GTVLLSLVADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILV 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 502831299 1055 FNTTDGNQSVSDSREIRAVALYDKIPYFTTAAASIAAVAAMKSRAEGEISVRPLQA 1110
Cdd:COG0458 456 INTLLGAKSLGDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATA 511
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
128-346 |
1.12e-74 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 245.68 E-value: 1.12e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 128 DRKLFREAMDRIGLENPKATIISAPKLEngkydisagvrQALIDLEHIGLPAIIRPAFTLGGTGGGVAYNRDDYEAIVRS 207
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEE-----------EALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFAL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 208 GLDASPVA----QVLIDESLLGWKEYEMEVVRDKADNAIIVCSIENVDPMgvHTGDSITVAPALTLTDKEYQIMRNGSIA 283
Cdd:pfam02786 70 ALAEAPAAfgnpQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502831299 284 VLREIGVETGGsNVQWAINPKDGRMVVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLD 346
Cdd:pfam02786 148 IARHLGYVGAG-TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
435-557 |
5.65e-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: 189.58 E-value: 5.65e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 435 VIKAISRQTPDRMRLIAQAMRHGLSDEEIVTATAFDPWFLARIREIVEAEAAIRKNGLP-LDEKGLRKLKMMGFTDARLA 513
Cdd:smart01096 1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDeLDADLLRKAKRLGFSDRQIA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 502831299 514 KLTGRDEGQVRRARRNLGVTAVFKRIDTCAAEFEAQTPYMYSTY 557
Cdd:smart01096 81 KLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
983-1084 |
1.69e-40 |
|
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: 144.93 E-value: 1.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 983 GRVFLSIKDADKsDDLANAARDLIAMGFTLVATRGTGAWLKEKGVEAEAVNKVYEGRPNIVDRLKNGDIALVFNTTDGNQ 1062
Cdd:cd01424 1 GTVFISVADRDK-PEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEGRPNIVDLIKNGEIQLVINTPSGKR 79
|
90 100
....*....|....*....|..
gi 502831299 1063 SVSDSREIRAVALYDKIPYFTT 1084
Cdd:cd01424 80 AIRDGFSIRRAALEYKVPYFTT 101
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
1-1109 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 2031.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 1 MPKRTDIQSILIIGAGPIIIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPITPEVVAKIIEK 80
Cdd:PRK05294 1 MPKRTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 81 ERPDALLPTMGGQTGLNTSLALADMGVLEKFGVELIGANREAIEMAEDRKLFREAMDRIGLENPKATIISApklengkyd 160
Cdd:PRK05294 81 ERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHS--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 161 isagVRQALIDLEHIGLPAIIRPAFTLGGTGGGVAYNRDDYEAIVRSGLDASPVAQVLIDESLLGWKEYEMEVVRDKADN 240
Cdd:PRK05294 152 ----MEEALEVAEEIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 241 AIIVCSIENVDPMGVHTGDSITVAPALTLTDKEYQIMRNGSIAVLREIGVETGGSNVQWAINPKDGRMVVIEMNPRVSRS 320
Cdd:PRK05294 228 CIIVCSIENIDPMGVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVETGGCNVQFALNPKDGRYIVIEMNPRVSRS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 321 SALASKATGFPIAKIAAKLAVGYTLDELDNDITKVTPASFEPTIDYVVTKIPRFAFEKFPGSKPELTTAMKSVGEAMAIG 400
Cdd:PRK05294 308 SALASKATGYPIAKVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 401 RTFHESVQKALASMETGLTGFDEIAIEGApDKAAVIKAISRQTPDRMRLIAQAMRHGLSDEEIVTATAFDPWFLARIREI 480
Cdd:PRK05294 388 RTFEESLQKALRSLEIGVTGLDEDLFEEE-SLEELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEI 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 481 VEAEAAIRKNGLPLDEKGLRKLKMMGFTDARLAKLTGRDEGQVRRARRNLGVTAVFKRIDTCAAEFEAQTPYMYSTYEvp 560
Cdd:PRK05294 467 VELEEELKENGLPLDAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYE-- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 561 amgdVECEARPSDRKKVVILGGGPNRIGQGIEFDYCCCHACFALTKAGYETIMINCNPETVSTDYDTSDRLYFEPLTLEH 640
Cdd:PRK05294 545 ----EECESNPSDRKKVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLED 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 641 VLEILRVEQDngtlHGVIVQFGGQTPLKLANALEAEGIPILGTTPDAIDLAEDRERFQQLLNDLELKQPVNGIASTEAQA 720
Cdd:PRK05294 621 VLEIIEKEKP----KGVIVQFGGQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEA 696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 721 FEIAGRVGYPLVIRPSYVLGGRAMEIVRDTEHLKRYITTAVTVSGDSPVLLDSYLSGAIEVDVDALSDGKTVHVAGIMQH 800
Cdd:PRK05294 697 LEVAEEIGYPVLVRPSYVLGGRAMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICDGEDVLIGGIMEH 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 801 IEEAGVHSGDSACSLPPYSLSRETVAELKAQTEKMALALGVVGLMNVQFAIKDGVIYVLEVNPRASRTVPFVAKATDSAI 880
Cdd:PRK05294 777 IEEAGVHSGDSACSLPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPL 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 881 ASIAARLMAGEPMANFPlraaYPEGVGPetplpfadpltladpntPWFSVKEAVLPFARFPGVDTLLGPEMRSTGEVMGW 960
Cdd:PRK05294 857 AKIAARVMLGKKLAELG----YTKGLIP-----------------PYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGI 915
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 961 DRNFPRAFLKAQMGAGTHLPESGRVFLSIKDADKsDDLANAARDLIAMGFTLVATRGTGAWLKEKGVEAEAVNKVYEGRP 1040
Cdd:PRK05294 916 DRTFGEAFAKAQLAAGNRLPTSGTVFLSVRDRDK-EEVVELAKRLLELGFKILATSGTAKFLREAGIPVELVNKVHEGRP 994
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502831299 1041 NIVDRLKNGDIALVFNTTDGNQSVSDSREIRAVALYDKIPYFTTAAASIAAVAAMKSRAEGEISVRPLQ 1109
Cdd:PRK05294 995 HIVDLIKNGEIDLVINTPTGRQAIRDGFSIRRAALEYKVPYITTLAGARAAVKAIEALKFGELEVRSLQ 1063
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
2-1084 |
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: 1506.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 2 PKRTDIQSILIIGAGPIIIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPITPEVVAKIIEKE 81
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 82 RPDALLPTMGGQTGLNTSLALADMGVLEKFGVELIGANREAIEMAEDRKLFREAMDRIGLENPKATIISApklengkydi 161
Cdd:TIGR01369 81 RPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHS---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 162 sagVRQALIDLEHIGLPAIIRPAFTLGGTGGGVAYNRDDYEAIVRSGLDASPVAQVLIDESLLGWKEYEMEVVRDKADNA 241
Cdd:TIGR01369 151 ---VEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNC 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 242 IIVCSIENVDPMGVHTGDSITVAPALTLTDKEYQIMRNGSIAVLREIGVEtGGSNVQWAINPKDGRMVVIEMNPRVSRSS 321
Cdd:TIGR01369 228 ITVCNMENFDPMGVHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIE-GGCNVQFALNPDSGRYYVIEVNPRVSRSS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 322 ALASKATGFPIAKIAAKLAVGYTLDELDNDITKVTPASFEPTIDYVVTKIPRFAFEKFPGSKPELTTAMKSVGEAMAIGR 401
Cdd:TIGR01369 307 ALASKATGYPIAKVAAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 402 TFHESVQKALASMETGLTGFDEIAIEGAPDKAaVIKAISRQTPDRMRLIAQAMRHGLSDEEIVTATAFDPWFLARIREIV 481
Cdd:TIGR01369 387 TFEEALQKALRSLEIGATGFDLPDREVEPDED-LWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 482 EAEAAIRKNGL-PLDEKGLRKLKMMGFTDARLAKLTGRDEGQVRRARRNLGVTAVFKRIDTCAAEFEAQTPYMYSTYEvp 560
Cdd:TIGR01369 466 DLEEELEEVKLtDLDPELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYE-- 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 561 amGDVEcEARPSDRKKVVILGGGPNRIGQGIEFDYCCCHACFALTKAGYETIMINCNPETVSTDYDTSDRLYFEPLTLEH 640
Cdd:TIGR01369 544 --GERD-DVPFTDKKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFED 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 641 VLEILRVEQdngtLHGVIVQFGGQTPLKLANALEAEGIPILGTTPDAIDLAEDRERFQQLLNDLELKQPVNGIASTEAQA 720
Cdd:TIGR01369 621 VMNIIELEK----PEGVIVQFGGQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEA 696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 721 FEIAGRVGYPLVIRPSYVLGGRAMEIVRDTEHLKRYITTAVTVSGDSPVLLDSYLSGAIEVDVDALSDGKTVHVAGIMQH 800
Cdd:TIGR01369 697 VEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEH 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 801 IEEAGVHSGDSACSLPPYSLSRETVAELKAQTEKMALALGVVGLMNVQFAIKDGVIYVLEVNPRASRTVPFVAKATDSAI 880
Cdd:TIGR01369 777 IEEAGVHSGDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPL 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 881 ASIAARLMAGEPMANFplraaypeGVGPETPLPFadpltladpntpwFSVKEAVLPFARFPGVDTLLGPEMRSTGEVMGW 960
Cdd:TIGR01369 857 AKLAVRVMLGKKLEEL--------GVGKEKEPKY-------------VAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGI 915
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 961 DRNFPRAFLKAQMGAGTHLPESGRVFLSIKDADKsDDLANAARDLIAMGFTLVATRGTGAWLKEKGVEAEAVNKVYEGRP 1040
Cdd:TIGR01369 916 GRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDK-EELLDLARKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEGRP 994
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*
gi 502831299 1041 NIVDRLKNGDIALVFNTTD-GNQSVSDSREIRAVALYDKIPYFTT 1084
Cdd:TIGR01369 995 NILDLIKNGEIELVINTTSkGAGTATDGYKIRREALDYGVPLITT 1039
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
3-1109 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 1454.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 3 KRTDIQSILIIGAGPIIIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPITPEVVAKIIEKER 82
Cdd:PLN02735 19 KRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 83 PDALLPTMGGQTGLNTSLALADMGVLEKFGVELIGANREAIEMAEDRKLFREAMDRIGLENPKATIisAPKLEngkydis 162
Cdd:PLN02735 99 PDALLPTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGI--ATTLD------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 163 agvrQALIDLEHIG-LPAIIRPAFTLGGTGGGVAYNRDDYEAIVRSGLDASPVAQVLIDESLLGWKEYEMEVVRDKADNA 241
Cdd:PLN02735 170 ----ECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDLADNV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 242 IIVCSIENVDPMGVHTGDSITVAPALTLTDKEYQIMRNGSIAVLREIGVETGGSNVQWAINPKDGRMVVIEMNPRVSRSS 321
Cdd:PLN02735 246 VIICSIENIDPMGVHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVECGGSNVQFAVNPVDGEVMIIEMNPRVSRSS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 322 ALASKATGFPIAKIAAKLAVGYTLDELDNDITKVTPASFEPTIDYVVTKIPRFAFEKFPGSKPELTTAMKSVGEAMAIGR 401
Cdd:PLN02735 326 ALASKATGFPIAKMAAKLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 402 TFHESVQKALASMETGLTGFDEIAIEGAP-DKAAVIKAISRQTPDRMRLIAQAMRHGLSDEEIVTATAFDPWFLARIREI 480
Cdd:PLN02735 406 TFQESFQKALRSLETGFSGWGCAKVKELDwDWEQLKYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKEL 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 481 VEAEAAIRKNGLP-LDEKGLRKLKMMGFTDARLAKLTGRDEGQVRRARRNLGVTAVFKRIDTCAAEFEAQTPYMYSTYev 559
Cdd:PLN02735 486 VDVEQFLKSRSLSeLSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSY-- 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 560 pamgDVECEARPSDRKKVVILGGGPNRIGQGIEFDYCCCHACFALTKAGYETIMINCNPETVSTDYDTSDRLYFEPLTLE 639
Cdd:PLN02735 564 ----DGECESAPTNKKKVLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVE 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 640 HVLEILRVEQDNgtlhGVIVQFGGQTPLKLA----NALEAEGIP---------ILGTTPDAIDLAEDRERFQQLLNDLEL 706
Cdd:PLN02735 640 DVLNVIDLERPD----GIIVQFGGQTPLKLAlpiqKYLDKNPPPsasgngnvkIWGTSPDSIDAAEDRERFNAILNELKI 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 707 KQPVNGIASTEAQAFEIAGRVGYPLVIRPSYVLGGRAMEIVRDTEHLKRYITTAVTVSGDSPVLLDSYLSGAIEVDVDAL 786
Cdd:PLN02735 716 EQPKGGIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDAL 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 787 SDGK-TVHVAGIMQHIEEAGVHSGDSACSLPPYSLSRETVAELKAQTEKMALALGVVGLMNVQFAI-KDGVIYVLEVNPR 864
Cdd:PLN02735 796 ADSEgNVVIGGIMEHIEQAGVHSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAItPSGEVYIIEANPR 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 865 ASRTVPFVAKATDSAIASIAARLMAGEPMANFplraAYPEGVGPetplpfadpltladpntPWFSVKEAVLPFARFPGVD 944
Cdd:PLN02735 876 ASRTVPFVSKAIGHPLAKYASLVMSGKSLKDL----GFTEEVIP-----------------AHVSVKEAVLPFDKFQGCD 934
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 945 TLLGPEMRSTGEVMGWDRNFPRAFLKAQMGAGTHLPESGRVFLSIKDADKsDDLANAARDLIAMGFTLVATRGTGAWLKE 1024
Cdd:PLN02735 935 VLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLPLSGTVFISLNDLTK-PHLVPIARGFLELGFRIVSTSGTAHFLEL 1013
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 1025 KGVEAEAVNKVYEGRPNIVDRLKNGDIALVFNTTDGN-QSVSDSREIRAVALYDKIPYFTTAAASIAAVAAMKSRAEGEI 1103
Cdd:PLN02735 1014 AGIPVERVLKLHEGRPHAGDMLANGQIQLMVITSSGDaLDQKDGRQLRRMALAYKVPIITTVAGALATAQAVKSLKECPI 1093
|
....*.
gi 502831299 1104 SVRPLQ 1109
Cdd:PLN02735 1094 EMIALQ 1099
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
1-1109 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1422.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 1 MPKRTDIQSILIIGAGPIIIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPITPEVVAKIIEK 80
Cdd:PRK12815 1 MPKDTDIQKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 81 ERPDALLPTMGGQTGLNTSLALADMGVLEKFGVELIGANREAIEMAEDRKLFREAMDRIGLENPKATIISApklengkyd 160
Cdd:PRK12815 81 EKPDALLATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTS--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 161 isagVRQALIDLEHIGLPAIIRPAFTLGGTGGGVAYNRDDYEAIVRSGLDASPVAQVLIDESLLGWKEYEMEVVRDKADN 240
Cdd:PRK12815 152 ----VEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEESIAGWKEIEYEVMRDRNGN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 241 AIIVCSIENVDPMGVHTGDSITVAPALTLTDKEYQIMRNGSIAVLREIGVeTGGSNVQWAINPKDGRMVVIEMNPRVSRS 320
Cdd:PRK12815 228 CITVCNMENIDPVGIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGV-VGGCNIQFALDPKSKQYYLIEVNPRVSRS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 321 SALASKATGFPIAKIAAKLAVGYTLDELDNDITKVTPASFEPTIDYVVTKIPRFAFEKFPGSKPELTTAMKSVGEAMAIG 400
Cdd:PRK12815 307 SALASKATGYPIAKIAAKLAVGYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 401 RTFHESVQKALASMETGLTGFdEIAIEGAPDKAAVIKAISRqTPDRMRLIA--QAMRHGLSDEEIVTATAFDPWFLARIR 478
Cdd:PRK12815 387 RNFESAFQKALRSLEIKRNGL-SLPIELSGKSDEELLQDLR-HPDDRRLFAllEALRRGITYEEIHELTKIDPFFLQKFE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 479 EIVEAEAAIRKNGLPLDEKGLRKLKMMGFTDARLAKLTGRDEGQVRRARRNLGVTAVFKRIDTCAAEFEAQTPYMYSTYe 558
Cdd:PRK12815 465 HIVALEKKLAEDGLDLSADLLRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTY- 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 559 vpamgDVECEARPS-DRKKVVILGGGPNRIGQGIEFDYCCCHACFALTKAGYETIMINCNPETVSTDYDTSDRLYFEPLT 637
Cdd:PRK12815 544 -----FGESEAEPSsEKKKVLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLT 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 638 LEHVLEILRVEQdngtLHGVIVQFGGQTPLKLANALEAEGIPILGTTPDAIDLAEDRERFQQLLNDLELKQPVNGIASTE 717
Cdd:PRK12815 619 LEDVLNVAEAEN----IKGVIVQFGGQTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDE 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 718 AQAFEIAGRVGYPLVIRPSYVLGGRAMEIVRDTEHLKRYITTAvtVSGDSPVLLDSYLSGaIEVDVDALSDGKTVHVAGI 797
Cdd:PRK12815 695 EEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAEN--ASQLYPILIDQFIDG-KEYEVDAISDGEDVTIPGI 771
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 798 MQHIEEAGVHSGDSACSLPPYSLSRETVAELKAQTEKMALALGVVGLMNVQFAIKDGVIYVLEVNPRASRTVPFVAKATD 877
Cdd:PRK12815 772 IEHIEQAGVHSGDSIAVLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATG 851
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 878 SAIASIAARLMAGEPMANfplrAAYPEGVGPETPLpfadpltladpntpwFSVKEAVLPFARFPGVDTLLGPEMRSTGEV 957
Cdd:PRK12815 852 VPLAKLATKVLLGKSLAE----LGYPNGLWPGSPF---------------IHVKMPVFSYLKYPGVDNTLGPEMKSTGEV 912
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 958 MGWDRNFPRAFLKAQMGAGTHLPESGRVFLSIKDADKSdDLANAARDLIAMGFTLVATRGTGAWLKEKGVEAEAVNKVYE 1037
Cdd:PRK12815 913 MGIDKDLEEALYKGYEASDLHIPSYGTIFISVRDEDKP-EVTKLARRFAQLGFKLLATEGTANWLAEEGITTGVVEKVQE 991
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502831299 1038 GRPNIVDRLKNGDIALVFNTTDGNQSVSDSREIRAVALYDKIPYFTTAAASIAAVAAMKSRAEGEISVRPLQ 1109
Cdd:PRK12815 992 GSPSLLERIKQHRIVLVVNTSLSDSASEDAIKIRDEALSTHIPVFTELETAQAFLQVLESLALTTQPIQELQ 1063
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
580-1110 |
0e+00 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 722.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 580 LGGGPNRIGQGIEFDYCCCHACFALTKAGYETIMINCNPETVSTDYDTSDRLYFEPLTLEHVLEILRVEQDNGtlhgVIV 659
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDG----VIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 660 QFGGQTPLKLANALEA----EGIPILGTTPDAIDLAEDRERFQQLLNDLELKQPVNGIASTEAQAFEIAGRVGYPLVIRP 735
Cdd:COG0458 77 QFGGQTALNLAVELEEagilEGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 736 SYVLGGRAMEIVRDTEHLKRYITTAVTVSGDSPVLLDSYLSGAIEVDVDALSDGK-TVHVAGIMQHIEEAGVHSGDSACS 814
Cdd:COG0458 157 SYVLGGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEdNVIIVGIMEHIEPAGVHSGDSICV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 815 LPPYSLSRETVAELKAQTEKMALALGVVGLMNVQFAIKDGVIYVLEVNPRASRTVPFVAKATDSAIASIAARLMAGEPMA 894
Cdd:COG0458 237 APPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 895 NFPlraaYPEGVGPEtplpfadpltladpnTPWFSVKEAVLPFARFPGVDTLLGPEMRSTGEVMGWDRNFPRAFLKAQMG 974
Cdd:COG0458 317 ELG----NDTGFEPT---------------LDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 975 AGTHLPesGRVFLSIKDADKSDDLANAARDLIAMGFTLVATRGTGAWLKEKGVEAEAVNKVYEGRPNIVDRLKNGDIALV 1054
Cdd:COG0458 378 LEIGLP--GTVLLSLVADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILV 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 502831299 1055 FNTTDGNQSVSDSREIRAVALYDKIPYFTTAAASIAAVAAMKSRAEGEISVRPLQA 1110
Cdd:COG0458 456 INTLLGAKSLGDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATA 511
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
22-582 |
0e+00 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 688.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 22 QACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPITPEVVAKIIEKERPDALLPTMGGQTGLNTSLA 101
Cdd:COG0458 10 QGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGGQTALNLAVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 102 LADMGVLEkfGVELIGANREAIEMAEDRKLFREAMDRIGLENPKATIISAPKlengkydisagvrQALIDLEHIGLPAII 181
Cdd:COG0458 90 LEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVE-------------EALAIAEEIGYPVIV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 182 RPAFTLGGTGGGVAYNRDDYEAIVRSGLDASPVAQVLIDESLLGWKEYEMEVVRDKADNAIIVCSIENVDPMGVHTGDSI 261
Cdd:COG0458 155 RPSYVLGGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 262 TVAPALTLTDKEYQIMRNGSIAVLREIGVEtGGSNVQWAInpKDGRMVVIEMNPRVSRSSALASKATGFPIAKIAAKLAV 341
Cdd:COG0458 235 CVAPPQTLSDKEYQRLRDATLKIARALGVV-GLCNIQFAV--DDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLAL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 342 GYTLDELDNDiTKvtpasFEPTIDYVVTKIPRFAFEKFPGSKPELTTAMKSVGEAMAIGRTFHESVQKALASMETGLTGf 421
Cdd:COG0458 312 GYTLDELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPG- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 422 dEIAIEGAPDKAAVIKAISRQTPDRMRLIAQAMRHGLSDEEIVTATAFDPWFLARIREIVEAEaaIRKNGLPLDEKGLRK 501
Cdd:COG0458 385 -TVLLSLVADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDE--IELEEIILVINTLLG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 502 LKMMGFTDARLAKLTGRDEGQVRRARRNLGVTAVFKRIDTCAAEFEAQTPYMYSTYEvpamgdVECEARPSDRKKVVILG 581
Cdd:COG0458 462 AKSLGDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYE------YENESEETEEPKVVVIG 535
|
.
gi 502831299 582 G 582
Cdd:COG0458 536 S 536
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
128-346 |
1.12e-74 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 245.68 E-value: 1.12e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 128 DRKLFREAMDRIGLENPKATIISAPKLEngkydisagvrQALIDLEHIGLPAIIRPAFTLGGTGGGVAYNRDDYEAIVRS 207
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEE-----------EALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFAL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 208 GLDASPVA----QVLIDESLLGWKEYEMEVVRDKADNAIIVCSIENVDPMgvHTGDSITVAPALTLTDKEYQIMRNGSIA 283
Cdd:pfam02786 70 ALAEAPAAfgnpQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502831299 284 VLREIGVETGGsNVQWAINPKDGRMVVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLD 346
Cdd:pfam02786 148 IARHLGYVGAG-TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
555-971 |
1.87e-64 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 238.14 E-value: 1.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 555 STYEVPAMGDVECEARPSDRKKVVILGGGPNRIGQGIEFDYCCCHACFALTKAGYETIMINCNPETVSTDYDTSDRLYFE 634
Cdd:PLN02735 4 ADTVTRAWSAATKAGKRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 635 PLTLEHVLEILRVEQDNGTLHgvivQFGGQTPLKLANALEAEGI------PILGTTPDAIDLAEDRERFQQLLNDLELKQ 708
Cdd:PLN02735 84 PMTPELVEQVIAKERPDALLP----TMGGQTALNLAVALAESGIlekygvELIGAKLDAIKKAEDRELFKQAMEKIGLKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 709 PVNGIASTEAQAFEIAGRVG-YPLVIRPSYVLGGRAMEIVRDTEHLKRYITTAVTVSGDSPVLLDSYLSGAIEVDVDALS 787
Cdd:PLN02735 160 PPSGIATTLDECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGWKEYELEVMR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 788 D-GKTVHVAGIMQHIEEAGVHSGDSACSLPPYSLSRETVAELKAQTEKMALALGV-VGLMNVQFAI--KDGVIYVLEVNP 863
Cdd:PLN02735 240 DlADNVVIICSIENIDPMGVHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVeCGGSNVQFAVnpVDGEVMIIEMNP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 864 RASRTVPFVAKATDSAIASIAARLMAGEPMANFplraayPEGVGPETPLPFadpltlaDPNTPWFSVKEAVLPFARFPGV 943
Cdd:PLN02735 320 RVSRSSALASKATGFPIAKMAAKLSVGYTLDQI------PNDITLKTPASF-------EPSIDYVVTKIPRFAFEKFPGS 386
|
410 420
....*....|....*....|....*...
gi 502831299 944 DTLLGPEMRSTGEVMGWDRNFPRAFLKA 971
Cdd:PLN02735 387 QPILTTQMKSVGEAMALGRTFQESFQKA 414
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
435-557 |
5.65e-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: 189.58 E-value: 5.65e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 435 VIKAISRQTPDRMRLIAQAMRHGLSDEEIVTATAFDPWFLARIREIVEAEAAIRKNGLP-LDEKGLRKLKMMGFTDARLA 513
Cdd:smart01096 1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDeLDADLLRKAKRLGFSDRQIA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 502831299 514 KLTGRDEGQVRRARRNLGVTAVFKRIDTCAAEFEAQTPYMYSTY 557
Cdd:smart01096 81 KLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
983-1084 |
1.69e-40 |
|
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: 144.93 E-value: 1.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 983 GRVFLSIKDADKsDDLANAARDLIAMGFTLVATRGTGAWLKEKGVEAEAVNKVYEGRPNIVDRLKNGDIALVFNTTDGNQ 1062
Cdd:cd01424 1 GTVFISVADRDK-PEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEGRPNIVDLIKNGEIQLVINTPSGKR 79
|
90 100
....*....|....*....|..
gi 502831299 1063 SVSDSREIRAVALYDKIPYFTT 1084
Cdd:cd01424 80 AIRDGFSIRRAALEYKVPYFTT 101
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
693-893 |
5.40e-30 |
|
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: 118.56 E-value: 5.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 693 DRERFQQLLNDLELKQP--VNGIASTEAQAFEIAGRVGYPLVIRPSYVLGGRAMEIVRDTEHLKRYITTAVTVS----GD 766
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVpgTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 767 SPVLLDSYLSGAIEVDVDALSD--GKTVHVaGIMQHIEEagVHSGDSACSLPPYSLSRETVAELKAQTEKMALALGVVGL 844
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDahGNCITV-CNRECSDQ--RRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502831299 845 MNVQFAI--KDGVIYVLEVNPRASRTVPFVAKATDSAIASIAARLMAGEPM 893
Cdd:pfam02786 158 GTVEFALdpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
437-515 |
3.72e-29 |
|
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: 111.31 E-value: 3.72e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502831299 437 KAISRQTPDRMRLIAQAMRHGLSDEEIVTATAFDPWFLARIREIVEAEAAIRKNGLPLDEKGLRKLKMMGFTDARLAKL 515
Cdd:pfam02787 1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAGLDLDAELLREAKRLGFSDRQIAKL 79
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
997-1083 |
7.19e-25 |
|
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: 99.47 E-value: 7.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 997 DLANAARDLIAMGFTLVATRGTGAWLKEKGVE--AEAVNKVYEGRPNIVDRLKNGDIALVFNTTDGN--QSVSDSREIRA 1072
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPvvKTLHPKVHGGIPQILDLIKNGEIDLVINTLYPFeaQAHEDGYSIRR 80
|
90
....*....|.
gi 502831299 1073 VALYDKIPYFT 1083
Cdd:smart00851 81 AAENIDIPGPT 91
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
997-1083 |
2.73e-22 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 460462 [Multi-domain] Cd Length: 93 Bit Score: 92.17 E-value: 2.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 997 DLANAARDLIAMGFTLVATRGTGAWLKEKGVEAEAV-NKVYEGRPN----IVDRLKNGDIALVFNTTDGNQS-VSDSREI 1070
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVvEKTGEGRPGgrvqIGDLIKNGEIDLVINTLYPFKAtVHDGYAI 80
|
90
....*....|...
gi 502831299 1071 RAVALYDKIPYFT 1083
Cdd:pfam02142 81 RRAAENIDIPGPT 93
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
668-892 |
6.43e-22 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 96.48 E-value: 6.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 668 KLANALeaeGIPilGTTPDAIDLAEDRERFQQLLNDLELKQPVNGIASTEAQAFEIAGRVGYPLVIRPSYVLGGRAMEIV 747
Cdd:COG0439 34 ELAEEL---GLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 748 RDTEHLKRYITTAVT----VSGDSPVLLDSYLSGaIEVDVDALSDGKTVHVAGIMQHIEEA--GVHSGDSAcslpPYSLS 821
Cdd:COG0439 109 RDEEELEAALAEARAeakaGSPNGEVLVEEFLEG-REYSVEGLVRDGEVVVCSITRKHQKPpyFVELGHEA----PSPLP 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502831299 822 RETVAELKAQTEKMALALGVV-GLMNVQFAI-KDGVIYVLEVNPRAS--RTVPFVAKATDSAIASIAARLMAGEP 892
Cdd:COG0439 184 EELRAEIGELVARALRALGYRrGAFHTEFLLtPDGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEP 258
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
72-342 |
7.78e-19 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 87.62 E-value: 7.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 72 EVVAKIIEKERPDALLptmggqtglntslALADMGVL------EKFGveLIGANREAIEMAEDRKLFREAMDRIGLENPK 145
Cdd:COG0439 7 AAAAELARETGIDAVL-------------SESEFAVEtaaelaEELG--LPGPSPEAIRAMRDKVLMREALAAAGVPVPG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 146 atiisapklengkYDISAGVRQALIDLEHIGLPAIIRPAFTLGGTGGGVAYNRDDYEA----IVRSGLDASPVAQVLIDE 221
Cdd:COG0439 72 -------------FALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAalaeARAEAKAGSPNGEVLVEE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 222 SLLGwKEYEMEVVRDkaDNAIIVCSI---ENVDPMGVHTGDsitVAPALtLTDKEYQIMRNGSIAVLREIGVETGGSNVQ 298
Cdd:COG0439 139 FLEG-REYSVEGLVR--DGEVVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELVARALRALGYRRGAFHTE 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 502831299 299 WAINPkDGRMVVIEMNPRVS--RSSALASKATGFPIAKIAAKLAVG 342
Cdd:COG0439 212 FLLTP-DGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALG 256
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
638-897 |
1.25e-16 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 82.24 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 638 LEHVLEILRVEQdngtLHGVIVqfGGQTPLKL----ANALEAEGIPILGTTPDAIDLAEDRERFQQLLNDLELKQPVNGI 713
Cdd:PRK12767 58 IDRLLDICKKEK----IDLLIP--LIDPELPLlaqnRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 714 ASTEAQAFEI--AGRVGYPLVIRPSYVLGGRAMEIVRDTEHLKRYITTAvtvsgdSPVLLDSYLSGaIEVDVDALSD--G 789
Cdd:PRK12767 132 PESLEDFKAAlaKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYV------PNLIIQEFIEG-QEYTVDVLCDlnG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 790 KTVHVAgIMQHIEeagVHSGDSacslppyslSR-ETV--AELKAQTEKMALALGVVGLMNVQFAIKDGVIYVLEVNPRAS 866
Cdd:PRK12767 205 EVISIV-PRKRIE---VRAGET---------SKgVTVkdPELFKLAERLAEALGARGPLNIQCFVTDGEPYLFEINPRFG 271
|
250 260 270
....*....|....*....|....*....|.
gi 502831299 867 RTVPFvakatdsaiasiaaRLMAGepmANFP 897
Cdd:PRK12767 272 GGYPL--------------SYMAG---ANEP 285
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
668-864 |
5.82e-13 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 72.71 E-value: 5.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 668 KLANALEAEGIPILGTTPDAIDLAEDRERFQQLLNDLELkqPV-----NGIASTEaQAFEIAGRVGYPLVIRPSYVLGGR 742
Cdd:PRK08654 90 EFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGV--PVlpgteEGIEDIE-EAKEIAEEIGYPVIIKASAGGGGI 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 743 AMEIVRDTEHLKRYITTAVTVS----GDSPVLLDSYLSGA--IEVDVDALSDGKTVHVagimqhieeagvhsGDSACSL- 815
Cdd:PRK08654 167 GMRVVYSEEELEDAIESTQSIAqsafGDSTVFIEKYLEKPrhIEIQILADKHGNVIHL--------------GDRECSIq 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502831299 816 ----------PPYSLSRETVAELKAQTEKMALALGVVGLMNVQFAIKDGVIYVLEVNPR 864
Cdd:PRK08654 233 rrhqklieeaPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTR 291
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
672-864 |
1.92e-12 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 70.33 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 672 ALEAEGIPILGTTPDAIDLAEDRERFQQLLNDLELKQPVngIASTEAQAfeiagrvGYPLVIRPSYVLGGRAMEIVRDTE 751
Cdd:COG2232 91 ERLARRLPLLGNPPEVVRRVKDPLRFFALLDELGIPHPE--TRFEPPPD-------PGPWLVKPIGGAGGWHIRPADSEA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 752 hlkryittavtvSGDSPVLLDSYLSGaIEVDVDALSDGKTVHVAGI-MQHIEEAGVH----SGdsacSLPPYSLSRETVA 826
Cdd:COG2232 162 ------------PPAPGRYFQRYVEG-TPASVLFLADGSDARVLGFnRQLIGPAGERpfryGG----NIGPLALPPALAE 224
|
170 180 190
....*....|....*....|....*....|....*...
gi 502831299 827 ELKAQTEKMALALGVVGLMNVQFAIKDGVIYVLEVNPR 864
Cdd:COG2232 225 EMRAIAEALVAALGLVGLNGVDFILDGDGPYVLEVNPR 262
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
570-906 |
1.22e-11 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 67.65 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 570 RPSDRKKVVILGGGPNrigqgiefDYCCCHAcfaLTKAGYETIMINCNPETVSTDYDTSDRLYFEPLT-------LEHVL 642
Cdd:COG3919 1 AMTMRFRVVVLGGDIN--------ALAVARS---LGEAGVRVIVVDRDPLGPAARSRYVDEVVVVPDPgddpeafVDALL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 643 EILRVEQdngtlHGVIVQFGGQTPLKLANALE--AEGIPILGTTPDAIDLAEDRERFQQLLNDLELKQPVNGIASTEAQA 720
Cdd:COG3919 70 ELAERHG-----PDVLIPTGDEYVELLSRHRDelEEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 721 FEIAGRVGYPLVIRPSY--------VLGGRAMEIVRDTEHLKRYITTAVTVSGDspVLLDSYLSGAI--EVDVDALSD-- 788
Cdd:COG3919 145 DALAEDLGFPVVVKPADsvgydelsFPGKKKVFYVDDREELLALLRRIAAAGYE--LIVQEYIPGDDgeMRGLTAYVDrd 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 789 GKTVHVAG---IMQHIEEAGVhsgdsacslppySLSRETV--AELKAQTEKMALALGVVGLMNVQFAI--KDGVIYVLEV 861
Cdd:COG3919 223 GEVVATFTgrkLRHYPPAGGN------------SAARESVddPELEEAARRLLEALGYHGFANVEFKRdpRDGEYKLIEI 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 502831299 862 NPRASRTVPFVAKA-TDsaIASIAARLMAGEPmanFPLRAAYPEGV 906
Cdd:COG3919 291 NPRFWRSLYLATAAgVN--FPYLLYDDAVGRP---LEPVPAYREGV 331
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
984-1084 |
4.86e-11 |
|
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to produce methylglyoxal. The family also includes the C-terminal domain in carbamoyl phosphate synthetase (CPS) where it catalyzes the last phosphorylation of a coaboxyphosphate intermediate to form the product carbamoyl phosphate and may also play a regulatory role. This family also includes inosine monophosphate cyclohydrolase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 238297 [Multi-domain] Cd Length: 112 Bit Score: 60.99 E-value: 4.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 984 RVFLSIKDADKSDdLANAARDLIAMGFTLVATRGTGAWLKEKGVEAEAVNKVYE-GRPNIVDRLKN-GDIALVFNTTDGN 1061
Cdd:cd00532 1 GVFLSVSDHVKAM-LVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRHEdGEPTVDAAIAEkGKFDVVINLRDPR 79
|
90 100
....*....|....*....|....*.
gi 502831299 1062 QSVS---DSREIRAVALYDKIPYFTT 1084
Cdd:cd00532 80 RDRCtdeDGTALLRLARLYKIPVTTP 105
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
691-864 |
1.76e-10 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 60.48 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 691 AEDRERFQQLLNDLELKQPvngiastEAQAFEIAGRVGYPLVIRPSYVLGGRAMEIVRDTEHLKRYIttavtvsgdSPVL 770
Cdd:pfam02655 1 ASDKLKTYKALKNAGVPTP-------ETLQAEELLREEKKYVVKPRDGCGGEGVRKVENGREDEAFI---------ENVL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 771 LDSYLSGaIEVDVDALSDGKTVHVAGI-MQHIEEAGVHSGDSACSLP-PYSLSRETVAELKAQTEKMAlalGVVGLMNVQ 848
Cdd:pfam02655 65 VQEFIEG-EPLSVSLLSDGEKALPLSVnRQYIDNGGSGFVYAGNVTPsRTELKEEIIELAEEVVECLP---GLRGYVGVD 140
|
170
....*....|....*.
gi 502831299 849 FAIKDGVIYVLEVNPR 864
Cdd:pfam02655 141 LVLKDNEPYVIEVNPR 156
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
985-1083 |
2.48e-10 |
|
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases (CPS), including ammonia-dependent CPS Type I, and glutamine-dependent CPS Type III. These are multidomain proteins, in which MGS is the C-terminal domain.
Pssm-ID: 238711 [Multi-domain] Cd Length: 116 Bit Score: 58.85 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 985 VFLSIKDADKSDdLANAARDLIAMGFTLVATRGTGAWLKEKGVEAEAVNKVYE----GRPNIVDRLKNGDIALVFNTTDG 1060
Cdd:cd01423 3 ILISIGSYSKPE-LLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEepqnDKPSLRELLAEGKIDLVINLPSN 81
|
90 100
....*....|....*....|....*
gi 502831299 1061 NQ-SVSDSR-EIRAVALYDKIPYFT 1083
Cdd:cd01423 82 RGkRVLDNDyVMRRAADDFAVPLIT 106
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
667-863 |
2.78e-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: 62.65 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 667 LKLANALEAEGIPILGTtPDAIDLAEDRERFQQLLNDLELKQPVNGIASTEAQAFEIAGRVGYPLVIRPSYVLGGRAMEI 746
Cdd:COG0189 71 LALLRQLEAAGVPVVND-PEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 747 VRDTEHLKRYITTaVTVSGDSPVLLDSYLSGAIEVDVDAL-SDGKTVH-VAGIMQHIEEAG-VHSGDSACslpPYSLSre 823
Cdd:COG0189 150 VEDEDALESILEA-LTELGSEPVLVQEFIPEEDGRDIRVLvVGGEPVAaIRRIPAEGEFRTnLARGGRAE---PVELT-- 223
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502831299 824 tvAELKAQTEKMA--LALGVVGlmnVQFAIKDGVIYVLEVNP 863
Cdd:COG0189 224 --DEERELALRAApaLGLDFAG---VDLIEDDDGPLVLEVNV 260
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
27-342 |
1.15e-09 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 61.48 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 27 DYSGAQACKALREEGYRVILVNSNPATIMT------------DPEMADATYIEpitpeVVAKIIEKERPDALLPTMGGqt 94
Cdd:COG3919 14 DINALAVARSLGEAGVRVIVVDRDPLGPAArsryvdevvvvpDPGDDPEAFVD-----ALLELAERHGPDVLIPTGDE-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 95 glnTSLALADM-GVLEKfGVELIGANREAIEMAEDRKLFREAMDRIGLENPKATIISapklengkydisaGVRQALIDLE 173
Cdd:COG3919 87 ---YVELLSRHrDELEE-HYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLD-------------SADDLDALAE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 174 HIGLPAIIRPA--------FTLGGTGGGVAYNRDDYEAIVRSGLDAS--PVAQVLI---DESLLGwkeyeMEVVRDKADN 240
Cdd:COG3919 150 DLGFPVVVKPAdsvgydelSFPGKKKVFYVDDREELLALLRRIAAAGyeLIVQEYIpgdDGEMRG-----LTAYVDRDGE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 241 AIIVCSIENV--DPMGVHTGDSITVAPALTLTDKeyqimrngSIAVLREIGVeTGGSNVQWAINPKDGRMVVIEMNPRVS 318
Cdd:COG3919 225 VVATFTGRKLrhYPPAGGNSAARESVDDPELEEA--------ARRLLEALGY-HGFANVEFKRDPRDGEYKLIEINPRFW 295
|
330 340
....*....|....*....|....
gi 502831299 319 RSSALASKAtGFPIAKIAAKLAVG 342
Cdd:COG3919 296 RSLYLATAA-GVNFPYLLYDDAVG 318
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
670-894 |
1.44e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 61.69 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 670 ANALEAEGIPILGTTPDAI----DLAEDRERFQqllndlELKQPV----NGIASTEAQAFEIAGRVGYPLVIRPSYVLGG 741
Cdd:PRK12833 95 AEAVEAAGLIFVGPDAQTIrtmgDKARARRTAR------RAGVPTvpgsDGVVASLDAALEVAARIGYPLMIKAAAGGGG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 742 RAMEIVRDTEHLKRYI----TTAVTVSGDSPVLLDSYLSGAIEVDVDALSDGKTVhvagimqhieeagVHSGDSACSL-- 815
Cdd:PRK12833 169 RGIRVAHDAAQLAAELplaqREAQAAFGDGGVYLERFIARARHIEVQILGDGERV-------------VHLFERECSLqr 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 816 ---------PPYSLSRETVAELKAQTEKMALALGVVGLMNVQFAIKD--GVIYVLEVNPRASRTVPFVAKATDSAIASIA 884
Cdd:PRK12833 236 rrqkileeaPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDarGEFYFIEMNTRIQVEHPVTEAITGIDLVQEM 315
|
250
....*....|
gi 502831299 885 ARLMAGEPMA 894
Cdd:PRK12833 316 LRIADGEPLR 325
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
669-864 |
1.18e-08 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 59.38 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 669 LANALEAEGIPILGTTPDAIDLAEDRERFQQLLNDLELkqPVngIASTE------AQAFEIAGRVGYPLVIRPSYVLGGR 742
Cdd:PRK12999 95 FARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGV--PV--IPGSEgpiddiEEALEFAEEIGYPIMLKASAGGGGR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 743 AMEIVRDTEHLKRYITTAVTVS----GDSPVLLDSYLSGA--IEVDVDALSDGKTVHvagimqhieeagVHSGDsaCSL- 815
Cdd:PRK12999 171 GMRIVRSEEELEEAFERAKREAkaafGNDEVYLEKYVENPrhIEVQILGDKHGNVVH------------LYERD--CSVq 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 816 ----------PPYSLSRETVAELKAQTEKMALALGVVGLMNVQFAI-KDGVIYVLEVNPR 864
Cdd:PRK12999 237 rrhqkvveiaPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVdADGNFYFIEVNPR 296
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
669-894 |
1.27e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 58.50 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 669 LANALEAEGIPILGTTPDAIDLAEDRERFQQLLNdlELKQP-VNGIAS---TEAQAFEIAGRVGYPLVIRPSYVLGGRAM 744
Cdd:PRK06111 91 FAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQ--AAGVPvVPGITTnleDAEEAIAIARQIGYPVMLKASAGGGGIGM 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 745 EIVRDTEHLKRYI----TTAVTVSGDSPVLLDSYLSGA--IEVDVDALSDGKTVHVagimqhieeagvhsGDSACSL--- 815
Cdd:PRK06111 169 QLVETEQELTKAFesnkKRAANFFGNGEMYIEKYIEDPrhIEIQLLADTHGNTVYL--------------WERECSVqrr 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 816 --------PPYSLSRETVAELKAQTEKMALALGVVGLMNVQFAI-KDGVIYVLEVNPRASRTVPFVAKATDSAIASIAAR 886
Cdd:PRK06111 235 hqkvieeaPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVdEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLR 314
|
....*...
gi 502831299 887 LMAGEPMA 894
Cdd:PRK06111 315 IAAGEKLS 322
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
677-902 |
1.27e-08 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 59.48 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 677 GIPilGTTPDAIDLAEDRERFQQLLNDLELKQPVNGIASTEAQAFEIAGRVGYPLVIRPSYVLGGRAMEIVRDTEHLKRY 756
Cdd:PRK02186 93 GLP--AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAH 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 757 ITTAVTVSGDSpVLLDSYLSGAiEVDVDALSDGKTVHVAGIMqhieeaGVHSGDSACSLP-----PYSLSRETVAELKAQ 831
Cdd:PRK02186 171 CAALRRAGTRA-ALVQAYVEGD-EYSVETLTVARGHQVLGIT------RKHLGPPPHFVEighdfPAPLSAPQRERIVRT 242
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502831299 832 TEKMALALGV-VGLMNVQFAIKDGVIYVLEVNPR-ASRTVP-FVAKATDSAIASIAARLMAGEPMANFPLRAAY 902
Cdd:PRK02186 243 VLRALDAVGYaFGPAHTELRVRGDTVVIIEINPRlAGGMIPvLLEEAFGVDLLDHVIDLHLGVAAFADPTAKRY 316
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
674-864 |
4.10e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 57.06 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 674 EAEGIPILGTTPDAIDLAEDRERFQQLLNdlELKQPV----NGIASTEAQAFEIAGRVGYPLVIRPSYVLGGRAMEIVRD 749
Cdd:PRK08462 98 SHHNIKFIGPSVEVMALMSDKSKAKEVMK--RAGVPVipgsDGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVED 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 750 TEHLKRYI----TTAVTVSGDSPVLLDSYLSGA--IEVDVDALSDGKTVHVagimqhieeagvhsGDSACSL-------- 815
Cdd:PRK08462 176 ESDLENLYlaaeSEALSAFGDGTMYMEKFINNPrhIEVQILGDKHGNVIHV--------------GERDCSLqrrhqkli 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502831299 816 ---PPYSLSRETVAELKAQTEKMALALGVVGLMNVQFAI-KDGVIYVLEVNPR 864
Cdd:PRK08462 242 eesPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLdSNLDFYFMEMNTR 294
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
668-864 |
7.02e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 56.35 E-value: 7.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 668 KLANALEAEGIPILGTTPDAIDLAEDRERFQQLLndLELKQPV----NGIASTEAQAFEIAGRVGYPLVIRPSYVLGGRA 743
Cdd:PRK08591 90 DFAEICEDSGFTFIGPSAETIRLMGDKVTAKATM--KKAGVPVvpgsDGPVDDEEEALAIAKEIGYPVIIKATAGGGGRG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 744 MEIVRDTEHLKRYITT----AVTVSGDSPVLLDSYLSGAIEVDVDALSDGKTvHVagimqhieeagVHSGDSACSL---- 815
Cdd:PRK08591 168 MRVVRTEAELEKAFSMaraeAKAAFGNPGVYMEKYLENPRHIEIQVLADGHG-NA-----------IHLGERDCSLqrrh 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502831299 816 -------PPYSLSRETVAELKAQTEKMALALGVVGLMNVQFAI-KDGVIYVLEVNPR 864
Cdd:PRK08591 236 qkvleeaPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYeKNGEFYFIEMNTR 292
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
668-864 |
1.58e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 55.10 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 668 KLANALEAEGIPILGTTPDAIDLAEDRERFQQLLNDLELkqPV----NGIASTEAQAFEIAGRVGYPLVIRPSYVLGGRA 743
Cdd:PRK05586 90 KFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGV--PVvpgsEGEIENEEEALEIAKEIGYPVMVKASAGGGGRG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 744 MEIVRDTEHLKRYITTAVTVS----GDSPVLLDSYLSGAIEVDVDALSD--GKTVHVagimqhieeagvhsGDSACSL-- 815
Cdd:PRK05586 168 IRIVRSEEELIKAFNTAKSEAkaafGDDSMYIEKFIENPKHIEFQILGDnyGNVVHL--------------GERDCSLqr 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502831299 816 ---------PPYSLSRETVAELKAQTEKMALALGVVGLMNVQFAI-KDGVIYVLEVNPR 864
Cdd:PRK05586 234 rnqkvleeaPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEMNTR 292
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
30-330 |
8.60e-07 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 52.19 E-value: 8.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 30 GAQACKALREE--GYRVILV---NSNPATIMTD-----PEMADATYIEpitpeVVAKIIEKERPDALLPtmGGQTGLNTS 99
Cdd:PRK12767 12 RVQLVKALKKSllKGRVIGAdisELAPALYFADkfyvvPKVTDPNYID-----RLLDICKKEKIDLLIP--LIDPELPLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 100 LALADMgvLEKFGVELIGANREAIEMAEDRKLFREAMDRIGLENPKatIISAPKLENGKYDISAGvrqalidleHIGLPA 179
Cdd:PRK12767 85 AQNRDR--FEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPK--SYLPESLEDFKAALAKG---------ELQFPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 180 IIRPAFTLGGTGGGVAYNRDDYEAIVRSGLDasPVAQVLIDEsllgwKEYEMEVVRDKADNaiiVCSIENVDPMGVHTGD 259
Cdd:PRK12767 152 FVKPRDGSASIGVFKVNDKEELEFLLEYVPN--LIIQEFIEG-----QEYTVDVLCDLNGE---VISIVPRKRIEVRAGE 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502831299 260 SITvapALTLTDKEYQIMrngSIAVLREIGvETGGSNVQWAINpkDGRMVVIEMNPRVSRSSALASKAtGF 330
Cdd:PRK12767 222 TSK---GVTVKDPELFKL---AERLAEALG-ARGPLNIQCFVT--DGEPYLFEINPRFGGGYPLSYMA-GA 282
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
109-353 |
3.86e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 50.75 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 109 EKFGVELIGANREAIEMAEDRKLFREAMDRIGLenpkatiisaPKLENGKYDISaGVRQALIDLEHIGLPAIIRPAFTLG 188
Cdd:PRK08654 96 EKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGV----------PVLPGTEEGIE-DIEEAKEIAEEIGYPVIIKASAGGG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 189 GTGGGVAYNRDDYEAIVRSgldASPVAQ-------VLIDESLLGWKEYEMEVVRDKADNAIIV----CSIENvdpmgVHT 257
Cdd:PRK08654 165 GIGMRVVYSEEELEDAIES---TQSIAQsafgdstVFIEKYLEKPRHIEIQILADKHGNVIHLgdreCSIQR-----RHQ 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 258 gDSITVAPALTLTDKEYQIMRNGSIAVLREIGVETGGSnVQWAINpkDGRMVVIEMNPRVSRSSALASKATGFPIAKIAA 337
Cdd:PRK08654 237 -KLIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGT-VEFLYS--NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQI 312
|
250
....*....|....*.
gi 502831299 338 KLAVGYTLDELDNDIT 353
Cdd:PRK08654 313 KIAAGEELSFKQEDIT 328
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
669-864 |
6.90e-06 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 50.46 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 669 LANALEAEGIPILGTTPDAIDLAEDRERFQQLLndLELKQPVngIASTE------AQAFEIAGRVGYPLVIRPSYVLGGR 742
Cdd:COG1038 94 FARACEEAGITFIGPSPEVLEMLGDKVAARAAA--IEAGVPV--IPGTEgpvddlEEALAFAEEIGYPVMLKAAAGGGGR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 743 AMEIVRDTEHLKRYITTAVTVS----GDSPVLLDSYLSGA--IEVDVDALSDGKTVHVagimqhieeagvHSGDsaCSL- 815
Cdd:COG1038 170 GMRVVRSEEELEEAFESARREAkaafGDDEVFLEKYIERPkhIEVQILGDKHGNIVHL------------FERD--CSVq 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 816 ----------PPYSLSRETVAELKAQTEKMALALGVVGLMNVQFAI-KDGVIYVLEVNPR 864
Cdd:COG1038 236 rrhqkvveiaPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVdDDGNFYFIEVNPR 295
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
84-352 |
1.86e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 48.56 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 84 DALLPTMGGqtgLNTSLALADmgVLEKFGVELIGANREAIEMAEDRKLFREAMDriglenpKATIISAPKLENGKYDISA 163
Cdd:PRK07178 75 DALHPGYGF---LSENAELAE--ICAERGIKFIGPSAEVIRRMGDKTEARRAMI-------KAGVPVTPGSEGNLADLDE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 164 GVRQAlidlEHIGLPAIIRPafTLGGTGGGV------AYNRDDYEAIVRSGLDASPVAQVLIDESLLGWKEYEMEVVRDK 237
Cdd:PRK07178 143 ALAEA----ERIGYPVMLKA--TSGGGGRGIrrcnsrEELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 238 ADNAIIV----CSIENvdpmgvHTGDSITVAPALTLTDKEYQIMRNGSIAVLREIGVETGGSnVQWAINpKDGRMVVIEM 313
Cdd:PRK07178 217 HGNVVHLferdCSIQR------RNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGT-VEFLLD-ADGEVYFMEM 288
|
250 260 270
....*....|....*....|....*....|....*....
gi 502831299 314 NPRVSRSSALASKATGFPIAKIAAKLAVGYTLDELDNDI 352
Cdd:PRK07178 289 NTRVQVEHTITEEITGIDIVREQIRIASGLPLSYKQEDI 327
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
768-906 |
3.10e-05 |
|
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to carbamoyl phosphate synthetase. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.
Pssm-ID: 434824 [Multi-domain] Cd Length: 131 Bit Score: 44.91 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 768 PVLLDSYLSGAiEVDVDALSDGKTVHVA-------GIMQHIEEagvhsgdsacslppyslsRETVAELkaqTEKMALALG 840
Cdd:pfam15632 4 PLLVMEYLPGP-EYSVDCLAGHGELIAAvprrkgdGGIQTLED------------------DPELIEA---ARRLAEAFG 61
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502831299 841 VVGLMNVQFAIKDGVIYVLEVNPRASRTVPfVAKATDSAIASIAARLMAGEPMA-----NFPLRAAYPEGV 906
Cdd:pfam15632 62 LDGLFNVQFRYDGDGPKLLEINPRMSGGIG-YSCLAGVNLPYLALKLLLGLETPdpvepRLGLRVREIEKV 131
|
|
| PRK14572 |
PRK14572 |
D-alanyl-alanine synthetase A; Provisional |
673-875 |
3.23e-05 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173036 [Multi-domain] Cd Length: 347 Bit Score: 47.59 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 673 LEAEGIPILGTTPDAIDLAEDRERFQQLLndLELKQPVNGIASTEAQAFEIAGR--------VGYPLVIRPsyVLGGRAM 744
Cdd:PRK14572 110 LDTLGIPYTGSGVLASALAMDKTRANQIF--LQSGQKVAPFFELEKLKYLNSPRktllklesLGFPQFLKP--VEGGSSV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 745 EI--VRDTEHLKRYIttAVTVSGDSPVLLDSYLSGaIEVDVDALS---DGKTVHVAGIMQHIE--------EAGVHSGDS 811
Cdd:PRK14572 186 STykITNAEQLMTLL--ALIFESDSKVMSQSFLSG-TEVSCGVLEryrGGKRNPIALPATEIVpggeffdfESKYKQGGS 262
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502831299 812 AcSLPPYSLSRETVAELKAQTEKMALALGVVGLMNVQFAIKDGVIYVLEVN--PRASRT--VPFVAKA 875
Cdd:PRK14572 263 E-EITPARISDQEMKRVQELAIRAHESLGCKGYSRTDFIIVDGEPHILETNtlPGMTETslIPQQAKA 329
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
727-864 |
5.13e-05 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 316093 [Multi-domain] Cd Length: 160 Bit Score: 44.58 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 727 VGYPLVIRPSYVLGGRAMEIVRDTEHLKRYI------------TTAVTVSGDSPVLLDSYLSGAiEVDVDAL--SDGKTV 792
Cdd:pfam13535 1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAFaaireeieqwkeMYPEAVVDGGSFLVEEYIEGE-EFAVDAYfdENGEPV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502831299 793 hVAGIMQHiEEAGVHSGDSACSLPPYSLSRETVAELKAQTEKMALALGVV-GLMNVQFAI-KDGVIYVLEVNPR 864
Cdd:pfam13535 80 -ILNILKH-DFASSEDVSDRIYVTSASIIRETQAAFTEFLKRINALLGLKnFPVHIELRVdEDGQIIPIEVNPL 151
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
603-863 |
5.31e-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: 46.64 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 603 ALTKAGYETIMINCNPETVSTDYDTS--DRLYfePLtlehvleilrveqdngtLHGVivqFG--GQTPLklanALEAEGI 678
Cdd:COG1181 27 ALDKAGYDVVPIGIDVEDLPAALKELkpDVVF--PA-----------------LHGR---GGedGTIQG----LLELLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 679 PILGTTPDAIDLAEDRERFQQLLNDLELKQP----VNgiASTEAQAFEIAGRVGYPLVIRPsyVLGG--RAMEIVRDTEH 752
Cdd:COG1181 81 PYTGSGVLASALAMDKALTKRVLAAAGLPTPpyvvLR--RGELADLEAIEEELGLPLFVKP--AREGssVGVSKVKNAEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 753 LKRYITTAVTVsgDSPVLLDSYLSGaIEVDVdALSDGKTVHVAGIMQHIEEAGV-------HSGDSACSLPPySLSRETV 825
Cdd:COG1181 157 LAAALEEAFKY--DDKVLVEEFIDG-REVTV-GVLGNGGPRALPPIEIVPENGFydyeakyTDGGTEYICPA-RLPEELE 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 502831299 826 AELKAQTEKMALALGVVGLMNVQFAI-KDGVIYVLEVNP 863
Cdd:COG1181 232 ERIQELALKAFRALGCRGYARVDFRLdEDGEPYLLEVNT 270
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
657-894 |
4.78e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 43.94 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 657 VIVQFGGQTPLKlaNALEAEGIPIlgtTPDAidlaedrerfqqllndlelkqpvNGIASTEAQAFEIAGRVGYPLVIRPS 736
Cdd:PRK07178 108 VIRRMGDKTEAR--RAMIKAGVPV---TPGS-----------------------EGNLADLDEALAEAERIGYPVMLKAT 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 737 YVLGGRAMEIVRDTEHLK----RYITTAVTVSGDSPVLLDSYLSGA--IEVDVDALSDGKTVHV----AGIMQH----IE 802
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEqnfpRVISEATKAFGSAEVFLEKCIVNPkhIEVQILADSHGNVVHLferdCSIQRRnqklIE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 803 EAgvhsgdsacslPPYSLSRETVAELKAQTEKMALALGVVGLMNVQFAI-KDGVIYVLEVNPRASRTVPFVAKATDSAIA 881
Cdd:PRK07178 240 IA-----------PSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLdADGEVYFMEMNTRVQVEHTITEEITGIDIV 308
|
250
....*....|...
gi 502831299 882 SIAARLMAGEPMA 894
Cdd:PRK07178 309 REQIRIASGLPLS 321
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
59-352 |
2.64e-03 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 41.72 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 59 EMADATY---IEPIT----PEVVAKIIEKERPDALLPTMGGqtgLNTSLALADMgvLEKFGVELIGANREAIEMAEDRKL 131
Cdd:PRK08463 43 KIADEAYrigTDPIKgyldVKRIVEIAKACGADAIHPGYGF---LSENYEFAKA--VEDAGIIFIGPKSEVIRKMGNKNI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 132 FREAMDRIGlenpkatIISAPKLEN-GKYDISAGVRQAlidlEHIGLPAIIRPAFTLGGTGGGVAYNRDD----YEAIVR 206
Cdd:PRK08463 118 ARYLMKKNG-------IPIVPGTEKlNSESMEEIKIFA----RKIGYPVILKASGGGGGRGIRVVHKEEDlenaFESCKR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 207 SGLDASPVAQVLIDESLLGWKEYEMEVVRDKADNAIIV----CSIENvdpmgvHTGDSITVAPALTLTDKEYQIMRNGSI 282
Cdd:PRK08463 187 EALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLcerdCSIQR------RHQKVIEIAPCPSISDNLRKTMGVTAV 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 283 AVLREIGVETGGSnVQWAINPKDgRMVVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLDELDNDI 352
Cdd:PRK08463 261 AAAKAVGYTNAGT-IEFLLDDYN-RFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEILDLEQSDI 328
|
|
| PRK14571 |
PRK14571 |
D-alanyl-alanine synthetase A; Provisional |
654-885 |
2.98e-03 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 184751 [Multi-domain] Cd Length: 299 Bit Score: 40.96 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 654 LHGVIVQFGgqtplKLANALEAEGIPILGTTPDAIDLAedrerFQQLLNDLELKQPVNGIASTEAQAFEIAGRVGYPLVI 733
Cdd:PRK14571 61 LHGTFGEDG-----TLQAILDFLGIRYTGSDAFSSMIC-----FDKLLTYRFLKGTVEIPDFVEIKEFMKTSPLGYPCVV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502831299 734 RPSYVLGGRAMEIVRDTEHLKRYITTAVTVSGDspVLLDSYLSGAiEVDVDALSDGKTVHVAGIMQ-------HIEEAGV 806
Cdd:PRK14571 131 KPRREGSSIGVFICESDEEFQHALKEDLPRYGS--VIVQEYIPGR-EMTVSILETEKGFEVLPILElrpkrrfYDYVAKY 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502831299 807 HSGDSACSLPPySLSRETVAELKAQTEKMALALGVVGLMNVQFAIKDGVIYVLEVNprasrTVPFVAKATDSAIASIAA 885
Cdd:PRK14571 208 TKGETEFILPA-PLNPEEERLVKETALKAFVEAGCRGFGRVDGIFSDGRFYFLEIN-----TVPGLTELSDLPASAKAG 280
|
|
| |
