|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02327 |
PLN02327 |
CTP synthase |
1-557 |
0e+00 |
|
CTP synthase
Pssm-ID: 215186 [Multi-domain] Cd Length: 557 Bit Score: 929.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 1 MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDI 80
Cdd:PLN02327 1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 81 NLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAIQEWVMNQAKVSVDGNKEDPQICVIELGGTIGDIEGMAFV 160
Cdd:PLN02327 81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAKIPVDGKEGPADVCVIELGGTVGDIESMPFI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 161 EAFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ 240
Cdd:PLN02327 161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 241 VICIHDVSSIYRVPLLLEEQGVVKYFQERLGLPINDCSSNLLfKWKAMADRYERLQKICSIALVGKYTKLRDCYASVFKA 320
Cdd:PLN02327 241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLSVAREPDLE-EWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 321 LEHSALAINHKLNLMYIDSIDLEPVTKAEDPVKFHEAWQKLCLADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGICL 400
Cdd:PLN02327 320 LLHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGICL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 401 GMQLAVIEFARNCLNLKDANSTEFEPNTPVPLVIDMPEHNPGDLGGTMRLGLRRTVFTTENSILKKLYGDVPYIEERHRH 480
Cdd:PLN02327 400 GMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDERHRH 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569012122 481 RYEVNPNLINQFENKDLCFVGEDVDGKRMEIVELTSHPYFIGVQFHPEFSSRPMKPSPPYLGLLLAATGNLNAHLQQ 557
Cdd:PLN02327 480 RYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVLNS 556
|
|
| PyrG |
COG0504 |
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ... |
1-547 |
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: 842.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 1 MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDI 80
Cdd:COG0504 1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 81 NLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAIQEWVMNQAKvsvdgnKEDPQICVIELGGTIGDIEGMAFV 160
Cdd:COG0504 81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAE------ESGADVVIVEIGGTVGDIESLPFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 161 EAFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ 240
Cdd:COG0504 155 EAIRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 241 VICIHDVSSIYRVPLLLEEQGVVKYFQERLGLpinDCSSNLLFKWKAMADRYERLQKICSIALVGKYTKLRDCYASVFKA 320
Cdd:COG0504 235 VISAPDVDSIYEVPLMLHEQGLDEIVLKKLGL---EAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 321 LEHSALAINHKLNLMYIDSIDLEPvtkaedpvkfHEAWQKLCLADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGICL 400
Cdd:COG0504 312 LKHAGIANGVKVNIKWIDSEDLEE----------ENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 401 GMQLAVIEFARNCLNLKDANSTEFEPNTPVPlVID-MPE-HNPGDLGGTMRLGLRRTVfTTENSILKKLYGDvPYIEERH 478
Cdd:COG0504 382 GMQLAVIEFARNVLGLEDANSTEFDPNTPHP-VIDlMPEqKDVSDLGGTMRLGAYPCK-LKPGTLAAEAYGK-EEISERH 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569012122 479 RHRYEVNPNLINQFENKDLCFVGEDVDGKRMEIVELTSHPYFIGVQFHPEFSSRPMKPSPPYLGLLLAA 547
Cdd:COG0504 459 RHRYEFNNEYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAA 527
|
|
| pyrG |
PRK05380 |
CTP synthetase; Validated |
1-547 |
0e+00 |
|
CTP synthetase; Validated
Pssm-ID: 235437 [Multi-domain] Cd Length: 533 Bit Score: 839.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 1 MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDI 80
Cdd:PRK05380 2 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 81 NLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAIQEWVMNQAkvsvdgnkEDPQICVIELGGTIGDIEGMAFV 160
Cdd:PRK05380 82 NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAG--------TDADVVIVEIGGTVGDIESLPFL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 161 EAFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ 240
Cdd:PRK05380 154 EAIRQLRLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 241 VICIHDVSSIYRVPLLLEEQGVVKYFQERLGLpinDCSSNLLFKWKAMADRYERLQKICSIALVGKYTKLRDCYASVFKA 320
Cdd:PRK05380 234 VISAPDVDSIYEVPLLLHEQGLDDIVLERLGL---EAPEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 321 LEHSALAINHKLNLMYIDSIDLEPVTKAEdpvkfheawqKLCLADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGICL 400
Cdd:PRK05380 311 LKHAGIANDVKVNIKWIDSEDLEEENVAE----------LLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 401 GMQLAVIEFARNCLNLKDANSTEFEPNTPVPlVID-MPE-HNPGDLGGTMRLGLRRTVFtTENSILKKLYGDvPYIEERH 478
Cdd:PRK05380 381 GMQLAVIEFARNVLGLEDANSTEFDPDTPHP-VIDlMPEqKDVSDLGGTMRLGAYPCKL-KPGTLAAEIYGK-EEIYERH 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569012122 479 RHRYEVNPNLINQFENKDLCFVGEDVDGKRMEIVELTSHPYFIGVQFHPEFSSRPMKPSPPYLGLLLAA 547
Cdd:PRK05380 458 RHRYEVNNKYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAA 526
|
|
| PyrG |
TIGR00337 |
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ... |
1-546 |
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: 801.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 1 MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDI 80
Cdd:TIGR00337 1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 81 NLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAIQEWVMNQAKvsvdgnKEDPQICVIELGGTIGDIEGMAFV 160
Cdd:TIGR00337 81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAK------ISGPDVVIVEIGGTVGDIESLPFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 161 EAFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ 240
Cdd:TIGR00337 155 EAIRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 241 VICIHDVSSIYRVPLLLEEQGVVKYFQERLGLpinDCSSNLLFKWKAMADRYERLQKICSIALVGKYTKLRDCYASVFKA 320
Cdd:TIGR00337 235 VISAKDVSSIYEVPLLLLKQGLDDYLCRRLNL---NCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 321 LEHSALAINHKLNLMYIDSIDLEPVTkaedpVKFHEAwqklclADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGICL 400
Cdd:TIGR00337 312 LKHAGAKLDTKVNIKWIDSEDLEEEG-----VEFLKG------LDGILVPGGFGERGVEGKILAIKYARENNIPFLGICL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 401 GMQLAVIEFARNCLNLKDANSTEFEPNTPVPLVIDMPEHNP-GDLGGTMRLGLRRTVFtTENSILKKLYGDvPYIEERHR 479
Cdd:TIGR00337 381 GMQLAVIEFARNVAGLEGANSTEFDPDTKYPVVDLLPEQKDiSDLGGTMRLGLYPCIL-KPGTLAFKLYGK-EEVYERHR 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569012122 480 HRYEVNPNLINQFENKDLCFVGEDVDGKRMEIVELTSHPYFIGVQFHPEFSSRPMKPSPPYLGLLLA 546
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 ... |
2-272 |
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: 556.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 2 KYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDIN 81
Cdd:pfam06418 1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 82 LYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAIQEWVMNQAKvsvdgnKEDPQICVIELGGTIGDIEGMAFVE 161
Cdd:pfam06418 81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAK------EVGPDVVIVEIGGTVGDIESLPFLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 162 AFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQV 241
Cdd:pfam06418 155 AIRQLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAV 234
|
250 260 270
....*....|....*....|....*....|.
gi 569012122 242 ICIHDVSSIYRVPLLLEEQGVVKYFQERLGL 272
Cdd:pfam06418 235 ISAPDVSSIYEVPLLLEEQGLDDIILKRLNL 265
|
|
| CTPS_N |
cd03113 |
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ... |
2-268 |
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: 530.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 2 KYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDIN 81
Cdd:cd03113 1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 82 LYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAIQEWVMNQAKVSVdgnkedPQICVIELGGTIGDIEGMAFVE 161
Cdd:cd03113 81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIPE------PDVCIVEIGGTVGDIESLPFLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 162 AFRQFQFKAKKENFYNIHVSLVPQPSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQV 241
Cdd:cd03113 155 ALRQFQFEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAV 234
|
250 260
....*....|....*....|....*..
gi 569012122 242 ICIHDVSSIYRVPLLLEEQGVVKYFQE 268
Cdd:cd03113 235 ISVHDVSSIYEVPLLLEKQGLDDYILR 261
|
|
| GATase1_CTP_Synthase |
cd01746 |
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ... |
299-544 |
1.94e-134 |
|
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: 391.15 E-value: 1.94e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 299 CSIALVGKYTKLRDCYASVFKALEHSALAINHKLNLMYIDSIDLEPVTkaedpvkfheAWQKLCLADGILVPGGFGIRGT 378
Cdd:cd01746 1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEEEN----------AEEALKGADGILVPGGFGIRGV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 379 LGKLQAISWARTKKIPFLGICLGMQLAVIEFARNCLNLKDANSTEFEPNTPVPLVIDMPE-HNPGDLGGTMRLGLRRTVF 457
Cdd:cd01746 71 EGKILAIKYARENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEqKGVKDLGGTMRLGAYPVIL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 458 tTENSILKKLYGdVPYIEERHRHRYEVNPNLINQFENKDLCFVGEDVDGKRMEIVELTSHPYFIGVQFHPEFSSRPMKPS 537
Cdd:cd01746 151 -KPGTLAHKYYG-KDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPEFKSRPLKPH 228
|
....*..
gi 569012122 538 PPYLGLL 544
Cdd:cd01746 229 PLFVGFV 235
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
310-546 |
6.88e-43 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 152.01 E-value: 6.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 310 LRDCYASVFKALEHSALAINHKLNLMYIDSIDLEpvTKAEDPvkfheawqklclaDGILVPGGFGIRGTLG-KLQAISWA 388
Cdd:pfam00117 2 LIDNGDSFTYNLARALRELGVEVTVVPNDTPAEE--ILEENP-------------DGIILSGGPGSPGAAGgAIEAIREA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 389 RTKKIPFLGICLGMQLAVIEFARNCLNLKDanstefepntpvplvidmpehnPGDLGGTMRLGLRRTvfttensilKKLY 468
Cdd:pfam00117 67 RELKIPILGICLGHQLLALAFGGKVVKAKK----------------------FGHHGKNSPVGDDGC---------GLFY 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569012122 469 GDVPYIEERHRHRYEVNPNlinqFENKDLCFVGEDVDG-KRMEIVELTSHpyFIGVQFHPEFSSRPMKPSPPYLGLLLA 546
Cdd:pfam00117 116 GLPNVFIVRRYHSYAVDPD----TLPDGLEVTATSENDgTIMGIRHKKLP--IFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| PRK06186 |
PRK06186 |
hypothetical protein; Validated |
301-547 |
1.25e-29 |
|
hypothetical protein; Validated
Pssm-ID: 180452 [Multi-domain] Cd Length: 229 Bit Score: 116.60 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 301 IALVGKYTKLRDCYASVFKALEHSALAINHKLNLMYIDSIDLepvTKAEDPVKFHEAWqklcladgiLVPGGfGIRGTLG 380
Cdd:PRK06186 4 IALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPTPEI---TDPEDLAGFDGIW---------CVPGS-PYRNDDG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 381 KLQAISWARTKKIPFLGICLGMQLAVIEFARNCLNLKDANSTEFEPNTP----VPLVIDMPEHNpgdlgGTMRLglrrtv 456
Cdd:PRK06186 71 ALTAIRFARENGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEGDrpviAPLSCSLVEKT-----GDIRL------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 457 ftTENSILKKLYGdVPYIEERHRHRYEVNPNLINQFENKDLCFVGEDVDGkrmEI--VELTSHPYFIGVQFHPEFSSRPM 534
Cdd:PRK06186 140 --RPGSLIARAYG-TLEIEEGYHCRYGVNPEFVAALESGDLRVTGWDEDG---DVraVELPGHPFFVATLFQPERAALAG 213
|
250
....*....|...
gi 569012122 535 KPSPPYLGLLLAA 547
Cdd:PRK06186 214 RPPPLVRAFLRAA 226
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
301-407 |
6.35e-10 |
|
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: 56.84 E-value: 6.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 301 IALVGKYTKLRDCYASVFKALEHSAlainhklnlmyidsIDLEPVTKAEDPVkfhEAWQKLCLADGILVPGGFGIRGTL- 379
Cdd:cd01653 1 VAVLLFPGFEELELASPLDALREAG--------------AEVDVVSPDGGPV---ESDVDLDDYDGLILPGGPGTPDDLa 63
|
90 100 110
....*....|....*....|....*....|.
gi 569012122 380 ---GKLQAISWARTKKIPFLGICLGMQLAVI 407
Cdd:cd01653 64 rdeALLALLREAAAAGKPILGICLGAQLLVL 94
|
|
| PuuD |
COG2071 |
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
330-529 |
9.27e-10 |
|
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: 59.03 E-value: 9.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 330 HKLNLMYIDSID-------LEPVTKAEDPVKfheawQKLCLADGILVPGG-------FG--IRGTLGK---------LQA 384
Cdd:COG2071 14 HYLPEDYVRAVRaagglpvLLPPVGDEEDLD-----ELLDRLDGLVLTGGadvdpalYGeePHPELGPidperdafeLAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 385 ISWARTKKIPFLGICLGMQLaviefarncLNlkdanstefepntpV----PLVIDMPEHNPGDLG---GTMRLGLRRTVF 457
Cdd:COG2071 89 IRAALERGKPVLGICRGMQL---------LN--------------ValggTLYQDLPDQVPGALDhrqPAPRYAPRHTVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 458 TTENSILKKLYGdvpyieerhRHRYEVNpnlinqfenkdlCF-------VGEDV-------DGkrmeIVE---LTSHPYF 520
Cdd:COG2071 146 IEPGSRLARILG---------EEEIRVN------------SLhhqavkrLGPGLrvsarapDG----VIEaieSPGAPFV 200
|
....*....
gi 569012122 521 IGVQFHPEF 529
Cdd:COG2071 201 LGVQWHPEW 209
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
301-404 |
2.03e-08 |
|
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: 51.82 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 301 IALVGKYTKLRDCYASVFKALEHSAlainhklnlmyidsIDLEPVTKAEDPVkfhEAWQKLCLADGILVPGGFGIRGTL- 379
Cdd:cd03128 1 VAVLLFGGSEELELASPLDALREAG--------------AEVDVVSPDGGPV---ESDVDLDDYDGLILPGGPGTPDDLa 63
|
90 100
....*....|....*....|....*...
gi 569012122 380 ---GKLQAISWARTKKIPFLGICLGMQL 404
Cdd:cd03128 64 wdeALLALLREAAAAGKPVLGICLGAQL 91
|
|
| hisH |
PRK13181 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
359-532 |
2.37e-06 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 48.32 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 359 QKLCLADGILVPG----GFGIRG--TLGKLQAISWARTKKIPFLGICLGMQLavieFAR-------NCLNLKDANSTEFE 425
Cdd:PRK13181 33 EEIAGADKVILPGvgafGQAMRSlrESGLDEALKEHVEKKQPVLGICLGMQL----LFEsseegnvKGLGLIPGDVKRFR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 426 PNT-PVPlvidmpehnpgdlggtmRLGLRRTVFTTENSILKKlygdvpyIEERHR----HRYEVNPNlinqfenkdlcfV 500
Cdd:PRK13181 109 SEPlKVP-----------------QMGWNSVKPLKESPLFKG-------IEEGSYfyfvHSYYVPCE------------D 152
|
170 180 190
....*....|....*....|....*....|....*
gi 569012122 501 GEDVDGKRMEIVELTSHPY---FIGVQFHPEFSSR 532
Cdd:PRK13181 153 PEDVLATTEYGVPFCSAVAkdnIYAVQFHPEKSGK 187
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
392-528 |
7.91e-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: 47.25 E-value: 7.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 392 KIPFLGICLGMQLAVIEFARNcLNLkDANStefepntpVPLVIDMPEHNPGDLGGTmrlglRRTVFTTENSILKKLYGDv 471
Cdd:pfam07722 105 GKPILGICRGFQLLNVALGGT-LYQ-DIQE--------QPGFTDHREHCQVAPYAP-----SHAVNVEPGSLLASLLGS- 168
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569012122 472 pyiEErhrhrYEVNpNLINQFENK---DLCFVGEDVDGKrMEIVELTSHPYF-IGVQFHPE 528
Cdd:pfam07722 169 ---EE-----FRVN-SLHHQAIDRlapGLRVEAVAPDGT-IEAIESPNAKGFaLGVQWHPE 219
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
2-66 |
4.73e-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: 42.80 E-value: 4.73e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569012122 2 KYILVTGGViSGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAG--------------TFSPYEHGEVFVLNDGGE 66
Cdd:cd01983 1 RVIAVTGGK-GGVGKTTLAAALAVALAAKGYKVLLIDLDDYVLIDGGggletglllgtivaLLALKKADEVIVVVDPEL 78
|
|
| HisH |
COG0118 |
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
364-404 |
4.74e-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: 44.64 E-value: 4.74e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 569012122 364 ADGILVPG-G-FG-----IRGtLGKLQAISWARTKKIPFLGICLGMQL 404
Cdd:COG0118 39 ADRLVLPGvGaFGdamenLRE-RGLDEAIREAVAGGKPVLGICLGMQL 85
|
|
| hisH |
PRK13143 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
364-404 |
1.24e-04 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237289 [Multi-domain] Cd Length: 200 Bit Score: 43.32 E-value: 1.24e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 569012122 364 ADGILVPG--GFGIRGT-LGKL-QAISWARTKKIPFLGICLGMQL 404
Cdd:PRK13143 39 ADGIVLPGvgAFGAAMEnLSPLrDVILEAARSGKPFLGICLGMQL 83
|
|
| GATase1_Glutamyl_Hydrolase |
cd01747 |
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ... |
359-528 |
2.45e-04 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153218 [Multi-domain] Cd Length: 273 Bit Score: 43.08 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 359 QKLCLADGILVPGGFGirgtlgKLQAISWARTKKI---------------PFLGICLGMQLAVIEFARNCLNLKDANSTE 423
Cdd:cd01747 50 KLFKSINGILFPGGAV------DIDTSGYARTAKIiynlalerndagdyfPVWGTCLGFELLTYLTSGETLLLEATEATN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 424 fepntpvplvIDMPEHNPGDLggtmrlgLRRTVF-TTENSILKKLyGDVPYIEerHRHRYEVNPN------LINQFENkd 496
Cdd:cd01747 124 ----------SALPLNFTEDA-------LQSRLFkRFPPDLLKSL-ATEPLTM--NNHRYGISPEnftengLLSDFFN-- 181
|
170 180 190
....*....|....*....|....*....|...
gi 569012122 497 LCFVGEDVDGKR-MEIVELTSHPYFiGVQFHPE 528
Cdd:cd01747 182 VLTTNDDWNGVEfISTVEAYKYPIY-GVQWHPE 213
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
364-532 |
4.53e-04 |
|
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: 41.71 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 364 ADGILVPG----GFGIRG--TLGKLQAISWARTKKIPFLGICLGMQLAvieFAR-------NCLNLKDANSTEFEPNTPV 430
Cdd:cd01748 37 ADKLILPGvgafGDAMANlrERGLIEALKEAIASGKPFLGICLGMQLL---FESseegggtKGLGLIPGKVVRFPASEGL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 431 PLvidmPeHnpgdlggtMrlGLRRTVFTTENSILKklygdvpYIEERHR----HRYEVNPNlinqfENKDL---CFVGED 503
Cdd:cd01748 114 KV----P-H--------M--GWNQLEITKESPLFK-------GIPDGSYfyfvHSYYAPPD-----DPDYIlatTDYGGK 166
|
170 180
....*....|....*....|....*....
gi 569012122 504 VDGkrmeIVEltsHPYFIGVQFHPEFSSR 532
Cdd:cd01748 167 FPA----AVE---KDNIFGTQFHPEKSGK 188
|
|
| hisH |
PRK13141 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
315-404 |
6.65e-04 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 41.27 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569012122 315 ASVFKALEhsalainhKLNLMYIdsidlepVTKaeDPvkfheawQKLCLADGILVPG--GFG-----IRGTlGKLQAISW 387
Cdd:PRK13141 13 RSVEKALE--------RLGAEAV-------ITS--DP-------EEILAADGVILPGvgAFPdamanLRER-GLDEVIKE 67
|
90
....*....|....*..
gi 569012122 388 ARTKKIPFLGICLGMQL 404
Cdd:PRK13141 68 AVASGKPLLGICLGMQL 84
|
|
| hisH |
PRK13146 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
364-404 |
8.94e-04 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237290 [Multi-domain] Cd Length: 209 Bit Score: 40.92 E-value: 8.94e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 569012122 364 ADGILVPG---------GFGIRGTLGKLQAISWARTKkiPFLGICLGMQL 404
Cdd:PRK13146 42 ADRVVLPGvgafadcmrGLRAVGLGEAVIEAVLAAGR--PFLGICVGMQL 89
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
382-404 |
6.69e-03 |
|
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440284 [Multi-domain] Cd Length: 225 Bit Score: 38.39 E-value: 6.69e-03
10 20
....*....|....*....|...
gi 569012122 382 LQAISWARTKKIPFLGICLGMQL 404
Cdd:COG0518 72 PALIREAFELGKPVLGICYGAQL 94
|
|
| |
