|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02327 |
PLN02327 |
CTP synthase |
1-552 |
0e+00 |
|
CTP synthase
Pssm-ID: 215186 [Multi-domain] Cd Length: 557 Bit Score: 1223.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 1 MKYVIVTGGVVSGLGKGVTASSIGVVLQSCGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80
Cdd:PLN02327 1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 81 TLTKNNNITTGKIYQSVIDAERRGDYLGKTVQVVPHITVEIQEWIERVAVVPVDGKEGAADVCVIELGGTIGDIESSPFV 160
Cdd:PLN02327 81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAKIPVDGKEGPADVCVIELGGTVGDIESMPFI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 161 EALRQFQFRVGQENFCLVHVSLIPVLGVVGEQKTKPTQHSVQALRALGLTPDLLGCRSAKPLEQCTREKLSQFCHVPAGH 240
Cdd:PLN02327 161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 241 ILSIHDVSNIWHVPLLLRDQNVHLAILKKLNLSS-APQPELSEWTQRAERSDALSIPVKIGMVGKYTGLSDSYLSVLKAL 319
Cdd:PLN02327 241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLSvAREPDLEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 320 THASLACGRKLVIEWVASTDLEDGSPR---DLHDAAWAALKSVDGILVPGGFGDRGTQGKVLAAKYARENNVPYLGVCLG 396
Cdd:PLN02327 321 LHASVACSRKLVIDWVAASDLEDETAKetpDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGICLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 397 MQIAVIEFARSVLGLDGANSTEFDPATPHPCVLYMPEISRTHKGGTMRLGVRRTFFQKPNCLTSKLYGNESFVDERHRHR 476
Cdd:PLN02327 401 MQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDERHRHR 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1376929165 477 YEVNPELVDRLEEAGLTFVGKDETGRRMEIVELPEHKYFVGVQFHPEFKSRPGKPSPVFLGLILAASKQMDSYLAS 552
Cdd:PLN02327 481 YEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVLNS 556
|
|
| pyrG |
PRK05380 |
CTP synthetase; Validated |
1-545 |
0e+00 |
|
CTP synthetase; Validated
Pssm-ID: 235437 [Multi-domain] Cd Length: 533 Bit Score: 886.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 1 MKYVIVTGGVVSGLGKGVTASSIGVVLQSCGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80
Cdd:PRK05380 2 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 81 TLTKNNNITTGKIYQSVIDAERRGDYLGKTVQVVPHITVEIQEWIERVAvvpvdgkeGAADVCVIELGGTIGDIESSPFV 160
Cdd:PRK05380 82 NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAG--------TDADVVIVEIGGTVGDIESLPFL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 161 EALRQFQFRVGQENFCLVHVSLIPVLGVVGEQKTKPTQHSVQALRALGLTPDLLGCRSAKPLEQCTREKLSQFCHVPAGH 240
Cdd:PRK05380 154 EAIRQLRLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 241 ILSIHDVSNIWHVPLLLRDQNVHLAILKKLNLsSAPQPELSEWTQRAERSDALSIPVKIGMVGKYTGLSDSYLSVLKALT 320
Cdd:PRK05380 234 VISAPDVDSIYEVPLLLHEQGLDDIVLERLGL-EAPEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 321 HASLACGRKLVIEWVASTDLEDGSPRDLhdaawaaLKSVDGILVPGGFGDRGTQGKVLAAKYARENNVPYLGVCLGMQIA 400
Cdd:PRK05380 313 HAGIANDVKVNIKWIDSEDLEEENVAEL-------LKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 401 VIEFARSVLGLDGANSTEFDPATPHPCVLYMPE-ISRTHKGGTMRLGVRRTFFqKPNCLTSKLYGNESfVDERHRHRYEV 479
Cdd:PRK05380 386 VIEFARNVLGLEDANSTEFDPDTPHPVIDLMPEqKDVSDLGGTMRLGAYPCKL-KPGTLAAEIYGKEE-IYERHRHRYEV 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1376929165 480 NPELVDRLEEAGLTFVGKDETGRRMEIVELPEHKYFVGVQFHPEFKSRPGKPSPVFLGLILAASKQ 545
Cdd:PRK05380 464 NNKYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALEN 529
|
|
| PyrG |
COG0504 |
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ... |
1-545 |
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: 884.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 1 MKYVIVTGGVVSGLGKGVTASSIGVVLQSCGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80
Cdd:COG0504 1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 81 TLTKNNNITTGKIYQSVIDAERRGDYLGKTVQVVPHITVEIQEWIERVAvvpvdgKEGAADVCVIELGGTIGDIESSPFV 160
Cdd:COG0504 81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAA------EESGADVVIVEIGGTVGDIESLPFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 161 EALRQFQFRVGQENFCLVHVSLIPVLGVVGEQKTKPTQHSVQALRALGLTPDLLGCRSAKPLEQCTREKLSQFCHVPAGH 240
Cdd:COG0504 155 EAIRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 241 ILSIHDVSNIWHVPLLLRDQNVHLAILKKLNLsSAPQPELSEWTQRAERSDALSIPVKIGMVGKYTGLSDSYLSVLKALT 320
Cdd:COG0504 235 VISAPDVDSIYEVPLMLHEQGLDEIVLKKLGL-EAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 321 HASLACGRKLVIEWVASTDLEDGSPRDLhdaawaaLKSVDGILVPGGFGDRGTQGKVLAAKYARENNVPYLGVCLGMQIA 400
Cdd:COG0504 314 HAGIANGVKVNIKWIDSEDLEEENAEEL-------LKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 401 VIEFARSVLGLDGANSTEFDPATPHPCVLYMPE-ISRTHKGGTMRLGVRRTFFqKPNCLTSKLYGNESfVDERHRHRYEV 479
Cdd:COG0504 387 VIEFARNVLGLEDANSTEFDPNTPHPVIDLMPEqKDVSDLGGTMRLGAYPCKL-KPGTLAAEAYGKEE-ISERHRHRYEF 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1376929165 480 NPELVDRLEEAGLTFVGKDETGRRMEIVELPEHKYFVGVQFHPEFKSRPGKPSPVFLGLILAASKQ 545
Cdd:COG0504 465 NNEYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEY 530
|
|
| PyrG |
TIGR00337 |
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ... |
1-541 |
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: 832.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 1 MKYVIVTGGVVSGLGKGVTASSIGVVLQSCGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80
Cdd:TIGR00337 1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 81 TLTKNNNITTGKIYQSVIDAERRGDYLGKTVQVVPHITVEIQEWIERVAvvpvdgKEGAADVCVIELGGTIGDIESSPFV 160
Cdd:TIGR00337 81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVA------KISGPDVVIVEIGGTVGDIESLPFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 161 EALRQFQFRVGQENFCLVHVSLIPVLGVVGEQKTKPTQHSVQALRALGLTPDLLGCRSAKPLEQCTREKLSQFCHVPAGH 240
Cdd:TIGR00337 155 EAIRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 241 ILSIHDVSNIWHVPLLLRDQNVHLAILKKLNLsSAPQPELSEWTQRAERSDALSIPVKIGMVGKYTGLSDSYLSVLKALT 320
Cdd:TIGR00337 235 VISAKDVSSIYEVPLLLLKQGLDDYLCRRLNL-NCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 321 HASLACGRKLVIEWVASTDLEDGSPRDlhdaawaaLKSVDGILVPGGFGDRGTQGKVLAAKYARENNVPYLGVCLGMQIA 400
Cdd:TIGR00337 314 HAGAKLDTKVNIKWIDSEDLEEEGVEF--------LKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGMQLA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 401 VIEFARSVLGLDGANSTEFDPATPHPCVLYMPEISR-THKGGTMRLGVRRTFFQkPNCLTSKLYGNESfVDERHRHRYEV 479
Cdd:TIGR00337 386 VIEFARNVAGLEGANSTEFDPDTKYPVVDLLPEQKDiSDLGGTMRLGLYPCILK-PGTLAFKLYGKEE-VYERHRHRYEV 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1376929165 480 NPELVDRLEEAGLTFVGKDETGRRMEIVELPEHKYFVGVQFHPEFKSRPGKPSPVFLGLILA 541
Cdd:TIGR00337 464 NNEYREQIENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 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: 540.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 2 KYVIVTGGVVSGLGKGVTASSIGVVLQSCGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDVT 81
Cdd:pfam06418 1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 82 LTKNNNITTGKIYQSVIDAERRGDYLGKTVQVVPHITVEIQEWIERVAvvpvdgKEGAADVCVIELGGTIGDIESSPFVE 161
Cdd:pfam06418 81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVA------KEVGPDVVIVEIGGTVGDIESLPFLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 162 ALRQFQFRVGQENFCLVHVSLIPVLGVVGEQKTKPTQHSVQALRALGLTPDLLGCRSAKPLEQCTREKLSQFCHVPAGHI 241
Cdd:pfam06418 155 AIRQLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAV 234
|
250 260 270
....*....|....*....|....*....|.
gi 1376929165 242 LSIHDVSNIWHVPLLLRDQNVHLAILKKLNL 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: 526.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 2 KYVIVTGGVVSGLGKGVTASSIGVVLQSCGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDVT 81
Cdd:cd03113 1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 82 LTKNNNITTGKIYQSVIDAERRGDYLGKTVQVVPHITVEIQEWIERVAVVPVdgkegaADVCVIELGGTIGDIESSPFVE 161
Cdd:cd03113 81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIPE------PDVCIVEIGGTVGDIESLPFLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 162 ALRQFQFRVGQENFCLVHVSLIPVLGVVGEQKTKPTQHSVQALRALGLTPDLLGCRSAKPLEQCTREKLSQFCHVPAGHI 241
Cdd:cd03113 155 ALRQFQFEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAV 234
|
250 260
....*....|....*....|....*..
gi 1376929165 242 LSIHDVSNIWHVPLLLRDQNVHLAILK 268
Cdd:cd03113 235 ISVHDVSSIYEVPLLLEKQGLDDYILR 261
|
|
| GATase1_CTP_Synthase |
cd01746 |
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ... |
297-539 |
3.64e-141 |
|
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: 410.41 E-value: 3.64e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 297 VKIGMVGKYTGLSDSYLSVLKALTHASLACGRKLVIEWVASTDLEDgsprdlhDAAWAALKSVDGILVPGGFGDRGTQGK 376
Cdd:cd01746 1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEE-------ENAEEALKGADGILVPGGFGIRGVEGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 377 VLAAKYARENNVPYLGVCLGMQIAVIEFARSVLGLDGANSTEFDPATPHPCVLYMPE-ISRTHKGGTMRLGVRRTFFqKP 455
Cdd:cd01746 74 ILAIKYARENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEqKGVKDLGGTMRLGAYPVIL-KP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 456 NCLTSKLYGNESfVDERHRHRYEVNPELVDRLEEAGLTFVGKDETGRRMEIVELPEHKYFVGVQFHPEFKSRPGKPSPVF 535
Cdd:cd01746 153 GTLAHKYYGKDE-VEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPEFKSRPLKPHPLF 231
|
....
gi 1376929165 536 LGLI 539
Cdd:cd01746 232 VGFV 235
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
310-541 |
5.11e-44 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 155.86 E-value: 5.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 310 DSYLSVLKALTHASLACGRKLVIEWVASTDLEDGSprdlhdaawaalKSVDGILVPGGFGDRGT-QGKVLAAKYARENNV 388
Cdd:pfam00117 4 DNGDSFTYNLARALRELGVEVTVVPNDTPAEEILE------------ENPDGIILSGGPGSPGAaGGAIEAIREARELKI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 389 PYLGVCLGMQIAVIEFARSVLgldganstefdpatphpcvlymPEISRTHKGGTMRLGVRRtffqkpnclTSKLYGNESF 468
Cdd:pfam00117 72 PILGICLGHQLLALAFGGKVV----------------------KAKKFGHHGKNSPVGDDG---------CGLFYGLPNV 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1376929165 469 VDERHRHRYEVNPElvdrLEEAGLTFVGKDETG-RRMEIVElpEHKYFVGVQFHPEFKSRPGKPSPVFLGLILA 541
Cdd:pfam00117 121 FIVRRYHSYAVDPD----TLPDGLEVTATSENDgTIMGIRH--KKLPIFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| PRK06186 |
PRK06186 |
hypothetical protein; Validated |
296-545 |
2.52e-39 |
|
hypothetical protein; Validated
Pssm-ID: 180452 [Multi-domain] Cd Length: 229 Bit Score: 144.34 E-value: 2.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 296 PVKIGMVGKYTGLSDSYLSVLKALTHASLACGRKLVIEWVASTDLEDGSPRDLHDAAWaalksvdgiLVPGGfGDRGTQG 375
Cdd:PRK06186 1 TLRIALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPTPEITDPEDLAGFDGIW---------CVPGS-PYRNDDG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 376 KVLAAKYARENNVPYLGVCLGMQIAVIEFARSVLGLDGANSTEFDPA------TPHPCVLympeisrTHKGGTMRLGvrr 449
Cdd:PRK06186 71 ALTAIRFARENGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEgdrpviAPLSCSL-------VEKTGDIRLR--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 450 tffqkPNCLTSKLYGNESfVDERHRHRYEVNPELVDRLEEAGLTFVGKDETGrrmEI--VELPEHKYFVGVQFHPEFKSR 527
Cdd:PRK06186 141 -----PGSLIARAYGTLE-IEEGYHCRYGVNPEFVAALESGDLRVTGWDEDG---DVraVELPGHPFFVATLFQPERAAL 211
|
250
....*....|....*...
gi 1376929165 528 PGKPSPVFLGLILAASKQ 545
Cdd:PRK06186 212 AGRPPPLVRAFLRAARAA 229
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
299-402 |
3.62e-09 |
|
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: 54.91 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 299 IGMVGKYTGLSDSYLSVLKALTHASLAcgrklvIEWVASTDLEDGSPRDLHDAawaalksvDGILVPGGFGDRGT----Q 374
Cdd:cd01653 1 VAVLLFPGFEELELASPLDALREAGAE------VDVVSPDGGPVESDVDLDDY--------DGLILPGGPGTPDDlardE 66
|
90 100
....*....|....*....|....*...
gi 1376929165 375 GKVLAAKYARENNVPYLGVCLGMQIAVI 402
Cdd:cd01653 67 ALLALLREAAAAGKPILGICLGAQLLVL 94
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
299-399 |
1.19e-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: 49.89 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 299 IGMVGKYTGLSDSYLSVLKALTHASLAcgrklvIEWVASTDLEDGSPRDLHDAawaalksvDGILVPGGFGD----RGTQ 374
Cdd:cd03128 1 VAVLLFGGSEELELASPLDALREAGAE------VDVVSPDGGPVESDVDLDDY--------DGLILPGGPGTpddlAWDE 66
|
90 100
....*....|....*....|....*
gi 1376929165 375 GKVLAAKYARENNVPYLGVCLGMQI 399
Cdd:cd03128 67 ALLALLREAAAAGKPVLGICLGAQL 91
|
|
| PuuD |
COG2071 |
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
345-544 |
1.28e-07 |
|
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: 52.86 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 345 PRDLHDAAWAALKSVDGILVPGG-------FGDRGTQGKV----------LA-AKYARENNVPYLGVCLGMQ-IAViefa 405
Cdd:COG2071 36 PVGDEEDLDELLDRLDGLVLTGGadvdpalYGEEPHPELGpidperdafeLAlIRAALERGKPVLGICRGMQlLNV---- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 406 rsVLG--LDGANSTEFDPATPHpcVLYMPEISRTHkggTMRLgvrrtffqKPNCLTSKLYGNESF-VDERHRhryevnpE 482
Cdd:COG2071 112 --ALGgtLYQDLPDQVPGALDH--RQPAPRYAPRH---TVEI--------EPGSRLARILGEEEIrVNSLHH-------Q 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1376929165 483 LVDRLEEaGLTFVGKDETGrrmeIVE---LPEHKYFVGVQFHPEFKSRPGKPS-PVFLGLILAASK 544
Cdd:COG2071 170 AVKRLGP-GLRVSARAPDG----VIEaieSPGAPFVLGVQWHPEWLAASDPLSrRLFEAFVEAARA 230
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
354-523 |
3.89e-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: 48.41 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 354 AALKSVDGILVPGG-------FGDRGTQG-------------KVLAAKYARenNVPYLGVCLGMQIAVIEFARSvLGLDg 413
Cdd:pfam07722 54 AILDRLDGLLLTGGpnvdphfYGEEPSESggpydpardayelALIRAALAR--GKPILGICRGFQLLNVALGGT-LYQD- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 414 anstefdpatphpcvLYMPEISRTHKGGTMRLGV--RRTFFQKPNCLTSKLYGNESF-VDERHRhryevnpELVDRLEEa 490
Cdd:pfam07722 130 ---------------IQEQPGFTDHREHCQVAPYapSHAVNVEPGSLLASLLGSEEFrVNSLHH-------QAIDRLAP- 186
|
170 180 190
....*....|....*....|....*....|....
gi 1376929165 491 GLTFVGKDETGRrMEIVELPEHKYFV-GVQFHPE 523
Cdd:pfam07722 187 GLRVEAVAPDGT-IEAIESPNAKGFAlGVQWHPE 219
|
|
| IMP_synth_hisH |
TIGR01855 |
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ... |
355-530 |
2.14e-05 |
|
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273836 [Multi-domain] Cd Length: 196 Bit Score: 45.78 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 355 ALKSVDGILVPG--GFGDrgtqgkvlAAKYARENNV------------PYLGVCLGMQIAvieFARSV-------LGLDG 413
Cdd:TIGR01855 33 EAELADKLILPGvgAFGA--------AMARLRENGLdlfvelvvrlgkPVLGICLGMQLL---FERSEegggvpgLGLIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 414 ANSTEFDPAT-PHpcvlympeisrthkggtmrLGVRRTFFQKPNCLTSKLYGNES--FVderhrHRYEVNPElvdrlEEA 490
Cdd:TIGR01855 102 GNVVKLEARKvPH-------------------MGWNEVHPVKESPLLNGIDEGAYfyFV-----HSYYAVCE-----EEA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1376929165 491 GLTFvgkdeTGRRMEIVELPEHKYFVGVQFHPEFKSRPGK 530
Cdd:TIGR01855 153 VLAY-----ADYGEKFPAAVQKGNIFGTQFHPEKSGKTGL 187
|
|
| hisH |
PRK13146 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
314-431 |
3.93e-05 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237290 [Multi-domain] Cd Length: 209 Bit Score: 45.16 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 314 SVLKALTHAslACGRKLVIewvasTDledgsprDLHDAAWAalksvDGILVPG---------GFGDRGTQGKVLAAkyAR 384
Cdd:PRK13146 16 SAAKALERA--GAGADVVV-----TA-------DPDAVAAA-----DRVVLPGvgafadcmrGLRAVGLGEAVIEA--VL 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1376929165 385 ENNVPYLGVCLGMQIAvieFARSV-------LGLDGANSTEFDPATPHPCVLYM 431
Cdd:PRK13146 75 AAGRPFLGICVGMQLL---FERGLehgdtpgLGLIPGEVVRFQPDGPALKVPHM 125
|
|
| GATase1_Glutamyl_Hydrolase |
cd01747 |
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ... |
356-523 |
5.22e-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: 42.31 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 356 LKSVDGILVPGGFGDRGTQGKVLAAK----YARENN-----VPYLGVCLGMQIAVIEFARSVLGLDGANSTEFdpATPhp 426
Cdd:cd01747 52 FKSINGILFPGGAVDIDTSGYARTAKiiynLALERNdagdyFPVWGTCLGFELLTYLTSGETLLLEATEATNS--ALP-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 427 cvLYMPEISRthkggtmrlgVRRTFFQKPNCLTSKLyGNESFVdeRHRHRYEVNPElvdRLEEAGLT--F-----VGKDE 499
Cdd:cd01747 128 --LNFTEDAL----------QSRLFKRFPPDLLKSL-ATEPLT--MNNHRYGISPE---NFTENGLLsdFfnvltTNDDW 189
|
170 180
....*....|....*....|....*.
gi 1376929165 500 TGrrMEIVELPEH-KY-FVGVQFHPE 523
Cdd:cd01747 190 NG--VEFISTVEAyKYpIYGVQWHPE 213
|
|
| hisH |
PRK13143 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
314-530 |
8.90e-04 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237289 [Multi-domain] Cd Length: 200 Bit Score: 41.01 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 314 SVLKALTHAslacGRKLVIewvaSTDLEDgsprdlhdaawaaLKSVDGILVPG--GFGD-----RGTQGKVLAAkyaREN 386
Cdd:PRK13143 15 SVSKALERA----GAEVVI----TSDPEE-------------ILDADGIVLPGvgAFGAamenlSPLRDVILEA---ARS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 387 NVPYLGVCLGMQIAvieFARS-----VLGLD---GANsTEFDPA--TPHpcvlympeisrthkggtmrLGVRRTFFQKPN 456
Cdd:PRK13143 71 GKPFLGICLGMQLL---FESSeegggVRGLGlfpGRV-VRFPAGvkVPH-------------------MGWNTVKVVKDC 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1376929165 457 CLTSKLygNES---FVderhrHRYEVNPELVDRleeagltFVGKDETGRRMEIVELPEHKYfvGVQFHPEFKSRPGK 530
Cdd:PRK13143 128 PLFEGI--DGEyvyFV-----HSYYAYPDDEDY-------VVATTDYGIEFPAAVCNDNVF--GTQFHPEKSGETGL 188
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
356-524 |
6.69e-03 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153216 [Multi-domain] Cd Length: 189 Bit Score: 38.33 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 356 LKSVDGILVPGG--------FGDRGTQGKVLA----------AKYARENNVPYLGVCLGMQ-IAViefarsvlgldgans 416
Cdd:cd01745 51 LELLDGLLLTGGgdvdpplyGEEPHPELGPIDperdafelalLRAALERGKPILGICRGMQlLNV--------------- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376929165 417 tefdpatphpcvlympeisrtHKGGTMR--LGVrrtffqkpNCLtsklygnesfvderhrHRYevnpeLVDRLEEaGLTF 494
Cdd:cd01745 116 ---------------------ALGGTLYqdIRV--------NSL----------------HHQ-----AIKRLAD-GLRV 144
|
170 180 190
....*....|....*....|....*....|
gi 1376929165 495 VGKDETGRrMEIVELPEHKYFVGVQFHPEF 524
Cdd:cd01745 145 EARAPDGV-IEAIESPDRPFVLGVQWHPEW 173
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
349-423 |
7.45e-03 |
|
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 129966 [Multi-domain] Cd Length: 188 Bit Score: 38.06 E-value: 7.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1376929165 349 HDAAWAALKSVD--GILVPGGFGDRGTQGKVLAAKYARENNVPYLGVCLGMQIAVIEFARSVlglDGANSTEFDPAT 423
Cdd:TIGR00888 30 NTTPLEEIREKNpkGIILSGGPSSVYAENAPRADEKIFELGVPVLGICYGMQLMAKQLGGEV---GRAEKREYGKAE 103
|
|
| |
