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Conserved domains on  [gi|1370452107|ref|XP_024309320|]
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CTP synthase 1 isoform X1 [Homo sapiens]

Protein Classification

CTP synthase( domain architecture ID 11476640)

cytidine triphosphate (CTP) synthase catalyzes the conversion of UTP to CTP in the last committed step in pyrimidine nucleotide biosynthesis

CATH:  3.40.50.880
EC:  6.3.4.2
Gene Ontology:  GO:0003883|GO:0005524|GO:0006241|GO:0042802

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02327 PLN02327
CTP synthase
 8-563 0e+00

CTP synthase


:

Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 954.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107   8 MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDI 87
Cdd:PLN02327    1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107  88 RLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFI 167
Cdd:PLN02327   81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAKIPVDGKEGPADVCVIELGGTVGDIESMPFI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 168 EAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ 247
Cdd:PLN02327  161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 248 VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLP-IERQPRkmLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYASVIK 326
Cdd:PLN02327  241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLsVAREPD--LEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLK 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 327 ALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVC 406
Cdd:PLN02327  319 ALLHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGIC 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 407 LGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLEERHR 486
Cdd:PLN02327  399 LGMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDERHR 478

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370452107 487 HRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGRLSHYLQ 563
Cdd:PLN02327  479 HRYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVLN 555
 
Name Accession Description Interval E-value
PLN02327 PLN02327
CTP synthase
 8-563 0e+00

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 954.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107   8 MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDI 87
Cdd:PLN02327    1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107  88 RLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFI 167
Cdd:PLN02327   81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAKIPVDGKEGPADVCVIELGGTVGDIESMPFI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 168 EAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ 247
Cdd:PLN02327  161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 248 VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLP-IERQPRkmLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYASVIK 326
Cdd:PLN02327  241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLsVAREPD--LEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLK 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 327 ALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVC 406
Cdd:PLN02327  319 ALLHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGIC 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 407 LGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLEERHR 486
Cdd:PLN02327  399 LGMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDERHR 478

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370452107 487 HRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGRLSHYLQ 563
Cdd:PLN02327  479 HRYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVLN 555
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 8-557 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: 854.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107   8 MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDI 87
Cdd:COG0504     1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107  88 RLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQAlipvDEDGLEpqVCVIELGGTVGDIESMPFI 167
Cdd:COG0504    81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAA----EESGAD--VVIVEIGGTVGDIESLPFL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 168 EAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ 247
Cdd:COG0504   155 EAIRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 248 VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPiERQPRkmLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYASVIKA 327
Cdd:COG0504   235 VISAPDVDSIYEVPLMLHEQGLDEIVLKKLGLE-AREPD--LSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEA 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 328 LEHSALAINHKLEIKYIDSADLEPitsqeepvryHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCL 407
Cdd:COG0504   312 LKHAGIANGVKVNIKWIDSEDLEE----------ENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICL 381

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 408 GMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPE-HNPGQMGGTMRLGKRR-TLfqTKNSVMRKLYGdADYLEERH 485
Cdd:COG0504   382 GMQLAVIEFARNVLGLEDANSTEFDPNTPHPVIDLMPEqKDVSDLGGTMRLGAYPcKL--KPGTLAAEAYG-KEEISERH 458

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370452107 486 RHRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGR 557
Cdd:COG0504   459 RHRYEFNNEYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEY 530
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 8-553 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: 803.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107   8 MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDI 87
Cdd:TIGR00337   1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107  88 RLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQAlipvdeDGLEPQVCVIELGGTVGDIESMPFI 167
Cdd:TIGR00337  81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVA------KISGPDVVIVEIGGTVGDIESLPFL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 168 EAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ 247
Cdd:TIGR00337 155 EAIRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 248 VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPiERQPRkmLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYASVIKA 327
Cdd:TIGR00337 235 VISAKDVSSIYEVPLLLLKQGLDDYLCRRLNLN-CDEAD--LSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEA 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 328 LEHSALAINHKLEIKYIDSADLEPitsqeepvryhEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCL 407
Cdd:TIGR00337 312 LKHAGAKLDTKVNIKWIDSEDLEE-----------EGVEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICL 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 408 GMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPEHNP-GQMGGTMRLGKRRTLFQtKNSVMRKLYGDaDYLEERHR 486
Cdd:TIGR00337 381 GMQLAVIEFARNVAGLEGANSTEFDPDTKYPVVDLLPEQKDiSDLGGTMRLGLYPCILK-PGTLAFKLYGK-EEVYERHR 458

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370452107 487 HRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLA 553
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 ...
 9-279 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: 570.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107   9 KYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDIR 88
Cdd:pfam06418   1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107  89 LTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQALIpvdedgLEPQVCVIELGGTVGDIESMPFIE 168
Cdd:pfam06418  81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKE------VGPDVVIVEIGGTVGDIESLPFLE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 169 AFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQV 248
Cdd:pfam06418 155 AIRQLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAV 234

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1370452107 249 ICVHDVSSIYRVPLLLEEQGVVDYFLRRLDL 279
Cdd:pfam06418 235 ISAPDVSSIYEVPLLLEEQGLDDIILKRLNL 265
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
 9-275 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: 544.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107   9 KYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDIR 88
Cdd:cd03113     1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107  89 LTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQALIPvdedglEPQVCVIELGGTVGDIESMPFIE 168
Cdd:cd03113    81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIP------EPDVCIVEIGGTVGDIESLPFLE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 169 AFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQV 248
Cdd:cd03113   155 ALRQFQFEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAV 234

                         250       260
                  ....*....|....*....|....*..
gi 1370452107 249 ICVHDVSSIYRVPLLLEEQGVVDYFLR 275
Cdd:cd03113   235 ISVHDVSSIYEVPLLLEKQGLDDYILR 261
 
Name Accession Description Interval E-value
PLN02327 PLN02327
CTP synthase
 8-563 0e+00

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 954.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107   8 MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDI 87
Cdd:PLN02327    1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107  88 RLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFI 167
Cdd:PLN02327   81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAKIPVDGKEGPADVCVIELGGTVGDIESMPFI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 168 EAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ 247
Cdd:PLN02327  161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 248 VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLP-IERQPRkmLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYASVIK 326
Cdd:PLN02327  241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLsVAREPD--LEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLK 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 327 ALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVC 406
Cdd:PLN02327  319 ALLHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGIC 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 407 LGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLEERHR 486
Cdd:PLN02327  399 LGMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDERHR 478

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370452107 487 HRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGRLSHYLQ 563
Cdd:PLN02327  479 HRYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVLN 555
pyrG PRK05380
CTP synthetase; Validated
 7-557 0e+00

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 857.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107   7 KMKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLD 86
Cdd:PRK05380    1 MTKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107  87 IRLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQAlipvdedgLEPQVCVIELGGTVGDIESMPF 166
Cdd:PRK05380   81 TNLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAG--------TDADVVIVEIGGTVGDIESLPF 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 167 IEAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPE 246
Cdd:PRK05380  153 LEAIRQLRLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEE 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 247 QVICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPIeRQPRkmLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYASVIK 326
Cdd:PRK05380  233 AVISAPDVDSIYEVPLLLHEQGLDDIVLERLGLEA-PEPD--LSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIE 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 327 ALEHSALAINHKLEIKYIDSADLEPitsqeepvryHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVC 406
Cdd:PRK05380  310 ALKHAGIANDVKVNIKWIDSEDLEE----------ENVAELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGIC 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 407 LGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPE-HNPGQMGGTMRLGKRRTLFQtKNSVMRKLYGdADYLEERH 485
Cdd:PRK05380  380 LGMQLAVIEFARNVLGLEDANSTEFDPDTPHPVIDLMPEqKDVSDLGGTMRLGAYPCKLK-PGTLAAEIYG-KEEIYERH 457

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370452107 486 RHRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGR 557
Cdd:PRK05380  458 RHRYEVNNKYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALEN 529
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 8-557 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: 854.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107   8 MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDI 87
Cdd:COG0504     1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107  88 RLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQAlipvDEDGLEpqVCVIELGGTVGDIESMPFI 167
Cdd:COG0504    81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAA----EESGAD--VVIVEIGGTVGDIESLPFL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 168 EAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ 247
Cdd:COG0504   155 EAIRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 248 VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPiERQPRkmLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYASVIKA 327
Cdd:COG0504   235 VISAPDVDSIYEVPLMLHEQGLDEIVLKKLGLE-AREPD--LSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEA 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 328 LEHSALAINHKLEIKYIDSADLEPitsqeepvryHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCL 407
Cdd:COG0504   312 LKHAGIANGVKVNIKWIDSEDLEE----------ENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICL 381

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 408 GMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPE-HNPGQMGGTMRLGKRR-TLfqTKNSVMRKLYGdADYLEERH 485
Cdd:COG0504   382 GMQLAVIEFARNVLGLEDANSTEFDPNTPHPVIDLMPEqKDVSDLGGTMRLGAYPcKL--KPGTLAAEAYG-KEEISERH 458

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370452107 486 RHRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGR 557
Cdd:COG0504   459 RHRYEFNNEYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEY 530
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 8-553 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: 803.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107   8 MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDI 87
Cdd:TIGR00337   1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107  88 RLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQAlipvdeDGLEPQVCVIELGGTVGDIESMPFI 167
Cdd:TIGR00337  81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVA------KISGPDVVIVEIGGTVGDIESLPFL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 168 EAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ 247
Cdd:TIGR00337 155 EAIRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 248 VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPiERQPRkmLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYASVIKA 327
Cdd:TIGR00337 235 VISAKDVSSIYEVPLLLLKQGLDDYLCRRLNLN-CDEAD--LSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEA 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 328 LEHSALAINHKLEIKYIDSADLEPitsqeepvryhEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCL 407
Cdd:TIGR00337 312 LKHAGAKLDTKVNIKWIDSEDLEE-----------EGVEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICL 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 408 GMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPEHNP-GQMGGTMRLGKRRTLFQtKNSVMRKLYGDaDYLEERHR 486
Cdd:TIGR00337 381 GMQLAVIEFARNVAGLEGANSTEFDPDTKYPVVDLLPEQKDiSDLGGTMRLGLYPCILK-PGTLAFKLYGK-EEVYERHR 458

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370452107 487 HRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLA 553
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 ...
 9-279 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: 570.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107   9 KYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDIR 88
Cdd:pfam06418   1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107  89 LTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQALIpvdedgLEPQVCVIELGGTVGDIESMPFIE 168
Cdd:pfam06418  81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKE------VGPDVVIVEIGGTVGDIESLPFLE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 169 AFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQV 248
Cdd:pfam06418 155 AIRQLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAV 234

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1370452107 249 ICVHDVSSIYRVPLLLEEQGVVDYFLRRLDL 279
Cdd:pfam06418 235 ISAPDVSSIYEVPLLLEEQGLDDIILKRLNL 265
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
 9-275 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: 544.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107   9 KYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDIR 88
Cdd:cd03113     1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107  89 LTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQALIPvdedglEPQVCVIELGGTVGDIESMPFIE 168
Cdd:cd03113    81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIP------EPDVCIVEIGGTVGDIESLPFLE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 169 AFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQV 248
Cdd:cd03113   155 ALRQFQFEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAV 234

                         250       260
                  ....*....|....*....|....*..
gi 1370452107 249 ICVHDVSSIYRVPLLLEEQGVVDYFLR 275
Cdd:cd03113   235 ISVHDVSSIYEVPLLLEKQGLDDYILR 261
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 306-551 3.87e-139

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: 403.86  E-value: 3.87e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 306 CSIALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSADLEPITsqeepvryheAWQKLCSAHGVLVPGGFGVRGT 385
Cdd:cd01746     1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEEEN----------AEEALKGADGILVPGGFGIRGV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 386 EGKIQAIAWARNQKKPFLGVCLGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPE-HNPGQMGGTMRLGKRRTLF 464
Cdd:cd01746    71 EGKILAIKYARENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEqKGVKDLGGTMRLGAYPVIL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 465 QtKNSVMRKLYGdADYLEERHRHRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPS 544
Cdd:cd01746   151 K-PGTLAHKYYG-KDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPEFKSRPLKPH 228


                  ....*..
gi 1370452107 545 PPYFGLL 551
Cdd:cd01746   229 PLFVGFV 235
GATase pfam00117
Glutamine amidotransferase class-I;
319-553 2.14e-37

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 136.98  E-value: 2.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 319 DSYASVIKALEHSALAINHKLEIKYIDSADLEPItsQEEPvryheawqklcsaHGVLVPGGFGVRGT-EGKIQAIAWARN 397
Cdd:pfam00117   4 DNGDSFTYNLARALRELGVEVTVVPNDTPAEEIL--EENP-------------DGIILSGGPGSPGAaGGAIEAIREARE 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 398 QKKPFLGVCLGMQLAVVEFSRNVLgwqdanstefdpttshpvvvdmPEHNPGQMGGTMRLGKRRTlfqtknsvmRKLYGD 477
Cdd:pfam00117  69 LKIPILGICLGHQLLALAFGGKVV----------------------KAKKFGHHGKNSPVGDDGC---------GLFYGL 117

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370452107 478 ADYLEERHRHRFEVNPVwkkcLEEQGLKFVGQDVEGE-RMEIVELEDhPFFvGVQYHPEFLSRPIKPSPPYFGLLLA 553
Cdd:pfam00117 118 PNVFIVRRYHSYAVDPD----TLPDGLEVTATSENDGtIMGIRHKKL-PIF-GVQFHPESILTPHGPEILFNFFIKA 188
PRK06186 PRK06186
hypothetical protein; Validated
 305-557 7.15e-37

hypothetical protein; Validated


Pssm-ID: 180452 [Multi-domain]  Cd Length: 229  Bit Score: 137.02  E-value: 7.15e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 305 TCSIALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSADlepITSQEEPVRYHEAWqklcsahgvLVPGGfGVRG 384
Cdd:PRK06186    1 TLRIALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPTPE---ITDPEDLAGFDGIW---------CVPGS-PYRN 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 385 TEGKIQAIAWARNQKKPFLGVCLGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMP----EHNpgqmgGTMRLgkr 460
Cdd:PRK06186   68 DDGALTAIRFARENGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEGDRPVIAPLScslvEKT-----GDIRL--- 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 461 rtlfqTKNSVMRKLYGdADYLEERHRHRFEVNPVWKKCLEEQGLKFVGQDVEGErMEIVELEDHPFFVGVQYHPEFLSRP 540
Cdd:PRK06186  140 -----RPGSLIARAYG-TLEIEEGYHCRYGVNPEFVAALESGDLRVTGWDEDGD-VRAVELPGHPFFVATLFQPERAALA 212

                         250
                  ....*....|....*..
gi 1370452107 541 IKPSPPYFGLLLASVGR 557
Cdd:PRK06186  213 GRPPPLVRAFLRAARAA 229
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 389-557 8.54e-13

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: 68.27  E-value: 8.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 389 IQAIAWARNQKKPFLGVCLGMQLAVVefsrnVLG---WQDaNSTEFDPTTSH--PVVVDMPEHnpgqmggTMRLgkrrtl 463
Cdd:COG2071    86 LALIRAALERGKPVLGICRGMQLLNV-----ALGgtlYQD-LPDQVPGALDHrqPAPRYAPRH-------TVEI------ 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 464 fqTKNSVMRKLYGdadyleerhRHRFEVNpvwkkCLEEQGLKFVGQD-----------VEGermeiVELEDHPFFVGVQY 532
Cdd:COG2071   147 --EPGSRLARILG---------EEEIRVN-----SLHHQAVKRLGPGlrvsarapdgvIEA-----IESPGAPFVLGVQW 205

                         170       180
                  ....*....|....*....|....*
gi 1370452107 533 HPEFLSRPIKPSPPYFGLLLASVGR 557
Cdd:COG2071   206 HPEWLAASDPLSRRLFEAFVEAARA 230
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 308-414 1.39e-11

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: 61.85  E-value: 1.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 308 IALVGKYTKFSDSYASVIKALEHsalainHKLEIKYIdSADLEPITSQEEPVRYHeawqklcsahGVLVPGGFGVRGT-- 385
Cdd:cd01653     1 VAVLLFPGFEELELASPLDALRE------AGAEVDVV-SPDGGPVESDVDLDDYD----------GLILPGGPGTPDDla 63

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1370452107 386 --EGKIQAIAWARNQKKPFLGVCLGMQLAVV 414
Cdd:cd01653    64 rdEALLALLREAAAAGKPILGICLGAQLLVL 94
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 308-411 3.70e-10

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: 56.83  E-value: 3.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 308 IALVGKYTKFSDSYASVIKALEHsalainHKLEIKYIdSADLEPITSQEEPVRYHeawqklcsahGVLVPGGFGV----R 383
Cdd:cd03128     1 VAVLLFGGSEELELASPLDALRE------AGAEVDVV-SPDGGPVESDVDLDDYD----------GLILPGGPGTpddlA 63

                          90       100
                  ....*....|....*....|....*...
gi 1370452107 384 GTEGKIQAIAWARNQKKPFLGVCLGMQL 411
Cdd:cd03128    64 WDEALLALLREAAAAGKPVLGICLGAQL 91
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 398-535 1.64e-08

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: 55.34  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 398 QKKPFLGVCLGMQLAVVefsrnVLG---WQDANSTefdpttshPVVVDMPEHNPGQMGGTmrlgkRRTLFQTKNSVMRKL 474
Cdd:pfam07722 104 RGKPILGICRGFQLLNV-----ALGgtlYQDIQEQ--------PGFTDHREHCQVAPYAP-----SHAVNVEPGSLLASL 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370452107 475 YGDADyleerhrhrFEVNpvwkkCLEEQGLKFVGQDVEGER------MEIVELEDHP-FFVGVQYHPE 535
Cdd:pfam07722 166 LGSEE---------FRVN-----SLHHQAIDRLAPGLRVEAvapdgtIEAIESPNAKgFALGVQWHPE 219
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 323-452 4.04e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 47.85  E-value: 4.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 323 SVIKALEHSAlainhkleikyidsADLEP-ITSQEEPVRyheawqklcSAHGVLVPG---------GFGVRGTEGKIQAI 392
Cdd:PRK13146   16 SAAKALERAG--------------AGADVvVTADPDAVA---------AADRVVLPGvgafadcmrGLRAVGLGEAVIEA 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370452107 393 AWARNqkKPFLGVCLGMQLAvveFSRNV-------LGWQDANSTEFDPTTSHPVVvdmPehnpgQMG 452
Cdd:PRK13146   73 VLAAG--RPFLGICVGMQLL---FERGLehgdtpgLGLIPGEVVRFQPDGPALKV---P-----HMG 126
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 323-446 1.99e-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: 45.80  E-value: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 323 SVIKALEHsalainhkLEIKYIDSADLEpitsqeepvryheawqKLCSAHGVLVPG-G-FG-----VRGTEGkIQAIAWA 395
Cdd:COG0118    15 SVAKALER--------LGAEVVVTSDPD----------------EIRAADRLVLPGvGaFGdamenLRERGL-DEAIREA 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370452107 396 RNQKKPFLGVCLGMQL-------------------AVVEFSRNVL-----GWqdaNSTEFdpTTSHPVVVDMPEH 446
Cdd:COG0118    70 VAGGKPVLGICLGMQLlferseengdteglglipgEVVRFPASDLkvphmGW---NTVEI--AKDHPLFAGIPDG 139
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 322-411 6.07e-05

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 44.35  E-value: 6.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 322 ASVIKALEhsalainhKLEIKYIDSADLEpitsqeepvryheawqKLCSAHGVLVPG--GFGV-------RGTEGKIQAI 392
Cdd:PRK13141   13 RSVEKALE--------RLGAEAVITSDPE----------------EILAADGVILPGvgAFPDamanlreRGLDEVIKEA 68

                          90
                  ....*....|....*....
gi 1370452107 393 AwarNQKKPFLGVCLGMQL 411
Cdd:PRK13141   69 V---ASGKPLLGICLGMQL 84
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 389-537 6.25e-05

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: 44.10  E-value: 6.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 389 IQAIAWARNQKKPFLGVCLGMQLAVVEFsrnvlgwqdanstefdpttshpvvvdmpehnpgqmGGTmrlgkrrtlfqtkn 468
Cdd:cd01745    90 LALLRAALERGKPILGICRGMQLLNVAL-----------------------------------GGT-------------- 120

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370452107 469 svmrkLYGDAdyleerhrhrfEVNpvwkkCLEEQGLKFVGQDVEGER------MEIVELEDHPFFVGVQYHPEFL 537
Cdd:cd01745   121 -----LYQDI-----------RVN-----SLHHQAIKRLADGLRVEArapdgvIEAIESPDRPFVLGVQWHPEWL 174
puuD PRK11366
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
 458-538 3.96e-04

gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional


Pssm-ID: 183101 [Multi-domain]  Cd Length: 254  Bit Score: 42.58  E-value: 3.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 458 GKRRTLFQTKNSVMRKLYGDADYLEERHRHRFEV-------------------------NPVWKKCLEEQGLKFVGQDVE 512
Cdd:PRK11366  116 GLQELVVATGGSLHRKLCEQPELLEHREDPELPVeqqyapshevqveeggllsallpecSNFWVNSLHGQGAKVVSPRLR 195

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1370452107 513 GER------MEIVELEDHPFFVGVQYHPEFLS 538
Cdd:PRK11366  196 VEArspdglVEAVSVINHPFALGVQWHPEWNS 227
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 389-451 4.87e-04

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: 41.86  E-value: 4.87e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 389 IQAIAWARNQKKPFLGVCLGMQL------AVVEFSRNV-LGWqdansTEFDPTTSHPVVVDMPEHNPGQM 451
Cdd:COG0518    72 PALIREAFELGKPVLGICYGAQLlahalgGKVEPGPGReIGW-----APVELTEADPLFAGLPDEFTVWM 136
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 366-435 7.07e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 41.00  E-value: 7.07e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370452107 366 QKLCSAHGVLVPG----GFGVRGTE--GKIQAIAWARNQKKPFLGVCLGMQL---AVVEFSRNVLGWQDANSTEFDPTT 435
Cdd:PRK13181   33 EEIAGADKVILPGvgafGQAMRSLResGLDEALKEHVEKKQPVLGICLGMQLlfeSSEEGNVKGLGLIPGDVKRFRSEP 111
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 322-411 1.06e-03

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: 40.56  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 322 ASVIKALEHsalainhkLEIKYIDSADLEPITSqeepvryheawqklcsAHGVLVPG----GFGVRGTE--GKIQAIAWA 395
Cdd:cd01748    12 RSVANALER--------LGAEVIITSDPEEILS----------------ADKLILPGvgafGDAMANLRerGLIEALKEA 67

                          90
                  ....*....|....*.
gi 1370452107 396 RNQKKPFLGVCLGMQL 411
Cdd:cd01748    68 IASGKPFLGICLGMQL 83
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 323-411 1.31e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 40.24  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452107 323 SVIKALEHsalainhkleikyidsADLEP-ITSQEEpvryheawqKLCSAHGVLVPG----GFGVRGTEGKIQAIAWARN 397
Cdd:PRK13143   15 SVSKALER----------------AGAEVvITSDPE---------EILDADGIVLPGvgafGAAMENLSPLRDVILEAAR 69

                          90
                  ....*....|....
gi 1370452107 398 QKKPFLGVCLGMQL 411
Cdd:PRK13143   70 SGKPFLGICLGMQL 83
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 9-55 4.55e-03

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: 37.03  E-value: 4.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1370452107   9 KYILVTGGViSGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAG 55
Cdd:cd01983     1 RVIAVTGGK-GGVGKTTLAAALAVALAAKGYKVLLIDLDDYVLIDGG 46
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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