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Conserved domains on  [gi|1301392553|gb|PKB60464|]
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MAG: phosphoribosylformylglycinamidine synthase II, partial [SAR202 cluster bacterium Ae2-Chloro-G1]

Protein Classification

phosphoribosylformylglycinamidine synthase subunit PurL( domain architecture ID 11479458)

phosphoribosylformylglycinamidine synthase subunit PurL is part of the enzyme complex that catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate; involved in the biosynthetic pathway of purines

EC:  6.3.5.3
Gene Symbol:  purL
Gene Ontology:  GO:0004642|GO:0005524
PubMed:  2531746

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRK01213 PRK01213
phosphoribosylformylglycinamidine synthase subunit PurL;
1-635 0e+00

phosphoribosylformylglycinamidine synthase subunit PurL;


:

Pssm-ID: 234921 [Multi-domain]  Cd Length: 724  Bit Score: 913.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553   1 GAATGVGGIVRDILAMGARPIALLNSLRFGPLDHERNRYLFEGVVSGISGYGNCIGIPNIGGEVGFATSYTGNPLVNAMC 80
Cdd:PRK01213  101 GAATGVGGILRDIFSMGARPIALLDSLRFGELDHPKTRYLLEGVVAGIGGYGNCIGVPTVGGEVYFDESYNGNPLVNAMC 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  81 IGLVEIKNLVRATSGDKGNVLLLVGSGTGRDGIHGASgLASRTFEED-RELRPTVQVGNPFLEKILIESCLEAVQTGLVD 159
Cdd:PRK01213  181 VGLVRHDDIVLAKASGVGNPVVYVGAKTGRDGIGGAS-FASAELSEEsEEKRPAVQVGDPFMEKLLIEACLELIKTGLVV 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 160 GLQDLGAAGLTSASVECASNGGTGIKLFMDKIPLRDDGMEPYEIMLSETQERMLLSVKRDNLNRVSQVFDKWDVENTVIG 239
Cdd:PRK01213  260 GIQDMGAAGLTCSSSEMAAKGGLGIELDLDKVPLREEGMTPYEIMLSESQERMLLVVKPGKEEEVLAIFEKWDLDAAVIG 339
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 240 QVVDGDAIELIEEGVTKGHIPINLLTD-PPLYRPDGVKPDYLKDLQSyeldrvplPTASPSAVFLDLIASPNISSRVSVY 318
Cdd:PRK01213  340 EVTDDGRLRVYHHGEVVADVPAEALADeAPVYDRPYKEPAYLDELQA--------DPEDLKEALLKLLSSPNIASKEWVY 411
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 319 RQYDHQVQTNTVIPPGNEAALLRIKGTSKGLSAATDGNSRACYLDPFVGGVISVAEACRNVSCTGAEPIALTNCLNFGNP 398
Cdd:PRK01213  412 EQYDHEVQTNTVVKPGGDAAVLRIRGGGKGLALTTDCNPRYVYLDPYEGAKLAVAEAARNLAAVGATPLAITDCLNFGNP 491
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 399 ENPEVYYQLEHCVRGIVSASESFDAPVISGNVSLYNETGNKSIYPTPVIGAVGLTENVSRHCDIAFKEVGDIVVLLGASm 478
Cdd:PRK01213  492 EKPEVMWQFVEAVRGLADACRALGTPVVGGNVSLYNETGGTAIYPTPVIGMVGLIDDVSKRTTSGFKKEGDLIYLLGET- 570
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 479 vagyTSSLSGSEYLEVIHNLVAGQ-PSIDIDKELSVQAACRRLISEGLAKSAHDCSDGGLAVAIVESSIQGNLGFGGTVV 557
Cdd:PRK01213  571 ----KDELGGSEYLKVIHGHVGGRpPKVDLEAEKRLQELVREAIREGLVTSAHDVSEGGLAVALAEMAIAGGLGAEVDLS 646
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1301392553 558 IEGRWDAALFGEDQSRIVVSINHKDLDLCSSVCEEYSVEWCVLGNVQEGRFSFSGLIDLPMSQLSEIWTQSLERVAGG 635
Cdd:PRK01213  647 DGLRPDALLFSESQGRYVVSVPPENEEAFEALAEAAGVPATRIGVVGGDALKVKGNDTESLEELREAWEGALPRLLGG 724
 
Name Accession Description Interval E-value
PRK01213 PRK01213
phosphoribosylformylglycinamidine synthase subunit PurL;
1-635 0e+00

phosphoribosylformylglycinamidine synthase subunit PurL;


Pssm-ID: 234921 [Multi-domain]  Cd Length: 724  Bit Score: 913.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553   1 GAATGVGGIVRDILAMGARPIALLNSLRFGPLDHERNRYLFEGVVSGISGYGNCIGIPNIGGEVGFATSYTGNPLVNAMC 80
Cdd:PRK01213  101 GAATGVGGILRDIFSMGARPIALLDSLRFGELDHPKTRYLLEGVVAGIGGYGNCIGVPTVGGEVYFDESYNGNPLVNAMC 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  81 IGLVEIKNLVRATSGDKGNVLLLVGSGTGRDGIHGASgLASRTFEED-RELRPTVQVGNPFLEKILIESCLEAVQTGLVD 159
Cdd:PRK01213  181 VGLVRHDDIVLAKASGVGNPVVYVGAKTGRDGIGGAS-FASAELSEEsEEKRPAVQVGDPFMEKLLIEACLELIKTGLVV 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 160 GLQDLGAAGLTSASVECASNGGTGIKLFMDKIPLRDDGMEPYEIMLSETQERMLLSVKRDNLNRVSQVFDKWDVENTVIG 239
Cdd:PRK01213  260 GIQDMGAAGLTCSSSEMAAKGGLGIELDLDKVPLREEGMTPYEIMLSESQERMLLVVKPGKEEEVLAIFEKWDLDAAVIG 339
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 240 QVVDGDAIELIEEGVTKGHIPINLLTD-PPLYRPDGVKPDYLKDLQSyeldrvplPTASPSAVFLDLIASPNISSRVSVY 318
Cdd:PRK01213  340 EVTDDGRLRVYHHGEVVADVPAEALADeAPVYDRPYKEPAYLDELQA--------DPEDLKEALLKLLSSPNIASKEWVY 411
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 319 RQYDHQVQTNTVIPPGNEAALLRIKGTSKGLSAATDGNSRACYLDPFVGGVISVAEACRNVSCTGAEPIALTNCLNFGNP 398
Cdd:PRK01213  412 EQYDHEVQTNTVVKPGGDAAVLRIRGGGKGLALTTDCNPRYVYLDPYEGAKLAVAEAARNLAAVGATPLAITDCLNFGNP 491
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 399 ENPEVYYQLEHCVRGIVSASESFDAPVISGNVSLYNETGNKSIYPTPVIGAVGLTENVSRHCDIAFKEVGDIVVLLGASm 478
Cdd:PRK01213  492 EKPEVMWQFVEAVRGLADACRALGTPVVGGNVSLYNETGGTAIYPTPVIGMVGLIDDVSKRTTSGFKKEGDLIYLLGET- 570
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 479 vagyTSSLSGSEYLEVIHNLVAGQ-PSIDIDKELSVQAACRRLISEGLAKSAHDCSDGGLAVAIVESSIQGNLGFGGTVV 557
Cdd:PRK01213  571 ----KDELGGSEYLKVIHGHVGGRpPKVDLEAEKRLQELVREAIREGLVTSAHDVSEGGLAVALAEMAIAGGLGAEVDLS 646
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1301392553 558 IEGRWDAALFGEDQSRIVVSINHKDLDLCSSVCEEYSVEWCVLGNVQEGRFSFSGLIDLPMSQLSEIWTQSLERVAGG 635
Cdd:PRK01213  647 DGLRPDALLFSESQGRYVVSVPPENEEAFEALAEAAGVPATRIGVVGGDALKVKGNDTESLEELREAWEGALPRLLGG 724
PurL1 COG0046
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and ...
1-632 0e+00

Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and metabolism]; Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439816 [Multi-domain]  Cd Length: 747  Bit Score: 782.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553   1 GAATGVGGIVRDILAMGARPIALLNSLRFGPLDHE--RNRYLFEGVVSGISGYGNCIGIPNIGGEVGFATSYTGNPLVNA 78
Cdd:COG0046   112 GAATGVGGIIRDIFGMGARPIAGLDSLRFGNLDQPpaSPRYILIGVVAGIADYGNCFGVPTVGGEVRFDESYEGNPLVNA 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  79 MCIGLVEIKNLVRATSGDKGNVLLLVGSGTGRDGIHGASgLASRTFEEDREL-RPTVQVGNPFLEKILIESCLEAVQTGL 157
Cdd:COG0046   192 GGVGIIRADHIFKAKAPGVGNKVVYVGGPTGRDGIGGAT-FASEELGEDSELdRPAVQVGDPFMEKRLIEAILELGDTGL 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 158 VDGLQDLGAAGLTSASVECASNGGTGIKLFMDKIPLRDDGMEPYEIMLSETQERMLLSVKRDNLNRVSQVFDKWDVENTV 237
Cdd:COG0046   271 IVGIQDMGAGGLSSASSEMAAKGGLGAEIDLDKVPLREPGMSPYEIWLSESQERMLLVVKPEKLEEFEAIFERWRLPAAV 350
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 238 IGQVVDGDAIELIEEGVTKGHIPINLLTD-PPLYRPDGVKPDYLKDLQsyeldrVPLPtASPSAVFLDLIASPNISSRVS 316
Cdd:COG0046   351 IGEVTDDGRLVVTDHGETVADLPLDFLAGgAPKYHRPAKRPAYLEPLD------LPEP-IDLEEALLRLLSSPNVASKEW 423
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 317 VYRQYDHQVQTNTVI-PPGNEAALLRIKGTSKGLSAATDGNSRACYLDPFVGGVISVAEACRNVSCTGAEPIALTNCLNF 395
Cdd:COG0046   424 LYRQYDREVGGNTVRdPGVADAAVVRVDGTYKGLAMSTGENPRYALLDPYAGARMAVAEAARNLAAVGAEPLAITDCLNW 503
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 396 GNPENPEVYYQLEHCVRGIVSASESFDAPVISGNVSLYNET--GNKSIYPTPVIGAVGLTENVSRHCDIAFKEVGDIVVL 473
Cdd:COG0046   504 GNPEKPEEMAQLVEAVKGLADACRALGIPVPSGNVSLYNETkdGKVAIPPTPVIGAVGLVDDVRKTVTPDLKKEGDLLYL 583
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 474 LGASmvagyTSSLSGSEYLEVIhNLVAGQ-PSIDIDKELSVQAACRRLISEGLAKSAHDCSDGGLAVAIVESSIQGNLGF 552
Cdd:COG0046   584 IGET-----KNELGGSEYAQVL-GQLGGEpPDVDLEAEKALFEAVQELIREGLILAAHDVSDGGLAVALAEMAFAGGLGA 657
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 553 GGTV--VIEGRWDAALFGEDQSRIVVSINHKDLDLCSSVCEEYSVEWCVLGNV-QEGRFSFSG----LIDLPMSQLSEIW 625
Cdd:COG0046   658 DIDLdaLGDLRPDAALFSESQGRAVVQVAPEDAEAVEALLAEAGLPAHVIGTVtGDDRLVIRRggetLLSLSLAELRDAW 737

                  ....*..
gi 1301392553 626 TQSLERV 632
Cdd:COG0046   738 EETLPRL 744
FGAM_synth_II TIGR01736
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ...
1-632 0e+00

phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a single, long polypeptide in most Proteobacteria and eukarotes. Three proteins are required in Bacillus subtilis and many other species. This is the longest of the three and is designated PurL, phosphoribosylformylglycinamidine synthase II, or FGAM synthase II. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273781 [Multi-domain]  Cd Length: 715  Bit Score: 757.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553   1 GAATGVGGIVRDILAMGARPIALLNSLRFGPLDHERNRYLFEGVVSGISGYGNCIGIPNIGGEVGFATSYTGNPLVNAMC 80
Cdd:TIGR01736  89 GAATGVGGILRDILSMGARPIALLDSLRFGPLDDPKNRYLFEGVVAGISDYGNRIGVPTVGGEVEFDESYNGNPLVNVMC 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  81 IGLVEIKNLVRATSGDKGNVLLLVGSGTGRDGIHGASgLASRTFEED--RELRPTVQVGNPFLEKILIESCLEAVQTGLV 158
Cdd:TIGR01736 169 VGLVRKDDIVTGKAKGPGNKLVLVGGKTGRDGIGGAT-FASEELSEEaeEEDRPAVQVGDPFTEKLLIEATLEAVDTGLV 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 159 DGLQDLGAAGLTSASVECASNGGTGIKLFMDKIPLRDDGMEPYEIMLSETQERMLLSVKRDNLNRVSQVFDKWDVENTVI 238
Cdd:TIGR01736 248 KGIKDLGAAGLTSASSEMAAKGGLGAEIYLDKVPLREPGMTPYEIMLSESQERMLLVVAPEDVEEVLEIFEKYELPASVI 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 239 GQVVDGDAIELIEEGVTKGHIPINLLTDPPLYRPDGVKPDYlkdlqsYELDRVPLPTASPSAVFLDLIASPNISSRVSVY 318
Cdd:TIGR01736 328 GEVTDEGRIRLYYKGEVVADLPIELLADAPEYERPSEPPKY------PEEEKEPEPPADLEDAFLKVLSSPNIASKEWVY 401
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 319 RQYDHQVQTNTVIPPGNEAALLRIKGTSK-GLSAATDGNSRACYLDPFVGGVISVAEACRNVSCTGAEPIALTNCLNFGN 397
Cdd:TIGR01736 402 RQYDHEVQTRTVVKPGEDAAVLRIKETGKlGLALTADCNPRYVYLDPYAGAAGAVAEAYRNLAAVGAEPLAAVDCLNFGN 481
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 398 PENPEVYYQLEHCVRGIVSASESFDAPVISGNVSLYNETGNKSIYPTPVIGAVGLTENVSRHCDIAFKEVGDIVVLLGAS 477
Cdd:TIGR01736 482 PERPEVYWQFVEAVKGLGDACRALGTPVVGGNVSLYNETNGVPIAPTPTIGMVGLVEDVEKLLTSNFKKEGDAIYLIGET 561
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 478 mvagyTSSLSGSEYLEVIHNLVAGQ-PSIDIDKELSVQAACRRLISEGLAKSAHDCSDGGLAVAIVESSIQGNLGFggTV 556
Cdd:TIGR01736 562 -----KDELGGSEYLRVIHGIVSGQvPAVDLEEEKELADAVREAIRAGLVSAAHDVSRGGLAVALAEMAAASGIGA--EV 634
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 557 VIEG----RWDAALFGEDQSRIVVSINHKDldlCSSVCEEYSVEWCVLGNVQEGRFSFSGL---IDLPMSQLSEIWTQSL 629
Cdd:TIGR01736 635 DIDEiasaRPDELLFSESNGRAIVAVPEEK---AEEAVKSKGVPAKVIGKTGGDRLTIKTGddtISVSVKELRDAWEEAL 711

                  ...
gi 1301392553 630 ERV 632
Cdd:TIGR01736 712 PEY 714
PurL_repeat1 cd02203
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ...
1-263 9.57e-123

PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, phosphate, and glutamate in the fourth step of the purine biosynthetic pathway. In eukaryotes and Gram-negative bacteria, FGAR-AT is encoded by the purL gene as a multidomain protein with a molecular mass of about 140 kDa. In Gram-positive bacteria and archaea FGAR-AT is a complex of three proteins: PurS, PurL, and PurQ. PurL itself contains two tandem N- and C-terminal domains (four domains altogether). The N-terminal domains bind ATP and are related to the ATP-binding domains of HypE, ThiL, SelD and PurM.


Pssm-ID: 100034 [Multi-domain]  Cd Length: 313  Bit Score: 366.03  E-value: 9.57e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553   1 GAATGVGGIVRDILAMGARPIALLNSLRFGPLDHE--------RNRYLFEGVVSGISGYGNCIGIPNIGGEVGFATSYTG 72
Cdd:cd02203    46 GAATGVGGIIRDILSMGARPIALLDGLRFGDLDIPgyepkgklSPRRILDGVVAGISDYGNCIGIPTVGGEVRFDPSYYG 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  73 NPLVNAMCIGLVEIKNLVRATSGDKGNVLLLVGSGTGRDGIHGASGlASRTFEEDREL--RPTVQVGNPFLEKILIESCL 150
Cdd:cd02203   126 NPLVNVGCVGIVPKDHIVKSKAPGPGDLVVLVGGRTGRDGIGGATF-SSKELSENSSEldRPAVQVGDPFMEKKLQEAIL 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 151 EAVQTGLVDGLQDLGAAGLTSASVECASNGGTGIKLFMDKIPLRDDGMEPYEIMLSETQERMLLSVKRDNLNRVSQVFDK 230
Cdd:cd02203   205 EARETGLIVGIQDLGAGGLSSAVSEMAAKGGLGAEIDLDKVPLREPGMSPWEIWISESQERMLLVVPPEDLEEFLAICKK 284
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1301392553 231 WDVENTVIGQVVDGDAIELIEegvtKGHIPINL 263
Cdd:cd02203   285 EDLEAAVIGEVTDDGRLRLYY----KGEVVADL 313
AIRS_C pfam02769
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ...
98-250 2.26e-32

AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site.


Pssm-ID: 460684 [Multi-domain]  Cd Length: 152  Bit Score: 122.07  E-value: 2.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  98 GNVLLLVGSgtgrDGIHGASGLASRTFEEDrELRPTVQVGNPFLEKILIES-CLEAVQTGLVDGLQDLGAAGLTSASVEC 176
Cdd:pfam02769   3 GDVLILLGS----SGLHGAGLSLSRKGLED-SGLAAVQLGDPLLEPTLIYVkLLLAALGGLVKAMHDITGGGLAGALAEM 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1301392553 177 ASNGGTGIKLFMDKIPLRDDGMEPYEIMLSETQERMLLSVKRDNLNRVSQVFDKWDVENTVIGQVVDGDAIELI 250
Cdd:pfam02769  78 APASGVGAEIDLDKVPIFEELMLPLEMLLSENQGRGLVVVAPEEAEAVLAILEKEGLEAAVIGEVTAGGRLTVI 151
 
Name Accession Description Interval E-value
PRK01213 PRK01213
phosphoribosylformylglycinamidine synthase subunit PurL;
1-635 0e+00

phosphoribosylformylglycinamidine synthase subunit PurL;


Pssm-ID: 234921 [Multi-domain]  Cd Length: 724  Bit Score: 913.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553   1 GAATGVGGIVRDILAMGARPIALLNSLRFGPLDHERNRYLFEGVVSGISGYGNCIGIPNIGGEVGFATSYTGNPLVNAMC 80
Cdd:PRK01213  101 GAATGVGGILRDIFSMGARPIALLDSLRFGELDHPKTRYLLEGVVAGIGGYGNCIGVPTVGGEVYFDESYNGNPLVNAMC 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  81 IGLVEIKNLVRATSGDKGNVLLLVGSGTGRDGIHGASgLASRTFEED-RELRPTVQVGNPFLEKILIESCLEAVQTGLVD 159
Cdd:PRK01213  181 VGLVRHDDIVLAKASGVGNPVVYVGAKTGRDGIGGAS-FASAELSEEsEEKRPAVQVGDPFMEKLLIEACLELIKTGLVV 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 160 GLQDLGAAGLTSASVECASNGGTGIKLFMDKIPLRDDGMEPYEIMLSETQERMLLSVKRDNLNRVSQVFDKWDVENTVIG 239
Cdd:PRK01213  260 GIQDMGAAGLTCSSSEMAAKGGLGIELDLDKVPLREEGMTPYEIMLSESQERMLLVVKPGKEEEVLAIFEKWDLDAAVIG 339
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 240 QVVDGDAIELIEEGVTKGHIPINLLTD-PPLYRPDGVKPDYLKDLQSyeldrvplPTASPSAVFLDLIASPNISSRVSVY 318
Cdd:PRK01213  340 EVTDDGRLRVYHHGEVVADVPAEALADeAPVYDRPYKEPAYLDELQA--------DPEDLKEALLKLLSSPNIASKEWVY 411
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 319 RQYDHQVQTNTVIPPGNEAALLRIKGTSKGLSAATDGNSRACYLDPFVGGVISVAEACRNVSCTGAEPIALTNCLNFGNP 398
Cdd:PRK01213  412 EQYDHEVQTNTVVKPGGDAAVLRIRGGGKGLALTTDCNPRYVYLDPYEGAKLAVAEAARNLAAVGATPLAITDCLNFGNP 491
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 399 ENPEVYYQLEHCVRGIVSASESFDAPVISGNVSLYNETGNKSIYPTPVIGAVGLTENVSRHCDIAFKEVGDIVVLLGASm 478
Cdd:PRK01213  492 EKPEVMWQFVEAVRGLADACRALGTPVVGGNVSLYNETGGTAIYPTPVIGMVGLIDDVSKRTTSGFKKEGDLIYLLGET- 570
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 479 vagyTSSLSGSEYLEVIHNLVAGQ-PSIDIDKELSVQAACRRLISEGLAKSAHDCSDGGLAVAIVESSIQGNLGFGGTVV 557
Cdd:PRK01213  571 ----KDELGGSEYLKVIHGHVGGRpPKVDLEAEKRLQELVREAIREGLVTSAHDVSEGGLAVALAEMAIAGGLGAEVDLS 646
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1301392553 558 IEGRWDAALFGEDQSRIVVSINHKDLDLCSSVCEEYSVEWCVLGNVQEGRFSFSGLIDLPMSQLSEIWTQSLERVAGG 635
Cdd:PRK01213  647 DGLRPDALLFSESQGRYVVSVPPENEEAFEALAEAAGVPATRIGVVGGDALKVKGNDTESLEELREAWEGALPRLLGG 724
PurL1 COG0046
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and ...
1-632 0e+00

Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and metabolism]; Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439816 [Multi-domain]  Cd Length: 747  Bit Score: 782.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553   1 GAATGVGGIVRDILAMGARPIALLNSLRFGPLDHE--RNRYLFEGVVSGISGYGNCIGIPNIGGEVGFATSYTGNPLVNA 78
Cdd:COG0046   112 GAATGVGGIIRDIFGMGARPIAGLDSLRFGNLDQPpaSPRYILIGVVAGIADYGNCFGVPTVGGEVRFDESYEGNPLVNA 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  79 MCIGLVEIKNLVRATSGDKGNVLLLVGSGTGRDGIHGASgLASRTFEEDREL-RPTVQVGNPFLEKILIESCLEAVQTGL 157
Cdd:COG0046   192 GGVGIIRADHIFKAKAPGVGNKVVYVGGPTGRDGIGGAT-FASEELGEDSELdRPAVQVGDPFMEKRLIEAILELGDTGL 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 158 VDGLQDLGAAGLTSASVECASNGGTGIKLFMDKIPLRDDGMEPYEIMLSETQERMLLSVKRDNLNRVSQVFDKWDVENTV 237
Cdd:COG0046   271 IVGIQDMGAGGLSSASSEMAAKGGLGAEIDLDKVPLREPGMSPYEIWLSESQERMLLVVKPEKLEEFEAIFERWRLPAAV 350
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 238 IGQVVDGDAIELIEEGVTKGHIPINLLTD-PPLYRPDGVKPDYLKDLQsyeldrVPLPtASPSAVFLDLIASPNISSRVS 316
Cdd:COG0046   351 IGEVTDDGRLVVTDHGETVADLPLDFLAGgAPKYHRPAKRPAYLEPLD------LPEP-IDLEEALLRLLSSPNVASKEW 423
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 317 VYRQYDHQVQTNTVI-PPGNEAALLRIKGTSKGLSAATDGNSRACYLDPFVGGVISVAEACRNVSCTGAEPIALTNCLNF 395
Cdd:COG0046   424 LYRQYDREVGGNTVRdPGVADAAVVRVDGTYKGLAMSTGENPRYALLDPYAGARMAVAEAARNLAAVGAEPLAITDCLNW 503
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 396 GNPENPEVYYQLEHCVRGIVSASESFDAPVISGNVSLYNET--GNKSIYPTPVIGAVGLTENVSRHCDIAFKEVGDIVVL 473
Cdd:COG0046   504 GNPEKPEEMAQLVEAVKGLADACRALGIPVPSGNVSLYNETkdGKVAIPPTPVIGAVGLVDDVRKTVTPDLKKEGDLLYL 583
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 474 LGASmvagyTSSLSGSEYLEVIhNLVAGQ-PSIDIDKELSVQAACRRLISEGLAKSAHDCSDGGLAVAIVESSIQGNLGF 552
Cdd:COG0046   584 IGET-----KNELGGSEYAQVL-GQLGGEpPDVDLEAEKALFEAVQELIREGLILAAHDVSDGGLAVALAEMAFAGGLGA 657
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 553 GGTV--VIEGRWDAALFGEDQSRIVVSINHKDLDLCSSVCEEYSVEWCVLGNV-QEGRFSFSG----LIDLPMSQLSEIW 625
Cdd:COG0046   658 DIDLdaLGDLRPDAALFSESQGRAVVQVAPEDAEAVEALLAEAGLPAHVIGTVtGDDRLVIRRggetLLSLSLAELRDAW 737

                  ....*..
gi 1301392553 626 TQSLERV 632
Cdd:COG0046   738 EETLPRL 744
FGAM_synth_II TIGR01736
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ...
1-632 0e+00

phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a single, long polypeptide in most Proteobacteria and eukarotes. Three proteins are required in Bacillus subtilis and many other species. This is the longest of the three and is designated PurL, phosphoribosylformylglycinamidine synthase II, or FGAM synthase II. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273781 [Multi-domain]  Cd Length: 715  Bit Score: 757.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553   1 GAATGVGGIVRDILAMGARPIALLNSLRFGPLDHERNRYLFEGVVSGISGYGNCIGIPNIGGEVGFATSYTGNPLVNAMC 80
Cdd:TIGR01736  89 GAATGVGGILRDILSMGARPIALLDSLRFGPLDDPKNRYLFEGVVAGISDYGNRIGVPTVGGEVEFDESYNGNPLVNVMC 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  81 IGLVEIKNLVRATSGDKGNVLLLVGSGTGRDGIHGASgLASRTFEED--RELRPTVQVGNPFLEKILIESCLEAVQTGLV 158
Cdd:TIGR01736 169 VGLVRKDDIVTGKAKGPGNKLVLVGGKTGRDGIGGAT-FASEELSEEaeEEDRPAVQVGDPFTEKLLIEATLEAVDTGLV 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 159 DGLQDLGAAGLTSASVECASNGGTGIKLFMDKIPLRDDGMEPYEIMLSETQERMLLSVKRDNLNRVSQVFDKWDVENTVI 238
Cdd:TIGR01736 248 KGIKDLGAAGLTSASSEMAAKGGLGAEIYLDKVPLREPGMTPYEIMLSESQERMLLVVAPEDVEEVLEIFEKYELPASVI 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 239 GQVVDGDAIELIEEGVTKGHIPINLLTDPPLYRPDGVKPDYlkdlqsYELDRVPLPTASPSAVFLDLIASPNISSRVSVY 318
Cdd:TIGR01736 328 GEVTDEGRIRLYYKGEVVADLPIELLADAPEYERPSEPPKY------PEEEKEPEPPADLEDAFLKVLSSPNIASKEWVY 401
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 319 RQYDHQVQTNTVIPPGNEAALLRIKGTSK-GLSAATDGNSRACYLDPFVGGVISVAEACRNVSCTGAEPIALTNCLNFGN 397
Cdd:TIGR01736 402 RQYDHEVQTRTVVKPGEDAAVLRIKETGKlGLALTADCNPRYVYLDPYAGAAGAVAEAYRNLAAVGAEPLAAVDCLNFGN 481
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 398 PENPEVYYQLEHCVRGIVSASESFDAPVISGNVSLYNETGNKSIYPTPVIGAVGLTENVSRHCDIAFKEVGDIVVLLGAS 477
Cdd:TIGR01736 482 PERPEVYWQFVEAVKGLGDACRALGTPVVGGNVSLYNETNGVPIAPTPTIGMVGLVEDVEKLLTSNFKKEGDAIYLIGET 561
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 478 mvagyTSSLSGSEYLEVIHNLVAGQ-PSIDIDKELSVQAACRRLISEGLAKSAHDCSDGGLAVAIVESSIQGNLGFggTV 556
Cdd:TIGR01736 562 -----KDELGGSEYLRVIHGIVSGQvPAVDLEEEKELADAVREAIRAGLVSAAHDVSRGGLAVALAEMAAASGIGA--EV 634
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 557 VIEG----RWDAALFGEDQSRIVVSINHKDldlCSSVCEEYSVEWCVLGNVQEGRFSFSGL---IDLPMSQLSEIWTQSL 629
Cdd:TIGR01736 635 DIDEiasaRPDELLFSESNGRAIVAVPEEK---AEEAVKSKGVPAKVIGKTGGDRLTIKTGddtISVSVKELRDAWEEAL 711

                  ...
gi 1301392553 630 ERV 632
Cdd:TIGR01736 712 PEY 714
PurL_repeat1 cd02203
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ...
1-263 9.57e-123

PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, phosphate, and glutamate in the fourth step of the purine biosynthetic pathway. In eukaryotes and Gram-negative bacteria, FGAR-AT is encoded by the purL gene as a multidomain protein with a molecular mass of about 140 kDa. In Gram-positive bacteria and archaea FGAR-AT is a complex of three proteins: PurS, PurL, and PurQ. PurL itself contains two tandem N- and C-terminal domains (four domains altogether). The N-terminal domains bind ATP and are related to the ATP-binding domains of HypE, ThiL, SelD and PurM.


Pssm-ID: 100034 [Multi-domain]  Cd Length: 313  Bit Score: 366.03  E-value: 9.57e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553   1 GAATGVGGIVRDILAMGARPIALLNSLRFGPLDHE--------RNRYLFEGVVSGISGYGNCIGIPNIGGEVGFATSYTG 72
Cdd:cd02203    46 GAATGVGGIIRDILSMGARPIALLDGLRFGDLDIPgyepkgklSPRRILDGVVAGISDYGNCIGIPTVGGEVRFDPSYYG 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  73 NPLVNAMCIGLVEIKNLVRATSGDKGNVLLLVGSGTGRDGIHGASGlASRTFEEDREL--RPTVQVGNPFLEKILIESCL 150
Cdd:cd02203   126 NPLVNVGCVGIVPKDHIVKSKAPGPGDLVVLVGGRTGRDGIGGATF-SSKELSENSSEldRPAVQVGDPFMEKKLQEAIL 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 151 EAVQTGLVDGLQDLGAAGLTSASVECASNGGTGIKLFMDKIPLRDDGMEPYEIMLSETQERMLLSVKRDNLNRVSQVFDK 230
Cdd:cd02203   205 EARETGLIVGIQDLGAGGLSSAVSEMAAKGGLGAEIDLDKVPLREPGMSPWEIWISESQERMLLVVPPEDLEEFLAICKK 284
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1301392553 231 WDVENTVIGQVVDGDAIELIEegvtKGHIPINL 263
Cdd:cd02203   285 EDLEAAVIGEVTDDGRLRLYY----KGEVVADL 313
PRK14090 PRK14090
phosphoribosylformylglycinamidine synthase subunit PurL;
1-451 2.49e-103

phosphoribosylformylglycinamidine synthase subunit PurL;


Pssm-ID: 184499 [Multi-domain]  Cd Length: 601  Bit Score: 326.04  E-value: 2.49e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553   1 GAATGVGGIVRDILAMGARPIALLNSLRFgpldhernRYLFEGVVSGISGYGNCIGIPNIGGEVGFATSYTGNPLVNAMC 80
Cdd:PRK14090   81 GAATGVGGIIRDVLAMGARPTAIFDSLHM--------SRIIDGIIEGIADYGNSIGVPTVGGELRISSLYAHNPLVNVLA 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  81 IGLVEIKNLVRATSGDKGNVLLLVGSGTGRDGIHGASgLASRTFEEDRELRPTVQVGNPFLEKILIESCLEAVQTGLVDG 160
Cdd:PRK14090  153 AGVVRNDMLVDSKASRPGQVIVIFGGATGRDGIHGAS-FASEDLTGEKATKLSIQVGDPFAEKMLIEAFLEMVEEGLVEG 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 161 LQDLGAAGLTSASVECASNGGTGIKLFMDKIPLRDDGMEPYEIMLSETQERMLLSVKRDNLNRVSQVFDKWDVENTVIGQ 240
Cdd:PRK14090  232 AQDLGAGGVLSATSELVAKGGLGAIVHLDRVPLREPDMEPWEILISESQERMAVVTSPEKASRILEIAKKHLLFGDIVAE 311
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 241 VVDGDAIELIEEGVTKGHIPINLLTDPPlyrpdgvkpdyLKDLQSYELDRVPlptaspsaVFLDLIASPNISSRvsVYRQ 320
Cdd:PRK14090  312 VIDDPIYRVMYRDDLVMEVPVQLLANAP-----------EEEIVEYTPGEIP--------EFKRVEFEEVNARE--VFEQ 370
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 321 YDHQVQTNTVIPPGNEAALLRIKGTSkGLSAATDGNSRACYLDPFVGGVISVAEACRNVSCTGAEPIALTNCLNFGNPEN 400
Cdd:PRK14090  371 YDHMVGTDTVLPPGFGAAVMRIKRDG-GYSLVTHSRADLALQDTYWGTFIAVLESVRKTLSVGAEPLAITNCVNYGDPDV 449
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1301392553 401 PEVyyQLEHCVRGIVSASESFDAPVISGNVSLYNETGNKSIYPTPVIGAVG 451
Cdd:PRK14090  450 DPV--GLSAMMTALKDACEFSGVPVASGNASLYNTYQGKPIPPTLVVGMLG 498
PurL_repeat2 cd02204
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ...
336-603 7.75e-92

PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, phosphate, and glutamate in the fourth step of the purine biosynthetic pathway. In eukaryotes and Gram-negative bacteria, FGAR-AT is encoded by the purL gene as a multidomain protein with a molecular mass of about 140 kDa. In Gram-positive bacteria and archaea FGAR-AT is a complex of three proteins: PurS, PurL, and PurQ. PurL itself contains two tandem N- and C-terminal domains (four domains altogether). The N-terminal domains bind ATP and are related to the ATP-binding domains of HypE, ThiL, SelD and PurM.


Pssm-ID: 100035 [Multi-domain]  Cd Length: 264  Bit Score: 284.81  E-value: 7.75e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 336 EAALLRIKGTS-KGLSAATDGNSRACYLDPFVGGVISVAEACRNVSCTGAEPIALTNCLNFGNPENPE-VYYQLEHCVRG 413
Cdd:cd02204     1 DAAVLRIPGETdKGLAMSTGENPRYSLLDPYAGAALAVAEAVRNLVAVGADPLAITDCLNFGNPEKPEgEMGQLVEAVLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 414 IVSASESFDAPVISGNVSLYNETGNKSIYPTPVIGAVGLTENVSRHCDIAFKEVGDIVVLLGASmvagyTSSLSGSEYLE 493
Cdd:cd02204    81 LGDACRALGTPVIGGKDSLYNETEGVAIPPTLVIGAVGVVDDVRKIVTLDFKKEGDLLYLIGET-----KDELGGSEYAL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 494 VIHNLVAGQ-PSIDIDKELSVQAACRRLISEGLAKSAHDCSDGGLAVAIVESSIQGNLGFGGTVVIEGRWDAALFGEDQS 572
Cdd:cd02204   156 AYHGLGGGApPLVDLEREKALFDAVQELIKEGLVLSAHDVSDGGLAVALAEMAFAGGLGAEVDLSKDDAEDELLFSESLG 235
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1301392553 573 RIVVSINHKDLDLCSsvCEEYSVEWCVLGNV 603
Cdd:cd02204   236 RVLVEVKPENEEVFE--AEEAGVPATVIGTV 264
PurL cd02193
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ...
1-241 2.55e-44

Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, phosphate, and glutamate in the fourth step of the purine biosynthetic pathway. In eukaryotes and Gram-negative bacteria, FGAR-AT is encoded by the purL gene as a multidomain protein with a molecular mass of about 140 kDa. In Gram-positive bacteria and archaea FGAR-AT is a complex of three proteins: PurS, PurL, and PurQ. PurL itself contains two tandem N- and C-terminal domains (four domains altogether). The N-terminal domains bind ATP and are related to the ATP-binding domains of HypE, ThiL, SelD and PurM.


Pssm-ID: 100029 [Multi-domain]  Cd Length: 272  Bit Score: 159.38  E-value: 2.55e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553   1 GAATGVGGIVRDILAMG--ARPIALLNSLRFGPLDHERNRYLFEGVvSGISGYGNCIGIPNIGGEVGFATSY-------- 70
Cdd:cd02193    21 GAATGVGGAIRDIAATGidAKPIALSANWMASAGHPGEDAILYDAV-KGVAELCNQLGLPIPVGKDRMSMKTrwqegneq 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  71 ---TGNPLVNAMCIGLVEIKNLVRATSGDKGNVLLLVGSGTGRDGIHGASgLASRTFEEDRELRPTVQVGNPFLEKILIE 147
Cdd:cd02193   100 remTHPPSLVISAFGRVRDDRHTLPQLSTEGNALLLIGGGKGHNGLGGTA-LASVALSYRQLGDKSAQVRDPAQEKGFYE 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 148 SCLEAVQTGLVDGLQDLGAAGLTSASVECASNGGTGIKLFMDKIPLRDDGMEPYEIMLSETQERMLLSVKRDNLNRVSQV 227
Cdd:cd02193   179 AMQALVAAGKLLAWHDRGAGGLLVALAELVFAGHCGVQVDLAALGDDEPDMEPLEIALFESQERGVIQVRAEDRDAVEEA 258
                         250
                  ....*....|....
gi 1301392553 228 FDKWDVENTVIGQV 241
Cdd:cd02193   259 QYGLADCVHVLGQA 272
AIRS_C pfam02769
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ...
98-250 2.26e-32

AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site.


Pssm-ID: 460684 [Multi-domain]  Cd Length: 152  Bit Score: 122.07  E-value: 2.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  98 GNVLLLVGSgtgrDGIHGASGLASRTFEEDrELRPTVQVGNPFLEKILIES-CLEAVQTGLVDGLQDLGAAGLTSASVEC 176
Cdd:pfam02769   3 GDVLILLGS----SGLHGAGLSLSRKGLED-SGLAAVQLGDPLLEPTLIYVkLLLAALGGLVKAMHDITGGGLAGALAEM 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1301392553 177 ASNGGTGIKLFMDKIPLRDDGMEPYEIMLSETQERMLLSVKRDNLNRVSQVFDKWDVENTVIGQVVDGDAIELI 250
Cdd:pfam02769  78 APASGVGAEIDLDKVPIFEELMLPLEMLLSENQGRGLVVVAPEEAEAVLAILEKEGLEAAVIGEVTAGGRLTVI 151
AIRS pfam00586
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ...
348-452 6.56e-24

AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.


Pssm-ID: 459859 [Multi-domain]  Cd Length: 104  Bit Score: 96.36  E-value: 6.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 348 GLSAATDGNSRACYLDPFVG-GVISVAEACRNVSCTGAEPIALTNCLNFgnPENPEVYYQLEHCVRGIVSASESFDAPVI 426
Cdd:pfam00586   4 AVAVTTDGHGTPSLVDPYHFpGAKAVAGNLSDIAAMGARPLAFLDSLAL--PGGPEVEWVLEEIVEGIAEACREAGVPLV 81
                          90       100
                  ....*....|....*....|....*.
gi 1301392553 427 SGNVSLYNETGNksiyPTPVIGAVGL 452
Cdd:pfam00586  82 GGDTSFDPEGGK----PTISVTAVGI 103
AIRS pfam00586
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ...
2-84 4.39e-22

AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.


Pssm-ID: 459859 [Multi-domain]  Cd Length: 104  Bit Score: 91.35  E-value: 4.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553   2 AATGVGGIVRDILAMGARPIALLNSLRFGPLDHErnRYLFEGVVSGISGYGNCIGIPNIGGEVGFATSYtGNPLVNAMCI 81
Cdd:pfam00586  25 GAKAVAGNLSDIAAMGARPLAFLDSLALPGGPEV--EWVLEEIVEGIAEACREAGVPLVGGDTSFDPEG-GKPTISVTAV 101

                  ...
gi 1301392553  82 GLV 84
Cdd:pfam00586 102 GIV 104
PurM-like cd00396
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ...
1-240 1.32e-19

AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM (formylglycinamidine ribonucleotide) synthase and Selenophosphate synthetase (SelD). The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.


Pssm-ID: 100027 [Multi-domain]  Cd Length: 222  Bit Score: 87.84  E-value: 1.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553   1 GAATGVGGIVRDILAMGARPIALLNSLRFGPLDHERnryLFEGVVSGISGYGNCIGIPNIGGEVGFATSYTG-NPLVNAM 79
Cdd:cd00396    20 GGRLAVGGAVNDIAAMGARPIALLASLSLSNGLEVD---ILEDVVDGVAEACNQLGVPIVGGHTSVSPGTMGhKLSLAVF 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  80 CIGLVEIknlVRATSGDK---GNVLLLVGsgtgrdgihgasglasrtfeedrelrptvqvgnpflekilIESCLEAVQTG 156
Cdd:cd00396    97 AIGVVEK---DRVIDSSGarpGDVLILTG----------------------------------------VDAVLELVAAG 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 157 LVDGLQDLGAAGLTSASVECASNGGTGIKLFMDKIPLRDDGME-----PYEIMLSETQERMLLSVKRDNLNRVSQVFDKW 231
Cdd:cd00396   134 DVHAMHDITDGGLLGTLPELAQASGVGAEIDLEAIPLDEVVRWlcvehIEEALLFNSSGGLLIAVPAEEADAVLLLLNGN 213

                  ....*....
gi 1301392553 232 DVENTVIGQ 240
Cdd:cd00396   214 GIDAAVIGR 222
FGAM_synth_II TIGR01736
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ...
328-623 9.53e-17

phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a single, long polypeptide in most Proteobacteria and eukarotes. Three proteins are required in Bacillus subtilis and many other species. This is the longest of the three and is designated PurL, phosphoribosylformylglycinamidine synthase II, or FGAM synthase II. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273781 [Multi-domain]  Cd Length: 715  Bit Score: 84.28  E-value: 9.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 328 NTVIPPGNEAALLRIKGtskGLSAATDGNSR--ACYLDPF------VGGVIsvaeacRNVSCTGAEPIALTNCLNFGNPE 399
Cdd:TIGR01736  51 NVIQGPGEDAGVVDIGD---GYAVVFKMESHnhPSAIEPYngaatgVGGIL------RDILSMGARPIALLDSLRFGPLD 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 400 NPEVYYQLEHCVRGIVSASESFDAPVISGNVS---LYNEtgnksiYPTPVIGAVGLTenvsRHCDIAF---KEVGDIVVL 473
Cdd:TIGR01736 122 DPKNRYLFEGVVAGISDYGNRIGVPTVGGEVEfdeSYNG------NPLVNVMCVGLV----RKDDIVTgkaKGPGNKLVL 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 474 LGASM----VAGYT-SSLSGSEYLEV-------IHNLVAGQPSIDidkelsvqaACRRLISEGLAKSAHDCSDGGLAVAI 541
Cdd:TIGR01736 192 VGGKTgrdgIGGATfASEELSEEAEEedrpavqVGDPFTEKLLIE---------ATLEAVDTGLVKGIKDLGAAGLTSAS 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 542 VESSIQGnlGFGGTVVIE---------GRWDAALfGEDQSRIVVSINHKDLDLCSSVCEEYSVEWCVLGNV-QEGRF--S 609
Cdd:TIGR01736 263 SEMAAKG--GLGAEIYLDkvplrepgmTPYEIML-SESQERMLLVVAPEDVEEVLEIFEKYELPASVIGEVtDEGRIrlY 339
                         330
                  ....*....|....*.
gi 1301392553 610 FSG--LIDLPMSQLSE 623
Cdd:TIGR01736 340 YKGevVADLPIELLAD 355
PurL_repeat2 cd02204
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ...
1-241 1.04e-16

PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, phosphate, and glutamate in the fourth step of the purine biosynthetic pathway. In eukaryotes and Gram-negative bacteria, FGAR-AT is encoded by the purL gene as a multidomain protein with a molecular mass of about 140 kDa. In Gram-positive bacteria and archaea FGAR-AT is a complex of three proteins: PurS, PurL, and PurQ. PurL itself contains two tandem N- and C-terminal domains (four domains altogether). The N-terminal domains bind ATP and are related to the ATP-binding domains of HypE, ThiL, SelD and PurM.


Pssm-ID: 100035 [Multi-domain]  Cd Length: 264  Bit Score: 80.27  E-value: 1.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553   1 GAATGVGGIVRDILAMGARPIALLNSLRFG-PLDHERNRYLFEGVVSGISGYGNCIGIPNIGGEVGF--ATSYTGNP--L 75
Cdd:cd02204    33 GAALAVAEAVRNLVAVGADPLAITDCLNFGnPEKPEGEMGQLVEAVLGLGDACRALGTPVIGGKDSLynETEGVAIPptL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  76 VNAMcIGLVE-IKNLVRATSGDKGNVLLLVGSGTGRDGihgASGLASRTFEEDRELRPTVqvgNPFLEKILIESCLEAVQ 154
Cdd:cd02204   113 VIGA-VGVVDdVRKIVTLDFKKEGDLLYLIGETKDELG---GSEYALAYHGLGGGAPPLV---DLEREKALFDAVQELIK 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 155 TGLVDGLQDLGAAGLTSASVECASNGGTGIKLFMDKIPLRDdgmepyEIMLSETQERMLLSVKRDNLNRVSQVFdkWDVE 234
Cdd:cd02204   186 EGLVLSAHDVSDGGLAVALAEMAFAGGLGAEVDLSKDDAED------ELLFSESLGRVLVEVKPENEEVFEAEE--AGVP 257

                  ....*..
gi 1301392553 235 NTVIGQV 241
Cdd:cd02204   258 ATVIGTV 264
PurL_repeat1 cd02203
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ...
360-608 3.32e-15

PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, phosphate, and glutamate in the fourth step of the purine biosynthetic pathway. In eukaryotes and Gram-negative bacteria, FGAR-AT is encoded by the purL gene as a multidomain protein with a molecular mass of about 140 kDa. In Gram-positive bacteria and archaea FGAR-AT is a complex of three proteins: PurS, PurL, and PurQ. PurL itself contains two tandem N- and C-terminal domains (four domains altogether). The N-terminal domains bind ATP and are related to the ATP-binding domains of HypE, ThiL, SelD and PurM.


Pssm-ID: 100034 [Multi-domain]  Cd Length: 313  Bit Score: 76.74  E-value: 3.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 360 CYLDPF------VGGVIsvaeacRNVSCTGAEPIALTNCLNFGNPENPEVY--------YQLEHCVRGIVSASESFDAPV 425
Cdd:cd02203    39 SAIEPFggaatgVGGII------RDILSMGARPIALLDGLRFGDLDIPGYEpkgklsprRILDGVVAGISDYGNCIGIPT 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 426 ISGNVSLYnetGNKSIYPTPVIGAVGL--TENVSRHCDIafkEVGDIVVLLG-------------ASMVAGYTSSLSGSe 490
Cdd:cd02203   113 VGGEVRFD---PSYYGNPLVNVGCVGIvpKDHIVKSKAP---GPGDLVVLVGgrtgrdgiggatfSSKELSENSSELDR- 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 491 ylevihnlvagqPSIDI-DKELS--VQAACRRLISEGLAKSAHDCSDGGLAVAIVESSIQGNLGfggtVVIEgrWDAALF 567
Cdd:cd02203   186 ------------PAVQVgDPFMEkkLQEAILEARETGLIVGIQDLGAGGLSSAVSEMAAKGGLG----AEID--LDKVPL 247
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1301392553 568 GED------------QSRIVVSINHKDLDLCSSVCEEYSVEWCVLGNV-QEGRF 608
Cdd:cd02203   248 REPgmspweiwisesQERMLLVVPPEDLEEFLAICKKEDLEAAVIGEVtDDGRL 301
AIRS_C pfam02769
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ...
466-607 2.81e-12

AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site.


Pssm-ID: 460684 [Multi-domain]  Cd Length: 152  Bit Score: 64.67  E-value: 2.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 466 EVGDIVVLLGasmvagyTSSLSGSEYLEVIHNL----VAGQPSIDIDKELSVQAACRRLI-SEGLAKSAHDCSDGGLAVA 540
Cdd:pfam02769   1 KPGDVLILLG-------SSGLHGAGLSLSRKGLedsgLAAVQLGDPLLEPTLIYVKLLLAaLGGLVKAMHDITGGGLAGA 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1301392553 541 IVESSIQGNLGF-----GGTVVIEGRWD-AALFGEDQSRIVVSINHKDLDLCSSVCEEYSVEWCVLGNVQEGR 607
Cdd:pfam02769  74 LAEMAPASGVGAeidldKVPIFEELMLPlEMLLSENQGRGLVVVAPEEAEAVLAILEKEGLEAAVIGEVTAGG 146
PurM-like cd00396
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ...
352-551 5.23e-12

AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM (formylglycinamidine ribonucleotide) synthase and Selenophosphate synthetase (SelD). The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.


Pssm-ID: 100027 [Multi-domain]  Cd Length: 222  Bit Score: 65.88  E-value: 5.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 352 ATDGNSRACYLDPFVGGVISVAEACRNVSCTGAEPIALTNCLNFGNPENPEVyyqLEHCVRGIVSASESFDAPVISGNVS 431
Cdd:cd00396     5 STDGINPPLAINPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNGLEVDI---LEDVVDGVAEACNQLGVPIVGGHTS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 432 LYNETGnkSIYPTPVIGAVGLTENVsRHCDIAFKEVGDIVVLLGasmvagytsslsgseYLEVIHnlvagqpsididkel 511
Cdd:cd00396    82 VSPGTM--GHKLSLAVFAIGVVEKD-RVIDSSGARPGDVLILTG---------------VDAVLE--------------- 128
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1301392553 512 svqaacrrLISEGLAKSAHDCSDGGLAVAIVESSIQGNLG 551
Cdd:cd00396   129 --------LVAAGDVHAMHDITDGGLLGTLPELAQASGVG 160
PurL cd02193
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ...
362-603 1.89e-11

Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, phosphate, and glutamate in the fourth step of the purine biosynthetic pathway. In eukaryotes and Gram-negative bacteria, FGAR-AT is encoded by the purL gene as a multidomain protein with a molecular mass of about 140 kDa. In Gram-positive bacteria and archaea FGAR-AT is a complex of three proteins: PurS, PurL, and PurQ. PurL itself contains two tandem N- and C-terminal domains (four domains altogether). The N-terminal domains bind ATP and are related to the ATP-binding domains of HypE, ThiL, SelD and PurM.


Pssm-ID: 100029 [Multi-domain]  Cd Length: 272  Bit Score: 65.01  E-value: 1.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 362 LDPFVGGVISVAEACRNVSCTG--AEPIALTNCLNFGNPeNPEVYYQLEHCVRGIVSASESFDAPVISGNVSLYNETGNK 439
Cdd:cd02193    16 IDPAAGAATGVGGAIRDIAATGidAKPIALSANWMASAG-HPGEDAILYDAVKGVAELCNQLGLPIPVGKDRMSMKTRWQ 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 440 SIY--------PTPVIGAVGLTENVsRHCDIAFKEVGDIVVLLGASmvAGYTSSLSGSEYLEVIHNLVAGQPSIDID--- 508
Cdd:cd02193    95 EGNeqremthpPSLVISAFGRVRDD-RHTLPQLSTEGNALLLIGGG--KGHNGLGGTALASVALSYRQLGDKSAQVRdpa 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 509 KELSVQAACRRLISEGLAKSAHDCSDGGLAVAIVESSIQGNLgfGGTVVIE---------GRWDAALFgEDQSRIVVSIN 579
Cdd:cd02193   172 QEKGFYEAMQALVAAGKLLAWHDRGAGGLLVALAELVFAGHC--GVQVDLAalgddepdmEPLEIALF-ESQERGVIQVR 248
                         250       260
                  ....*....|....*....|....
gi 1301392553 580 HKDLDLCSSVCEEYSVEWCVLGNV 603
Cdd:cd02193   249 AEDRDAVEEAQYGLADCVHVLGQA 272
PRK05297 PRK05297
phosphoribosylformylglycinamidine synthase; Provisional
1-224 4.16e-11

phosphoribosylformylglycinamidine synthase; Provisional


Pssm-ID: 235394 [Multi-domain]  Cd Length: 1290  Bit Score: 66.36  E-value: 4.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553    1 GAATGVGGIVRDILA--MGARPIALL------NsLR-----------FG-------PLDhernrYLFEGVVSGiSGYGNC 54
Cdd:PRK05297   303 GAATGSGGEIRDEGAtgRGSKPKAGLtgfsvsN-LRipgfeqpweedYGkperiasALD-----IMIEGPLGG-AAFNNE 375
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553   55 IGIPNIGG--------EVGFATSYTG--NPLVNAMCIG-----LVEIKNLvraTSGDKGNVL----LLVGSGTGrdgihG 115
Cdd:PRK05297   376 FGRPNLLGyfrtfeqkVNSHNEEVRGyhKPIMLAGGIGniradHVQKGEI---PVGAKLIVLggpaMRIGLGGG-----A 447
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  116 ASGLASRTFEEDRELrPTVQVGNPFLEKI---LIESCleaVQTGlvDG-----LQDLGAAGLTSASVECASNGGTGIKLF 187
Cdd:PRK05297   448 ASSMASGQSSEDLDF-ASVQRGNPEMERRcqeVIDRC---WQLG--DDnpilsIHDVGAGGLSNAFPELVNDGGRGGRFD 521
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1301392553  188 MDKIPLRDDGMEPYEIMLSETQERMLLSVKRDNLNRV 224
Cdd:PRK05297   522 LRKIPNDEPGMSPLEIWCNESQERYVLAIAPEDLELF 558
PurM-like1 cd06061
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ...
12-241 2.41e-09

AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM related proteins includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM synthase and Selenophosphate synthetase (SelD). They all contain two conserved domains and seem to dimerize. The N-terminal domain forms the dimer interface and is a putative ATP binding domain.


Pssm-ID: 100037 [Multi-domain]  Cd Length: 298  Bit Score: 58.76  E-value: 2.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  12 DILAMGARPIALLNSLRFgPLDHERNRylFEGVVSGISGYGNCIGIPNIGGEVGFATSyTGNPLVNAMCIGLVEIKNLVR 91
Cdd:cd06061    70 DIATSGARPRWLLVTLLL-PPGTDEEE--LKAIMREINEAAKELGVSIVGGHTEVTPG-VTRPIISVTAIGKGEKDKLVT 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  92 ATSGDKGNVLLLVGSGtgrdGIhGASGLASRTFEE-------DRELRPTVQvgnpFLEKI-LIESCLEAVQTGlVDGLQD 163
Cdd:cd06061   146 PSGAKPGDDIVMTKGA----GI-EGTAILANDFEEelkkrlsEEELREAAK----LFYKIsVVKEALIAAEAG-VTAMHD 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 164 LGAAGLTSASVECASNGGTGIKLFMDKIPLRDD--------GMEPYEIMLSETqerMLLSVKRDNLNRVSQVFDKWDVEN 235
Cdd:cd06061   216 ATEGGILGALWEVAEASGVGLRIEKDKIPIRQEtkeicealGIDPLRLISSGT---LLITVPPEKGDELVDALEEAGIPA 292

                  ....*.
gi 1301392553 236 TVIGQV 241
Cdd:cd06061   293 SVIGKI 298
ThiL COG0611
Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
12-250 2.05e-07

Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate kinase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440376 [Multi-domain]  Cd Length: 321  Bit Score: 53.23  E-value: 2.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  12 DILAMGARPIALLNSLRFGP-LDHERnrylFEGVVSGISGYGNCIGIPNIGGEvgfaTSyTGNPLV-NAMCIGLVEIKNL 89
Cdd:COG0611    73 DLAAMGARPLAALLSLALPPdTDVEW----LEEFARGLAEAADRYGVDLVGGD----TT-RSPELTiSVTAIGEVPGGRP 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  90 VR---ATSGDkgnvLLLVgSGTgrdgiHGASGLA-------SRTFEEDRE------LRPTVQVGnpflekiLIescLEAV 153
Cdd:COG0611   144 LLrsgARPGD----LVYV-TGT-----LGDAAAGlalllrgLRVPLEAREyllerhLRPEPRLA-------LG---RALA 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 154 QTGLV-------DGL-QDLGAagLTSASvecasngGTGIKLFMDKIPLRDD------GMEPYEIMLS-----EtqerMLL 214
Cdd:COG0611   204 EAGLAtamidisDGLaADLGH--IAEAS-------GVGAEIDLDALPLSPAlreaalGLDPLELALTggedyE----LLF 270
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1301392553 215 SVKRDNLNRVSQVFDKWDVenTVIGQVVDGDAIELI 250
Cdd:COG0611   271 TVPPEALEALEAAALGVPL--TVIGRVTEGEGVTLD 304
PLN03206 PLN03206
phosphoribosylformylglycinamidine synthase; Provisional
95-255 2.42e-06

phosphoribosylformylglycinamidine synthase; Provisional


Pssm-ID: 178745 [Multi-domain]  Cd Length: 1307  Bit Score: 50.92  E-value: 2.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553   95 GDKGnVLLLVGSGTGRDGIhGASGLAsRTFEedrelrptvQVGN--PFLEKIL-IESCLEAVQTGLVDGL----QDLGAA 167
Cdd:PLN03206   824 GDDG-VLLHVDLGKGKRRL-GGSALA-QAYD---------QIGDdcPDLDDVAyLKKAFEATQDLIAKRLisagHDISDG 891
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  168 GLTSASVECASNGGTGIKLfmdKIPLRDDGmePYEIMLSEtQERMLLSVKRDNLNRVSQVFDKWDVENTVIGQVVDGDAI 247
Cdd:PLN03206   892 GLVVTLLEMAFAGNCGINV---DLPSSGHS--AFETLFAE-ELGLVLEVSRKNLDAVMEKLAAAGVTAEVIGQVTASPLI 965

                   ....*...
gi 1301392553  248 ELIEEGVT 255
Cdd:PLN03206   966 EVKVDGAT 973
PHA03366 PHA03366
FGAM-synthase; Provisional
362-634 4.68e-06

FGAM-synthase; Provisional


Pssm-ID: 223058 [Multi-domain]  Cd Length: 1304  Bit Score: 50.02  E-value: 4.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  362 LDPFVGGVISVAEACRNvsctgaepIALTNCLNFGN---------PENPEVYYQLEHCVRG-------------IVSASE 419
Cdd:PHA03366   704 LDPILGAKYAIVEALTN--------LMLAPVANLEDititlsvtwPPTDQAASELYRALAAckefcrelgvnftFTSASS 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  420 SFDAPVISGNVSLYNE---TGN---KSIYP--TPVigavgltenvsrhcdiaFKEVGDIVVLLgaSMVAGYTssLSGSEY 491
Cdd:PHA03366   776 SPRQDQPPQPGPLFNTivfTASapvPSSTPrlTPD-----------------LKKPGSALVHL--SISPEYT--LAGSVF 834
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  492 lEVIHNLVAGQPsIDID----KEL--SVQAacrrLISEGLAKSAHDCSDGGLAVAIVESSIQGnlGFGGTVVIEGRWDAA 565
Cdd:PHA03366   835 -EQIFGLKSGTL-PDISpsylKNLfrAVQH----LISEGLVVSGHDVSDGGLIACLAEMALAG--GRGVTITVPAGEDPL 906
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1301392553  566 --LFGEDQSrIVVSINHKDLDLCSSVCEEYSVEWCVLGNV----QEGRFSFSglidlpmSQLSEIWTQSLERVAG 634
Cdd:PHA03366   907 qfLFSETPG-VVIEVPPSHLSAVLTRLRSRNIICYPIGTVgpsgPSNTFSVS-------HNGTVLFRESLSSLRS 973
PLN03206 PLN03206
phosphoribosylformylglycinamidine synthase; Provisional
520-631 6.56e-06

phosphoribosylformylglycinamidine synthase; Provisional


Pssm-ID: 178745 [Multi-domain]  Cd Length: 1307  Bit Score: 49.38  E-value: 6.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  520 LISEGLAKSAHDCSDGGLAVAIVESSIQGNLGFGGTVVIEGRWD-AALFGEDQSrIVVSINHKDLDLCSSVCEEYSVEWC 598
Cdd:PLN03206   876 LIAKRLISAGHDISDGGLVVTLLEMAFAGNCGINVDLPSSGHSAfETLFAEELG-LVLEVSRKNLDAVMEKLAAAGVTAE 954
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1301392553  599 VLGNVQEGR---FSFSGL--IDLPMSQLSEIWTQS---LER 631
Cdd:PLN03206   955 VIGQVTASPlieVKVDGAtcLSEKTASLRDMWEETsfqLEK 995
PurM-like1 cd06061
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ...
329-552 1.33e-05

AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM related proteins includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM synthase and Selenophosphate synthetase (SelD). They all contain two conserved domains and seem to dimerize. The N-terminal domain forms the dimer interface and is a putative ATP binding domain.


Pssm-ID: 100037 [Multi-domain]  Cd Length: 298  Bit Score: 47.59  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 329 TVIPPGNE--AALLRIKGtsKGLSAATDgnsrACYLDPFVGGVISVAEACRNVSCTGAEPIALTNCLNF--GNPENpevy 404
Cdd:cd06061    25 VLVGPGGGedAAVVDFGG--KVLVVSTD----PITGAGKDAGWLAVHIAANDIATSGARPRWLLVTLLLppGTDEE---- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 405 yQLEHCVRGIVSASESFDAPVISGNVslynETGNKSIYPTPVIGAVGLTENVSRHCDIAFKeVGDIVVLLGASMVAGyTS 484
Cdd:cd06061    95 -ELKAIMREINEAAKELGVSIVGGHT----EVTPGVTRPIISVTAIGKGEKDKLVTPSGAK-PGDDIVMTKGAGIEG-TA 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 485 SLSGSEYLEVIHNLVAG--QPSIDIDKELSVQAAcRRLISEGLAKSAHDCSDGGLAVAIVESSIQGNLGF 552
Cdd:cd06061   168 ILANDFEEELKKRLSEEelREAAKLFYKISVVKE-ALIAAEAGVTAMHDATEGGILGALWEVAEASGVGL 236
ThiL cd02194
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ...
12-242 1.20e-04

ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage of exogenous thiamine. Thiamine salvage occurs in two steps, with thiamine kinase catalyzing the formation of thiamine phosphate, and ThiL catalyzing the conversion of this intermediate to thiamine pyrophosphate. The N-terminal domain of ThiL binds ATP and is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, FGAM synthase and selenophosphate synthetase (SelD).


Pssm-ID: 100030 [Multi-domain]  Cd Length: 291  Bit Score: 44.47  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  12 DILAMGARPIALLNSLRFGPLDHERNrylFEGVVSGISGYGNCIGIPNIGGEvgfaTSyTGNPLV-NAMCIGLVEIKNLV 90
Cdd:cd02194    70 DLAAMGARPLGFLLSLGLPPDTDEEW---LEEFYRGLAEAADRYGVPLVGGD----TT-SGSELViSVTALGEVEKGKPL 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  91 R---ATSGDkgnvlLLVGSGTgrdgiHGASGLASRTFEEDRELRPTvqvGNPFLEKILI--ESCLEAVQ---TGLV---- 158
Cdd:cd02194   142 RrsgAKPGD-----LLYVTGT-----LGDAAAGLALLLGGLKLPEE---LYEELIERHLrpEPRLELGRalaEGLAtami 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 159 ---DGL-QDLGaagltsasvECASNGGTGIKLFMDKIPL------RDDGMEPYEIMLS--ETQErMLLSVKRDNLNRVSQ 226
Cdd:cd02194   209 disDGLlADLG---------HIAEASGVGAVIDLDKLPLspalraAELGEDALELALSggEDYE-LLFTVPPENAEAAAA 278
                         250
                  ....*....|....*.
gi 1301392553 227 VFdkwDVENTVIGQVV 242
Cdd:cd02194   279 KL---GVPVTVIGRVT 291
PurM-like3 cd02192
AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM ...
10-239 2.20e-04

AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM related proteins includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM synthase and Selenophosphate synthetase (SelD). They all contain two conserved domains and seem to dimerize. The N-terminal domain forms the dimer interface and is a putative ATP binding domain.


Pssm-ID: 100028 [Multi-domain]  Cd Length: 283  Bit Score: 43.35  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  10 VRDILAMGARPIALLNSLRFGplDHERNRYLFEGVVSGISGYgnciGIPNIGGEVGFATSYTGnplVNAMCIGLVEiKNL 89
Cdd:cd02192    76 VSDIAAMGGRPLAMVDALWSP--SAEAAAQVLEGMRDAAEKF----GVPIVGGHTHPDSPYNA---LSVAILGRAR-KDL 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  90 VRATSGDKGNVLLLVGSGTGRdgIHGASGLA--SRTFEEDRELRPTvqvgnpflekilIESCLEAVQTGLVDGLQDLGAA 167
Cdd:cd02192   146 LISFGAKPGDRLILAIDLDGR--VHPSPPPNwdATTMKSPALLRRQ------------IALLPELAERGLVHAAKDISNP 211
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1301392553 168 GLTSASVECASNGGTGIKLFMDKIPlRDDGMEPYEIMLSETQERMLLSVKRDNLNRVSQVFDKWDVENTVIG 239
Cdd:cd02192   212 GIIGTLGMLLEASGVGAEIDLDAIP-RPEGVDLERWLKCFPGFGFLLTARPENADEVVAVFAAVGITAAVIG 282
thiL TIGR01379
thiamine-phosphate kinase; This model describes thiamine-monophosphate kinase, an enzyme that ...
12-255 4.00e-04

thiamine-phosphate kinase; This model describes thiamine-monophosphate kinase, an enzyme that converts thiamine monophosphate into thiamine pyrophosphate (TPP, coenzyme B1), an enzyme cofactor. Thiamine monophosphate may be derived from de novo synthesis or from unphosphorylated thiamine, known as vitamin B1. Proteins scoring between the trusted and noise cutoff for this model include short forms from the Thermoplasmas (which lack the N-terminal region) and a highly derived form from Campylobacter jejuni. Eukaryotes lack this enzyme, and add pyrophosphate from ATP to unphosphorylated thiamine in a single step. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 273589 [Multi-domain]  Cd Length: 317  Bit Score: 43.09  E-value: 4.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  12 DILAMGARPIALLNSLRFgPLDHERNRylFEGVVSGISGYGNCIGIPNIGGEvgfaTSYTGNPLVNAMCIGLVEiKNLVR 91
Cdd:TIGR01379  71 DLAAMGATPKWFLLSLGL-PSDLDEAW--LEAFYDGLFEAAKQYGVPLVGGD----TVSSPELVVTVTAIGEAP-KGRAL 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  92 ATSGDKGNVLLLVgsgTGRDGIHGA------SGLASRTFEED-----RELRPTVQVGnpflEKILIescleavqTGLVDG 160
Cdd:TIGR01379 143 LRSGAKPGDLVFV---TGTLGDSAAglalllKGKKEPDEEDDeallqRHLRPEPRVE----EGLAL--------AGYANA 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553 161 LQDLgAAGLTSASVECASNGGTGIKLFMDKIPLRD------DGMEPYEIMLS--ETQErMLLSVKRDNLNRVSQVFDKwd 232
Cdd:TIGR01379 208 AIDV-SDGLAADLGHIAEASGVGIVIDLDRLPLSSelaawaEGKNPLEWALSggEDYE-LVFTVPPERREALLDAAKG-- 283
                         250       260
                  ....*....|....*....|...
gi 1301392553 233 vENTVIGQVVDGDAIELIEEGVT 255
Cdd:TIGR01379 284 -PLTRIGRVTEGEGVVLLADGKT 305
PurM cd02196
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ...
10-161 6.57e-04

PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for purine biosynthesis, catalyzes the conversion of formylglycinamide ribonucleotide (FGAM) and ATP to AIR, ADP, and Pi, the fifth step in de novo purine biosynthesis. The N-terminal domain of PurM is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, selenophosphate synthetase (SelD), and FGAM synthase and is thought to bind ATP.


Pssm-ID: 100032 [Multi-domain]  Cd Length: 297  Bit Score: 42.08  E-value: 6.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  10 VRDILAMGARPIALLNSLRFGPLDHERNRYLFEGVVSGisgygnCI--GIPNIGGE---------------VGFatsytg 72
Cdd:cd02196    54 VNDILCQGAEPLFFLDYIATGKLDPEVAAEIVKGIAEG------CRqaGCALLGGEtaempgvyaegeydlAGF------ 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301392553  73 nplvnamCIGLVEIKNLVratSGDK---GNVLLLVGSgtgrDGIH--GASgLASRTFEE------DRELRPTVQVGNPFL 141
Cdd:cd02196   122 -------AVGVVEKDKII---DGSKikpGDVLIGLPS----SGLHsnGYS-LVRKILFEegldydDPEPGLGKTLGEELL 186
                         170       180
                  ....*....|....*....|..
gi 1301392553 142 E--KILIESCLEAVQTGLVDGL 161
Cdd:cd02196   187 TptRIYVKPILPLLEKVLVKGM 208
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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