|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02327 |
PLN02327 |
CTP synthase |
1-556 |
0e+00 |
|
CTP synthase
Pssm-ID: 215186 [Multi-domain] Cd Length: 557 Bit Score: 900.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 1 MKYILVTGGVISGVGKGVIASSFGTLLKSCGLDVTSIKIDPYINIDAGTFSPYEHGEVYVLDDGAEVDLDLGNYERFLDV 80
Cdd:PLN02327 1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 81 TLHRDNNITTGKIYKLVIEKERTGEYLGKTVQVVPHITDAIQEWVERVAQTPVQGSSKP-QVCIVELGGTIGDIEGMPFV 159
Cdd:PLN02327 81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAKIPVDGKEGPaDVCVIELGGTVGDIESMPFI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 160 EAFRQFQFRVKRENFCLAHVSLVPLPKATGEPKTKPTQSSVRELRGCGLSPDLIVCRSEKPIGLEVKEKISNFCHVGPDQ 239
Cdd:PLN02327 161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 240 VICIHDLNSIYHVPLLM-EQNGVIEYLNerlQLNIDMSKRTKCLQQWRDLARRTETVRREVCIAVVGKYTKFTDSYASVV 318
Cdd:PLN02327 241 ILNLHDVSNIWHVPLLLrDQKAHEAILK---VLNLLSVAREPDLEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 319 KALQHAALAVNRKLELVFIESCLLEEETLHSEPSKYHKEWQKLCDSHGILVPGGFGSRGMEGKIRACQWARENQKPLLGI 398
Cdd:PLN02327 318 KALLHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 399 CLGLQAAVIEFARNKLGLKDANTTEIDPNTANALVIDMPEHHTGQLGGTMRLGKRITVFSDGPSVIRQLYGNPKSVQERH 478
Cdd:PLN02327 398 CLGMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDERH 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665410394 479 RHRYEVNPKYVHLLEEQGMRFVGTDVDKTRMEIIELSGHPYFVATQYHPEYLSRPLKPSPPFLGLILASVDRLNQYIQ 556
Cdd:PLN02327 478 RHRYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVLN 555
|
|
| PyrG |
COG0504 |
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ... |
1-550 |
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: 834.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 1 MKYILVTGGVISGVGKGVIASSFGTLLKSCGLDVTSIKIDPYINIDAGTFSPYEHGEVYVLDDGAEVDLDLGNYERFLDV 80
Cdd:COG0504 1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 81 TLHRDNNITTGKIYKLVIEKERTGEYLGKTVQVVPHITDAIQEWVERVAQTpvqgsSKPQVCIVELGGTIGDIEGMPFVE 160
Cdd:COG0504 81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAEE-----SGADVVIVEIGGTVGDIESLPFLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 161 AFRQFQFRVKRENFCLAHVSLVPLPKATGEPKTKPTQSSVRELRGCGLSPDLIVCRSEKPIGLEVKEKISNFCHVGPDQV 240
Cdd:COG0504 156 AIRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 241 ICIHDLNSIYHVPLLMEQNGVIEYLNERLQLN---IDMSKrtkclqqWRDLARRTETVRREVCIAVVGKYTKFTDSYASV 317
Cdd:COG0504 236 ISAPDVDSIYEVPLMLHEQGLDEIVLKKLGLEarePDLSE-------WEELVERIKNPKKEVTIALVGKYVELPDAYKSV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 318 VKALQHAALAVNRKLELVFIESCLLEEETLHSepskyhkewqKLCDSHGILVPGGFGSRGMEGKIRACQWARENQKPLLG 397
Cdd:COG0504 309 VEALKHAGIANGVKVNIKWIDSEDLEEENAEE----------LLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 398 ICLGLQAAVIEFARNKLGLKDANTTEIDPNTANAlVID-MPE-HHTGQLGGTMRLGKRITVFSDGpSVIRQLYGNPKsVQ 475
Cdd:COG0504 379 ICLGMQLAVIEFARNVLGLEDANSTEFDPNTPHP-VIDlMPEqKDVSDLGGTMRLGAYPCKLKPG-TLAAEAYGKEE-IS 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665410394 476 ERHRHRYEVNPKYVHLLEEQGMRFVGTDVDKTRMEIIELSGHPYFVATQYHPEYLSRPLKPSPPFLGLILASVDR 550
Cdd:COG0504 456 ERHRHRYEFNNEYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEY 530
|
|
| 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: 779.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 1 MKYILVTGGVISGVGKGVIASSFGTLLKSCGLDVTSIKIDPYINIDAGTFSPYEHGEVYVLDDGAEVDLDLGNYERFLDV 80
Cdd:TIGR00337 1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 81 TLHRDNNITTGKIYKLVIEKERTGEYLGKTVQVVPHITDAIQEWVERVAQtpvqgSSKPQVCIVELGGTIGDIEGMPFVE 160
Cdd:TIGR00337 81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAK-----ISGPDVVIVEIGGTVGDIESLPFLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 161 AFRQFQFRVKRENFCLAHVSLVPLPKATGEPKTKPTQSSVRELRGCGLSPDLIVCRSEKPIGLEVKEKISNFCHVGPDQV 240
Cdd:TIGR00337 156 AIRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 241 ICIHDLNSIYHVPLLMEQNGVIEYLNERLQLNIDMSKrtkcLQQWRDLARRTETVRREVCIAVVGKYTKFTDSYASVVKA 320
Cdd:TIGR00337 236 ISAKDVSSIYEVPLLLLKQGLDDYLCRRLNLNCDEAD----LSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 321 LQHAALAVNRKLELVFIESCLLEEETLhsepskyhkewQKLCDSHGILVPGGFGSRGMEGKIRACQWARENQKPLLGICL 400
Cdd:TIGR00337 312 LKHAGAKLDTKVNIKWIDSEDLEEEGV-----------EFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 401 GLQAAVIEFARNKLGLKDANTTEIDPNTANALVIDMPEH-HTGQLGGTMRLGKRITVFSDGpSVIRQLYGNPKsVQERHR 479
Cdd:TIGR00337 381 GMQLAVIEFARNVAGLEGANSTEFDPDTKYPVVDLLPEQkDISDLGGTMRLGLYPCILKPG-TLAFKLYGKEE-VYERHR 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665410394 480 HRYEVNPKYVHLLEEQGMRFVGTDVDKTRMEIIELSGHPYFVATQYHPEYLSRPLKPSPPFLGLILA 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 ... |
2-271 |
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: 537.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 2 KYILVTGGVISGVGKGVIASSFGTLLKSCGLDVTSIKIDPYINIDAGTFSPYEHGEVYVLDDGAEVDLDLGNYERFLDVT 81
Cdd:pfam06418 1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 82 LHRDNNITTGKIYKLVIEKERTGEYLGKTVQVVPHITDAIQEWVERVAQTpvqgsSKPQVCIVELGGTIGDIEGMPFVEA 161
Cdd:pfam06418 81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKE-----VGPDVVIVEIGGTVGDIESLPFLEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 162 FRQFQFRVKRENFCLAHVSLVPLPKATGEPKTKPTQSSVRELRGCGLSPDLIVCRSEKPIGLEVKEKISNFCHVGPDQVI 241
Cdd:pfam06418 156 IRQLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVI 235
|
250 260 270
....*....|....*....|....*....|
gi 665410394 242 CIHDLNSIYHVPLLMEQNGVIEYLNERLQL 271
Cdd:pfam06418 236 SAPDVSSIYEVPLLLEEQGLDDIILKRLNL 265
|
|
| CTPS_N |
cd03113 |
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ... |
2-267 |
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: 523.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 2 KYILVTGGVISGVGKGVIASSFGTLLKSCGLDVTSIKIDPYINIDAGTFSPYEHGEVYVLDDGAEVDLDLGNYERFLDVT 81
Cdd:cd03113 1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 82 LHRDNNITTGKIYKLVIEKERTGEYLGKTVQVVPHITDAIQEWVERVAQTPvqgssKPQVCIVELGGTIGDIEGMPFVEA 161
Cdd:cd03113 81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIP-----EPDVCIVEIGGTVGDIESLPFLEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 162 FRQFQFRVKRENFCLAHVSLVPLPKATGEPKTKPTQSSVRELRGCGLSPDLIVCRSEKPIGLEVKEKISNFCHVGPDQVI 241
Cdd:cd03113 156 LRQFQFEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVI 235
|
250 260
....*....|....*....|....*.
gi 665410394 242 CIHDLNSIYHVPLLMEQNGVIEYLNE 267
Cdd:cd03113 236 SVHDVSSIYEVPLLLEKQGLDDYILR 261
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02327 |
PLN02327 |
CTP synthase |
1-556 |
0e+00 |
|
CTP synthase
Pssm-ID: 215186 [Multi-domain] Cd Length: 557 Bit Score: 900.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 1 MKYILVTGGVISGVGKGVIASSFGTLLKSCGLDVTSIKIDPYINIDAGTFSPYEHGEVYVLDDGAEVDLDLGNYERFLDV 80
Cdd:PLN02327 1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 81 TLHRDNNITTGKIYKLVIEKERTGEYLGKTVQVVPHITDAIQEWVERVAQTPVQGSSKP-QVCIVELGGTIGDIEGMPFV 159
Cdd:PLN02327 81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAKIPVDGKEGPaDVCVIELGGTVGDIESMPFI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 160 EAFRQFQFRVKRENFCLAHVSLVPLPKATGEPKTKPTQSSVRELRGCGLSPDLIVCRSEKPIGLEVKEKISNFCHVGPDQ 239
Cdd:PLN02327 161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 240 VICIHDLNSIYHVPLLM-EQNGVIEYLNerlQLNIDMSKRTKCLQQWRDLARRTETVRREVCIAVVGKYTKFTDSYASVV 318
Cdd:PLN02327 241 ILNLHDVSNIWHVPLLLrDQKAHEAILK---VLNLLSVAREPDLEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 319 KALQHAALAVNRKLELVFIESCLLEEETLHSEPSKYHKEWQKLCDSHGILVPGGFGSRGMEGKIRACQWARENQKPLLGI 398
Cdd:PLN02327 318 KALLHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 399 CLGLQAAVIEFARNKLGLKDANTTEIDPNTANALVIDMPEHHTGQLGGTMRLGKRITVFSDGPSVIRQLYGNPKSVQERH 478
Cdd:PLN02327 398 CLGMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDERH 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665410394 479 RHRYEVNPKYVHLLEEQGMRFVGTDVDKTRMEIIELSGHPYFVATQYHPEYLSRPLKPSPPFLGLILASVDRLNQYIQ 556
Cdd:PLN02327 478 RHRYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVLN 555
|
|
| PyrG |
COG0504 |
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ... |
1-550 |
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: 834.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 1 MKYILVTGGVISGVGKGVIASSFGTLLKSCGLDVTSIKIDPYINIDAGTFSPYEHGEVYVLDDGAEVDLDLGNYERFLDV 80
Cdd:COG0504 1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 81 TLHRDNNITTGKIYKLVIEKERTGEYLGKTVQVVPHITDAIQEWVERVAQTpvqgsSKPQVCIVELGGTIGDIEGMPFVE 160
Cdd:COG0504 81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAEE-----SGADVVIVEIGGTVGDIESLPFLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 161 AFRQFQFRVKRENFCLAHVSLVPLPKATGEPKTKPTQSSVRELRGCGLSPDLIVCRSEKPIGLEVKEKISNFCHVGPDQV 240
Cdd:COG0504 156 AIRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 241 ICIHDLNSIYHVPLLMEQNGVIEYLNERLQLN---IDMSKrtkclqqWRDLARRTETVRREVCIAVVGKYTKFTDSYASV 317
Cdd:COG0504 236 ISAPDVDSIYEVPLMLHEQGLDEIVLKKLGLEarePDLSE-------WEELVERIKNPKKEVTIALVGKYVELPDAYKSV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 318 VKALQHAALAVNRKLELVFIESCLLEEETLHSepskyhkewqKLCDSHGILVPGGFGSRGMEGKIRACQWARENQKPLLG 397
Cdd:COG0504 309 VEALKHAGIANGVKVNIKWIDSEDLEEENAEE----------LLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 398 ICLGLQAAVIEFARNKLGLKDANTTEIDPNTANAlVID-MPE-HHTGQLGGTMRLGKRITVFSDGpSVIRQLYGNPKsVQ 475
Cdd:COG0504 379 ICLGMQLAVIEFARNVLGLEDANSTEFDPNTPHP-VIDlMPEqKDVSDLGGTMRLGAYPCKLKPG-TLAAEAYGKEE-IS 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665410394 476 ERHRHRYEVNPKYVHLLEEQGMRFVGTDVDKTRMEIIELSGHPYFVATQYHPEYLSRPLKPSPPFLGLILASVDR 550
Cdd:COG0504 456 ERHRHRYEFNNEYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEY 530
|
|
| pyrG |
PRK05380 |
CTP synthetase; Validated |
1-550 |
0e+00 |
|
CTP synthetase; Validated
Pssm-ID: 235437 [Multi-domain] Cd Length: 533 Bit Score: 826.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 1 MKYILVTGGVISGVGKGVIASSFGTLLKSCGLDVTSIKIDPYINIDAGTFSPYEHGEVYVLDDGAEVDLDLGNYERFLDV 80
Cdd:PRK05380 2 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 81 TLHRDNNITTGKIYKLVIEKERTGEYLGKTVQVVPHITDAIQEWVERVAqtpvqgsSKPQVCIVELGGTIGDIEGMPFVE 160
Cdd:PRK05380 82 NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAG-------TDADVVIVEIGGTVGDIESLPFLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 161 AFRQFQFRVKRENFCLAHVSLVPLPKATGEPKTKPTQSSVRELRGCGLSPDLIVCRSEKPIGLEVKEKISNFCHVGPDQV 240
Cdd:PRK05380 155 AIRQLRLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 241 ICIHDLNSIYHVPLLMEQNGVIEYLNERLQLN---IDMSKrtkclqqWRDLARRTETVRREVCIAVVGKYTKFTDSYASV 317
Cdd:PRK05380 235 ISAPDVDSIYEVPLLLHEQGLDDIVLERLGLEapePDLSE-------WEELVERLKNPKGEVTIALVGKYVELPDAYKSV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 318 VKALQHAALAVNRKLELVFIESCLLEEETLHSepskyhkewqKLCDSHGILVPGGFGSRGMEGKIRACQWARENQKPLLG 397
Cdd:PRK05380 308 IEALKHAGIANDVKVNIKWIDSEDLEEENVAE----------LLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 398 ICLGLQAAVIEFARNKLGLKDANTTEIDPNTANAlVID-MPEHHT-GQLGGTMRLGKRITVFSDGpSVIRQLYGNpKSVQ 475
Cdd:PRK05380 378 ICLGMQLAVIEFARNVLGLEDANSTEFDPDTPHP-VIDlMPEQKDvSDLGGTMRLGAYPCKLKPG-TLAAEIYGK-EEIY 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665410394 476 ERHRHRYEVNPKYVHLLEEQGMRFVGTDVDKTRMEIIELSGHPYFVATQYHPEYLSRPLKPSPPFLGLILASVDR 550
Cdd:PRK05380 455 ERHRHRYEVNNKYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALEN 529
|
|
| 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: 779.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 1 MKYILVTGGVISGVGKGVIASSFGTLLKSCGLDVTSIKIDPYINIDAGTFSPYEHGEVYVLDDGAEVDLDLGNYERFLDV 80
Cdd:TIGR00337 1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 81 TLHRDNNITTGKIYKLVIEKERTGEYLGKTVQVVPHITDAIQEWVERVAQtpvqgSSKPQVCIVELGGTIGDIEGMPFVE 160
Cdd:TIGR00337 81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAK-----ISGPDVVIVEIGGTVGDIESLPFLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 161 AFRQFQFRVKRENFCLAHVSLVPLPKATGEPKTKPTQSSVRELRGCGLSPDLIVCRSEKPIGLEVKEKISNFCHVGPDQV 240
Cdd:TIGR00337 156 AIRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 241 ICIHDLNSIYHVPLLMEQNGVIEYLNERLQLNIDMSKrtkcLQQWRDLARRTETVRREVCIAVVGKYTKFTDSYASVVKA 320
Cdd:TIGR00337 236 ISAKDVSSIYEVPLLLLKQGLDDYLCRRLNLNCDEAD----LSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 321 LQHAALAVNRKLELVFIESCLLEEETLhsepskyhkewQKLCDSHGILVPGGFGSRGMEGKIRACQWARENQKPLLGICL 400
Cdd:TIGR00337 312 LKHAGAKLDTKVNIKWIDSEDLEEEGV-----------EFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 401 GLQAAVIEFARNKLGLKDANTTEIDPNTANALVIDMPEH-HTGQLGGTMRLGKRITVFSDGpSVIRQLYGNPKsVQERHR 479
Cdd:TIGR00337 381 GMQLAVIEFARNVAGLEGANSTEFDPDTKYPVVDLLPEQkDISDLGGTMRLGLYPCILKPG-TLAFKLYGKEE-VYERHR 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665410394 480 HRYEVNPKYVHLLEEQGMRFVGTDVDKTRMEIIELSGHPYFVATQYHPEYLSRPLKPSPPFLGLILA 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 ... |
2-271 |
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: 537.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 2 KYILVTGGVISGVGKGVIASSFGTLLKSCGLDVTSIKIDPYINIDAGTFSPYEHGEVYVLDDGAEVDLDLGNYERFLDVT 81
Cdd:pfam06418 1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 82 LHRDNNITTGKIYKLVIEKERTGEYLGKTVQVVPHITDAIQEWVERVAQTpvqgsSKPQVCIVELGGTIGDIEGMPFVEA 161
Cdd:pfam06418 81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKE-----VGPDVVIVEIGGTVGDIESLPFLEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 162 FRQFQFRVKRENFCLAHVSLVPLPKATGEPKTKPTQSSVRELRGCGLSPDLIVCRSEKPIGLEVKEKISNFCHVGPDQVI 241
Cdd:pfam06418 156 IRQLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVI 235
|
250 260 270
....*....|....*....|....*....|
gi 665410394 242 CIHDLNSIYHVPLLMEQNGVIEYLNERLQL 271
Cdd:pfam06418 236 SAPDVSSIYEVPLLLEEQGLDDIILKRLNL 265
|
|
| CTPS_N |
cd03113 |
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ... |
2-267 |
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: 523.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 2 KYILVTGGVISGVGKGVIASSFGTLLKSCGLDVTSIKIDPYINIDAGTFSPYEHGEVYVLDDGAEVDLDLGNYERFLDVT 81
Cdd:cd03113 1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 82 LHRDNNITTGKIYKLVIEKERTGEYLGKTVQVVPHITDAIQEWVERVAQTPvqgssKPQVCIVELGGTIGDIEGMPFVEA 161
Cdd:cd03113 81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIP-----EPDVCIVEIGGTVGDIESLPFLEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 162 FRQFQFRVKRENFCLAHVSLVPLPKATGEPKTKPTQSSVRELRGCGLSPDLIVCRSEKPIGLEVKEKISNFCHVGPDQVI 241
Cdd:cd03113 156 LRQFQFEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVI 235
|
250 260
....*....|....*....|....*.
gi 665410394 242 CIHDLNSIYHVPLLMEQNGVIEYLNE 267
Cdd:cd03113 236 SVHDVSSIYEVPLLLEKQGLDDYILR 261
|
|
| GATase1_CTP_Synthase |
cd01746 |
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ... |
299-544 |
1.90e-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: 392.69 E-value: 1.90e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 299 VCIAVVGKYTKFTDSYASVVKALQHAALAVNRKLELVFIESCLLEEETLhsepskyhkeWQKLCDSHGILVPGGFGSRGM 378
Cdd:cd01746 1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEEENA----------EEALKGADGILVPGGFGIRGV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 379 EGKIRACQWARENQKPLLGICLGLQAAVIEFARNKLGLKDANTTEIDPNTANALVIDMPE-HHTGQLGGTMRLGKRITVF 457
Cdd:cd01746 71 EGKILAIKYARENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEqKGVKDLGGTMRLGAYPVIL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 458 SDGPSVirQLYGNPKSVQERHRHRYEVNPKYVHLLEEQGMRFVGTDVDKTRMEIIELSGHPYFVATQYHPEYLSRPLKPS 537
Cdd:cd01746 151 KPGTLA--HKYYGKDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPEFKSRPLKPH 228
|
....*..
gi 665410394 538 PPFLGLI 544
Cdd:cd01746 229 PLFVGFV 235
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
312-546 |
1.12e-36 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 135.44 E-value: 1.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 312 DSYASVVKALQHAALAVNRKLELVFIESCLleEETLHSEPskyhkewqklcdsHGILVPGGFGSRG-MEGKIRACQWARE 390
Cdd:pfam00117 4 DNGDSFTYNLARALRELGVEVTVVPNDTPA--EEILEENP-------------DGIILSGGPGSPGaAGGAIEAIREARE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 391 NQKPLLGICLGLQAAVIEFARNklglkdantteidpntanalVIDMP--EHHtgqlGGTMRLGKRITvfsdgpsviRQLY 468
Cdd:pfam00117 69 LKIPILGICLGHQLLALAFGGK--------------------VVKAKkfGHH----GKNSPVGDDGC---------GLFY 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665410394 469 GNPKSVQERHRHRYEVNPKyvhlLEEQGMRFVGTDV-DKTRMEIIELSGHpyFVATQYHPEYLSRPLKPSPPFLGLILA 546
Cdd:pfam00117 116 GLPNVFIVRRYHSYAVDPD----TLPDGLEVTATSEnDGTIMGIRHKKLP--IFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| PRK06186 |
PRK06186 |
hypothetical protein; Validated |
301-538 |
3.28e-33 |
|
hypothetical protein; Validated
Pssm-ID: 180452 [Multi-domain] Cd Length: 229 Bit Score: 127.00 E-value: 3.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 301 IAVVGKYTKFTDSYASVVKALQHAALAVNRKLELVFIESclleeETLHSEPSkyhkewqkLCDSHGI-LVPGgfgS--RG 377
Cdd:PRK06186 4 IALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPT-----PEITDPED--------LAGFDGIwCVPG---SpyRN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 378 MEGKIRACQWARENQKPLLGICLGLQAAVIEFARNKLGLKDANTTEIDPNTANALVIDMPEHHTGQLGgtmrlgkRITVF 457
Cdd:PRK06186 68 DDGALTAIRFARENGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEGDRPVIAPLSCSLVEKTG-------DIRLR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 458 SDgpSVIRQLYGNPKSVqERHRHRYEVNPKYVHLLEEQGMRFVGTDVDKtrmEI--IELSGHPYFVATQYHPEYLSRPLK 535
Cdd:PRK06186 141 PG--SLIARAYGTLEIE-EGYHCRYGVNPEFVAALESGDLRVTGWDEDG---DVraVELPGHPFFVATLFQPERAALAGR 214
|
...
gi 665410394 536 PSP 538
Cdd:PRK06186 215 PPP 217
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
301-407 |
1.02e-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: 59.15 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 301 IAVVGKYTKFTDSYASVVKALQHAALAVnrklelvfiesclleeeTLHSEPSKYHKEWQKLCDSHGILVPGGFGS----R 376
Cdd:cd01653 1 VAVLLFPGFEELELASPLDALREAGAEV-----------------DVVSPDGGPVESDVDLDDYDGLILPGGPGTpddlA 63
|
90 100 110
....*....|....*....|....*....|.
gi 665410394 377 GMEGKIRACQWARENQKPLLGICLGLQAAVI 407
Cdd:cd01653 64 RDEALLALLREAAAAGKPILGICLGAQLLVL 94
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
301-404 |
2.96e-09 |
|
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: 54.51 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 301 IAVVGKYTKFTDSYASVVKALQHAALAVnrklelvfiesclleeeTLHSEPSKYHKEWQKLCDSHGILVPGGFGS----R 376
Cdd:cd03128 1 VAVLLFGGSEELELASPLDALREAGAEV-----------------DVVSPDGGPVESDVDLDDYDGLILPGGPGTpddlA 63
|
90 100
....*....|....*....|....*...
gi 665410394 377 GMEGKIRACQWARENQKPLLGICLGLQA 404
Cdd:cd03128 64 WDEALLALLREAAAAGKPVLGICLGAQL 91
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
2-48 |
3.88e-04 |
|
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: 40.11 E-value: 3.88e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 665410394 2 KYILVTGGViSGVGKGVIASSFGTLLKSCGLDVTSIKIDPYINIDAG 48
Cdd:cd01983 1 RVIAVTGGK-GGVGKTTLAAALAVALAAKGYKVLLIDLDDYVLIDGG 46
|
|
| hisH |
PRK13141 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
359-403 |
2.24e-03 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 39.73 E-value: 2.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 665410394 359 QKLCDSHGILVPG--GFG-------SRGMEGKIRacQWArENQKPLLGICLGLQ 403
Cdd:PRK13141 33 EEILAADGVILPGvgAFPdamanlrERGLDEVIK--EAV-ASGKPLLGICLGMQ 83
|
|
| HisH |
COG0118 |
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
316-403 |
2.72e-03 |
|
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: 39.25 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410394 316 SVVKALQHAALAVnrklelvfiesclleeeTLHSEPskyhkewQKLCDSHGILVPG-G-FGS-------RGMEGKIRAcq 386
Cdd:COG0118 15 SVAKALERLGAEV-----------------VVTSDP-------DEIRAADRLVLPGvGaFGDamenlreRGLDEAIRE-- 68
|
90
....*....|....*..
gi 665410394 387 wARENQKPLLGICLGLQ 403
Cdd:COG0118 69 -AVAGGKPVLGICLGMQ 84
|
|
| |
