|
Name |
Accession |
Description |
Interval |
E-value |
| guaA |
PRK00074 |
GMP synthase; Reviewed |
21-686 |
0e+00 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 524.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 21 VVILDAGAQYGKVIDRRVRELFVQSEIFPLETPAFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGM 100
Cdd:PRK00074 6 ILILDFGSQYTQLIARRVRELGVYSEIVPYDISAEEIRAFNPKGIILSGGPASVYEEGAPRADPEIFELGVPVLGICYGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 101 QMMNKVFGGTVHKKSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNI-VAGIANESKKLYG 179
Cdd:PRK00074 86 QLMAHQLGGKVERAGKREYGRAELEVDNDSPLFKGLPEEQDVWMSHGDKVTELPEGFKVIASTENCpIAAIANEERKFYG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 180 AQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVLVLLSGGVDSTVCTALLNRALNqEQVI 259
Cdd:PRK00074 166 VQFHPEVTHTPQGKKLLENFVFDICGCKGDWTMENFIEEAIEEIREQVGDKKVILGLSGGVDSSVAAVLLHKAIG-DQLT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 260 AVHIDNGFMRKRESQSVEEAL-KKLGIQVKVINAAHSFYN---GtttlpISDedrtprkrisktlnmttsPEEKRKIIGD 335
Cdd:PRK00074 245 CVFVDHGLLRKNEAEQVMEMFrEHFGLNLIHVDASDRFLSalaG-----VTD------------------PEEKRKIIGR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 336 TFVKIANEVIGEmnLKPEEvFLAQGTLRPDLIESASlvaSGKAELIKTHHNDTELIRKLREegKVIEPLKDFHKDEVRIL 415
Cdd:PRK00074 302 EFIEVFEEEAKK--LGGVK-FLAQGTLYPDVIESGG---TKKAATIKSHHNVGGLPEDMKL--KLVEPLRELFKDEVRKL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 416 GRELGLPEELVSRHPFPGPGLAIRVICaeepyickdfpetnnilkivadfsaSVKKPH-TLLQRVKACTTEEdqeklmqi 494
Cdd:PRK00074 374 GLELGLPEEIVYRHPFPGPGLAIRILG-------------------------EVTKEKlDILREADAIFIEE-------- 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 495 tsLHSLN-------AF--LLPIKTVGVQGDCRSYSYVCGIsskdepdwesliflarliprmchnvnRVVyifgppvkepp 565
Cdd:PRK00074 421 --LRKAGlydkiwqAFavLLPVKSVGVMGDGRTYDYVVAL--------------------------RAV----------- 461
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 566 tdvtptflttgvlstlrqadfeahnilrESgyagkisqmpviltplhfdrdplqkqpscqrsvvirtfitSDFMTGIPAt 645
Cdd:PRK00074 462 ----------------------------TS----------------------------------------IDGMTADWA- 472
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 2217346693 646 pgnEIPVEVVLKMVTEI-KKIPGISRIMYDLTSKPPGTTEWE 686
Cdd:PRK00074 473 ---RLPYDFLEKISNRIiNEVKGVNRVVYDITSKPPATIEWE 511
|
|
| GuaA2 |
COG0519 |
GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, ... |
21-686 |
1.37e-155 |
|
GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, PP-ATPase domain/subunit is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440285 [Multi-domain] Cd Length: 512 Bit Score: 459.29 E-value: 1.37e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 21 VVILDAGAQYGKVIDRRVRELFVQSEIFPLETPAFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGM 100
Cdd:COG0519 6 IIVLDFGGQYQQLIARRRREEGVYSEIIPPDTAAEEIKAKGPPGIILSGGPSSVYEEGAPPDDPELFELGGPILGICYGG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 101 QMMNKVFGGTVHKKSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNI-VAGIANESKKLYG 179
Cdd:COG0519 86 QLMLHLLGGGVVRAERREYGGALLLVDDESDLFAGGPEELQVWMSHGDRVTELPPGFEVIASTENCpVAAIANEERKLYG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 180 AQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQN-RElECIREIKERVGTSKVLVLLSGGVDSTVCTALLNRALNqEQV 258
Cdd:COG0519 166 VQFHPEVVHTEQGKEILKNFLFDICGCKGDWTMENfIE-EAIEEIREQVGDGKVICALSGGVDSSVAAALLHKAIG-DQL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 259 IAVHIDNGFMRKRESQSVEEALK-KLGIQVKVINAAHSFYN---GtttlpISDedrtprkrisktlnmttsPEEKRKIIG 334
Cdd:COG0519 244 TCVFVDHGLLRKGEAEQVEETFKeHFGLNLIYVDASERFLSalkG-----VTD------------------PEEKRKIIG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 335 DTFVKIANEVIGEmnLKPEEvFLAQGTLRPDLIESASlvASGKAELIKTHHN------DTELirklreegKVIEPLKDFH 408
Cdd:COG0519 301 EEFIEVFEEEAKK--LGGAK-FLAQGTLYPDVIESGS--VKGPAATIKSHHNvgglpeDMKF--------KLVEPLRELF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 409 KDEVRILGRELGLPEELVSRHPFPGPGLAIRVICAeepyickdfpetnnilkivadfsasVKKPH-TLLQRVKACTTEED 487
Cdd:COG0519 368 KDEVRALGRELGLPEEIVYRHPFPGPGLAIRILGE-------------------------VTKEKlEILREADAIFIEEL 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 488 QE-----KLMQitslhslnAF--LLPIKTVGVQGDCRSYSYVCGIsskdepdwesliflarliprmchnvnrvvyifgpp 560
Cdd:COG0519 423 RKaglydKVWQ--------AFavLLPVKSVGVMGDERTYEYVVAL----------------------------------- 459
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 561 vkepptdvtptflttgvlstlrqadfeahnilresgyagkisqmpviltplhfdrdplqkqpscqRSVVirtfiTSDFMT 640
Cdd:COG0519 460 -----------------------------------------------------------------RAVT-----SVDGMT 469
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2217346693 641 GIPAtpgnEIPVEVVLKMVTEI-KKIPGISRIMYDLTSKPPGTTEWE 686
Cdd:COG0519 470 ADWA----RLPYEVLERISNRIiNEVKGVNRVVYDITSKPPATIEWE 512
|
|
| GMP_synthase_C |
cd01997 |
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ... |
223-686 |
7.61e-155 |
|
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP synthetase (glutamine-hydrolyzing, EC 6.3.5.2) contains two subdomains: the ATP pyrophosphatase domain at the N-terminal and the dimerization domain at the C-terminal end. The ATP-PPase domain is a twisted, five-stranded parallel beta-sheet sandwiched between helical layers. It has a signature nucleotide-binding motif, or PP-loop, at the end of the first-beta strand. GMP synthetase is a homodimer, but in some archaea, it is a heterodimer made up of ATP pyrophosphatase (ATP-PPase) and a GATase subunit. In eukaryotes and bacteria, the two catalytic units are encoded by a single gene producing a two-domain-type GMP with a GATase domain in the N-terminus and an ATP-PPase domain in the C-terminus.
Pssm-ID: 467501 [Multi-domain] Cd Length: 311 Bit Score: 449.68 E-value: 7.61e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 223 IKERVGTSKVLVLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIqvkvinaahsfyngttt 302
Cdd:cd01997 1 IKRTVGDKKVLCLVSGGVDSTVCAALLHKALGDERVIAVHIDNGLMRKNESEQVEEALKKLGV----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 303 lpISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMNLKPEEVFLAQGTLRPDLIESASLVASGKAELIK 382
Cdd:cd01997 64 --INLAKVDASKRFLKKLKGVTDPEEKRKIIGDTFIEVFDEVAKELNLDPDDVYLAQGTLYPDLIESASSLASSKADTIK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 383 THHNDTELIRKLrEEGKVIEPLKDFHKDEVRILGRELGLPEELVSRHPFPGPGLAIRVICAEEPyickdfpetnnilkiv 462
Cdd:cd01997 142 THHNVGGLPREL-LKGKLVEPLRDLFKDEVRELGRELGLPEELVWRHPFPGPGLAIRVLGEVTP---------------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 463 adfsasvkkphtllqrvkactteedqeklmqitslhslnafllpiktvgvqgdcrsysyvcgisskdepdwesliflarl 542
Cdd:cd01997 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 543 iprmchnvnrvvyifgppvkepptdvtptflttGVLSTLRQADFEAHNILRESGYAGKISQMPVILTPLHfdrdPLQKQP 622
Cdd:cd01997 205 ---------------------------------EKLEILREADAIVEEELREAGLYDKISQAFAVLLPIK----SVGVQG 247
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217346693 623 SCQRS---VVIRTFITSDFMTGIPATPgneiPVEVVLKMVTEI-KKIPGISRIMYDLTSKPPGTTEWE 686
Cdd:cd01997 248 DGRTYgyvVALRAVETEDFMTAEWARP----PYEVLDKISNRItNEVPGVNRVVYDITSKPPATIEWE 311
|
|
| PLN02347 |
PLN02347 |
GMP synthetase |
12-555 |
7.49e-127 |
|
GMP synthetase
Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 386.35 E-value: 7.49e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 12 DGHHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETPAFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTI-- 89
Cdd:PLN02347 4 EAAKSYLDVVLILDYGSQYTHLITRRVRELGVYSLLLSGTASLDRIASLNPRVVILSGGPHSVHVEGAPTVPEGFFDYcr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 90 --GKPVLGICYGMQMMNKVFGGTVHKKSVREDGVFNISVDNTCSLFRGLQKE--EVVLLTHGDSVDKVADGFKVVARS-- 163
Cdd:PLN02347 84 erGVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCGSQLFGDLPSGetQTVWMSHGDEAVKLPEGFEVVAKSvq 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 164 GNIVAgIANESKKLYGAQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVG-TSKVLVLLSGGVDS 242
Cdd:PLN02347 164 GAVVA-IENRERRIYGLQYHPEVTHSPKGMETLRHFLFDVCGVTADWKMQDVLEEQIELIKATVGpDEHVICALSGGVDS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 243 TVCTALLNRALNqEQVIAVHIDNGFMRKRESQSVEEALKK-LGIQVKVINAAHSFyngtttlpisdedrtprkrISKtLN 321
Cdd:PLN02347 243 TVAATLVHKAIG-DRLHCVFVDNGLLRYKEQERVMETFKRdLHLPVTCVDASERF-------------------LSK-LK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 322 MTTSPEEKRKIIGDTFVKI----ANEVIGEMNLKPEevFLAQGTLRPDLIESASLVASGK--AELIKTHHNDTELIRKLR 395
Cdd:PLN02347 302 GVTDPEKKRKIIGAEFIEVfdefAHKLEQKLGKKPA--FLVQGTLYPDVIESCPPPGSGRthSHTIKSHHNVGGLPKDMK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 396 EegKVIEPLKDFHKDEVRILGRELGLPEELVSRHPFPGPGLAIRVI---CAEepyickdfpetnNILKIvadfsasvkkp 472
Cdd:PLN02347 380 L--KLIEPLKLLFKDEVRKLGRLLGVPEAFLKRHPFPGPGLAVRVLgdvTEG------------NALDI----------- 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 473 htlLQRVKACTTEEDQE-----KLMQitslhslnAF--LLPIKTVGVQGDCRSYSYVCG---ISSKD--EPDWESL--IF 538
Cdd:PLN02347 435 ---LRQVDEIFINSIKDaglydEIWQ--------AFavFLPVKSVGVQGDQRTHSHVVAlraVTSEDgmTADWYHFehKF 503
|
570 580
....*....|....*....|
gi 2217346693 539 LARLIPRMCHNV---NRVVY 555
Cdd:PLN02347 504 LDDVSRKICNEVrgvNRVVY 523
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
21-200 |
7.77e-98 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153213 [Multi-domain] Cd Length: 181 Bit Score: 298.30 E-value: 7.77e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 21 VVILDAGAQYGKVIDRRVRELFVQSEIFPLETPAFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGM 100
Cdd:cd01742 1 ILILDFGSQYTHLIARRVRELGVYSEILPNTTPLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFELGVPVLGICYGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 101 QMMNKVFGGTVHKKSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGN-IVAGIANESKKLYG 179
Cdd:cd01742 81 QLIAKALGGKVERGDKREYGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEVVKLPEGFKVIASSDNcPVAAIANEEKKIYG 160
|
170 180
....*....|....*....|.
gi 2217346693 180 AQFHPEVGLTENGKVILKNFL 200
Cdd:cd01742 161 VQFHPEVTHTEKGKEILKNFL 181
|
|
| guaA_Cterm |
TIGR00884 |
GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit; This protein of purine ... |
218-686 |
1.48e-69 |
|
GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This C-terminal region would be the larger subunit [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273321 [Multi-domain] Cd Length: 311 Bit Score: 229.53 E-value: 1.48e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 218 ECIREIKERVGTSKVLVLLSGGVDSTVCTALLNRALNqEQVIAVHIDNGFMRKRESQSVEEALK-KLGIQVKVINAAHSF 296
Cdd:TIGR00884 5 EAVEEIREQVGDAKVIIALSGGVDSSVAAVLAHRAIG-DRLTCVFVDHGLLRKGEAEQVVKTFGdRLGLNLVYVDAKERF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 297 YngtttlpisdedrtprkrisKTLNMTTSPEEKRKIIGDTFVKIANEVIGEmnLKPEEvFLAQGTLRPDLIESASlvasG 376
Cdd:TIGR00884 84 L--------------------SALKGVTDPEEKRKIIGRVFIEVFEREAKK--IGDAE-YLAQGTIYPDVIESAA----G 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 377 KAELIKTHHNDTELIRKLREegKVIEPLKDFHKDEVRILGRELGLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETN 456
Cdd:TIGR00884 137 TAHVIKSHHNVGGLPEDMKL--KLVEPLRELFKDEVRKLGKELGLPEEIVWRHPFPGPGLAVRVLGEVTKEKLEILRRAD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 457 NILkivadfsasvkkphtllqrvkacttEEDQEKLMQITSLHSLNAFLLPIKTVGVQGDCRSYSYVcgisskdepdwesl 536
Cdd:TIGR00884 215 AIV-------------------------IEELKKAGLYDKVWQAFAVLLPVKSVGVMGDGRTYGYV-------------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 537 iflarliprmchnvnrvvyifgppvkepptdvtptflttgvlstlrqadfeahnilresgyagkisqmpviltplhfdrd 616
Cdd:TIGR00884 --------------------------------------------------------------------------------
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217346693 617 plqkqpscqrsVVIRTFITSDFMTGIPAtpgnEIPVEVVLKMVTEI-KKIPGISRIMYDLTSKPPGTTEWE 686
Cdd:TIGR00884 256 -----------IALRAVESIDGMTADWA----RLPYDFLERISNRItNEVPGVNRVVYDITSKPPATIEWE 311
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
21-206 |
1.15e-68 |
|
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 129966 [Multi-domain] Cd Length: 188 Bit Score: 222.58 E-value: 1.15e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 21 VVILDAGAQYGKVIDRRVRELFVQSEIFPLETPAFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGM 100
Cdd:TIGR00888 1 ILVLDFGSQYTQLIARRLRELGVYSELVPNTTPLEEIREKNPKGIILSGGPSSVYAENAPRADEKIFELGVPVLGICYGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 101 QMMNKVFGGTVHKKSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNI-VAGIANESKKLYG 179
Cdd:TIGR00888 81 QLMAKQLGGEVGRAEKREYGKAELEILDEDDLFRGLPDESTVWMSHGDKVKELPEGFKVLATSDNCpVAAMAHEEKPIYG 160
|
170 180
....*....|....*....|....*..
gi 2217346693 180 AQFHPEVGLTENGKVILKNFLYDIAGC 206
Cdd:TIGR00888 161 VQFHPEVTHTEYGNELLENFVYDVCGC 187
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
22-203 |
1.08e-50 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 174.35 E-value: 1.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 22 VILDAGAQYGKVIDRRVRELFVQSEIFPLETPAFAIKEQGFRAIIISGGPNSVYA-EDAPWFDPAIFTIGKPVLGICYGM 100
Cdd:pfam00117 1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAaGGAIEAIREARELKIPILGICLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 101 QMMNKVFGGTVHKKSVREDGVFNISVDNT-CSLFRGLQKEEVVLLTHGDSVDK--VADGFKVVARSGNI--VAGIANESK 175
Cdd:pfam00117 81 QLLALAFGGKVVKAKKFGHHGKNSPVGDDgCGLFYGLPNVFIVRRYHSYAVDPdtLPDGLEVTATSENDgtIMGIRHKKL 160
|
170 180
....*....|....*....|....*...
gi 2217346693 176 KLYGAQFHPEVGLTENGKVILKNFLYDI 203
Cdd:pfam00117 161 PIFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
21-203 |
1.75e-46 |
|
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440284 [Multi-domain] Cd Length: 225 Bit Score: 164.35 E-value: 1.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 21 VVILDAGA---QYGKVIDRRVRELFVQSEIFPL---ETPAFAIKEQGFRAIIISGGPNSVYaEDAPW------FDPAIFT 88
Cdd:COG0518 2 ILILDHDPfggQYPGLIARRLREAGIELDVLRVyagEILPYDPDLEDPDGLILSGGPMSVY-DEDPWledepaLIREAFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 89 IGKPVLGICYGMQMMNKVFGGTVHKKSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNI-V 167
Cdd:COG0518 81 LGKPVLGICYGAQLLAHALGGKVEPGPGREIGWAPVELTEADPLFAGLPDEFTVWMSHGDTVTELPEGAEVLASSDNCpN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217346693 168 AGIANEsKKLYGAQFHPEV------------------------------GLTENGKVILKNFLYDI 203
Cdd:COG0518 161 QAFRYG-RRVYGVQFHPEVthtmmeawleeradelaaeellaeaslhdpELREAGRRLLRNFLREI 225
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
21-200 |
1.78e-36 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 134.98 E-value: 1.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 21 VVILDAGAQYGKVIDRRVRELFVQSEIFPLETPAFAIKEQGfRAIIISGGP------NSV-YAEDapwfdpaiftIGKPV 93
Cdd:PRK00758 2 IVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTTPVEEIKAFE-DGLILSGGPdieragNCPeYLKE----------LDVPI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 94 LGICYGMQMMNKVFGGTVHKKSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNI-VAGIAN 172
Cdd:PRK00758 71 LGICLGHQLIAKAFGGEVGRGEYGEYALVEVEILDEDDILKGLPPEIRVWASHADEVKELPDGFEILARSDICeVEAMKH 150
|
170 180
....*....|....*....|....*...
gi 2217346693 173 ESKKLYGAQFHPEVGLTENGKVILKNFL 200
Cdd:PRK00758 151 KEKPIYGVQFHPEVAHTEYGEEIFKNFL 178
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
14-200 |
7.15e-25 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153212 [Multi-domain] Cd Length: 188 Bit Score: 102.32 E-value: 7.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 14 HHHYEGAVVILDAGAQYGKVIdrrvrelfVQSEIFPLETPAFAIKEQGFRAIIISGGPNSVYAEDAPWFDP------AIF 87
Cdd:cd01741 7 HDTPEGPGLFEDLLREAGAET--------IEIDVVDVYAGELLPDLDDYDGLVILGGPMSVDEDDYPWLKKlkelirQAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 88 TIGKPVLGICYGMQMMNKVFGGTVHK-KSVREDGVFNISVDNT---CSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARS 163
Cdd:cd01741 79 AAGKPVLGICLGHQLLARALGGKVGRnPKGWEIGWFPVTLTEAgkaDPLFAGLPDEFPVFHWHGDTVVELPPGAVLLASS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217346693 164 gnivAGIANE----SKKLYGAQFHPEvgltengKVILKNFL 200
Cdd:cd01741 159 ----EACPNQafryGDRALGLQFHPE-------ERLLRNFL 188
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
51-200 |
1.32e-19 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.
Pssm-ID: 153214 [Multi-domain] Cd Length: 184 Bit Score: 86.82 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 51 ETPAFAIKEQGFRAIIISGGPNSvyAEDAPWFDPAI--FTIGKPVLGICYGMQMMNKVFGGTV-HKKSVREDGVFNISVD 127
Cdd:cd01743 32 EITLEELELLNPDAIVISPGPGH--PEDAGISLEIIraLAGKVPILGVCLGHQAIAEAFGGKVvRAPEPMHGKTSEIHHD 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217346693 128 NTcSLFRGLQKEEVVLLTHGDSVDKVADG--FKVVARS-GNIVAGIANESKKLYGAQFHPEVGLTENGKVILKNFL 200
Cdd:cd01743 110 GS-GLFKGLPQPFTVGRYHSLVVDPDPLPdlLEVTASTeDGVIMALRHRDLPIYGVQFHPESILTEYGLRLLENFL 184
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
57-200 |
3.12e-19 |
|
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440278 [Multi-domain] Cd Length: 189 Bit Score: 85.86 E-value: 3.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 57 IKEQGFRAIIISGGPNSvyAEDAPWFDPAI--FTIGKPVLGICYGMQMMNKVFGGTVhkksVREDGVF-----NISVDNt 129
Cdd:COG0512 38 IEALAPDGIVLSPGPGT--PEEAGISLEVIraFAGKIPILGVCLGHQAIGEAFGGKV----VRAPEPMhgktsPITHDG- 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217346693 130 CSLFRGLQKEEVVLLTHgdS--VDK--VADGFKVVARSG-NIVAGIANESKKLYGAQFHPEVGLTENGKVILKNFL 200
Cdd:COG0512 111 SGLFAGLPNPFTATRYH--SlvVDRetLPDELEVTAWTEdGEIMGIRHRELPIEGVQFHPESILTEHGHQLLANFL 184
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
64-200 |
1.40e-17 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 81.33 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 64 AIIISGGPNSvyAEDAPWFDPAI--FTIGKPVLGICYGMQMMNKVFGGTV-HKKSVREDGVFNISVDNTcSLFRGLQKEE 140
Cdd:PRK05670 46 AIVLSPGPGT--PAEAGISLELIreFAGKVPILGVCLGHQAIGEAFGGKVvRAKEIMHGKTSPIEHDGS-GIFAGLPNPF 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217346693 141 VVLLTHGDSVDK--VADGFKVVARS-GNIVAGIANESKKLYGAQFHPEVGLTENGKVILKNFL 200
Cdd:PRK05670 123 TVTRYHSLVVDResLPDCLEVTAWTdDGEIMGVRHKELPIYGVQFHPESILTEHGHKLLENFL 185
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
64-185 |
4.17e-15 |
|
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.
Pssm-ID: 429620 [Multi-domain] Cd Length: 219 Bit Score: 74.99 E-value: 4.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 64 AIIISGGPN---SVYAEDAPW----FDPA--IFTI---------GKPVLGICYGMQMMNKVFGGTVHKK--------SVR 117
Cdd:pfam07722 61 GLLLTGGPNvdpHFYGEEPSEsggpYDPArdAYELaliraalarGKPILGICRGFQLLNVALGGTLYQDiqeqpgftDHR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 118 ED---GVFNIS-----VDNTCsLFR-GLQKEEVVLLTHGDSVDKVADGFKVVARSG-NIVAGI--ANESKKLYGAQFHPE 185
Cdd:pfam07722 141 EHcqvAPYAPShavnvEPGSL-LASlLGSEEFRVNSLHHQAIDRLAPGLRVEAVAPdGTIEAIesPNAKGFALGVQWHPE 219
|
|
| PuuD |
COG2071 |
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
64-185 |
9.47e-15 |
|
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains GATase1-like domain [Amino acid transport and metabolism];
Pssm-ID: 441674 [Multi-domain] Cd Length: 231 Bit Score: 74.05 E-value: 9.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 64 AIIISGGPN---SVYAEDAPW----FDPA--IFTI---------GKPVLGICYGMQMMNKVFGGTVH------------- 112
Cdd:COG2071 52 GLVLTGGADvdpALYGEEPHPelgpIDPErdAFELaliraalerGKPVLGICRGMQLLNVALGGTLYqdlpdqvpgaldh 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 113 -KKSVREDGVFNISVD-NTCsLFRGLQKEEVV---LltHGDSVDKVADGFKVVARSGN-IVAGIANESKK-LYGAQFHPE 185
Cdd:COG2071 132 rQPAPRYAPRHTVEIEpGSR-LARILGEEEIRvnsL--HHQAVKRLGPGLRVSARAPDgVIEAIESPGAPfVLGVQWHPE 208
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
25-185 |
6.11e-14 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153216 [Multi-domain] Cd Length: 189 Bit Score: 70.68 E-value: 6.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 25 DAGAQYGKVIDRRVRELFVQSE----IFPLETPAFAIKEQGFR--AIIISGGPNSV---YAEDAPW----FDPA--IFTI 89
Cdd:cd01745 11 EGGYERRDYLNQYYVDAVRKAGglpvLLPPVDDEEDLEQYLELldGLLLTGGGDVDpplYGEEPHPelgpIDPErdAFEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 90 ---------GKPVLGICYGMQMMNKVFGGTVHkksvredgvfnisvdntcslfrglQKEEVVLLtHGDSVDKVADGFKVV 160
Cdd:cd01745 91 allraalerGKPILGICRGMQLLNVALGGTLY------------------------QDIRVNSL-HHQAIKRLADGLRVE 145
|
170 180
....*....|....*....|....*..
gi 2217346693 161 ARSGN-IVAGIANESKKLY-GAQFHPE 185
Cdd:cd01745 146 ARAPDgVIEAIESPDRPFVlGVQWHPE 172
|
|
| GMP_synt_C |
pfam00958 |
GMP synthase C terminal domain; GMP synthetase is a glutamine amidotransferase from the de ... |
592-685 |
2.24e-13 |
|
GMP synthase C terminal domain; GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. This family is the C-terminal domain specific to the GMP synthases EC:6.3.5.2. In prokaryotes this domain mediates dimerization. Eukaryotic GMP synthases are monomers. This domain in eukaryotes includes several large insertions that may form globular domains.
Pssm-ID: 425963 [Multi-domain] Cd Length: 92 Bit Score: 66.28 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 592 LRESGYAGKISQMPVILTPLhfdrdplqkqpscqRSV-------------VIRTFITSDFMTGIPAtpgnEIPVEVVLKM 658
Cdd:pfam00958 3 IKKAGLYRKIWQAFAVLLPV--------------KSVgvmgdertyeyvvALRAVTSTDGMTADWA----RLPYEVLEKI 64
|
90 100
....*....|....*....|....*...
gi 2217346693 659 VTEI-KKIPGISRIMYDLTSKPPGTTEW 685
Cdd:pfam00958 65 SNRIvNEVPGVNRVVYDITSKPPATIEW 92
|
|
| PRK09065 |
PRK09065 |
glutamine amidotransferase; Provisional |
49-185 |
8.53e-12 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181635 [Multi-domain] Cd Length: 237 Bit Score: 65.37 E-value: 8.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 49 PLETPafaikeQGFRAIIISGGPN--------SVYAEDapWFDPAIfTIGKPVLGICYGMQMMNKVFGGTV--HKKSvRE 118
Cdd:PRK09065 48 PLPAP------DDFAGVIITGSWAmvtdrldwSERTAD--WLRQAA-AAGMPLLGICYGHQLLAHALGGEVgyNPAG-RE 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 119 DGVFNISVDNTCS---LFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANESKKLYGAQFHPE 185
Cdd:PRK09065 118 SGTVTVELHPAAAddpLFAGLPAQFPAHLTHLQSVLRLPPGAVVLARSAQDPHQAFRYGPHAWGVQFHPE 187
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
92-200 |
1.08e-11 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 64.17 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 92 PVLGICYGMQMMNKVFGGTVHKKSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVD--KVADGFKVVARSGNI-VA 168
Cdd:PRK08007 74 PILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEpdSLPACFEVTAWSETReIM 153
|
90 100 110
....*....|....*....|....*....|..
gi 2217346693 169 GIANESKKLYGAQFHPEVGLTENGKVILKNFL 200
Cdd:PRK08007 154 GIRHRQWDLEGVQFHPESILSEQGHQLLANFL 185
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
64-201 |
1.24e-11 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 67.43 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 64 AIIISGGPNSvyAEDAPWFDPAIFTIGK--PVLGICYGMQMMNKVFGGT-VHKKSVREDGVFNISVDNTcSLFRGLQKEE 140
Cdd:PRK14607 47 HIVISPGPGR--PEEAGISVEVIRHFSGkvPILGVCLGHQAIGYAFGGKiVHAKRILHGKTSPIDHNGK-GLFRGIPNPT 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217346693 141 VVLLTHGDSVDK--VADGFKVVARS--GNIVaGIANESKKLYGAQFHPEVGLTENGKVILKNFLY 201
Cdd:PRK14607 124 VATRYHSLVVEEasLPECLEVTAKSddGEIM-GIRHKEHPIFGVQFHPESILTEEGKRILKNFLN 187
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
62-200 |
3.03e-11 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 62.83 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 62 FRAIIISGGPnsvyaeDAPWFDPAIFTI------GKPVLGICYGMQMMNKVFGGTVHK-KSVREDGVFNISVDNTCSLFR 134
Cdd:PRK06895 44 FSHILISPGP------DVPRAYPQLFAMleryhqHKSILGVCLGHQTLCEFFGGELYNlNNVRHGQQRPLKVRSNSPLFD 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217346693 135 GLQKEEVVLLTHGDSVDK--VADGFKVVAR-SGNIVAGIANESKKLYGAQFHPEVGLTENGKVILKNFL 200
Cdd:PRK06895 118 GLPEEFNIGLYHSWAVSEenFPTPLEITAVcDENVVMAMQHKTLPIYGVQFHPESYISEFGEQILRNWL 186
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
57-200 |
5.23e-11 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 62.06 E-value: 5.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 57 IKEQGFRAIIISGGP----NSVYAEDA-PWFDPAIftigkPVLGICYGMQMMNKVFGGTVHKKSVREDGVFNISVDNTCS 131
Cdd:CHL00101 39 IKNLNIRHIIISPGPghprDSGISLDViSSYAPYI-----PILGVCLGHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDD 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217346693 132 LFRGLQKEEVVLLTHGDSVDKVA--DGFKVVA--RSGNIVAGIANESKKLYGAQFHPEVGLTENGKVILKNFL 200
Cdd:CHL00101 114 LFQGLPNPFTATRYHSLIIDPLNlpSPLEITAwtEDGLIMACRHKKYKMLRGIQFHPESLLTTHGQQILRNFL 186
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
21-185 |
7.07e-11 |
|
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.
Pssm-ID: 153215 [Multi-domain] Cd Length: 178 Bit Score: 61.36 E-value: 7.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 21 VVILDAGAQYGkvIDRRVRELFVQSEIFPLETPAFAIKEQGFRAIIISGGPNsvyaeDAPWFDPAIFTI------GKPVL 94
Cdd:cd01744 1 VVVIDFGVKHN--ILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPG-----DPALLDEAIKTVrkllgkKIPIF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 95 GICYGMQMMNKVFGGTVHKKSVREDGVfNISVDNTCSlfrglQKEEVVLLTHGDSVDK--VADGFKVVARSGN--IVAGI 170
Cdd:cd01744 74 GICLGHQLLALALGAKTYKMKFGHRGS-NHPVKDLIT-----GRVYITSQNHGYAVDPdsLPGGLEVTHVNLNdgTVEGI 147
|
170
....*....|....*
gi 2217346693 171 ANESKKLYGAQFHPE 185
Cdd:cd01744 148 RHKDLPVFSVQFHPE 162
|
|
| PRK07053 |
PRK07053 |
glutamine amidotransferase; Provisional |
14-188 |
8.83e-11 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 235919 [Multi-domain] Cd Length: 234 Bit Score: 62.65 E-value: 8.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 14 HHHYEGAVVILDAGAQYGkvidRRVRelFVQSEIFPLETPAFAikEQGFraIIISGGPNSVYAEDA-PWFDPAIFTI--- 89
Cdd:PRK07053 10 HVAFEDLGSFEQVLGARG----YRVR--YVDVGVDDLETLDAL--EPDL--LVVLGGPIGVYDDELyPFLAPEIALLrqr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 90 ---GKPVLGICYGMQMMNKVFGGTVHKKSVREDGVFNISV--DNTCSLFRGLQKEEVVLLTHGDSVDkVADGFKVVARSg 164
Cdd:PRK07053 80 laaGLPTLGICLGAQLIARALGARVYPGGQKEIGWAPLTLtdAGRASPLRHLGAGTPVLHWHGDTFD-LPEGATLLAST- 157
|
170 180
....*....|....*....|....*...
gi 2217346693 165 nivAGIANES----KKLYGAQFHPEVGL 188
Cdd:PRK07053 158 ---PACRHQAfawgNHVLALQFHPEARE 182
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
90-200 |
9.86e-11 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 61.99 E-value: 9.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 90 GKPVLGICYGMQMMNKVFGGTV-------HKK--SVREDGVfnisvdntcSLFRGLQKEEVVLLTHGDSV--DKVADGFK 158
Cdd:PRK07765 76 GTPLLGVCLGHQAIGVAFGATVdrapellHGKtsSVHHTGV---------GVLAGLPDPFTATRYHSLTIlpETLPAELE 146
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2217346693 159 VVARSGN-IVAGIANESKKLYGAQFHPEVGLTENGKVILKNFL 200
Cdd:PRK07765 147 VTARTDSgVIMAVRHRELPIHGVQFHPESVLTEGGHRMLANWL 189
|
|
| COG1606 |
COG1606 |
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only]; |
231-422 |
1.57e-10 |
|
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
Pssm-ID: 441214 [Multi-domain] Cd Length: 265 Bit Score: 62.05 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 231 KVLVLLSGGVDSTVCTALLNRALNqEQVIAVHIDNGFMRKREsqsVEEAL---KKLGIQVKVINaahsfyngttTLPISD 307
Cdd:COG1606 17 SVLVAFSGGVDSTLLAKVAHDVLG-DRVLAVTADSPSLPERE---LEEAKelaKEIGIRHEVIE----------TDELED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 308 ED--RTPRKR--ISKtlnmttspeekrKIIGDTFVKIANEvigemnlkpeevflaqgtlrpdliESASLVASGkaelikT 383
Cdd:COG1606 83 PEfvANPPDRcyHCK------------KELFSKLKELAKE------------------------LGYAVVADG------T 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2217346693 384 HHNDteL------IRKLREEGkVIEPLKD--FHKDEVRILGRELGLP 422
Cdd:COG1606 121 NADD--LgdyrpgLRAAKELG-VRSPLAEagLTKAEIRELARELGLP 164
|
|
| PRK13980 |
PRK13980 |
NAD synthetase; Provisional |
212-433 |
1.67e-10 |
|
NAD synthetase; Provisional
Pssm-ID: 184435 [Multi-domain] Cd Length: 265 Bit Score: 62.15 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 212 VQNRELECIREIKERVGTSKVLVLLSGGVDSTVCTALLNRALNQEQVIAVHidngfMRKRES--QSVEEAL---KKLGIQ 286
Cdd:PRK13980 13 VREIIVDFIREEVEKAGAKGVVLGLSGGIDSAVVAYLAVKALGKENVLALL-----MPSSVSppEDLEDAElvaEDLGIE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 287 VKVINAAhsfyngtttlPISDEdrtprkrISKTLnmttsPEEKRKIIGdtfvkianevigemNLKPEE--VFL---AQgt 361
Cdd:PRK13980 88 YKVIEIT----------PIVDA-------FFSAI-----PDADRLRVG--------------NIMARTrmVLLydyAN-- 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217346693 362 lrpdliESASLVA--SGKAELIK---THHNDtelirklreeGKV-IEPLKDFHKDEVRILGRELGLPEELVSRHPFPG 433
Cdd:PRK13980 130 ------RENRLVLgtGNKSELLLgyfTKYGD----------GAVdLNPIGDLYKTQVRELARHLGVPEDIIEKPPSAD 191
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
92-200 |
2.44e-10 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 60.28 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 92 PVLGICYGMQMMNKVFGGTVHKKSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSV--DKVADGFKVVA----RSGN 165
Cdd:PRK08857 74 PILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVknDTLPECFELTAwtelEDGS 153
|
90 100 110
....*....|....*....|....*....|....*..
gi 2217346693 166 I--VAGIANESKKLYGAQFHPEVGLTENGKVILKNFL 200
Cdd:PRK08857 154 MdeIMGFQHKTLPIEAVQFHPESIKTEQGHQLLANFL 190
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
92-200 |
8.48e-10 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 58.72 E-value: 8.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 92 PVLGICYGMQMMNKVFGGTVHKKSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHG--DSVDKVADGFKVVA---RSGNI 166
Cdd:PRK06774 74 PILGVCLGHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSlvIAADSLPGCFELTAwseRGGEM 153
|
90 100 110
....*....|....*....|....*....|....*.
gi 2217346693 167 --VAGIANESKKLYGAQFHPEVGLTENGKVILKNFL 200
Cdd:PRK06774 154 deIMGIRHRTLPLEGVQFHPESILSEQGHQLLDNFL 189
|
|
| AANH-like |
cd01986 |
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ... |
232-282 |
2.25e-09 |
|
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide alpha hydrolase (AANH)-like proteins includes N-type ATP PPases and ATP sulfurylases. The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.
Pssm-ID: 467490 [Multi-domain] Cd Length: 74 Bit Score: 54.38 E-value: 2.25e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2217346693 232 VLVLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKK 282
Cdd:cd01986 1 VVVGYSGGKDSSVALHLASRLGRKAEVAVVHIDHGIGFKEEAESVASIARR 51
|
|
| NAD_synthase |
cd00553 |
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ... |
220-503 |
2.40e-09 |
|
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de novo nicotinamide adenine dinucleotide (NAD(+)) biosynthesis, an amide transfer from either ammonia or glutamine to nicotinic acid adenine dinucleotide (NaAD). The conversion of NaAD to NAD(+) occurs via a NAD-adenylate intermediate and requires ATP and Mg(2+). The intermediate is subsequently cleaved into NAD(+) and AMP. In many prokaryotes, such as Escherichia coli, NAD synthase consists of a single domain and is strictly ammonia dependent. In contrast, eukaryotes and other prokaryotes have an additional N-terminal amidohydrolase domain that prefer glutamine. Interestingly, NAD(+) synthases in these prokaryotes, can also utilize ammonia as an amide source.
Pssm-ID: 467484 [Multi-domain] Cd Length: 248 Bit Score: 58.34 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 220 IREIKERVGTSKVLVLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAAHSFyng 299
Cdd:cd00553 14 LRDYLRKSGAKGFVLGLSGGIDSAVVAALAVRALGAENVLALIMPSRYSSKETRDDAKALAENLGIEYRTIDIDPIV--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 300 tttlpisdedrtprKRISKTLNMTTSPEEKRKIIGdtfvkianevigemNLKPEE-----VFLAQgtlrpdlIESASLVA 374
Cdd:cd00553 91 --------------DAFLKALEHAGGSEAEDLALG--------------NIQARLrmvllYALAN-------LLGGLVLG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 375 SG-KAELIK---THHNDTelirklreeGKVIEPLKDFHKDEVRILGRELGLPEELVSRHpfPGPGLAIrVICAEE----P 446
Cdd:cd00553 136 TGnKSELLLgyfTKYGDG---------AADINPIGDLYKTQVRELARYLGVPEEIIEKP--PSAELWP-GQTDEDelgmP 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217346693 447 YickdfPETNNILKivadfsasvKKPHTLLQRVKACTTEEDQEKLMQITSLHSLNAF 503
Cdd:cd00553 204 Y-----EELDLILY---------GLVDGKLGPEEILSPGEDEEKVKRIFRLYRRNEH 246
|
|
| NAD_synthase |
pfam02540 |
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ... |
220-433 |
5.00e-09 |
|
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is induced by stress factors such as heat shock and glucose limitation.
Pssm-ID: 396888 [Multi-domain] Cd Length: 241 Bit Score: 57.39 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 220 IREIKERVGTSKVLVLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKresQSVEEAL---KKLGIQVKVInaahsf 296
Cdd:pfam02540 9 LRDYVQKAGFKGVVLGLSGGIDSSLVAYLAVKALGKENVLALIMPSSQSSE---EDVQDALalaENLGIEYKTI------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 297 yngtttlPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANevigEMNLkpeevfLAQGTlrpdliesaslvaSG 376
Cdd:pfam02540 80 -------DIKPIVRAFSQLFQDASEDFAKGNLKARIRMAILYYIAN----KFNY------LVLGT-------------GN 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217346693 377 KAELIK---THHNDTelirklreeGKVIEPLKDFHKDEVRILGRELGLPEELVSRHP----FPG 433
Cdd:pfam02540 130 KSELAVgyfTKYGDG---------ACDIAPIGDLYKTQVYELARYLNVPERIIKKPPsadlWPG 184
|
|
| QueC-like |
cd01995 |
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ... |
231-425 |
1.17e-08 |
|
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC 6.3.4.20) is also called 7-cyano-7-carbaguanine synthase, preQ(0) synthase, or queuosine biosynthesis protein QueC. It catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)), as part of the biosynthesis pathway of queuosine (Q). Q is one of the most complex modifications occurring at the wobble position of tRNAs with GUN anticodons, and is implicated in a number of biological activities, including accuracy of decoding, virulence, and cellular differentiation. This subfamily belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.
Pssm-ID: 467499 [Multi-domain] Cd Length: 208 Bit Score: 55.70 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 231 KVLVLLSGGVDSTVCTALLNRalNQEQVIAVHIDNGFM-RKRESQSVEEALKKLGIQVKVINAahSFYN--GTTTLPISD 307
Cdd:cd01995 2 KAVVLLSGGLDSTTLLYWALK--EGYEVHALTFDYGQRhAKEELEAAKLIAKLLGIEHKVIDL--SFLGelGGSSLTDEG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 308 EDRTPRKRISKTLNMTTSPeeKRKIIgdtFVKIAN---EVIGEmnlkpEEVFLA--QGTL------RPDLIESA-SLVAS 375
Cdd:cd01995 78 EEVPDGEYDEESIPSTWVP--NRNLI---FLSIAAayaESLGA-----SAIVIGvnAEDAsgypdcRPEFVEAMnSALNL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2217346693 376 GKAELIkthhndtelirklreegKVIEPLKDFHKDEVRILGRELGLPEEL 425
Cdd:cd01995 148 GTATGV-----------------KVVAPLIGLSKAEIVKLGVELGVPLEL 180
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
57-200 |
1.18e-08 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 55.96 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 57 IKEQGFRAIIISGGPNSvyAEDAPWFDPAIFTIGK--PVLGICYGMQMMNKVFGGTV--------HKKS--VREDGvfni 124
Cdd:PLN02335 58 LKRKNPRGVLISPGPGT--PQDSGISLQTVLELGPlvPLFGVCMGLQCIGEAFGGKIvrspfgvmHGKSspVHYDE---- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 125 svDNTCSLFRGLQKEEVVLLTHGDSVDK---VADGFKVVA--RSGNIVAGIANESKKLYGAQFHPEVGLTENGKVILKNF 199
Cdd:PLN02335 132 --KGEEGLFSGLPNPFTAGRYHSLVIEKdtfPSDELEVTAwtEDGLIMAARHRKYKHIQGVQFHPESIITTEGKTIVRNF 209
|
.
gi 2217346693 200 L 200
Cdd:PLN02335 210 I 210
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
47-198 |
1.33e-08 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 58.00 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 47 IFPLEtpafAIKEQGFRAIIISGGPNSvyaedapwfdPAIF----TIGK------PVLGICYGMQMMNKVFGGT------ 110
Cdd:PRK13566 559 GFAEE----MLDRVNPDLVVLSPGPGR----------PSDFdckaTIDAalarnlPIFGVCLGLQAIVEAFGGElgqlay 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 111 -VHKKSVRedgvfnISVDNTCSLFRGLQKEEVVLLTHgdSV----DKVADGFKVVARSG-NIVAGIANESKKLYGAQFHP 184
Cdd:PRK13566 625 pMHGKPSR------IRVRGPGRLFSGLPEEFTVGRYH--SLfadpETLPDELLVTAETEdGVIMAIEHKTLPVAAVQFHP 696
|
170
....*....|....*..
gi 2217346693 185 EVGLT---ENGKVILKN 198
Cdd:PRK13566 697 ESIMTlggDVGLRIIEN 713
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
90-200 |
1.66e-08 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153219 [Multi-domain] Cd Length: 198 Bit Score: 55.20 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 90 GKPVLGICYGMQMMN------------KVFGGTVHKKSVREDGVF------NISVDNTCSLFRGLQKEEVVLLTHGDSVD 151
Cdd:cd01748 71 GKPFLGICLGMQLLFesseegggtkglGLIPGKVVRFPASEGLKVphmgwnQLEITKESPLFKGIPDGSYFYFVHSYYAP 150
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217346693 152 kVADGFKVVARS---GNIVAGIANESkkLYGAQFHPE----VGLTengkvILKNFL 200
Cdd:cd01748 151 -PDDPDYILATTdygGKFPAAVEKDN--IFGTQFHPEksgkAGLK-----LLKNFL 198
|
|
| hisH |
PRK13181 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
90-200 |
2.09e-08 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 54.87 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 90 GKPVLGICYGMQMMNK-----------VFGGTVHKKSVREDGV----FN-ISVDNTCSLFRGLQKEEVVLLTHgdsvdkv 153
Cdd:PRK13181 72 KQPVLGICLGMQLLFEsseegnvkglgLIPGDVKRFRSEPLKVpqmgWNsVKPLKESPLFKGIEEGSYFYFVH------- 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217346693 154 adGFKVVARSGNIVAGIAN---------ESKKLYGAQFHPEVGlTENGKVILKNFL 200
Cdd:PRK13181 145 --SYYVPCEDPEDVLATTEygvpfcsavAKDNIYAVQFHPEKS-GKAGLKLLKNFA 197
|
|
| LarE-like |
cd01990 |
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ... |
231-431 |
3.61e-08 |
|
Lactate racemization operon protein LarE and similar proteins; This subfamily includes Lactiplantibacillus plantarum LarE, a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family. LarE is part of the lar operon, encoding five Lar proteins (LarA-E) that collaboratively synthesize and incorporate a niacin-derived Ni-containing cofactor into LarA, an Ni-dependent lactate racemase. It catalyzes successive thiolation reactions by donating the sulfur atom of their exclusive cysteine residues to the substrate. The LarE-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. Proteins from this subfamily probably binds ATP. This domain is about 200 amino acids long with a strongly conserved motif SGGxDS at the N-terminus.
Pssm-ID: 467494 [Multi-domain] Cd Length: 222 Bit Score: 54.57 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 231 KVLVLLSGGVDSTVCTALLNRALNqEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVInaahsfyngtTTLPISDEDR 310
Cdd:cd01990 1 KVVVAFSGGVDSSLLAKLAKEVLG-DNVVAVTADSPLVPREELEEAKRIAEEIGIRHEII----------KTDELDDEEY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 311 TPRkrisktlnmttsPEEK----RKIIGDTFVKIANEVigemnlkpEEVFLAQGTLRPDLIEsaslvasgkaelikthhn 386
Cdd:cd01990 70 VAN------------DPDRcyhcKKALYSTLKEIAKER--------GYDVVLDGTNADDLKD------------------ 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217346693 387 DTELIRKLREEGkVIEPLKDFH--KDEVRILGRELGLPEE-------LVSRHPF 431
Cdd:cd01990 112 YRPGLLAAAELG-IRSPLPELGltKSEIRELARELGLPNWdkpasacLASRIPY 164
|
|
| hisH |
PRK13141 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
90-200 |
6.05e-08 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 53.60 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 90 GKPVLGICYGMQMMN------------KVFGGTVHKKSVRED------GVFNISVDNTCSLFRGLQKEEVVLLTHGDSVD 151
Cdd:PRK13141 72 GKPLLGICLGMQLLFesseefgeteglGLLPGRVRRFPPEEGlkvphmGWNQLELKKESPLLKGIPDGAYVYFVHSYYAD 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217346693 152 kVADGFKVVARS---GNIVAGIANesKKLYGAQFHPE----VGLTengkvILKNFL 200
Cdd:PRK13141 152 -PCDEEYVAATTdygVEFPAAVGK--DNVFGAQFHPEksgdVGLK-----ILKNFV 199
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
21-112 |
8.29e-08 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 51.06 E-value: 8.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 21 VVILDAGAQYG---KVIDRRVRELFVQSEIFPLETPA--FAIKEQGFRAIIISGGPNSVYAEDAPW----FDPAIFTIGK 91
Cdd:cd01653 1 VAVLLFPGFEElelASPLDALREAGAEVDVVSPDGGPveSDVDLDDYDGLILPGGPGTPDDLARDEallaLLREAAAAGK 80
|
90 100
....*....|....*....|.
gi 2217346693 92 PVLGICYGMQMMnkVFGGTVH 112
Cdd:cd01653 81 PILGICLGAQLL--VLGVQFH 99
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
21-103 |
2.63e-07 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 49.12 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 21 VVILDAGAQY---GKVIDRRVRELFVQSEIFPLETPA--FAIKEQGFRAIIISGGPNSVYAEDAPW----FDPAIFTIGK 91
Cdd:cd03128 1 VAVLLFGGSEeleLASPLDALREAGAEVDVVSPDGGPveSDVDLDDYDGLILPGGPGTPDDLAWDEallaLLREAAAAGK 80
|
90
....*....|..
gi 2217346693 92 PVLGICYGMQMM 103
Cdd:cd03128 81 PVLGICLGAQLL 92
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
92-200 |
3.10e-07 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 51.34 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 92 PVLGICYGMQMMNKVFGGTV-------HKK--SVREDGVfnisvdntcSLFRGLQKEEVVLLTHGDSVDK--VADGFKVV 160
Cdd:PRK07649 74 PIFGVCLGHQSIAQVFGGEVvraerlmHGKtsLMHHDGK---------TIFSDIPNPFTATRYHSLIVKKetLPDCLEVT 144
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2217346693 161 A--RSGNIVAgIANESKKLYGAQFHPEVGLTENGKVILKNFL 200
Cdd:PRK07649 145 SwtEEGEIMA-IRHKTLPIEGVQFHPESIMTSHGKELLQNFI 185
|
|
| QueC |
pfam06508 |
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ... |
231-291 |
6.45e-07 |
|
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis of 7-carboxy-7-deazaguanine. They catalyze the conversion of 7-deaza-7-carboxyguanine to preQ0.
Pssm-ID: 428982 [Multi-domain] Cd Length: 210 Bit Score: 50.69 E-value: 6.45e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217346693 231 KVLVLLSGGVDSTVCTALlnrALNQ-EQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVIN 291
Cdd:pfam06508 1 KAVVLLSGGLDSTTCLAW---AKKEgYEVYALSFDYGQRHRKELECAKKIAKALGVEHKILD 59
|
|
| QueC |
COG0603 |
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ... |
231-291 |
8.75e-07 |
|
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; 7-cyano-7-deazaguanine synthase (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440368 [Multi-domain] Cd Length: 223 Bit Score: 50.55 E-value: 8.75e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217346693 231 KVLVLLSGGVDSTVCTALlnrALNQ-EQVIAVHIDNGFMRKRESQSVEEALKKLGI-QVKVIN 291
Cdd:COG0603 4 KAVVLLSGGLDSTTCLAW---ALARgYEVYALSFDYGQRHRKELEAARRIAKALGVgEHKVID 63
|
|
| PRK09522 |
PRK09522 |
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ... |
84-200 |
1.13e-06 |
|
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;
Pssm-ID: 181927 [Multi-domain] Cd Length: 531 Bit Score: 51.57 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 84 PAIFT--IGK-PVLGICYGMQMMNKVFGGTV-------HKK--SVREDGVfnisvdntcSLFRGLQKEEVVLLTHGDSVD 151
Cdd:PRK09522 68 PELLTrlRGKlPIIGICLGHQAIVEAYGGYVgqageilHGKasSIEHDGQ---------AMFAGLTNPLPVARYHSLVGS 138
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2217346693 152 KVADGFKVVARSGNIVAGIANESKKLYGAQFHPEVGLTENGKVILKNFL 200
Cdd:PRK09522 139 NIPAGLTINAHFNGMVMAVRHDADRVCGFQFHPESILTTQGARLLEQTL 187
|
|
| hisH |
PRK13146 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
90-200 |
1.54e-06 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237290 [Multi-domain] Cd Length: 209 Bit Score: 49.40 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 90 GKPVLGICYGMQMM---NKVFGGTvhkksvreDGvfnisvdntCSLFRGlqkeEVVLLTHGDSVDKV------------- 153
Cdd:PRK13146 77 GRPFLGICVGMQLLferGLEHGDT--------PG---------LGLIPG----EVVRFQPDGPALKVphmgwntvdqtrd 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217346693 154 -----------------------ADGFKVVARS---GNIVAGIANESkkLYGAQFHPE----VGLTengkvILKNFL 200
Cdd:PRK13146 136 hplfagipdgarfyfvhsyyaqpANPADVVAWTdygGPFTAAVARDN--LFATQFHPEksqdAGLA-----LLRNFL 205
|
|
| NadE |
COG0171 |
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
223-291 |
2.26e-06 |
|
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 439941 [Multi-domain] Cd Length: 542 Bit Score: 50.62 E-value: 2.26e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217346693 223 IKERV---GTSKVLVLLSGGVDSTVCTALLNRALNQEQVIAVhidngFMRKRES--QSVEEAL---KKLGIQVKVIN 291
Cdd:COG0171 277 LRDYVrknGFKGVVLGLSGGIDSALVAALAVDALGPENVLGV-----TMPSRYTsdESLEDAEelaENLGIEYEEID 348
|
|
| MnmA_TRMU-like |
cd01998 |
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ... |
231-298 |
3.30e-06 |
|
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.
Pssm-ID: 467502 [Multi-domain] Cd Length: 349 Bit Score: 49.81 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 231 KVLVLLSGGVDSTVCTALLnralnQEQ---VIAVHI---DNGFMRKRESQSVEEAL------KKLGIQVKVINAAHSFYN 298
Cdd:cd01998 1 KVAVAMSGGVDSSVAAALL-----KEQgydVIGVFMknwDDEDNEKGGCCSEEDIEdarrvaDQLGIPLYVVDFSEEYWE 75
|
|
| TilS |
COG0037 |
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ... |
230-297 |
3.47e-06 |
|
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439807 [Multi-domain] Cd Length: 235 Bit Score: 48.68 E-value: 3.47e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217346693 230 SKVLVLLSGGVDSTVCTALLNRALNQE--QVIAVHIDNGF--MRKRESQSVEEALKKLGIQVKVINAAHSFY 297
Cdd:COG0037 16 DRILVAVSGGKDSLALLHLLAKLRRRLgfELVAVHVDHGLreESDEDAEFVAELCEELGIPLHVVRVDVPAI 87
|
|
| HisH |
COG0118 |
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
90-188 |
3.65e-06 |
|
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 439888 [Multi-domain] Cd Length: 196 Bit Score: 48.11 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 90 GKPVLGICYGMQMM-NK-----------VFGGTVHKksVREDGV------FN-ISVDNTCSLFRGLQKEEVVLLTHgdS- 149
Cdd:COG0118 73 GKPVLGICLGMQLLfERseengdteglgLIPGEVVR--FPASDLkvphmgWNtVEIAKDHPLFAGIPDGEYFYFVH--Sy 148
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2217346693 150 ---VDKVADgfkVVARS---GNIVAGIANESkkLYGAQFHPE----VGL 188
Cdd:COG0118 149 yvpPDDPED---VVATTdygVPFTAAVERGN--VFGTQFHPEksgaAGL 192
|
|
| TilS_N |
cd01992 |
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ... |
231-291 |
4.19e-06 |
|
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine synthase (EC 6.3.4.19), also called tRNA(Ile)-2-lysyl-cytidine synthase or tRNA(Ile)-lysidine synthetase, catalyzes the ligation of lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. This subfamily belongs to the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This domain has a strongly conserved motif SGGXD at the N-terminus.
Pssm-ID: 467496 [Multi-domain] Cd Length: 185 Bit Score: 47.59 E-value: 4.19e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217346693 231 KVLVLLSGGVDSTVCTALLNRA--LNQEQVIAVHIDNGfMR---KRESQSVEEALKKLGIQVKVIN 291
Cdd:cd01992 1 KILVAVSGGPDSMALLHLLKELrpKLGLKLVAVHVDHG-LReesAEEAQFVAKLCKKLGIPLHILT 65
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
9-185 |
4.90e-06 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 49.41 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 9 DLKDGHHHYEGAVVILDAGAQYGkvIDRRVRELFVQSEIFPLETPAFAIKEQGFRAIIISGGPNsvyaedapwfDPAIFT 88
Cdd:CHL00197 183 DNKRPHSSYQLKIIVIDFGVKYN--ILRRLKSFGCSITVVPATSPYQDILSYQPDGILLSNGPG----------DPSAIH 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 89 IGK-----------PVLGICYGMQMMNKVFGGTVHKKSVREDGVfnisvdNTCSLFRglQKEEVVLLTHGDSVDK---VA 154
Cdd:CHL00197 251 YGIktvkkllkyniPIFGICMGHQILSLALEAKTFKLKFGHRGL------NHPSGLN--QQVEITSQNHGFAVNLeslAK 322
|
170 180 190
....*....|....*....|....*....|...
gi 2217346693 155 DGFKVVARSGN--IVAGIANESKKLYGAQFHPE 185
Cdd:CHL00197 323 NKFYITHFNLNdgTVAGISHSPKPYFSVQYHPE 355
|
|
| MnmA |
COG0482 |
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ... |
231-297 |
8.69e-06 |
|
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]; tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440250 [Multi-domain] Cd Length: 353 Bit Score: 48.51 E-value: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 231 KVLVLLSGGVDSTVCTALLnralnQEQ---VIAVHI---DNGFMRKRES----QSVEEALK---KLGIQVKVINAAHSFY 297
Cdd:COG0482 2 RVVVGMSGGVDSSVAAALL-----KEQgyeVIGVTMklwDDDDASGSGGccslEDIEDARRvadKLGIPHYVVDFEEEFK 76
|
|
| Asn_synthase_B_C |
cd01991 |
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
231-290 |
1.32e-05 |
|
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or synthetase) B is always associated with an N-terminal amidotransferase domain. Family members that contain this domain catalyze the conversion of aspartate to asparagine. Asparagine synthase B catalyzes the synthesis of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase.
Pssm-ID: 467495 [Multi-domain] Cd Length: 224 Bit Score: 46.88 E-value: 1.32e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 231 KVLVLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVI 290
Cdd:cd01991 4 PVGVLLSGGLDSSLIAALAARLLPETPIDLFTVGFEGSPTPDRAAARRVAEELGTEHHEV 63
|
|
| mnmA |
PRK00143 |
tRNA-specific 2-thiouridylase MnmA; Reviewed |
231-298 |
1.57e-05 |
|
tRNA-specific 2-thiouridylase MnmA; Reviewed
Pssm-ID: 234664 [Multi-domain] Cd Length: 346 Bit Score: 47.76 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 231 KVLVLLSGGVDSTVCTALLnralnQEQ---VIAVHI---DNGFMRKRESQSVEEALK-------KLGIQVKVINAAHSFY 297
Cdd:PRK00143 2 RVVVGMSGGVDSSVAAALL-----KEQgyeVIGVFMklwDDDDETGKGGCCAEEDIAdarrvadKLGIPHYVVDFEKEFW 76
|
.
gi 2217346693 298 N 298
Cdd:PRK00143 77 D 77
|
|
| tRNA_Me_trans |
pfam03054 |
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ... |
231-298 |
3.91e-05 |
|
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.
Pssm-ID: 460787 [Multi-domain] Cd Length: 202 Bit Score: 45.32 E-value: 3.91e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217346693 231 KVLVLLSGGVDSTVCTALLNRAlnQEQVIAVHIDNGFMRKRES-----------QSVEEALKKLGIQVKVINAAHSFYN 298
Cdd:pfam03054 2 KVVVAMSGGVDSSVAAYLLKEQ--GHNVIGVFMKNWDEEQSLDeegkccseedlADAQRVCEQLGIPLYVVNFEKEYWE 78
|
|
| PRK08250 |
PRK08250 |
glutamine amidotransferase; Provisional |
61-185 |
3.92e-05 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181323 [Multi-domain] Cd Length: 235 Bit Score: 45.73 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 61 GFRAIIISGGPNS--VYAEDAPWFDP---------AIFTiGKPVLGICYGMQMMNKVFGGTVHKKSVREDGVFNISVDN- 128
Cdd:PRK08250 45 GFDLLIVMGGPQSprTTREECPYFDSkaeqrlinqAIKA-GKAVIGVCLGAQLIGEALGAKYEHSPEKEIGYFPITLTEa 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217346693 129 --TCSLFRGLQKEEVVLLTHGDsVDKVADGFKVVARSGNIVAGIANESKKLYGAQFHPE 185
Cdd:PRK08250 124 glKDPLLSHFGSTLTVGHWHND-MPGLTDQAKVLATSEGCPRQIVQYSNLVYGFQCHME 181
|
|
| PAPS_reductase-like_YbdN |
cd23947 |
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ... |
221-422 |
4.81e-05 |
|
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to Escherichia coli YbdN; This subgroup contains Escherichia coli YbdN and other phosphoadenosine phosphosulfate (PAPS) reductase (or PAPS sulfotransferase EC 1.8.4.8)-like proteins. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N-type ATP PPases and ATP sulfurylases. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP).
Pssm-ID: 467512 [Multi-domain] Cd Length: 206 Bit Score: 45.07 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 221 REIKERVGTSK--VLVLLSGGVDSTVCTALLNRAL--NQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAAHSF 296
Cdd:cd23947 2 LERIRKVFEEFdpVIVSFSGGKDSLVLLHLALEALrrLRKDVYVVFIDTGIEFPETIDFVEKLAETLGLDVEAARPPLFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 297 YNGTT-----TLPISDEDRTPRKRisktLNMTTSpeekrkiigdTFVKIANEVIgeMNLKPEEVFLAQGtLRPDliESAS 371
Cdd:cd23947 82 EWLTSnfqpqWDPIWDNPPPPRDY----RWCCDE----------LKLEPFTKWL--KEKKPEGVLLLVG-IRAD--ESLN 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2217346693 372 lvasgKAELIKTHHNDTELIRKLrEEGKVIEPLKDFHKDEVRILGRELGLP 422
Cdd:cd23947 143 -----RAKRPRVYRKYGWRNSTL-PGQIVAYPIKDWSVEDVWLYILRHGLP 187
|
|
| PPase_ThiI |
cd01712 |
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ... |
227-431 |
3.36e-04 |
|
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole synthesis in the thiamine biosynthesis pathway. ThiI is also responsible for the 4-thiouridine (S4U) modification at position 8 in some prokaryotic tRNAs. ThiI contains a PP-loop pyrophosphatase domain which binds ATP and activates tRNA by adenylation. The PP-loop pyrophosphatase catalytic domain of ThiI proteins is always accompanied by a THUMP domain towards the N terminus. THUMP domains are predicted to bind RNA and are widespread in bacteria, archaea, and eukaryotes. The acronym was derived from the names of RNA-modifying enzymes in which this domain is found, namely, thiouridine synthases (ThiI), methylases, and archaeal pseudouridine synthases. ThiI proteins from gamma-proteobacteria and from archaea of the genus Thermoplasma also contain a C-terminal extension of approximately 100 amino acid residues which accepts sulfur in the form of a persulfide on a cysteine residue. This persulfide is responsible for a nucleophilic attack of the adenylated tRNA substrate, completing the sulfur insertion forming a disulfide-bridge between the rhodanese-like domain and a second cysteine residue located in the PP-loop domain. The reaction releases AMP and modified tRNA, and leaves the enzyme in an oxidized state. The disulfide is then reductively cleaved to complete the enzymatic cycle. The pyrophosphatase domain of ThiI belongs to the adenine nucleotide hydrolase (AANH) superfamily and it binds to adenosine nucleotide.
Pssm-ID: 467485 [Multi-domain] Cd Length: 185 Bit Score: 42.15 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 227 VGTS-KVLVLLSGGVDSTVCTALL-NRALnqeQVIAVHIDNG-FMRKRESQSVEEALKKLgiqvkvinaahSFYNGTTTL 303
Cdd:cd01712 1 VGTSgKVLVLLSGGIDSPVAAWMMmKRGV---EVDFLHFHSGpYTSEKAVEKVKDLARVL-----------SEYQGGVKL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 304 ---PISDEDRTPRKRISKTLNMTTSpeEKRKiigdtFVKIANEVIGEMNLKPeevfLAQGtlrpdliESASLVASGKAEL 380
Cdd:cd01712 67 ylvPFTDKIQKEILEKVPESYRIVL--MRRM-----MYRIAEKIAERLGADA----LVTG-------ESLGQVASQTLEN 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2217346693 381 IKTHHNDTELIrklreegkVIEPLKDFHKDEVRILGRELGLPEelVSRHPF 431
Cdd:cd01712 129 LKVIDSVTDLP--------VLRPLIGMDKEEIIDIARRIGTYE--ISILPY 169
|
|
| lysidine_TilS_N |
TIGR02432 |
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ... |
231-291 |
4.57e-04 |
|
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble position of a tRNA must discriminate between G and A of mRNA are AUA (Ile) vs. AUG (Met) and UGA (stop) vs. UGG (Trp). In all bacteria, the wobble position of the tRNA(Ile) recognizing AUA is lysidine, a lysine derivative of cytidine. This family describes a protein domain found, apparently, in all bacteria in a single copy. Eukaryotic sequences appear to be organellar. The domain archictecture of this protein family is variable; some, including characterized proteins of E. coli and B. subtilis known to be tRNA(Ile)-lysidine synthetase, include a conserved 50-residue domain that many other members lack. This protein belongs to the ATP-binding PP-loop family ( pfam01171). It appears in the literature and protein databases as TilS, YacA, and putative cell cycle protein MesJ (a misnomer). [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 274129 [Multi-domain] Cd Length: 189 Bit Score: 41.85 E-value: 4.57e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217346693 231 KVLVLLSGGVDSTVCTALLNRALNQ--EQVIAVHIDNGfMR---KRESQSVEEALKKLGIQVKVIN 291
Cdd:TIGR02432 1 RILVAVSGGVDSMALLHLLLKLQPKikIKLIAAHVDHG-LRpesDEEAEFVQQFCRKLNIPLEIKK 65
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
21-185 |
4.61e-04 |
|
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 43.09 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 21 VVILDAGAQYGkvIDRRVRELFVQSEIFPLETPAFAIKEQGFRAIIISGGPNsvyaedapwfDP-----AIFTI------ 89
Cdd:COG0505 179 VVALDFGVKRN--ILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPG----------DPaaldyAIETIrellgk 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 90 GKPVLGICYGMQMMNKVFGGTVHK------------KSVREDGVFnISVDNtcslfrglqkeevvlltHGDSVDK---VA 154
Cdd:COG0505 247 GIPIFGICLGHQLLALALGAKTYKlkfghrganhpvKDLETGRVE-ITSQN-----------------HGFAVDEdslPA 308
|
170 180 190
....*....|....*....|....*....|...
gi 2217346693 155 DGFKVVARSGN--IVAGIANESKKLYGAQFHPE 185
Cdd:COG0505 309 TDLEVTHVNLNdgTVEGLRHKDLPAFSVQYHPE 341
|
|
| TIGR00364 |
TIGR00364 |
queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in ... |
233-291 |
5.53e-04 |
|
queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in synthesizing pre-Q0 from GTP en route to tRNA modification with queuosine. This protein family is represented by a single member in nearly every completed large (> 1000 genes) prokaryotic genome. In Rhizobium meliloti, the gene was designated exsB, possibly because of polar effects on exsA expression in a shared polycistronic mRNA. In Arthrobacter viscosus, the homologous gene was designated ALU1 and was associated with an aluminum tolerance phenotype. [Unknown function, General]
Pssm-ID: 129461 [Multi-domain] Cd Length: 201 Bit Score: 41.61 E-value: 5.53e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 233 LVLLSGGVDSTVCTALlnrALNQ-EQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVIN 291
Cdd:TIGR00364 2 IVVLSGGQDSTTCLLW---AKDEgYEVHAVTFDYGQRHSRELESARKIAEALGIEHHLLD 58
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
21-185 |
8.57e-04 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 42.19 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 21 VVILDAGaqYGKVIDRRVRELFVQSEIFPLETPAFAIKEQGFRAIIISGGPNSvyAEDAPWFDPAIFTI--GKPVLGICY 98
Cdd:PRK12838 170 VALIDFG--YKKSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGPGD--PKELQPYLPEIKKLisSYPILGICL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 99 GMQMMNKVFGGTVHKKSVREDGVfNISVDNTCSlfrglQKEEVVLLTHG-----DSVDKvaDGFKVVARSGN--IVAGIA 171
Cdd:PRK12838 246 GHQLIALALGADTEKLPFGHRGA-NHPVIDLTT-----GRVWMTSQNHGyvvdeDSLDG--TPLSVRFFNVNdgSIEGLR 317
|
170
....*....|....
gi 2217346693 172 NESKKLYGAQFHPE 185
Cdd:PRK12838 318 HKKKPVLSVQFHPE 331
|
|
| trmU |
TIGR00420 |
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ... |
231-298 |
1.32e-03 |
|
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase (trmU, asuE, or mnmA) is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine (mnm5s2U34) present in the wobble position of some tRNAs. This enzyme appears not to occur in the Archaea. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 273069 [Multi-domain] Cd Length: 352 Bit Score: 41.60 E-value: 1.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217346693 231 KVLVLLSGGVDSTVCTALLNRalNQEQVIAVHIDN----------GFMRKRESQSVEEALKKLGIQVKVINAAHSFYN 298
Cdd:TIGR00420 2 KVIVGLSGGVDSSVSAYLLKQ--QGYEVVGVFMKNweeddkndghGCTSAEDLRDAQAICEKLGIPLEKVNFQKEYWN 77
|
|
| nadE |
PRK00876 |
NAD(+) synthase; |
232-273 |
2.04e-03 |
|
NAD(+) synthase;
Pssm-ID: 179150 [Multi-domain] Cd Length: 326 Bit Score: 40.71 E-value: 2.04e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2217346693 232 VLVLLSGGVDSTVCTALLNRALNQEQVIAVhidngFMRKRES 273
Cdd:PRK00876 36 VVLGLSGGIDSSVTAALCVRALGKERVYGL-----LMPERDS 72
|
|
| PRK06490 |
PRK06490 |
glutamine amidotransferase; Provisional |
66-186 |
3.07e-03 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 180590 [Multi-domain] Cd Length: 239 Bit Score: 39.94 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 66 IISGGPNSVYAEDaPWFDPAIFTIG------KPVLGICYGMQMMNKVFGGTVhkkSVREDGVFNIS---VDNTcSLFRGL 136
Cdd:PRK06490 57 VIFGGPMSANDPD-DFIRREIDWISvplkenKPFLGICLGAQMLARHLGARV---APHPDGRVEIGyypLRPT-EAGRAL 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217346693 137 QK----------------EEVVLLTHGDSvdkvadgFKVVA-RSGnivagianesKKLYGAQFHPEV 186
Cdd:PRK06490 132 MHwpemvyhwhregfdlpAGAELLATGDD-------FPNQAfRYG----------DNAWGLQFHPEV 181
|
|
| hisH |
PRK13152 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
91-200 |
3.28e-03 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 171876 [Multi-domain] Cd Length: 201 Bit Score: 39.44 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 91 KPVLGICYGMQMMNKV-FGGTVHK-----------------KSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHG----- 147
Cdd:PRK13152 74 KPILGICLGMQLFLERgYEGGVCEglgfiegevvkfeedlnLKIPHMGWNELEILKQSPLYQGIPEKSDFYFVHSfyvkc 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346693 148 --DSVDKVAD-GFKVVArsgnivagiANESKKLYGAQFHPE----VGLTengkvILKNFL 200
Cdd:PRK13152 154 kdEFVSAKAQyGHKFVA---------SLQKDNIFATQFHPEksqnLGLK-----LLENFA 199
|
|
| TtuA-like |
cd01993 |
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ... |
229-300 |
5.64e-03 |
|
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) 2-sulfurtransferase, also called tRNA thiouridine synthetase TtuA, catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T). TtuA belongs to the adenine nucleotide alpha hydrolase superfamily (AANH) that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This domain has a strongly conserved motif SGGKD at the N-terminus.
Pssm-ID: 467497 [Multi-domain] Cd Length: 190 Bit Score: 38.46 E-value: 5.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217346693 229 TSKVLVLLSGGVDSTVCTALLNRAlnQEQVIAVHIDNGF--MRKRESQSVEEALKKLGIQVKVINAAHSFYNGT 300
Cdd:cd01993 8 DDKILVAVSGGKDSLALLAVLKKL--GYNVEALYINLGIgeYSEKSEEVVKKLAEKLNLPLHVVDLKEEYGLGI 79
|
|
| GATase1_CobQ |
cd01750 |
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ... |
64-103 |
5.69e-03 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ). CobQ plays a role in cobalamin biosythesis. CobQ catalyses amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide in the biosynthesis of cobalamin. CobQ belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobQ.
Pssm-ID: 153221 [Multi-domain] Cd Length: 194 Bit Score: 38.38 E-value: 5.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217346693 64 AIIISGGPNSV---YAEDAPWFDPAI---FTIGKPVLGICYGMQMM 103
Cdd:cd01750 40 LIILPGSKDTIqdlAWLRKRGLAEAIknyARAGGPVLGICGGYQML 85
|
|
| PRK13820 |
PRK13820 |
argininosuccinate synthase; Provisional |
228-296 |
9.17e-03 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 237521 Cd Length: 394 Bit Score: 39.14 E-value: 9.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217346693 228 GTSKVLVLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGfMRKRESQSVEEALKKLGIQVKVINAAHSF 296
Cdd:PRK13820 1 MMKKVVLAYSGGLDTSVCVPLLKEKYGYDEVITVTVDVG-QPEEEIKEAEEKAKKLGDKHYTIDAKEEF 68
|
|
| |
