|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02327 |
PLN02327 |
CTP synthase |
147-703 |
0e+00 |
|
CTP synthase
Pssm-ID: 215186 [Multi-domain] Cd Length: 557 Bit Score: 935.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 147 MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDI 226
Cdd:PLN02327 1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 227 NLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAVQEWVMNQAMVPVDGHKEEPQICVIELGGTIGDIEGMPFV 306
Cdd:PLN02327 81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAKIPVDGKEGPADVCVIELGGTVGDIESMPFI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 307 EAFRQFQFKAKRENFCNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ 386
Cdd:PLN02327 161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 387 VICIHDVSSTYRVPVLLEEQGIIKYFKERLDLPIGDSASSlLSKWRNMADRYERLQKTCSIALVGKYTKLRDCYASVFKA 466
Cdd:PLN02327 241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLSVAREPD-LEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 467 LEHSALAINHKLNLMYIDSIDLEQTTEVEDPVKFHEAWQKLCKADGVLVPGGFGIRGTLGKLQAISWARSRKIPFLGVCL 546
Cdd:PLN02327 320 LLHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGICL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 547 GMQLAVIEFARNCLNLKDADSTEFEPNARVPVVIDMPEHNPGNLGGTMRLGIRRTVFKTENSILRKLYGDVPFIEERHRH 626
Cdd:PLN02327 400 GMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDERHRH 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387298264 627 RYEVNPSLISQLEQKDLSFVGQDVDGERMEIIELANHPYFVGVQFHPEFSSRPMKPSPPYLGLLLAATGNLNAYLLQ 703
Cdd:PLN02327 480 RYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVLNS 556
|
|
| pyrG |
PRK05380 |
CTP synthetase; Validated |
147-693 |
0e+00 |
|
CTP synthetase; Validated
Pssm-ID: 235437 [Multi-domain] Cd Length: 533 Bit Score: 844.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 147 MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDI 226
Cdd:PRK05380 2 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 227 NLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAVQEWVMNQAmvpvdghkEEPQICVIELGGTIGDIEGMPFV 306
Cdd:PRK05380 82 NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAG--------TDADVVIVEIGGTVGDIESLPFL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 307 EAFRQFQFKAKRENFCNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ 386
Cdd:PRK05380 154 EAIRQLRLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 387 VICIHDVSSTYRVPVLLEEQGIIKYFKERLDLPIGDSAsslLSKWRNMADRYERLQKTCSIALVGKYTKLRDCYASVFKA 466
Cdd:PRK05380 234 VISAPDVDSIYEVPLLLHEQGLDDIVLERLGLEAPEPD---LSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 467 LEHSALAINHKLNLMYIDSIDLEQTTEVEdpvkfheawqKLCKADGVLVPGGFGIRGTLGKLQAISWARSRKIPFLGVCL 546
Cdd:PRK05380 311 LKHAGIANDVKVNIKWIDSEDLEEENVAE----------LLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 547 GMQLAVIEFARNCLNLKDADSTEFEPNARVPVVIDMPE-HNPGNLGGTMRLGIRRTVFKtENSILRKLYGDvPFIEERHR 625
Cdd:PRK05380 381 GMQLAVIEFARNVLGLEDANSTEFDPDTPHPVIDLMPEqKDVSDLGGTMRLGAYPCKLK-PGTLAAEIYGK-EEIYERHR 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387298264 626 HRYEVNPSLISQLEQKDLSFVGQDVDGERMEIIELANHPYFVGVQFHPEFSSRPMKPSPPYLGLLLAA 693
Cdd:PRK05380 459 HRYEVNNKYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAA 526
|
|
| PyrG |
COG0504 |
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ... |
147-693 |
0e+00 |
|
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440270 [Multi-domain] Cd Length: 535 Bit Score: 839.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 147 MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDI 226
Cdd:COG0504 1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 227 NLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAVQEWVMNqamvpvDGHKEEPQICVIELGGTIGDIEGMPFV 306
Cdd:COG0504 81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRR------AAEESGADVVIVEIGGTVGDIESLPFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 307 EAFRQFQFKAKRENFCNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ 386
Cdd:COG0504 155 EAIRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 387 VICIHDVSSTYRVPVLLEEQGIIKYFKERLDLPIGDSAsslLSKWRNMADRYERLQKTCSIALVGKYTKLRDCYASVFKA 466
Cdd:COG0504 235 VISAPDVDSIYEVPLMLHEQGLDEIVLKKLGLEAREPD---LSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 467 LEHSALAINHKLNLMYIDSIDLEQttevedpvkfHEAWQKLCKADGVLVPGGFGIRGTLGKLQAISWARSRKIPFLGVCL 546
Cdd:COG0504 312 LKHAGIANGVKVNIKWIDSEDLEE----------ENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 547 GMQLAVIEFARNCLNLKDADSTEFEPNARVPVVIDMPE-HNPGNLGGTMRLGIRRTVFKtENSILRKLYGDvPFIEERHR 625
Cdd:COG0504 382 GMQLAVIEFARNVLGLEDANSTEFDPNTPHPVIDLMPEqKDVSDLGGTMRLGAYPCKLK-PGTLAAEAYGK-EEISERHR 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387298264 626 HRYEVNPSLISQLEQKDLSFVGQDVDGERMEIIELANHPYFVGVQFHPEFSSRPMKPSPPYLGLLLAA 693
Cdd:COG0504 460 HRYEFNNEYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAA 527
|
|
| PyrG |
TIGR00337 |
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ... |
147-692 |
0e+00 |
|
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. The enzyme catalyzes the reaction L-glutamine + H2O + UTP + ATP = CTP + phosphate + ADP + L-glutamate. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. This gene has been found circa 500 bp 5' upstream of enolase in both beta (Nitrosomonas europaea) and gamma (E.coli) subdivisions of proteobacterium (FEMS Microbiol Lett 1998 Aug 1;165(1):153-7). [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273021 [Multi-domain] Cd Length: 525 Bit Score: 801.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 147 MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDI 226
Cdd:TIGR00337 1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 227 NLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAVQEWVMNQAmvpvdgHKEEPQICVIELGGTIGDIEGMPFV 306
Cdd:TIGR00337 81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVA------KISGPDVVIVEIGGTVGDIESLPFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 307 EAFRQFQFKAKRENFCNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ 386
Cdd:TIGR00337 155 EAIRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 387 VICIHDVSSTYRVPVLLEEQGIIKYFKERLDLpigDSASSLLSKWRNMADRYERLQKTCSIALVGKYTKLRDCYASVFKA 466
Cdd:TIGR00337 235 VISAKDVSSIYEVPLLLLKQGLDDYLCRRLNL---NCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 467 LEHSALAINHKLNLMYIDSIDLEQTTevedpVKFHEAwqklckADGVLVPGGFGIRGTLGKLQAISWARSRKIPFLGVCL 546
Cdd:TIGR00337 312 LKHAGAKLDTKVNIKWIDSEDLEEEG-----VEFLKG------LDGILVPGGFGERGVEGKILAIKYARENNIPFLGICL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 547 GMQLAVIEFARNCLNLKDADSTEFEPNARVPVVIDMPEHNP-GNLGGTMRLGIRRTVFKtENSILRKLYGDvPFIEERHR 625
Cdd:TIGR00337 381 GMQLAVIEFARNVAGLEGANSTEFDPDTKYPVVDLLPEQKDiSDLGGTMRLGLYPCILK-PGTLAFKLYGK-EEVYERHR 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387298264 626 HRYEVNPSLISQLEQKDLSFVGQDVDGERMEIIELANHPYFVGVQFHPEFSSRPMKPSPPYLGLLLA 692
Cdd:TIGR00337 459 HRYEVNNEYREQIENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
|
|
| CTP_synth_N |
pfam06418 |
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ... |
148-418 |
0e+00 |
|
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase protein (EC:6.3.4.2). This family is found in conjunction with pfam00117 located in the C-terminal region of the protein. CTP synthase catalyzes the synthesis of CTP from UTP by amination of the pyrimidine ring at the 4-position.
Pssm-ID: 461903 Cd Length: 265 Bit Score: 564.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 148 KYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDIN 227
Cdd:pfam06418 1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 228 LYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAVQEWVMNQAMvpvdghKEEPQICVIELGGTIGDIEGMPFVE 307
Cdd:pfam06418 81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAK------EVGPDVVIVEIGGTVGDIESLPFLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 308 AFRQFQFKAKRENFCNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQV 387
Cdd:pfam06418 155 AIRQLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAV 234
|
250 260 270
....*....|....*....|....*....|.
gi 1387298264 388 ICIHDVSSTYRVPVLLEEQGIIKYFKERLDL 418
Cdd:pfam06418 235 ISAPDVSSIYEVPLLLEEQGLDDIILKRLNL 265
|
|
| CTPS_N |
cd03113 |
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ... |
148-414 |
0e+00 |
|
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase (CTPS) is a two-domain protein, which consists of an N-terminal synthetase domain and C-terminal glutaminase domain. The enzymes hydrolyze the amide bond of glutamine to ammonia and glutamate at the glutaminase domains and transfer nascent ammonia to the acceptor substrate at the synthetase domain to form an aminated product.
Pssm-ID: 349767 Cd Length: 261 Bit Score: 540.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 148 KYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDIN 227
Cdd:cd03113 1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 228 LYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAVQEWVMNQAmvpvdgHKEEPQICVIELGGTIGDIEGMPFVE 307
Cdd:cd03113 81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVA------KIPEPDVCIVEIGGTVGDIESLPFLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 308 AFRQFQFKAKRENFCNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQV 387
Cdd:cd03113 155 ALRQFQFEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAV 234
|
250 260
....*....|....*....|....*..
gi 1387298264 388 ICIHDVSSTYRVPVLLEEQGIIKYFKE 414
Cdd:cd03113 235 ISVHDVSSIYEVPLLLEKQGLDDYILR 261
|
|
| GATase1_CTP_Synthase |
cd01746 |
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ... |
445-690 |
7.42e-128 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase (CTP). CTP is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. CTPs produce CTP from UTP and glutamine and regulate intracellular CTP levels through interactions with four ribonucleotide triphosphates. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. CTP is derived form UTP in three separate steps involving two active sites. In one active site, the UTP O4 oxygen is activated by Mg-ATP-dependent phosphorylation, followed by displacement of the resulting 4-phosphate moiety by ammonia. At a separate site, ammonia is generated via rate limiting glutamine hydrolysis (glutaminase) activity. A gated channel that spans between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion. CTPs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153217 [Multi-domain] Cd Length: 235 Bit Score: 379.20 E-value: 7.42e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 445 CSIALVGKYTKLRDCYASVFKALEHSALAINHKLNLMYIDSIDLEQTTevedpvkfheAWQKLCKADGVLVPGGFGIRGT 524
Cdd:cd01746 1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEEEN----------AEEALKGADGILVPGGFGIRGV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 525 LGKLQAISWARSRKIPFLGVCLGMQLAVIEFARNCLNLKDADSTEFEPNARVPVVIDMPE-HNPGNLGGTMRLGIRRTVF 603
Cdd:cd01746 71 EGKILAIKYARENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEqKGVKDLGGTMRLGAYPVIL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 604 KtENSILRKLYGdVPFIEERHRHRYEVNPSLISQLEQKDLSFVGQDVDGERMEIIELANHPYFVGVQFHPEFSSRPMKPS 683
Cdd:cd01746 151 K-PGTLAHKYYG-KDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPEFKSRPLKPH 228
|
....*..
gi 1387298264 684 PPYLGLL 690
Cdd:cd01746 229 PLFVGFV 235
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
456-692 |
3.47e-40 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 145.84 E-value: 3.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 456 LRDCYASVFKALEHSALAINHKLNLMYIDSIDLEQTTEvedpvkfheawqklcKADGVLVPGGFGIRGTLG-KLQAISWA 534
Cdd:pfam00117 2 LIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEE---------------NPDGIILSGGPGSPGAAGgAIEAIREA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 535 RSRKIPFLGVCLGMQLAVIEFARNCLNLKDadstefepnarvpvvidmpehnPGNLGGTMRLGIRRTvfktensilRKLY 614
Cdd:pfam00117 67 RELKIPILGICLGHQLLALAFGGKVVKAKK----------------------FGHHGKNSPVGDDGC---------GLFY 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387298264 615 GDVPFIEERHRHRYEVNPSlisqLEQKDLSFVGQDVDGE-RMEIIELANHpyFVGVQFHPEFSSRPMKPSPPYLGLLLA 692
Cdd:pfam00117 116 GLPNVFIVRRYHSYAVDPD----TLPDGLEVTATSENDGtIMGIRHKKLP--IFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| PRK06186 |
PRK06186 |
hypothetical protein; Validated |
444-693 |
1.81e-32 |
|
hypothetical protein; Validated
Pssm-ID: 180452 [Multi-domain] Cd Length: 229 Bit Score: 125.46 E-value: 1.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 444 TCSIALVGKYTKLRDCYASVFKALEHSALAINHKLNLMYIDsidleqTTEVEDPVKFHEAwqklckaDGV-LVPGGfGIR 522
Cdd:PRK06186 1 TLRIALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLP------TPEITDPEDLAGF-------DGIwCVPGS-PYR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 523 GTLGKLQAISWARSRKIPFLGVCLGMQLAVIEFARNCLNLKDADSTEFEPNARVPVVIDMP----EHNpgnlgGTMRLgi 598
Cdd:PRK06186 67 NDDGALTAIRFARENGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEGDRPVIAPLScslvEKT-----GDIRL-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 599 rrtvfkTENSILRKLYGdVPFIEERHRHRYEVNPSLISQLEQKDLSFVGQDVDGErMEIIELANHPYFVGVQFHPEFSSR 678
Cdd:PRK06186 140 ------RPGSLIARAYG-TLEIEEGYHCRYGVNPEFVAALESGDLRVTGWDEDGD-VRAVELPGHPFFVATLFQPERAAL 211
|
250
....*....|....*
gi 1387298264 679 PMKPSPPYLGLLLAA 693
Cdd:PRK06186 212 AGRPPPLVRAFLRAA 226
|
|
| PuuD |
COG2071 |
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
511-675 |
1.59e-09 |
|
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: 58.64 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 511 DGVLVPGG-------FG--IRGTLGK---------LQAISWARSRKIPFLGVCLGMQLaviefarncLNlkdadstefep 572
Cdd:COG2071 51 DGLVLTGGadvdpalYGeePHPELGPidperdafeLALIRAALERGKPVLGICRGMQL---------LN----------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 573 narvpvVI-------DMPEHNPGNLG---GTMRLGIRRTVFKTENSILRKLYGdvpfieerhRHRYEVNpSL----ISQL 638
Cdd:COG2071 111 ------VAlggtlyqDLPDQVPGALDhrqPAPRYAPRHTVEIEPGSRLARILG---------EEEIRVN-SLhhqaVKRL 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1387298264 639 EqKDLSFVGQDVDGerM-EIIELANHPYFVGVQFHPEF 675
Cdd:COG2071 175 G-PGLRVSARAPDG--ViEAIESPGAPFVLGVQWHPEW 209
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
447-553 |
1.44e-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: 53.37 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 447 IALVGKYTKLRDCYASVFKALEHSAlainhklnlmyidsIDLEQTTEVEDPVkfhEAWQKLCKADGVLVPGGFGIRGTL- 525
Cdd:cd01653 1 VAVLLFPGFEELELASPLDALREAG--------------AEVDVVSPDGGPV---ESDVDLDDYDGLILPGGPGTPDDLa 63
|
90 100 110
....*....|....*....|....*....|.
gi 1387298264 526 ---GKLQAISWARSRKIPFLGVCLGMQLAVI 553
Cdd:cd01653 64 rdeALLALLREAAAAGKPILGICLGAQLLVL 94
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
447-550 |
1.75e-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: 49.51 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 447 IALVGKYTKLRDCYASVFKALEHSAlainhklnlmyidsIDLEQTTEVEDPVkfhEAWQKLCKADGVLVPGGFGIRGTL- 525
Cdd:cd03128 1 VAVLLFGGSEELELASPLDALREAG--------------AEVDVVSPDGGPV---ESDVDLDDYDGLILPGGPGTPDDLa 63
|
90 100
....*....|....*....|....*...
gi 1387298264 526 ---GKLQAISWARSRKIPFLGVCLGMQL 550
Cdd:cd03128 64 wdeALLALLREAAAAGKPVLGICLGAQL 91
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
534-674 |
1.67e-06 |
|
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: 49.56 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 534 ARSRKIPFLGVCLGMQLAVIEFARNcLNLKdadstefepnarvpvvIDMPEHNPGNLGGTMRL--GIRRTVFKTENSILR 611
Cdd:pfam07722 101 ALARGKPILGICRGFQLLNVALGGT-LYQD----------------IQEQPGFTDHREHCQVApyAPSHAVNVEPGSLLA 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387298264 612 KLYGDVPFieerhrhryEVNpSL----ISQLEqKDLSFVGQDVDGeRMEIIELANHPYFV-GVQFHPE 674
Cdd:pfam07722 164 SLLGSEEF---------RVN-SLhhqaIDRLA-PGLRVEAVAPDG-TIEAIESPNAKGFAlGVQWHPE 219
|
|
| hisH |
PRK13181 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
505-577 |
4.78e-06 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 47.94 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 505 QKLCKADGVLVPG----GFGIRG--TLGKLQAISWARSRKIPFLGVCLGMQLavieFAR-------NCLNLKDADSTEFE 571
Cdd:PRK13181 33 EEIAGADKVILPGvgafGQAMRSlrESGLDEALKEHVEKKQPVLGICLGMQL----LFEsseegnvKGLGLIPGDVKRFR 108
|
....*..
gi 1387298264 572 PN-ARVP 577
Cdd:PRK13181 109 SEpLKVP 115
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
148-212 |
3.77e-05 |
|
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.
Pssm-ID: 349751 [Multi-domain] Cd Length: 107 Bit Score: 43.19 E-value: 3.77e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387298264 148 KYILVTGGViSGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAG--------------TFSPYEHGEVFVLNDGGE 212
Cdd:cd01983 1 RVIAVTGGK-GGVGKTTLAAALAVALAAKGYKVLLIDLDDYVLIDGGggletglllgtivaLLALKKADEVIVVVDPEL 78
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
461-678 |
5.98e-05 |
|
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: 44.80 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 461 ASVFKALEHsaLAINHKLnlmyidsidleqtteVEDPvkfheawQKLCKADGVLVPG----GFGIRG--TLGKLQAISWA 534
Cdd:cd01748 12 RSVANALER--LGAEVII---------------TSDP-------EEILSADKLILPGvgafGDAMANlrERGLIEALKEA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 535 RSRKIPFLGVCLGMQLAvieFAR-------NCLNLKDADSTEFEPNARVPVvidmPeHnpgnlggtMrlGIRRTVFKTEN 607
Cdd:cd01748 68 IASGKPFLGICLGMQLL---FESseegggtKGLGLIPGKVVRFPASEGLKV----P-H--------M--GWNQLEITKES 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387298264 608 SILRKL--YGDVPFIeerhrHRYEVNPslisqleqKDLSFVGQDVD-GERM-EIIELANhpyFVGVQFHPEFSSR 678
Cdd:cd01748 130 PLFKGIpdGSYFYFV-----HSYYAPP--------DDPDYILATTDyGGKFpAAVEKDN---IFGTQFHPEKSGK 188
|
|
| HisH |
COG0118 |
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
462-550 |
9.96e-05 |
|
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: 43.87 E-value: 9.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 462 SVFKALEHsaLAINHKLnlmyidsidleqtteVEDPvkfheawQKLCKADGVLVPG-G-FG-----IRGtLGKLQAISWA 534
Cdd:COG0118 15 SVAKALER--LGAEVVV---------------TSDP-------DEIRAADRLVLPGvGaFGdamenLRE-RGLDEAIREA 69
|
90
....*....|....*.
gi 1387298264 535 RSRKIPFLGVCLGMQL 550
Cdd:COG0118 70 VAGGKPVLGICLGMQL 85
|
|
| hisH |
PRK13141 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
461-679 |
3.52e-04 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 42.43 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 461 ASVFKALEHsaLAINHKLnlmyidsidleqtteVEDPvkfheawQKLCKADGVLVPG--GFG-----IRGTlGKLQAISW 533
Cdd:PRK13141 13 RSVEKALER--LGAEAVI---------------TSDP-------EEILAADGVILPGvgAFPdamanLRER-GLDEVIKE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387298264 534 ARSRKIPFLGVCLGMQL---AVIEFAR-NCLNLKDADSTEF--EPNARVPvvidmpeHnpgnlggtMrlGIRRTVFKTEN 607
Cdd:PRK13141 68 AVASGKPLLGICLGMQLlfeSSEEFGEtEGLGLLPGRVRRFppEEGLKVP-------H--------M--GWNQLELKKES 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387298264 608 SILRKlygdvpfIEERHR----HRYEVNPSlisqlEQKDL---SFVGQDVDGermeIIELANhpyFVGVQFHPEFSSRP 679
Cdd:PRK13141 131 PLLKG-------IPDGAYvyfvHSYYADPC-----DEEYVaatTDYGVEFPA----AVGKDN---VFGAQFHPEKSGDV 190
|
|
| hisH |
PRK13143 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
509-550 |
7.75e-04 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237289 [Multi-domain] Cd Length: 200 Bit Score: 41.39 E-value: 7.75e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1387298264 509 KADGVLVPG--GFGIRGT-LGKL-QAISWARSRKIPFLGVCLGMQL 550
Cdd:PRK13143 38 DADGIVLPGvgAFGAAMEnLSPLrDVILEAARSGKPFLGICLGMQL 83
|
|
| hisH |
PRK13146 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
510-550 |
1.48e-03 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237290 [Multi-domain] Cd Length: 209 Bit Score: 40.54 E-value: 1.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1387298264 510 ADGVLVPG---------GFGIRGTLGKLQAISWARSRkiPFLGVCLGMQL 550
Cdd:PRK13146 42 ADRVVLPGvgafadcmrGLRAVGLGEAVIEAVLAAGR--PFLGICVGMQL 89
|
|
| |
