|
Name |
Accession |
Description |
Interval |
E-value |
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
34-1554 |
0e+00 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 1782.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 34 KQGLYDPRNEHDACGVGFVAHLKGEKSHQIVRDGLFMLENLTHRGAVGADPLMGDGAGILVQIPDRFFREEMAKQGVTLP 113
Cdd:PRK11750 2 HMGLYDPSLERDNCGFGLIAHMEGEPSHKLVRTAIHALARMTHRGGIAADGKTGDGCGLLLQKPDRFFRAVAEEAGWRLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 114 KagEYAVGYLFMPRDEALIAHFKEVISEVVAEEGQIVLGFRDVPVDNSSLSkapDIA-ATEPHHVQVFIGAGREAaSSDE 192
Cdd:PRK11750 82 K--NYAVGMVFLNQDPELAAAARRILEEELQRETLSVVGWREVPTNPSVLG---EIAlSSLPRIEQVFVNAPAGW-RERD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 193 FERRLFTLRKVISNRIYAEADggdlgFYIVSLSTTTIVYKGMFLAYQVGAYYKDLADERFQSAVALVHQRFSTNTFPSWK 272
Cdd:PRK11750 156 FERRLFIARRRIEKRLADDKD-----FYVCSLSNLVIIYKGLMMPADLPRFYLDLADLRLESAICVFHQRFSTNTLPRWP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 273 LAHPYRMVAHNGEINTLRGNVNWMAARQASVSSPLFgDDISKLWPISYEGQSDTACFDNALEFLVRGGYSLSHAVMMLIP 352
Cdd:PRK11750 231 LAQPFRYLAHNGEINTITGNRQWARARAYKFQTPLI-PDLQEAAPFVNETGSDSSSLDNMLELLLAGGMDLFRAMRLLVP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 353 EAWAGNQLMSPERKAFYEYHAALMEPWDGPAAVAFTDGRQIGATLDRNGLRPARYIVTSDDRVIMASEAGVLPVAEDKIV 432
Cdd:PRK11750 310 PAWQNNPDMDPDLRAFYEFNSMHMEPWDGPAGIVMTDGRYAACNLDRNGLRPARYVITKDKLITLASEVGIWDYQPDEVV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 433 KKWRLQPGKMLLIDMEEGRIISDEEVKSSLAGKHPYRQWLDNTQLILEELKPVEPRALRR----DVSLIDRQQAFGYTHE 508
Cdd:PRK11750 390 EKGRVGPGELLVIDTRTGRILHSAEIDNDLKSRHPYKEWLEKNVRRLVPFEELPDEQVGSreldDDTLKSYQKQFQYSFE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 509 DTKLLMSPMATTGQEAIGSMGTDTPISAMSDKPKLLYTYFKQNFAQVTNPPIDPIREELVMSLVSFIGPRPNILdHEGMA 588
Cdd:PRK11750 470 ELDQVIRVLAENGQEAVGSMGDDTPMAVLSSQPRSIYDYFRQQFAQVTNPPIDPLREAHVMSLATCIGREMNVF-CETEG 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 589 HAKRLEVRQPILTNGDLEKIRSIGhtEDRFDTKTLDFTYDISRGaeGMLEMLDRLCERAEAAVKGGYNIIVLSDRQIGPD 668
Cdd:PRK11750 549 HAHRVIFKSPVLSYSDFKQLTTLD--EEHYRADTLDLNYDPEET--GLEAAIKRLCDEAEQAVRDGTVLLVLSDRNIAKG 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 669 RVAIPALLATAAVHHHLIRKGLRTSVGLVVESGEPREIHHFCLLAGYGAEAINPYLAFDTLVDMHKRGEFPKEVDEKEVV 748
Cdd:PRK11750 625 RLPIPAAMAVGAVQHRLVDKGLRCDANIIVETASARDPHHFAVLLGFGATAVYPYLAYETLGDLVDTGEILKDYRQVMLN 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 749 YRyiKAVGKGILKVMSKMGISTYQSYCGAQIFDAVGLSSALVGKYFFGTATTIEGIGLEEIAAETVARHKAAFgsdpvLA 828
Cdd:PRK11750 705 YR--KGINKGLYKIMSKMGISTIASYRGSQLFEAVGLHDDVVDLCFKGVVSRIGGASFEDFEQDQKNLSKRAW-----LA 777
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 829 N-TLDIGGEYAFRMRGESHAWTPDAIASLQHAVR-GNAEDrYREFSAMMNESAsrMNTIRGLFTIKGAEEvgrkPIPIEE 906
Cdd:PRK11750 778 RkPIDQGGLLKYVHGGEYHAYNPDVVNTLQKAVQsGDYSD-YQEYAKLVNERP--VATLRDLLALKPADN----PIPLDE 850
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 907 VEPAAEIVKRFSTGAMSFGSISREAHTTLAVAMNRIGGKSNTGEGGEESDRYlplpdgstNPER-SAIKQIASGRFGVTT 985
Cdd:PRK11750 851 VEPAEELFKRFDSAAMSIGALSPEAHEALAIAMNRLGGRSNSGEGGEDPARY--------GTEKvSKIKQVASGRFGVTP 922
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 986 EYLVNADVLQIKVAQGAKPGEGGQLPGHKVDATVAKTRHSTPGVGLISPPPHHDIYSIEDLAQLIYDLKNVNPEADVSVK 1065
Cdd:PRK11750 923 AYLVNAEVLQIKVAQGAKPGEGGQLPGDKVNPLIARLRYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKALVSVK 1002
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1066 LVSEVGVGTVAAGVAKARADHITIAGFDGGTGASPLTSLKHAGSPWEIGLAETQQTLVLNGLRSRIALQVDGGLKTGRDV 1145
Cdd:PRK11750 1003 LVSEPGVGTIATGVAKAYADLITISGYDGGTGASPLTSVKYAGSPWELGLAETHQALVANGLRHKIRLQVDGGLKTGLDV 1082
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1146 VIGALLGADEFGFATAPLIAAGCIMMRKCHLNTCPVGVATQDPVLRKR-FKGTPEHVVNYFFFVAEEVREILASLGARRL 1224
Cdd:PRK11750 1083 IKAAILGAESFGFGTGPMVALGCKYLRICHLNNCATGVATQDEKLRKNhYHGLPEMVMNYFEFIAEETREWMAQLGVRSL 1162
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1225 DDIIGSSDLLDR-DRMIEhwKARGLDFSRIFHKVEAPK-EATYWTERQNHPID-DILDRRLIEKAKLALETKVPVAFEAA 1301
Cdd:PRK11750 1163 EDLIGRTDLLEElEGETA--KQQKLDLSPLLETAEPPAgKALYCTEERNPPFDkGLLNEQMLQQAKPAIEAKQGGEFWFD 1240
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1302 IKNVDRSAGAMLSGALAKRWGHKGLKDDTIHVTLKGTAGQSFGAFLARGITFDLVGDGNDYVGKGLSGGRIIVRPPENAR 1381
Cdd:PRK11750 1241 IRNTDRSVGARLSGEIARRHGNQGMADAPIKLRFTGTAGQSFGVWNAGGLELYLEGDANDYVGKGMAGGKIVIRPPVGSA 1320
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1382 IVPHQSIIVGNTVLYGAISGECYFNGVAGERFAVRNSGAIAVVEGVGDHGCEYMTGGVVVVLGGTGRNFAAGMSGGVAYV 1461
Cdd:PRK11750 1321 FRSHETAIIGNTCLYGATGGKLFAAGRAGERFAVRNSGAIAVVEGIGDHGCEYMTGGIVCVLGKTGVNFGAGMTGGFAYV 1400
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1462 LDEEGDFARRCNMAMVELQPVPeeddmleklhhhggdlmhkgmvdvsgDMTRHdEERLYQLISNHLHYTGSVRAKEILDH 1541
Cdd:PRK11750 1401 LDEDGDFVDRVNHELVEILRVE--------------------------DLEIH-REHLRGLITEHVEETGSEWGEEILAN 1453
|
1530
....*....|...
gi 503610770 1542 WADYRPKFRKVMP 1554
Cdd:PRK11750 1454 FDDYLRKFWLVKP 1466
|
|
| GltB1 |
COG0067 |
Glutamate synthase domain 1 [Amino acid transport and metabolism]; Glutamate synthase domain 1 ... |
28-1574 |
0e+00 |
|
Glutamate synthase domain 1 [Amino acid transport and metabolism]; Glutamate synthase domain 1 is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 439837 [Multi-domain] Cd Length: 1520 Bit Score: 1447.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 28 PSGLPRKQGLYDPRNEHDACGVGFVAHLKGEKSHQIVRDGLFMLENLTHRGAVGADPLMGDGAGILVQIPDRFFREEMAK 107
Cdd:COG0067 4 NSGLPAAQGLYDPAFEHDACGVGFVAHIKGRKSHDIVEDALEALENLEHRGAVGADGKTGDGAGILIQIPDAFFRAEAAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 108 QGVTLPKAGEYAVGYLFMPRDEALIAHFKEVISEVVAEEGQIVLGFRDVPVDNSSLSKApdIAATEPHHVQVFIGAGrEA 187
Cdd:COG0067 84 LGIELPEPGEYAVGMVFLPQDEAARAAARAIIEEILAEEGLTVLGWRDVPVDPSVLGET--ARATEPVIEQVFVARP-DG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 188 ASSDEFERRLFTLRKVISNRIYAEADGGDlGFYIVSLSTTTIVYKGMFLAYQVGAYYKDLADERFQSAVALVHQRFSTNT 267
Cdd:COG0067 161 LDGDAFERKLYVARKRIEKAIRALGLDDE-DFYICSLSSRTIVYKGMLTPEQLGEFYPDLQDPRFESALALVHQRFSTNT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 268 FPSWKLAHPYRMVAHNGEINTLRGNVNWMAARQASVSSPLFGDDISKLWPISYEGQSDTACFDNALEFLVRGGYSLSHAV 347
Cdd:COG0067 240 FPSWPLAQPFRYLAHNGEINTLRGNRNWMRAREALLASPLFGDDLEKLLPIVNPGGSDSASLDNVLELLVLGGRSLPHAM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 348 MMLIPEAWAGNQLMSPERKAFYEYHAALMEPWDGPAAVAFTDGRQIGATLDRNGLRPARYIVTSDDRVIMASEAGVLPVA 427
Cdd:COG0067 320 MMLIPEAWENNPDMDPERRAFYEYHSALMEPWDGPAAIVFTDGRQIGATLDRNGLRPARYVVTKDGLVILASEVGVLDIP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 428 EDKIVKKWRLQPGKMLLIDMEEGRIISDEEVKSSLAGKHPYRQWLDNTQLILEELKPVEPRALRRDVSLIDRQQAFGYTH 507
Cdd:COG0067 400 PEDIVEKGRLQPGKMLLVDLEEGRIIDDEEIKAELAAAHPYGEWLKENRIRLEDLPEPEEEPAPDDDLLLRRQQAFGYTE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 508 EDTKLLMSPMATTGQEAIGSMGTDTPISAMSDKPKLLYTYFKQNFAQVTNPPIDPIREELVMSLVSFIGPRPNILDHEGM 587
Cdd:COG0067 480 EEELLLLLPMAAGGEEEGGSGGDDDPAALLSSSRLLLYYYFFQFFAQVTNPPPDIIREEVVSSLLTTGGGGNNLLLEEEE 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 588 AHAKRLEVRQPILTNGDLEKIRSIGHTEDRFDTKTLDFTYDISRGAEGMLEMLDRLCERAEAAVKGGYNIIVLSDRQIGP 667
Cdd:COG0067 560 ARRRLLLLPPPLLNELLLLLLRLLDGDFKSTTTITLLDLADGAGGGAAAAAAAAEAAAAAAAAAVLLILIIDLSDDDSDA 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 668 DRVAIPALLATAAVHHHLIRKGLRTSVGLVVESGEPREIHHFCLLAGYGAEAINPYLAFDTLVDMHKRGEfPKEVDEKEV 747
Cdd:COG0067 640 APAPLAAAAAAHHHHLHLLRRRTRLLVVVEVEAVEHHHHHLLLGGGGAAAAAAALYLALELLLDGLLLGL-EDAAAAAAA 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 748 VYRYIKAVGKGILKVMSKMGISTYQSYCGAQIFDAVGLSSALVGKYFFGTATTIEGIGLEEIAAETVARHKAAFGSDPVL 827
Cdd:COG0067 719 KKKKKKKKGKLKKKKMSGIISSSSGSYGAAAIFGALGLVVVVFFTFTTTTGGGGGGGGLDEEAEEEAARAAAAAAEPGGL 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 828 ANTLDIGGEYAFRMRGESHAWTPDAIASLQHAVRGNAEDRYREFSAMMNESASRMNTIRGLFTIKGAEEVgrkPIPIEEV 907
Cdd:COG0067 799 LLGLGGGGGGEYGRRREGELHLLLQAATAAAAAAYRAYKYYRFARYTALLDLLRLLLLLLLLLFEEEEEE---EEPEEEE 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 908 EPAAEIVKRFSTGAMSFGSISREAHTTLAVAMNRIGGKSNTGEGGEESDRylplpdGSTNPERSAIKQIASGRFGVTTEY 987
Cdd:COG0067 876 EEEESSAIAAASSAAASAAASAAAAAAAAGAGGGGGGGGGGGGGGGEGRR------ASGGSGSSSSASVAAAGGGVVVGA 949
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 988 LVNADVLQIKVAQGAKPGEGGQLPGHKVDATVAKTRHSTPGVGLISPPPHHDIYSIEDLAQLIYDLKNVNPEADVSVKLV 1067
Cdd:COG0067 950 GAAAAEGGGGGGGGGGGGGGGGGGGGGGVPGIAPPPPHPPPPGIILPPPPHDIIIIIILLLLILLLLALVAVAAAVAVVV 1029
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1068 SEVGVGTVAAGVAKARADHITIAGFDGGTGASPLTSLKHAGSPWEIGLAETQQTLVLNGLRSRIALQVDGGLKTGRDVVI 1147
Cdd:COG0067 1030 VAAAAGVAAAAAAAAAAAAVGSSGGGGGGGGGGGGSGAAGALGALGLLGLLLLLLLLLLLLLLGVVVLGGLGGGGGGGGG 1109
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1148 GALLGADEFGFATAPLIAAGCIMMRKCHLNTCPVGVATQDPVLRKRFKGTPEHVVNYFFFVAEEVREILASLGARRLDDI 1227
Cdd:COG0067 1110 AAALGAGALGGGAAALVVVGCGVAMCCVVLLCTVGGAAAGELERRRFRFAGEEVVVEEFFEAAEEEEEEALLELLRLLEE 1189
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1228 IGSSDLLDRDRMIEHWKARGLDFSRIFHKVEAPKEATYWTERQNHPIDDILDRRLI--EKAKLALETKVPVAFEAAIKNV 1305
Cdd:COG0067 1190 GLGVVELLLLLLLLLLLAKLLLLLLLLLLPLLPPDDPRDLALEEDDELLLLLALLLllLALALALLAAVRVALRAALGRA 1269
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1306 DRSAGAMLSGALAKRWGHKGLKDDTIHVTLKGTAGQSFGAFLARGITFDLVGDGNDYVGKGLSGGRIIVRPPENARIVPH 1385
Cdd:COG0067 1270 RRRGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 1349
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1386 QSIIVGNTVLYGAISGECYFNGVAGERFAVRNSGAIAVVEGVGDHGCEYMTGGVVVVLGGTGRNFAAGMSGGVAYVLDEE 1465
Cdd:COG0067 1350 GGGGGGGAGGGGGGGGGAGGGGGGGGGGVGGGGGGGGVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGLDL 1429
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1466 GDFARRCNMAMVELQPVPEEDDMLEKLHHHGGdlmhkgmvdvsgdmtrhdeerlyqlisnHLHYTGSVRAKEILDHWADY 1545
Cdd:COG0067 1430 DVVLDEEEEEELEELLLLLEEEEEEELELEEE----------------------------EAELLELADAALLLLLLVKV 1481
|
1530 1540
....*....|....*....|....*....
gi 503610770 1546 RPKFRKVMPVEYRRALEDMERMKMAEAAE 1574
Cdd:COG0067 1482 KAAVKVLLLLLLAAAAAAAEAAAAAAAAA 1510
|
|
| GATase_2 |
pfam00310 |
Glutamine amidotransferases class-II; |
47-471 |
0e+00 |
|
Glutamine amidotransferases class-II;
Pssm-ID: 395245 [Multi-domain] Cd Length: 420 Bit Score: 759.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 47 CGVGFVAHLKGEKSHQIVRDGLFMLENLTHRGAVGADPLMGDGAGILVQIPDRFFREEMAKQGVTLPKAGEYAVGYLFMP 126
Cdd:pfam00310 1 CGVGFIAHIKGKPSHKIVEDALEALENMEHRGACGADPDTGDGAGILTQIPDEFFRKEAKELGIELPEAGQYAVGMVFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 127 RDEALIAHFKEVISEVVAEEGQIVLGFRDVPVDNSSLSKAPdiAATEPHHVQVFIGAGrEAASSDEFERRLFTLRKVISN 206
Cdd:pfam00310 81 QDEAKRAEAKKIFEEIAEEEGLEVLGWREVPTNNSVLGEAA--LESEPQIEQVFVGSP-AGKSEDDFERKLYVARKRIEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 207 RIYAEADGGDlgFYIVSLSTTTIVYKGMFLAYQVGAYYKDLADERFQSAVALVHQRFSTNTFPSWKLAHPYRMVAHNGEI 286
Cdd:pfam00310 158 EIGVEGGDKD--FYICSLSSRTIVYKGMLTPEQLGQFYLDLQDPRFESAFALVHSRFSTNTFPSWPLAQPMRFLAHNGEI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 287 NTLRGNVNWMAARQASVSSPLFGDDISKLWPISYEGQSDTACFDNALEFLVRGGYSLSHAVMMLIPEAWAGNQLMSPERK 366
Cdd:pfam00310 236 NTLRGNRNWMRAREALLKSELFGDDLDKLLPIVNPGGSDSASLDNVLELLVLGGRSLPEALMMLIPEAWQNNPSMDPEKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 367 AFYEYHAALMEPWDGPAAVAFTDGRQIGATLDRNGLRPARYIVTSDDRVIMASEAGVLPVAEDKIVKKWRLQPGKMLLID 446
Cdd:pfam00310 316 AFYEYHSGLMEPWDGPALIVFTDGRYVGATLDRNGLRPARYYITKDGLIILASEVGVLDIPPERVVEKGRLGPGRMLLVD 395
|
410 420
....*....|....*....|....*
gi 503610770 447 MEEGRIISDEEVKSSLAGKHPYRQW 471
Cdd:pfam00310 396 LEEGRIIDDEEIKQQIASRHPYGEW 420
|
|
| GltS |
cd00713 |
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a ... |
47-466 |
0e+00 |
|
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a homodimer that synthesizes L-glutamate from 2-oxoglutarate and L-glutamine, an important step in ammonia assimilation in bacteria, cyanobacteria and plants. The N-terminal glutaminase domain catalyzes the hydrolysis of glutamine to glutamic acid and ammonia, and has a fold similar to that of other glutamine amidotransferases such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), and beta lactam synthetase (beta-LS), as well as the Ntn hydrolase folds of the proteasomal alpha and beta subunits.
Pssm-ID: 238365 [Multi-domain] Cd Length: 413 Bit Score: 724.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 47 CGVGFVAHLKGEKSHQIVRDGLFMLENLTHRGAVGADPLMGDGAGILVQIPDRFFREEMAKQGVTLPKAGEYAVGYLFMP 126
Cdd:cd00713 1 CGVGFVANIDGKPSHDIVQDALEALERMEHRGGVGADGKTGDGAGILIQIPHEFFREELAEAGIELPEAGEYAVGMLFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 127 RDEALIAHFKEVISEVVAEEGQIVLGFRDVPVDNSSLSkaPDIAATEPHHVQVFIGAgREAASSDEFERRLFTLRKVISN 206
Cdd:cd00713 81 RDEEAREAAKAIIEEELEAEGLRVLGWRDVPVDNSVLG--PTARATEPLIEQVFVGA-PSGDDGEAFERKLYLLRKRIEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 207 RIYAEADGgdlgFYIVSLSTTTIVYKGMFLAYQVGAYYKDLADERFQSAVALVHQRFSTNTFPSWKLAHPYRMVAHNGEI 286
Cdd:cd00713 158 AIRAADED----FYVCSLSSRTIVYKGMLLPEQLGQFYPDLQDPRFESAFALVHSRFSTNTFPSWPLAQPFRYLAHNGEI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 287 NTLRGNVNWMAARQASVSSPLFGDDISKLWPISYEGQSDTACFDNALEFLVRGGYSLSHAVMMLIPEAWAGNQLMSPERK 366
Cdd:cd00713 234 NTIRGNRNWMRAREGLLKSPLFGEDLKKLKPIINPGGSDSASLDNVLELLVRSGRSLPEAMMMLIPEAWQNNPTMDPELR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 367 AFYEYHAALMEPWDGPAAVAFTDGRQIGATLDRNGLRPARYIVTSDDRVIMASEAGVLPVAEDKIVKKWRLQPGKMLLID 446
Cdd:cd00713 314 AFYEYHSSLMEPWDGPAAIAFTDGRQVGASLDRNGLRPARYVITKDGLLIMSSEVGVVDVPPEKVVEKGRLGPGEMLLVD 393
|
410 420
....*....|....*....|
gi 503610770 447 MEEGRIISDEEVKSSLAGKH 466
Cdd:cd00713 394 LEEGRILDDEEIKDQLAKRH 413
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
34-1554 |
0e+00 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 1782.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 34 KQGLYDPRNEHDACGVGFVAHLKGEKSHQIVRDGLFMLENLTHRGAVGADPLMGDGAGILVQIPDRFFREEMAKQGVTLP 113
Cdd:PRK11750 2 HMGLYDPSLERDNCGFGLIAHMEGEPSHKLVRTAIHALARMTHRGGIAADGKTGDGCGLLLQKPDRFFRAVAEEAGWRLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 114 KagEYAVGYLFMPRDEALIAHFKEVISEVVAEEGQIVLGFRDVPVDNSSLSkapDIA-ATEPHHVQVFIGAGREAaSSDE 192
Cdd:PRK11750 82 K--NYAVGMVFLNQDPELAAAARRILEEELQRETLSVVGWREVPTNPSVLG---EIAlSSLPRIEQVFVNAPAGW-RERD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 193 FERRLFTLRKVISNRIYAEADggdlgFYIVSLSTTTIVYKGMFLAYQVGAYYKDLADERFQSAVALVHQRFSTNTFPSWK 272
Cdd:PRK11750 156 FERRLFIARRRIEKRLADDKD-----FYVCSLSNLVIIYKGLMMPADLPRFYLDLADLRLESAICVFHQRFSTNTLPRWP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 273 LAHPYRMVAHNGEINTLRGNVNWMAARQASVSSPLFgDDISKLWPISYEGQSDTACFDNALEFLVRGGYSLSHAVMMLIP 352
Cdd:PRK11750 231 LAQPFRYLAHNGEINTITGNRQWARARAYKFQTPLI-PDLQEAAPFVNETGSDSSSLDNMLELLLAGGMDLFRAMRLLVP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 353 EAWAGNQLMSPERKAFYEYHAALMEPWDGPAAVAFTDGRQIGATLDRNGLRPARYIVTSDDRVIMASEAGVLPVAEDKIV 432
Cdd:PRK11750 310 PAWQNNPDMDPDLRAFYEFNSMHMEPWDGPAGIVMTDGRYAACNLDRNGLRPARYVITKDKLITLASEVGIWDYQPDEVV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 433 KKWRLQPGKMLLIDMEEGRIISDEEVKSSLAGKHPYRQWLDNTQLILEELKPVEPRALRR----DVSLIDRQQAFGYTHE 508
Cdd:PRK11750 390 EKGRVGPGELLVIDTRTGRILHSAEIDNDLKSRHPYKEWLEKNVRRLVPFEELPDEQVGSreldDDTLKSYQKQFQYSFE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 509 DTKLLMSPMATTGQEAIGSMGTDTPISAMSDKPKLLYTYFKQNFAQVTNPPIDPIREELVMSLVSFIGPRPNILdHEGMA 588
Cdd:PRK11750 470 ELDQVIRVLAENGQEAVGSMGDDTPMAVLSSQPRSIYDYFRQQFAQVTNPPIDPLREAHVMSLATCIGREMNVF-CETEG 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 589 HAKRLEVRQPILTNGDLEKIRSIGhtEDRFDTKTLDFTYDISRGaeGMLEMLDRLCERAEAAVKGGYNIIVLSDRQIGPD 668
Cdd:PRK11750 549 HAHRVIFKSPVLSYSDFKQLTTLD--EEHYRADTLDLNYDPEET--GLEAAIKRLCDEAEQAVRDGTVLLVLSDRNIAKG 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 669 RVAIPALLATAAVHHHLIRKGLRTSVGLVVESGEPREIHHFCLLAGYGAEAINPYLAFDTLVDMHKRGEFPKEVDEKEVV 748
Cdd:PRK11750 625 RLPIPAAMAVGAVQHRLVDKGLRCDANIIVETASARDPHHFAVLLGFGATAVYPYLAYETLGDLVDTGEILKDYRQVMLN 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 749 YRyiKAVGKGILKVMSKMGISTYQSYCGAQIFDAVGLSSALVGKYFFGTATTIEGIGLEEIAAETVARHKAAFgsdpvLA 828
Cdd:PRK11750 705 YR--KGINKGLYKIMSKMGISTIASYRGSQLFEAVGLHDDVVDLCFKGVVSRIGGASFEDFEQDQKNLSKRAW-----LA 777
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 829 N-TLDIGGEYAFRMRGESHAWTPDAIASLQHAVR-GNAEDrYREFSAMMNESAsrMNTIRGLFTIKGAEEvgrkPIPIEE 906
Cdd:PRK11750 778 RkPIDQGGLLKYVHGGEYHAYNPDVVNTLQKAVQsGDYSD-YQEYAKLVNERP--VATLRDLLALKPADN----PIPLDE 850
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 907 VEPAAEIVKRFSTGAMSFGSISREAHTTLAVAMNRIGGKSNTGEGGEESDRYlplpdgstNPER-SAIKQIASGRFGVTT 985
Cdd:PRK11750 851 VEPAEELFKRFDSAAMSIGALSPEAHEALAIAMNRLGGRSNSGEGGEDPARY--------GTEKvSKIKQVASGRFGVTP 922
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 986 EYLVNADVLQIKVAQGAKPGEGGQLPGHKVDATVAKTRHSTPGVGLISPPPHHDIYSIEDLAQLIYDLKNVNPEADVSVK 1065
Cdd:PRK11750 923 AYLVNAEVLQIKVAQGAKPGEGGQLPGDKVNPLIARLRYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKALVSVK 1002
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1066 LVSEVGVGTVAAGVAKARADHITIAGFDGGTGASPLTSLKHAGSPWEIGLAETQQTLVLNGLRSRIALQVDGGLKTGRDV 1145
Cdd:PRK11750 1003 LVSEPGVGTIATGVAKAYADLITISGYDGGTGASPLTSVKYAGSPWELGLAETHQALVANGLRHKIRLQVDGGLKTGLDV 1082
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1146 VIGALLGADEFGFATAPLIAAGCIMMRKCHLNTCPVGVATQDPVLRKR-FKGTPEHVVNYFFFVAEEVREILASLGARRL 1224
Cdd:PRK11750 1083 IKAAILGAESFGFGTGPMVALGCKYLRICHLNNCATGVATQDEKLRKNhYHGLPEMVMNYFEFIAEETREWMAQLGVRSL 1162
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1225 DDIIGSSDLLDR-DRMIEhwKARGLDFSRIFHKVEAPK-EATYWTERQNHPID-DILDRRLIEKAKLALETKVPVAFEAA 1301
Cdd:PRK11750 1163 EDLIGRTDLLEElEGETA--KQQKLDLSPLLETAEPPAgKALYCTEERNPPFDkGLLNEQMLQQAKPAIEAKQGGEFWFD 1240
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1302 IKNVDRSAGAMLSGALAKRWGHKGLKDDTIHVTLKGTAGQSFGAFLARGITFDLVGDGNDYVGKGLSGGRIIVRPPENAR 1381
Cdd:PRK11750 1241 IRNTDRSVGARLSGEIARRHGNQGMADAPIKLRFTGTAGQSFGVWNAGGLELYLEGDANDYVGKGMAGGKIVIRPPVGSA 1320
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1382 IVPHQSIIVGNTVLYGAISGECYFNGVAGERFAVRNSGAIAVVEGVGDHGCEYMTGGVVVVLGGTGRNFAAGMSGGVAYV 1461
Cdd:PRK11750 1321 FRSHETAIIGNTCLYGATGGKLFAAGRAGERFAVRNSGAIAVVEGIGDHGCEYMTGGIVCVLGKTGVNFGAGMTGGFAYV 1400
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1462 LDEEGDFARRCNMAMVELQPVPeeddmleklhhhggdlmhkgmvdvsgDMTRHdEERLYQLISNHLHYTGSVRAKEILDH 1541
Cdd:PRK11750 1401 LDEDGDFVDRVNHELVEILRVE--------------------------DLEIH-REHLRGLITEHVEETGSEWGEEILAN 1453
|
1530
....*....|...
gi 503610770 1542 WADYRPKFRKVMP 1554
Cdd:PRK11750 1454 FDDYLRKFWLVKP 1466
|
|
| GltB1 |
COG0067 |
Glutamate synthase domain 1 [Amino acid transport and metabolism]; Glutamate synthase domain 1 ... |
28-1574 |
0e+00 |
|
Glutamate synthase domain 1 [Amino acid transport and metabolism]; Glutamate synthase domain 1 is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 439837 [Multi-domain] Cd Length: 1520 Bit Score: 1447.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 28 PSGLPRKQGLYDPRNEHDACGVGFVAHLKGEKSHQIVRDGLFMLENLTHRGAVGADPLMGDGAGILVQIPDRFFREEMAK 107
Cdd:COG0067 4 NSGLPAAQGLYDPAFEHDACGVGFVAHIKGRKSHDIVEDALEALENLEHRGAVGADGKTGDGAGILIQIPDAFFRAEAAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 108 QGVTLPKAGEYAVGYLFMPRDEALIAHFKEVISEVVAEEGQIVLGFRDVPVDNSSLSKApdIAATEPHHVQVFIGAGrEA 187
Cdd:COG0067 84 LGIELPEPGEYAVGMVFLPQDEAARAAARAIIEEILAEEGLTVLGWRDVPVDPSVLGET--ARATEPVIEQVFVARP-DG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 188 ASSDEFERRLFTLRKVISNRIYAEADGGDlGFYIVSLSTTTIVYKGMFLAYQVGAYYKDLADERFQSAVALVHQRFSTNT 267
Cdd:COG0067 161 LDGDAFERKLYVARKRIEKAIRALGLDDE-DFYICSLSSRTIVYKGMLTPEQLGEFYPDLQDPRFESALALVHQRFSTNT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 268 FPSWKLAHPYRMVAHNGEINTLRGNVNWMAARQASVSSPLFGDDISKLWPISYEGQSDTACFDNALEFLVRGGYSLSHAV 347
Cdd:COG0067 240 FPSWPLAQPFRYLAHNGEINTLRGNRNWMRAREALLASPLFGDDLEKLLPIVNPGGSDSASLDNVLELLVLGGRSLPHAM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 348 MMLIPEAWAGNQLMSPERKAFYEYHAALMEPWDGPAAVAFTDGRQIGATLDRNGLRPARYIVTSDDRVIMASEAGVLPVA 427
Cdd:COG0067 320 MMLIPEAWENNPDMDPERRAFYEYHSALMEPWDGPAAIVFTDGRQIGATLDRNGLRPARYVVTKDGLVILASEVGVLDIP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 428 EDKIVKKWRLQPGKMLLIDMEEGRIISDEEVKSSLAGKHPYRQWLDNTQLILEELKPVEPRALRRDVSLIDRQQAFGYTH 507
Cdd:COG0067 400 PEDIVEKGRLQPGKMLLVDLEEGRIIDDEEIKAELAAAHPYGEWLKENRIRLEDLPEPEEEPAPDDDLLLRRQQAFGYTE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 508 EDTKLLMSPMATTGQEAIGSMGTDTPISAMSDKPKLLYTYFKQNFAQVTNPPIDPIREELVMSLVSFIGPRPNILDHEGM 587
Cdd:COG0067 480 EEELLLLLPMAAGGEEEGGSGGDDDPAALLSSSRLLLYYYFFQFFAQVTNPPPDIIREEVVSSLLTTGGGGNNLLLEEEE 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 588 AHAKRLEVRQPILTNGDLEKIRSIGHTEDRFDTKTLDFTYDISRGAEGMLEMLDRLCERAEAAVKGGYNIIVLSDRQIGP 667
Cdd:COG0067 560 ARRRLLLLPPPLLNELLLLLLRLLDGDFKSTTTITLLDLADGAGGGAAAAAAAAEAAAAAAAAAVLLILIIDLSDDDSDA 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 668 DRVAIPALLATAAVHHHLIRKGLRTSVGLVVESGEPREIHHFCLLAGYGAEAINPYLAFDTLVDMHKRGEfPKEVDEKEV 747
Cdd:COG0067 640 APAPLAAAAAAHHHHLHLLRRRTRLLVVVEVEAVEHHHHHLLLGGGGAAAAAAALYLALELLLDGLLLGL-EDAAAAAAA 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 748 VYRYIKAVGKGILKVMSKMGISTYQSYCGAQIFDAVGLSSALVGKYFFGTATTIEGIGLEEIAAETVARHKAAFGSDPVL 827
Cdd:COG0067 719 KKKKKKKKGKLKKKKMSGIISSSSGSYGAAAIFGALGLVVVVFFTFTTTTGGGGGGGGLDEEAEEEAARAAAAAAEPGGL 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 828 ANTLDIGGEYAFRMRGESHAWTPDAIASLQHAVRGNAEDRYREFSAMMNESASRMNTIRGLFTIKGAEEVgrkPIPIEEV 907
Cdd:COG0067 799 LLGLGGGGGGEYGRRREGELHLLLQAATAAAAAAYRAYKYYRFARYTALLDLLRLLLLLLLLLFEEEEEE---EEPEEEE 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 908 EPAAEIVKRFSTGAMSFGSISREAHTTLAVAMNRIGGKSNTGEGGEESDRylplpdGSTNPERSAIKQIASGRFGVTTEY 987
Cdd:COG0067 876 EEEESSAIAAASSAAASAAASAAAAAAAAGAGGGGGGGGGGGGGGGEGRR------ASGGSGSSSSASVAAAGGGVVVGA 949
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 988 LVNADVLQIKVAQGAKPGEGGQLPGHKVDATVAKTRHSTPGVGLISPPPHHDIYSIEDLAQLIYDLKNVNPEADVSVKLV 1067
Cdd:COG0067 950 GAAAAEGGGGGGGGGGGGGGGGGGGGGGVPGIAPPPPHPPPPGIILPPPPHDIIIIIILLLLILLLLALVAVAAAVAVVV 1029
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1068 SEVGVGTVAAGVAKARADHITIAGFDGGTGASPLTSLKHAGSPWEIGLAETQQTLVLNGLRSRIALQVDGGLKTGRDVVI 1147
Cdd:COG0067 1030 VAAAAGVAAAAAAAAAAAAVGSSGGGGGGGGGGGGSGAAGALGALGLLGLLLLLLLLLLLLLLGVVVLGGLGGGGGGGGG 1109
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1148 GALLGADEFGFATAPLIAAGCIMMRKCHLNTCPVGVATQDPVLRKRFKGTPEHVVNYFFFVAEEVREILASLGARRLDDI 1227
Cdd:COG0067 1110 AAALGAGALGGGAAALVVVGCGVAMCCVVLLCTVGGAAAGELERRRFRFAGEEVVVEEFFEAAEEEEEEALLELLRLLEE 1189
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1228 IGSSDLLDRDRMIEHWKARGLDFSRIFHKVEAPKEATYWTERQNHPIDDILDRRLI--EKAKLALETKVPVAFEAAIKNV 1305
Cdd:COG0067 1190 GLGVVELLLLLLLLLLLAKLLLLLLLLLLPLLPPDDPRDLALEEDDELLLLLALLLllLALALALLAAVRVALRAALGRA 1269
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1306 DRSAGAMLSGALAKRWGHKGLKDDTIHVTLKGTAGQSFGAFLARGITFDLVGDGNDYVGKGLSGGRIIVRPPENARIVPH 1385
Cdd:COG0067 1270 RRRGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 1349
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1386 QSIIVGNTVLYGAISGECYFNGVAGERFAVRNSGAIAVVEGVGDHGCEYMTGGVVVVLGGTGRNFAAGMSGGVAYVLDEE 1465
Cdd:COG0067 1350 GGGGGGGAGGGGGGGGGAGGGGGGGGGGVGGGGGGGGVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGLDL 1429
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1466 GDFARRCNMAMVELQPVPEEDDMLEKLHHHGGdlmhkgmvdvsgdmtrhdeerlyqlisnHLHYTGSVRAKEILDHWADY 1545
Cdd:COG0067 1430 DVVLDEEEEEELEELLLLLEEEEEEELELEEE----------------------------EAELLELADAALLLLLLVKV 1481
|
1530 1540
....*....|....*....|....*....
gi 503610770 1546 RPKFRKVMPVEYRRALEDMERMKMAEAAE 1574
Cdd:COG0067 1482 KAAVKVLLLLLLAAAAAAAEAAAAAAAAA 1510
|
|
| GltB3 |
COG0070 |
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ... |
33-1574 |
0e+00 |
|
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 439840 [Multi-domain] Cd Length: 1508 Bit Score: 1417.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 33 RKQGLYDPRNEHDACGVGFVAHLKGEKSHQIVRDGLFMLENLTHRGAVGADPLMGDGAGILVQIPDRFFREEMAKQGVTL 112
Cdd:COG0070 1 GGGAGAMGAAAAAGGGGGGGGAGGDGLGGGGGGAAALGGGLGALAAAGAAGGAGAGGGGAGAGGGTGGGGGGGGGGGGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 113 PKAGEYAVGYLFMPRDEALIAHFKEVISEVVAEEGQIVLGFRDVPVDNSSLSKAPDIAATEPHHVQVFIGAGREAASSDE 192
Cdd:COG0070 81 GLGALLAGGGAFFAAGLAAGLLALAAAVEAEAEEAEEDEEEEERVLLLVLLEAETLVVLLALGVRAAALARREAELSELA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 193 FERRLFTLRKVISNRIYAEADGGDLGFYIVSLSTTTIVYKGMFLAYQVGAYYKDLADERFQSAVALVHQRFSTNTFPSWK 272
Cdd:COG0070 161 ARRRLRLRRLALLRRRRRRRRREFRRRSSSSLSSSSSSLYSLLLLVLLLLLLLLLLLLLLLLLFLSFLSRFTTTTTSSLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 273 LAHPYRMVAHNGEINTLRGNVNWMAARQASVSSPLFGDDISKLWPISYEGQSDTACFDNALEFLVRGGYSLSHAVMMLIP 352
Cdd:COG0070 241 LFFAPRTLAANNNNNNNNNNNNNNNRNAILNLSSRLEALSLELLPPLLPLLSDSSSDDLLLLLLLLLLLLLLLLLLMALA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 353 EAWAGNQLMSPERKAFYEYHAALMEPWDGPAAVAFTDGRQIGATLDRNGLRPARYIVTSDDRVIMASEAGVLPVAEDKIV 432
Cdd:COG0070 321 AAAPAPRAAAPPAAAAAFAAAADLYAAAAAAAAAAAGGDGDGGGLGLGGGRRRRRRLLRDRRLVRALSILVGLLILIEVV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 433 KKWRLQPGKMLLIDMEEGRIISDEEVKSSLAGKHPYRQWLDNTQLILEELKPvEPRALRRDVSLIDRQQAFGYTHEDTKL 512
Cdd:COG0070 401 GKGRELPGGGLLVGGGGGGLLDDEEEDAEELEELLPELQDLLLLLKLLLLLE-EEEELLLLEEELLQEREAELEQELLLL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 513 LMSPMATTGQEAIGSMGTDTPISAMSDKPKLLYTYFKQNFAQVTNPPIDPIREELVMSLVSFIGPRPNILDHEGMAHAKR 592
Cdd:COG0070 480 LLLLLAEALEEEEESGGAGAAAAALDLLDLLLLLDFQFLLLFFQQPPPPVVFPPIVLLLEPPPLLLLLLLLLLLLLLEEL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 593 LEVRQPILTNGDLEKIRSIGHTEDRFDTKTLDFTYDISRGAEGMLEMLDRLCERAEAAVKGGYNIIVLSDRQIGPDRVAI 672
Cdd:COG0070 560 LLLELLLLLLALALLLLLLLLLLLLGDATTLAAALEAAGGGGALAALLLAAEAAAAAAAAAVAAILAASIRDSALLLALL 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 673 PALLATAAVHHHLIRKGLRTSVGLVVESGEPREIHHFCLLAGYGAEAINPYLAFDTLVDMHKRGEfpKEVDEKEVVYRYI 752
Cdd:COG0070 640 PALLALLLLHHHLLRALGRVLVLLVEALLRERVVHVAALLAGAAAAAAAALAALAAAAALLLLAY--ALLGLLEAAAYKA 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 753 KAVGKGILKVMSKMGISTYQSYCGAQIFDAVGLSSALVGKYFFGTATTIEGIGLEEIAAETVARHKAAFGSDPVLANTLD 832
Cdd:COG0070 718 KAALKAGVKKKLKIGGSSISSSSGGGIIEGAGGGLGLLLELGGTTTTVGEGGGGGEILGEGGAARHAAAADAAAAAALAL 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 833 IGGEYAFRMRGESHAWTPDAIASLQHAVRGNAEDRYREFSAMMNESASRMNTIRGLFTIKGaeevGRKPIPIEEVEPAAE 912
Cdd:COG0070 798 GGGGGGGRGGGGEGHHGGHYHHLLQQLAARTAAALYDDYYAYEDRADELVNERLRLLLLFL----LRPPIPIEEVEPEEE 873
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 913 IVKRFSTGAMSFGSISREAHTTLAVAMNRIGGKSNTGEGGEESDRYLPLPDGSTNpeRSAIKQIASGRFGVTTEYLVNAD 992
Cdd:COG0070 874 IVKRFATGAMSGGSSSSEAHEELAIAMNRIGGKSNGGGGGEEEGREDPLRNGDSR--RSAIKQVASGRFGVTSEYLVNAD 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 993 VLQIKVAQGAKPGEGGQLPGHKVDATVAKTRHSTPGVGLISPPPHHDIYSIEDLAQLIYDLKNVNPEADVSVKLVSEVGV 1072
Cdd:COG0070 952 EIQIKMAQGAKPGEGGQLPGHKVYPWIARLRHSTPGVGLISPPPHHDIYSIEDLAQLIFDLKNANPAARISVKLVSEVGV 1031
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1073 GTVAAGVAKARADHITIAGFDGGTGASPLTSLKHAGSPWEIGLAETQQTLVLNGLRSRIALQVDGGLKTGRDVVIGALLG 1152
Cdd:COG0070 1032 GTIAAGVAKAAADVILISGHDGGTGASPLSSIKHAGLPWELGLAETQQTLVLNNLRRRVVVQTDGGLKTGRDVVIAALLG 1111
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1153 ADEFGFATAPLIAAGCIMMRKCHLNTCPVGVATQDPVLRKRFKGTPEHVVNYFFFVAEEVREILASLGARRLDDIIGSSD 1232
Cdd:COG0070 1112 AEEFGFATAPLVVLGCIMMRKCHLNTCPVGVATQDPELRKRFFGGPEHVVNFFFFFAEEVRELMAALGGRTLDEEIGRRD 1191
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1233 LLDRDRMIEHWKARGLDFSRIFHKVEAPKE-ATYWTERQNHPIDDILDRRLIEKAKLALETKVPVAFEAAIKNVDRSAGA 1311
Cdd:COG0070 1192 LLLVRRAVDHWKAKGLDLSPLLYKPDVPADvPRYCTEEQNHGLEGALDRELIEDARPAIENGEPVELEYPIRNTDRSVGT 1271
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1312 MLSGALAKRWGHKGLKDDTIHVTLKGTAGQSFGAFLARGITFDLVGDGNDYVGKGLSGGRIIVRPPENARIVPHQSIIVG 1391
Cdd:COG0070 1272 RLSGEIAKRYGNEGLPEDTITLRFTGSAGQSFGAFLAKGLTLELEGDANDYVGKGLSGGKIIVRPPAGSTFVAEENIIIG 1351
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1392 NTVLYGAISGECYFNGVAGERFAVRNSGAIAVVEGVGDHGCEYMtggvvvvlggtgRNFAAGMSGGVAYVLDEEGDFARR 1471
Cdd:COG0070 1352 NTCLYGATGGELYAAGRAGERFAVRNSGATAVVEGVGDHGCEYMtggvvvvlgptgRNFGAGMSGGIAYVLDEDGDFEDR 1431
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1472 CNMAMVELQPVPEEddmleklhhhggdlmhkgmvdvsgdmtrHDEERLYQLISNHLHYTGSVRAKEILDHWADYRPKFRK 1551
Cdd:COG0070 1432 CNPEMVELERLDEE----------------------------EDEEELRELIEEHVEYTGSARAKEILDNWDEYLPKFVK 1483
|
1530 1540
....*....|....*....|...
gi 503610770 1552 VMPVEYRRALEDMERMKMAEAAE 1574
Cdd:COG0070 1484 VMPKDYKRVLEAIAEAEAAGLDA 1506
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
676-1416 |
0e+00 |
|
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 439839 Cd Length: 728 Bit Score: 1014.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 676 LATAAVHHHLIRKGLRTSVGLVVESGEPREIHHFCLLAGYGAEAINPYLAFDTLVDMHKRGefPKEVDEKEVVYRYIKAV 755
Cdd:COG0069 1 LAAAAHHHLLRRKGRRTVSLIVVEGEERRVHHHAALLGGGGAAANPPYLAEEILDLLRRGG--LLGLDLEEAVKNYIKAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 756 GKGILKVMSKMGISTYQSYCGAQIFDAVGLSSALVGkyffgtattiegIGLEEIAAetvaRHKAAFgsdpvlANTLDIGG 835
Cdd:COG0069 79 EKGLLKIMSKMGISTLASYRGAQIFEAVGLSRELVD------------IGIADVLT----QHRHAI------LRNLPVGG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 836 EYAFR--------------MRGESHAWTPDAIASLQHAVRGnaEDRYREFSAMMNESASRMNTIRGLFTIKgaeeVGRKP 901
Cdd:COG0069 137 RYRYRfesigpeirqyffeSDGEEHPFNRETRSLLYQAAKN--EEDYKPFGTLVDYQPGYEWTLRSLFPFK----ADRPP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 902 IPIEE-VEPAAEIVKRFSTGAMSFGSISREAHTTLAVAMNRIGGKSNTGEGGEESDRYlplpdgsTNPERSAIKQIASGR 980
Cdd:COG0069 211 IPIGEpVEPPYSIVSRFNISAMSFGALSAEAHEALAIGMNRIGGKSNTGEGGESPYHL-------GDGGGDAIKQIASGR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 981 FGVTT---EYLVNADVLQIKVAQGAKPGEGGQLPGHKVDATVAKTRHSTPGVGLISPPPHHDIYSIEDLAQLIYDLKNVN 1057
Cdd:COG0069 284 FGVRDedgEYLPNAKMIEIKLAQGAKPGEGGQLPGAKVTPEIARIRGSTPGVDLISPPPHHDIYSIEDLAQLIFDLRELN 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1058 PEADVSVKLVSEVGVGTVAA--GVAK--ARADHITIAGFDGGTGASPLTSLKHAGSPWEIGLAETQQTLVLNGLRSRIAL 1133
Cdd:COG0069 364 PGAPVGVKLVSGAGVGTIAAckGVAKtgAYADFITIDGGEGGTGAAPLESIKHAGLPWELGLAEVHQTLVGNGLRDRIRL 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1134 QVDGGLKTGRDVVIGALLGADEFGFATAPLIAAGCIMMRKCHLNTCPVGVATQDPVLRKRFK--GTPEHVVNYFFFVAEE 1211
Cdd:COG0069 444 IADGKLKTGRDVAIAAALGADEFGFARAFMVALGCIMARKCHLNTCPVGVATQDPELRKGFVveGKPERVVNYFRFTAEE 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1212 VREILASLGARRLDDIIGSSDLLdRDRMIEHWKARGLDFSRIFHKVEAPK-EATYWTERQNHPIDDILDRRLIEKAKLAL 1290
Cdd:COG0069 524 VREILAALGVRSPDELIGRHDLL-RVRDGEHWKAKGLDLSPLLYKPELPEgVPRRCQEEQDHGLDKALDLELIAAAAAAA 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1291 ETKVPVAFEAAIKNVDRSAGAMLSGALAKRWGHKGLKDDTIHVTLKGTAGQSFGAFLARGITFDLVGDGNDYVGKGLSGG 1370
Cdd:COG0069 603 EEGKPVVLITNIRNNNRRVGGMLSGEIAKRYGGAGLPDDTIILGFAGGAGQSFGAFGAGGGLLLLEGDDNDYVGKGGGGG 682
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 503610770 1371 RIIVRPPENARIVPHQSIIVGNTVLYGAISGECYFNGVAGERFAVR 1416
Cdd:COG0069 683 GIIVPPPPGASFFPEENIIIGNTGLYGATGGGAYFAGGAGERFAVR 728
|
|
| GATase_2 |
pfam00310 |
Glutamine amidotransferases class-II; |
47-471 |
0e+00 |
|
Glutamine amidotransferases class-II;
Pssm-ID: 395245 [Multi-domain] Cd Length: 420 Bit Score: 759.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 47 CGVGFVAHLKGEKSHQIVRDGLFMLENLTHRGAVGADPLMGDGAGILVQIPDRFFREEMAKQGVTLPKAGEYAVGYLFMP 126
Cdd:pfam00310 1 CGVGFIAHIKGKPSHKIVEDALEALENMEHRGACGADPDTGDGAGILTQIPDEFFRKEAKELGIELPEAGQYAVGMVFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 127 RDEALIAHFKEVISEVVAEEGQIVLGFRDVPVDNSSLSKAPdiAATEPHHVQVFIGAGrEAASSDEFERRLFTLRKVISN 206
Cdd:pfam00310 81 QDEAKRAEAKKIFEEIAEEEGLEVLGWREVPTNNSVLGEAA--LESEPQIEQVFVGSP-AGKSEDDFERKLYVARKRIEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 207 RIYAEADGGDlgFYIVSLSTTTIVYKGMFLAYQVGAYYKDLADERFQSAVALVHQRFSTNTFPSWKLAHPYRMVAHNGEI 286
Cdd:pfam00310 158 EIGVEGGDKD--FYICSLSSRTIVYKGMLTPEQLGQFYLDLQDPRFESAFALVHSRFSTNTFPSWPLAQPMRFLAHNGEI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 287 NTLRGNVNWMAARQASVSSPLFGDDISKLWPISYEGQSDTACFDNALEFLVRGGYSLSHAVMMLIPEAWAGNQLMSPERK 366
Cdd:pfam00310 236 NTLRGNRNWMRAREALLKSELFGDDLDKLLPIVNPGGSDSASLDNVLELLVLGGRSLPEALMMLIPEAWQNNPSMDPEKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 367 AFYEYHAALMEPWDGPAAVAFTDGRQIGATLDRNGLRPARYIVTSDDRVIMASEAGVLPVAEDKIVKKWRLQPGKMLLID 446
Cdd:pfam00310 316 AFYEYHSGLMEPWDGPALIVFTDGRYVGATLDRNGLRPARYYITKDGLIILASEVGVLDIPPERVVEKGRLGPGRMLLVD 395
|
410 420
....*....|....*....|....*
gi 503610770 447 MEEGRIISDEEVKSSLAGKHPYRQW 471
Cdd:pfam00310 396 LEEGRIIDDEEIKQQIASRHPYGEW 420
|
|
| GltS |
cd00713 |
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a ... |
47-466 |
0e+00 |
|
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a homodimer that synthesizes L-glutamate from 2-oxoglutarate and L-glutamine, an important step in ammonia assimilation in bacteria, cyanobacteria and plants. The N-terminal glutaminase domain catalyzes the hydrolysis of glutamine to glutamic acid and ammonia, and has a fold similar to that of other glutamine amidotransferases such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), and beta lactam synthetase (beta-LS), as well as the Ntn hydrolase folds of the proteasomal alpha and beta subunits.
Pssm-ID: 238365 [Multi-domain] Cd Length: 413 Bit Score: 724.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 47 CGVGFVAHLKGEKSHQIVRDGLFMLENLTHRGAVGADPLMGDGAGILVQIPDRFFREEMAKQGVTLPKAGEYAVGYLFMP 126
Cdd:cd00713 1 CGVGFVANIDGKPSHDIVQDALEALERMEHRGGVGADGKTGDGAGILIQIPHEFFREELAEAGIELPEAGEYAVGMLFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 127 RDEALIAHFKEVISEVVAEEGQIVLGFRDVPVDNSSLSkaPDIAATEPHHVQVFIGAgREAASSDEFERRLFTLRKVISN 206
Cdd:cd00713 81 RDEEAREAAKAIIEEELEAEGLRVLGWRDVPVDNSVLG--PTARATEPLIEQVFVGA-PSGDDGEAFERKLYLLRKRIEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 207 RIYAEADGgdlgFYIVSLSTTTIVYKGMFLAYQVGAYYKDLADERFQSAVALVHQRFSTNTFPSWKLAHPYRMVAHNGEI 286
Cdd:cd00713 158 AIRAADED----FYVCSLSSRTIVYKGMLLPEQLGQFYPDLQDPRFESAFALVHSRFSTNTFPSWPLAQPFRYLAHNGEI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 287 NTLRGNVNWMAARQASVSSPLFGDDISKLWPISYEGQSDTACFDNALEFLVRGGYSLSHAVMMLIPEAWAGNQLMSPERK 366
Cdd:cd00713 234 NTIRGNRNWMRAREGLLKSPLFGEDLKKLKPIINPGGSDSASLDNVLELLVRSGRSLPEAMMMLIPEAWQNNPTMDPELR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 367 AFYEYHAALMEPWDGPAAVAFTDGRQIGATLDRNGLRPARYIVTSDDRVIMASEAGVLPVAEDKIVKKWRLQPGKMLLID 446
Cdd:cd00713 314 AFYEYHSSLMEPWDGPAAIAFTDGRQVGASLDRNGLRPARYVITKDGLLIMSSEVGVVDVPPEKVVEKGRLGPGEMLLVD 393
|
410 420
....*....|....*....|
gi 503610770 447 MEEGRIISDEEVKSSLAGKH 466
Cdd:cd00713 394 LEEGRILDDEEIKDQLAKRH 413
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
846-1222 |
0e+00 |
|
Conserved region in glutamate synthase; This family represents a region of the glutamate synthase protein. This region is expressed as a separate subunit in the glutamate synthase alpha subunit from archaebacteria, or part of a large multidomain enzyme in other organizms. The aligned region of these proteins contains a putative FMN binding site and Fe-S cluster.
Pssm-ID: 396287 [Multi-domain] Cd Length: 367 Bit Score: 572.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 846 HAWTPDAIASLQHAVRGNAEDRYREFSAMMNEsASRMNTIRGLFTIKGAEEvgrkPIPIEEVEPAAEIVKRFSTGAMSFG 925
Cdd:pfam01645 1 HRNEPEFIKTLQIAVQVESYPSYDKYREPLNE-RVPIGALRDLLEFDFAED----PIPLEEVEPALEIKTRFCTGAMSYG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 926 SISREAHTTLAVAMNRIGGKSNTGEGGEESDRYLPLPDGstnpersAIKQIASGRFGVTTEYLVNADVLQIKVAQGAKPG 1005
Cdd:pfam01645 76 ALSEEAHEALAKAMNRLGTKSNTGEGGEDPERLKYADNI-------AIKQVASGRFGVTPEYLNNADAIEIKIAQGAKPG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1006 EGGQLPGHKVDATVAKTRHSTPGVGLISPPPHHDIYSIEDLAQLIYDLKNVNPEADVSVKLVSEVGVGTVAAGVAKARAD 1085
Cdd:pfam01645 149 EGGHLPGEKVSPEIARIRGSPPGVGLISPPPHHDIYSIEDLAQLIYDLKEINPKAPISVKLVSGHGVGTIAAGVAKAGAD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1086 HITIAGFDGGTGASPLTSLKHAGSPWEIGLAETQQTLVLNGLRSRIALQVDGGLKTGRDVVIGALLGADEFGFATAPLIA 1165
Cdd:pfam01645 229 IILIDGYDGGTGASPKTSIKHAGLPWELALAEAHQTLKENGLRDRVSLIADGGLRTGADVAKAAALGADAVYIGTAALIA 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 503610770 1166 AGCIMMRKCHLNTCPVGVATQDPVLRKR--FKGTPEHVVNYFFFVAEEVREILASLGAR 1222
Cdd:pfam01645 309 LGCIMCRVCHTNTCPVGVATQDPELRKRldFEGAPERVVNYFRFLAEEVRELLAALGIN 367
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
850-1236 |
1.48e-171 |
|
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine via intramolecular channelling of ammonia, a reaction in the plant, yeast and bacterial pathway for ammonia assimilation. It is a multifunctional enzyme that functions through three distinct active centers, carrying out L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor.
Pssm-ID: 239202 [Multi-domain] Cd Length: 392 Bit Score: 520.56 E-value: 1.48e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 850 PDAIASLQHAVRG--NAEDRYREFSAMMNESASRMNTIRGLFTIK---------GAEEVGRKPIPIEEVEPAAEIVKRFS 918
Cdd:cd02808 2 LLEIERLEEIQYFvfNRAERYGVYNRAGNSRGRPFGTLRDLLEFGaqlakhplePDEEVDDRVTIGPNAEKPLKLDSPFN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 919 TGAMSFGSISREAHTTLAVAMNRIGGKSNTGEGGEESDRYLPlpdgstnpERSAIKQIASGRFGVTTEYLVNADVLQIKV 998
Cdd:cd02808 82 ISAMSFGALSKEAKEALAIGAALAGTASNTGEGGELPEEREG--------GGDIIKQVASGRFGVRPEYLNKADAIEIKI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 999 AQGAKPGEGGQLPGHKVDATVAKTRHSTPGVGLISPPPHHDIYSIEDLAQLIYDLKNVNPEADVSVKLVSEVGVGTVAAG 1078
Cdd:cd02808 154 GQGAKPGEGGHLPGEKVTEEIAKIRGIPPGVDLISPPPHHDIYSIEDLAQLIEDLREATGGKPIGVKLVAGHGEGDIAAG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1079 VAKARADHITIAGFDGGTGASPLTSLKHAGSPWEIGLAETQQTLVLNGLRSRIALQVDGGLKTGRDVVIGALLGADEFGF 1158
Cdd:cd02808 234 VAAAGADFITIDGAEGGTGAAPLTFIDHVGLPTELGLARAHQALVKNGLRDRVSLIASGGLRTGADVAKALALGADAVGI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1159 ATAPLIAAGCIMMRKCHLNTCPVGVATQDPVLRKR--FKGTPEHVVNYFFFVAEEVREILASLGARRLDDiIGSSDLLDR 1236
Cdd:cd02808 314 GTAALIALGCIQARKCHTNTCPVGVATQDPELRRRldVEGKAERVANYLKSLAEELRELAAALGKRSLEL-LGRSDLLAL 392
|
|
| Glu_syn_central |
pfam04898 |
Glutamate synthase central domain; The central domain of glutamate synthase connects the amino ... |
498-786 |
1.20e-170 |
|
Glutamate synthase central domain; The central domain of glutamate synthase connects the amino terminal amidotransferase domain with the FMN-binding domain and has an alpha / beta overall topology. This domain appears to be a rudimentary form of the FMN-binding TIM barrel according to SCOP.
Pssm-ID: 461469 [Multi-domain] Cd Length: 281 Bit Score: 513.85 E-value: 1.20e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 498 DRQQAFGYTHEDTKLLMSPMATTGQEAIGSMGTDTPISAMSDKPKLLYTYFKQNFAQVTNPPIDPIREELVMSLVSFIGP 577
Cdd:pfam04898 1 RRQKAFGYTQEDLEMLLKPMAETGKEPIGSMGDDTPLAVLSDKPRLLYDYFKQLFAQVTNPPIDPIREEIVMSLRTYLGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 578 RPNILDhEGMAHAKRLEVRQPILTNGDLEKIRSIGHteDRFDTKTLDFTYDisrgaeGMLEMLDRLCERAEAAVKGGYNI 657
Cdd:pfam04898 81 EGNLLE-ETPEHCRRLELPSPILTNEELEKLRSLKG--PGFKVATLDITFD------GLEAALERLCEEAEEAVRDGANI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 658 IVLSDRQIGPDRVAIPALLATAAVHHHLIRKGLRTSVGLVVESGEPREIHHFCLLAGYGAEAINPYLAFDTLVDMHKRGE 737
Cdd:pfam04898 152 LILSDRGVDADRAPIPSLLAVSAVHHHLVREGLRTKVSLVVESGEAREVHHFAVLLGYGADAVNPYLAFETIRDLIREGK 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 503610770 738 FPK-EVDEKEVVYRYIKAVGKGILKVMSKMGISTYQSYCGAQIFDAVGLS 786
Cdd:pfam04898 232 GKLtDEDLEEAVKNYRKAIEKGLLKIMSKMGISTLQSYRGAQIFEAIGLS 281
|
|
| gltB_C |
cd00982 |
gltb_C. This domain is found at the C-terminus of the large subunit (gltB) of glutamate ... |
1278-1554 |
1.25e-133 |
|
gltb_C. This domain is found at the C-terminus of the large subunit (gltB) of glutamate synthase (GltS). GltS encodes a complex iron-sulfur flavoprotein that catalyzes the synthesis of L-glutamate from L-glutamine and 2-oxoglutarate. It requires the transfer of ammonia and electrons among three distinct active centers that carry out L-Gln hydrolysis, conversion of 2-oxoglutarate into L-Glu, and electron uptake from a donor. These catalytic sites appear to occur in other domains within the protein, and not the domain in this CD. This particular domain has no known function, but it likely has a structural role as it interacts with the amidotransferase and FMN-binding domains of gltS.
Pssm-ID: 238482 [Multi-domain] Cd Length: 251 Bit Score: 413.46 E-value: 1.25e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1278 LDRRLIEKAKLAL-ETKVPVAFEAAIKNVDRSAGAMLSGALAKRWGHKGLKDDTIHVTLKGTAGQSFGAFLARGITFDLV 1356
Cdd:cd00982 1 LDDKLIADAEPALiENGEPVTLEYPIRNTDRAVGTMLSGEIAKRYGEEGLPEDTIKIKFEGSAGQSFGAFLAKGVTLELE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1357 GDGNDYVGKGLSGGRIIVRPPENARIVPHQSIIVGNTVLYGAISGECYFNGVAGERFAVRNSGAIAVVEGVGDHGCEYMT 1436
Cdd:cd00982 81 GDANDYVGKGLSGGRIVVRPPKDATFKPEENIIIGNVCLYGATSGEAFIRGRAGERFAVRNSGATAVVEGVGDHGCEYMT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1437 GGVVVVLGGTGRNFAAGMSGGVAYVLDEEGDFARRCNMAMVELQPVPEEddmleklhhhggdlmhkgmvdvsgdmtrHDE 1516
Cdd:cd00982 161 GGTVVVLGKTGRNFAAGMSGGVAYVLDEDGDFEKKVNHEMVDLERLEDA----------------------------EDE 212
|
250 260 270
....*....|....*....|....*....|....*...
gi 503610770 1517 ERLYQLISNHLHYTGSVRAKEILDHWADYRPKFRKVMP 1554
Cdd:cd00982 213 EQLKELIEEHVEYTGSEKAKEILANWEAYLKKFVKVIP 250
|
|
| GXGXG |
pfam01493 |
GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran ... |
1301-1487 |
9.74e-103 |
|
GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran dehydrogenase subunit c (FwdC) and molybdenum formylmethanofuran dehydrogenase subunit c (FmdC). A repeated G-XX-G-XXX-G motif is seen in the alignment.
Pssm-ID: 460231 [Multi-domain] Cd Length: 190 Bit Score: 325.91 E-value: 9.74e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1301 AIKNVDRSAGAMLSGALAKRWGHKGLKDDTIHVTLKGTAGQSFGAFLARGITFDLVGDGNDYVGKGLSGGRIIVRPPENA 1380
Cdd:pfam01493 2 EIRNTDRSVGTILSGEIAKRYGEDGLPDDTITIKFNGSAGQSFGAFLPKGLTLELEGDANDYVGKGLSGGKIIIYPPAES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1381 RIVPHQSIIVGNTVLYGAISGECYFNGVAGERFAVRNSGAIAVVEGVGDHGCEYMTGGVVVVLGGTGRNFAAGMSGGVAY 1460
Cdd:pfam01493 82 TFKAEENIIIGNTCLYGATGGELFINGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGRVVVLGKTGRNFGAGMSGGIAY 161
|
170 180
....*....|....*....|....*..
gi 503610770 1461 VLDEEGDFARRCNMAMVELQPVPEEDD 1487
Cdd:pfam01493 162 VLDEDGDFPEKLNKEMVELERVTDEDE 188
|
|
| GXGXG |
cd00504 |
GXGXG domain. This domain of unknown function is found at the C-terminus of the large subunit ... |
1307-1463 |
4.89e-53 |
|
GXGXG domain. This domain of unknown function is found at the C-terminus of the large subunit (gltB) of glutamate synthase (GltS), in subunit C of tungsten formylmethanofuran dehydrogenase (FwdC) and in subunit C of molybdenum formylmethanofuran dehydrogenase (FmdC). It is also found in a primarily archeal group of proteins predicted to encode part of the large subunit of GltS. It is characterized by a repeated GXXGXXXG motif. GltS is a complex iron-sulfur flavoprotein that catalyzes the synthesis of L-glutamate from L-glutamine and 2-oxoglutarate. It requires the transfer of ammonia and electrons among three distinct active centers that carry out L-Gln hydrolysis, conversion of 2-oxoglutarate into L-Glu, and electron uptake from a donor. These catalytic sites occur in other domains within the protein or or encoded by separate genes, and are not present in the domain in this CD. FwdC and FmdC are reversible ion pumps that catalyze the formylation and deformylation of methanofuran in hyperthermophiles and bacteria. They require the presence of either tungstun (FwdC) or molybdenum (FmdC). The specific function of this domain also remains unidentified in the formylmethanofuran dehydrogenases.
Pssm-ID: 238281 [Multi-domain] Cd Length: 149 Bit Score: 182.77 E-value: 4.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1307 RSAGAMLSGALAKRwghKGLKDDTIHVTLKGTAGQSFGAFLArGITFDLVGDGNDYVGKGLSGGRIIVRPPENarivpHQ 1386
Cdd:cd00504 1 RAVGTRGSRYIGKR---PGLPEDTVEIIINGSAGQSFGAFMA-GGTITVEGNANDYVGKGMSGGEIVIHPPAG-----DE 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503610770 1387 SIIVGNTVLYGAISGECYFNGVAGERFAVRNSGAIAVVEGVGD-HGCEYMTGGVVVVLGGTGRNFAAGMSGGVAYVLD 1463
Cdd:cd00504 72 NGIAGNVALYGATGGKIFVRGNAGERFGVRMSGGTIVVEGVGDdFGGEYMTGGTIVVLGDAGRNFGAGMSGGVIYVRG 149
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
240-443 |
2.34e-38 |
|
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.
Pssm-ID: 238212 [Multi-domain] Cd Length: 220 Bit Score: 143.36 E-value: 2.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 240 VGAYYKDLADERFQSAVALVHQRFSTNTFPSWKLAHPYR------MVAHNGEINTLRGNVNWMAARqasvssplfgddis 313
Cdd:cd00352 54 VSDVALDLLDEPLKSGVALGHVRLATNGLPSEANAQPFRsedgriALVHNGEIYNYRELREELEAR-------------- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 314 klwPISYEGQSDTACFDNALEFLVRGGYsLSHAVMMLIPEawagnqlmsperkafyeyhaalmepWDGPAAVAFTDG--R 391
Cdd:cd00352 120 ---GYRFEGESDSEVILHLLERLGREGG-LFEAVEDALKR-------------------------LDGPFAFALWDGkpD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503610770 392 QIGATLDRNGLRPARYIVTSDDRVIMASEAGVLpvAEDKIVKKWRLQPGKML 443
Cdd:cd00352 171 RLFAARDRFGIRPLYYGITKDGGLVFASEPKAL--LALPFKGVRRLPPGELL 220
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
211-445 |
3.06e-15 |
|
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine amidotransferase-like protein of unknown function found in bacteria and archaea. GlxB has a structural fold similar to that of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The GlxB fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238888 [Multi-domain] Cd Length: 249 Bit Score: 77.31 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 211 EADGGDLGFY------IVSLSTTTIVYKGMFLAYQVGAYYkDLadERFQSAVALVHQRFSTNTFPSWKLAHPYRM----V 280
Cdd:cd01907 31 PGDGAGFALYgdpdafVYSSGKDMEVFKGVGYPEDIARRY-DL--EEYKGYHWIAHTRQPTNSAVWWYGAHPFSIgdiaV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 281 AHNGEINTLRGNVNWMaarqasvssplfgddisKLWPISYEGQSDTACFDNALEFLVRGGYSLSHAVMMLIPEAWAGNQL 360
Cdd:cd01907 108 VHNGEISNYGSNREYL-----------------ERFGYKFETETDTEVIAYYLDLLLRKGGLPLEYYKHIIRMPEEEREL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 361 MSPERkafYEYHAALMepwDGPAAVAFTDGRQIGATLDRNGLRPArYIVTSDDRVIMASE----AGVLPVAEDKIvkkWR 436
Cdd:cd01907 171 LLALR---LTYRLADL---DGPFTIIVGTPDGFIVIRDRIKLRPA-VVAETDDYVAIASEecaiREIPDRDNAKV---WE 240
|
....*....
gi 503610770 437 LQPGKMLLI 445
Cdd:cd01907 241 PRPGEYVIW 249
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
1036-1160 |
1.10e-05 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 47.97 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610770 1036 PHHDIYSIEDLAQLIYDLKNVNPEADVSVKLVseVGVGTVAAGVAKARADHITIAGFDGGTGASPLTslkhagspweigl 1115
Cdd:cd04722 91 HGAVGYLAREDLELIRELREAVPDVKVVVKLS--PTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAV------------- 155
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 503610770 1116 AETQQTLVLNGLRSRIALQVDGGLKTGRDVVIGALLGADEFGFAT 1160
Cdd:cd04722 156 PIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
|